|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-565 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 541.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 19 ADWGSYARLLPYLRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASY 98
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 99 RYISTSADMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKL 178
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 179 FLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVA 258
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 259 SFMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFDTPAE 338
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 339 VLEGSSARAFPGLSEAIRFEDVALAHDG-RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAP 417
Cdd:COG1132 324 IPDPPGAVPLPPVRGEIEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 418 LSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQ 497
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 498 RIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
26-565 |
6.04e-153 |
|
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: 455.83 E-value: 6.04e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 26 RLLPYLRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSA 105
Cdd:COG2274 146 WFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 106 DMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINsDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVL 185
Cdd:COG2274 226 RIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 186 LPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAV 265
Cdd:COG2274 305 IPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 266 PGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFDTPAEVLEGSSA 345
Cdd:COG2274 385 SGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSK 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 346 RAFPGLSEAIRFEDVALAHDGRA--VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTL 423
Cdd:COG2274 465 LSLPRLKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDP 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 424 GSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALAR 503
Cdd:COG2274 545 ASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIAR 624
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 504 VLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGR 686
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
25-569 |
1.79e-117 |
|
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: 359.85 E-value: 1.79e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 25 ARLLPYLRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLprdMGALVAIGLAMIGV-------TIGNYAlnilas 97
Cdd:COG4987 4 LRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAAL---APPILNLFVPIVGVrafaigrTVFRYL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 98 YRYISTSA--DMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLD 175
Cdd:COG4987 75 ERLVSHDAtlRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 176 WKL-FLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLR 254
Cdd:COG4987 155 PALaLVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 255 MQVASFMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAF----MAyqsrLFSPIQVLMGLVSGLSSARVSLARIF 330
Cdd:COG4987 235 LARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLvlaaLA----LFEALAPLPAAAQHLGRVRAAARRLN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 331 ELFDTPAEVLEGSSARAFPGlSEAIRFEDVALAHDG--RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDA 408
Cdd:COG4987 311 ELLDAPPAVTEPAEPAPAPG-GPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 409 GRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERG 488
Cdd:COG4987 390 GSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 489 LALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGRAHM 568
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
.
gi 1730203856 569 R 569
Cdd:COG4987 550 Q 550
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
23-565 |
8.27e-108 |
|
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: 334.76 E-value: 8.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 23 SYARLLPYLRPYLGRLTLVLLVSLISTAlnlAQPYLS---KMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYR 99
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAA---TESTLAallKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 100 YISTSADMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLF 179
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 180 LLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVAS 259
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 260 FMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFDTPAEV 339
Cdd:TIGR02203 238 SISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 340 LEGSsaRAFPGLSEAIRFEDVALAH--DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAP 417
Cdd:TIGR02203 318 DTGT--RAIERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 418 LSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARP-EASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGER 496
Cdd:TIGR02203 396 LADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQR 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 497 QRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-565 |
5.56e-102 |
|
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: 321.00 E-value: 5.56e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 1 MPQRSIEPPGSTREPARIADWGSYARLLPYLRPYLGRLTLVLLVsLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGL 80
Cdd:COG5265 2 PSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLL-LLAAALALVVPPLLKDAIDALLSGAAALLVVPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 81 amigvtIGNYALnilasYRYISTSADMLFDI-----------RVAL--LRHLQTLSPRFYSRFRLGDLmSRinsdvsDIQ 147
Cdd:COG5265 81 ------LLAYGL-----LRLLSVLFGELRDAlfarvtqravrRLALevFRHLHALSLRFHLERQTGGL-SR------DIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 148 RVT--ADTML-----SVLSNLLMLTGGVAIMLWL-DWKLFLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLV 219
Cdd:COG5265 143 RGTkgIEFLLrfllfNILPTLLEIALVAGILLVKyDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 220 DTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFM 299
Cdd:COG5265 223 DSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 300 AYQSRLFSPIQVLmGLV-SGLSSARVSLARIFELFDTPAEVLEGSSARAFPGLSEAIRFEDVALAHDG-RAVLKGFTLEI 377
Cdd:COG5265 303 AYLIQLYIPLNFL-GFVyREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPeRPILKGVSFEV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 378 PRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASE 457
Cdd:COG5265 382 PAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 458 EAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVL 537
Cdd:COG5265 462 EEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA 541
|
570 580 590
....*....|....*....|....*....|
gi 1730203856 538 PEATIIAITHRpaLAEV--ADRIITIEEGR 565
Cdd:COG5265 542 RGRTTLVIAHR--LSTIvdADEILVLEAGR 569
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
26-565 |
4.06e-100 |
|
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: 314.77 E-value: 4.06e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 26 RLLPYLRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPR-DMGALVAIGLAMIGVTIGNYALNILASYRYISTS 104
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGaPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 105 ADMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTAD----TMLSVLSNLLMLtggvAIMLWLDWK--L 178
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARylpqLFLAALVPLLIL----VAVFPLDWLsgL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 179 FLLA----IVLLPACVGLF--VVFQRKLDRLTRtmrergsdLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEA- 251
Cdd:COG4988 163 ILLVtaplIPLFMILVGKGaaKASRRQWRALAR--------LSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRt 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 252 M--LRMQvasFMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGT--LVAFMAyqSRLFSPIQvLMGL-----VSGLSSA 322
Cdd:COG4988 235 MkvLRVA---FLSSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAalFVLLLA--PEFFLPLR-DLGSfyharANGIAAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 323 rvslARIFELFDTPAEVLEGSSARAFPGLSEAIRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLV 401
Cdd:COG4988 309 ----EKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 402 RYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLA 481
Cdd:COG4988 385 GFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 482 TPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITI 561
Cdd:COG4988 465 TPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVL 544
|
....
gi 1730203856 562 EEGR 565
Cdd:COG4988 545 DDGR 548
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
38-329 |
4.69e-87 |
|
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: 271.73 E-value: 4.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLR 117
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQ 197
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 198 RKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGV 277
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 278 ILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-565 |
5.67e-80 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 265.82 E-value: 5.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 26 RLLPYLRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNIL--ASYRYisT 103
Cdd:TIGR00958 151 RLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLrgGSFNY--T 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 104 SADMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAI 183
Cdd:TIGR00958 229 MARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 184 VLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFR---------ARNSAFVEAMLr 254
Cdd:TIGR00958 309 INLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKealeetlqlNKRKALAYAGY- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 255 MQVASFMagavpGTLLAVttsGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFD 334
Cdd:TIGR00958 388 LWTTSVL-----GMLIQV---LVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLD 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 335 TPAEvLEGSSARAFPGLSEAIRFEDVALAHDGRA---VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRI 411
Cdd:TIGR00958 460 RKPN-IPLTGTLAPLNLEGLIEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 412 LFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLAL 491
Cdd:TIGR00958 539 LLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQL 618
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 492 SAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQvlPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGS 690
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
168-565 |
5.71e-76 |
|
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: 254.79 E-value: 5.71e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 168 VAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSA 247
Cdd:TIGR03375 277 LLVIAIIGGPLVWVPLVAIPLILLPGLLLQRPLSRLAEESMRESAQRNAVLVESLSGLETIKALNAEGRFQRRWEQTVAA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 248 FVEAMLRMQVASFMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLA 327
Cdd:TIGR03375 357 LARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGELTMGGLIACVMLSGRALAPLGQLAGLLTRYQQAKTALQ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 328 RIFELFDTPAEVLEGSSARAFPGLSEAIRFEDVALAH--DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLD 405
Cdd:TIGR03375 437 SLDELMQLPVERPEGTRFLHRPRLQGEIEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 406 PDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAG 485
Cdd:TIGR03375 517 PTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIG 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 486 ERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:TIGR03375 597 ERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGR 676
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-565 |
3.52e-75 |
|
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: 253.12 E-value: 3.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 23 SYARLLPYLRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYIS 102
Cdd:TIGR01193 143 SLLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 103 TSADMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRInSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLA 182
Cdd:TIGR01193 223 LGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRF-TDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 183 IVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMA 262
Cdd:TIGR01193 302 LLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQ 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 263 GAVPgTLLAVTTSGVILY-GGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFDTPAEVLE 341
Cdd:TIGR01193 382 QAIK-AVTKLILNVVILWtGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFIN 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 342 GSSARAFPGLSEAIRFEDVALAHD-GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSA 420
Cdd:TIGR01193 461 KKKRTELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 421 FTLGSLREKVILLDQTPYLFNDTIGANIAF-ARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRI 499
Cdd:TIGR01193 541 IDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRI 620
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 500 ALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQvLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGK 685
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-549 |
1.69e-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: 246.89 E-value: 1.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 25 ARLLPYLRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLprdMGALVAIGLAMIGVTignyALNIL-ASYRYIS- 102
Cdd:TIGR02868 2 LRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAE---MPPVLYLSVAAVAVR----AFGIGrAVFRYLEr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 103 -TSAD----MLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWK 177
Cdd:TIGR02868 75 lVGHDaalrSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 178 L-FLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQ 256
Cdd:TIGR02868 155 AaLILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 257 VASFMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFDTP 336
Cdd:TIGR02868 235 AATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 337 AEVLEGSSARAFPGLSEA--IRFEDVALAHDGRA-VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF 413
Cdd:TIGR02868 315 GPVAEGSAPAAGAVGLGKptLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 414 DQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSA 493
Cdd:TIGR02868 395 DGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 494 GERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRP 549
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
355-565 |
7.27e-73 |
|
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: 232.89 E-value: 7.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH--DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVIL 432
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVL 512
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 513 ILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGK 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
355-565 |
2.69e-72 |
|
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: 231.35 E-value: 2.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALA-HDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILL 433
Cdd:cd03253 1 IEFENVTFAyDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLI 513
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 514 LDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRpaLAEV--ADRIITIEEGR 565
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHR--LSTIvnADKIIVLKDGR 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-566 |
1.31e-71 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 240.78 E-value: 1.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 21 WGSYARLLPYLRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVtignyALNIL-ASYR 99
Cdd:PRK10790 8 WPTLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAAYV-----GLQLLaAGLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 100 YISTsadMLF-------------DIRVALLRhlQTLSPrfYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTG 166
Cdd:PRK10790 83 YAQS---LLFnraavgvvqqlrtDVMDAALR--QPLSA--FDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 167 GVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNS 246
Cdd:PRK10790 156 MLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 247 AFVEAmlRMQ---VASFMAGAVPGTLLAVTTSGVILYGGYQIiEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSAR 323
Cdd:PRK10790 236 SHYMA--RMQtlrLDGFLLRPLLSLFSALILCGLLMLFGFSA-SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 324 VSLARIFELFDTPAEVLeGSSARafPGLSEAIRFEDVALA-HDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVR 402
Cdd:PRK10790 313 VAGERVFELMDGPRQQY-GNDDR--PLQSGRIDIDNVSFAyRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 403 YLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARpEASEEAIRTAAHQAGLDPLLERLPQGLAT 482
Cdd:PRK10790 390 YYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 483 PAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIE 562
Cdd:PRK10790 469 PLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLH 548
|
....
gi 1730203856 563 EGRA 566
Cdd:PRK10790 549 RGQA 552
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-565 |
2.37e-70 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 237.22 E-value: 2.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 21 WGSYARLLPYLRPYlgrlTLVLLVSLISTALNLAQP----YLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILA 96
Cdd:PRK11176 10 WQTFRRLWPTIAPF----KAGLIVAGVALILNAASDtfmlSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGITSFIS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 97 SYRYISTSADMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDW 176
Cdd:PRK11176 86 SYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 177 KLFLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQ 256
Cdd:PRK11176 166 QLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 257 VASFMAGAVPgTLLAVTTSGVILY-GGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFDT 335
Cdd:PRK11176 246 SASSISDPII-QLIASLALAFVLYaASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 336 PAEVLEG--SSARAfpglSEAIRFEDVALAHDGR--AVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRI 411
Cdd:PRK11176 325 EQEKDEGkrVIERA----KGDIEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 412 LFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEA-SEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLA 490
Cdd:PRK11176 401 LLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 491 LSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGE 555
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
34-561 |
4.09e-68 |
|
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: 229.87 E-value: 4.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 34 YLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLP-RDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIR 112
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAgEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 113 VALLRHLQTLSPRFYSRFRLGDLMSRINSDVSD----IQRVTADTMLSVLSNLLMLtggvAIMLWLDWKLFLLAIVLLPA 188
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEAldgyFARYLPQLVLAVIVPLAIL----AAVFPQDWISGLILLLTAPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 189 CVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGT 268
Cdd:TIGR02857 157 IPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 269 LLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFDTPAEVlEGSSARAF 348
Cdd:TIGR02857 237 FATLSVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRP-LAGKAPVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 349 PGLSEAIRFEDVALAHDGR-AVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLR 427
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 428 EKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLR 507
Cdd:TIGR02857 396 DQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITI 561
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
355-565 |
4.63e-68 |
|
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: 220.17 E-value: 4.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHD-GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILL 433
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLI 513
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 514 LDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGK 214
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
38-329 |
1.24e-67 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 221.23 E-value: 1.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLP----RDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRV 113
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQlgpgGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 114 ALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLF 193
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 194 VVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVT 273
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 274 TSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-565 |
1.73e-67 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 229.46 E-value: 1.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 24 YARLLPYLRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALnilasyryIST 103
Cdd:PRK13657 7 YARVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGDIFPLLAAWAGFGLFNIIAGVL--------VAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 104 SADML-FDIRVALL----RHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKL 178
Cdd:PRK13657 79 HADRLaHRRRLAVLteyfERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 179 FLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRArnsaFVEAMLRMQ-- 256
Cdd:PRK13657 159 SLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRD----IADNLLAAQmp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 257 VASFMAGAVPGTLLAVTTS--GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFD 334
Cdd:PRK13657 235 VLSWWALASVLNRAASTITmlAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVED 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 335 TPAEVLEGSSARAFPGLSEAIRFEDVALAHDGRA-VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF 413
Cdd:PRK13657 315 AVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 414 DQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSA 493
Cdd:PRK13657 395 DGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSG 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 494 GERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK13657 475 GERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGR 546
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
355-565 |
7.21e-66 |
|
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: 212.24 E-value: 7.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRA--VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVIL 432
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFNDTIGANIafarpeaseeairtaahqagldpllerlpqglatpagerglaLSAGERQRIALARVLLRRPDVL 512
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 513 ILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
38-329 |
1.05e-65 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 216.19 E-value: 1.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLR 117
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQ 197
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 198 RKLDRLTRTMRERGSDLGSLLVDT--IMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTS 275
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 276 GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
38-329 |
4.05e-63 |
|
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: 209.21 E-value: 4.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLR 117
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQ 197
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 198 RKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEamLRMQVASFMAGAVP-GTLLA-VTTS 275
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRD--LNIKLAKLLAKYWPlMDFLSgLQIV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 276 GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18542 239 LVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
38-329 |
4.43e-63 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-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. 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: 349988 [Multi-domain] Cd Length: 294 Bit Score: 209.17 E-value: 4.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPR--DMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVAL 115
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGqgDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 116 LRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVV 195
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 196 FQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTS 275
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 276 GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
38-329 |
2.98e-61 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 205.05 E-value: 2.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALL---------------PRDMGALVAIGLAMIGVTIGNYALNILASYRYIS 102
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGdkplpgllglapllgPDPLALLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 103 TSADMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLA 182
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 183 IVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMA 262
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 263 GAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
37-329 |
4.34e-61 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV 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: 349989 [Multi-domain] Cd Length: 293 Bit Score: 203.85 E-value: 4.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 37 RLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALL 116
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 117 RHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVF 196
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 197 QRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSG 276
Cdd:cd18545 161 RRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTAL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 277 VILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18545 241 VYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
355-565 |
3.55e-60 |
|
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: 199.69 E-value: 3.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRA---VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVI 431
Cdd:cd03249 1 IEFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 432 LLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDV 511
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 512 LILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQ 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
108-565 |
1.44e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 205.06 E-value: 1.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 108 LFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVsdiqrvtaDTM----LSVLSNL---LMLTGGVAIML-WLDWKL- 178
Cdd:PRK11160 92 LTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADV--------DTLdhlyLRLISPLvaaLVVILVLTIGLsFFDLTLa 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 179 FLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAahetERFRARNSAFVEAMLRMQVA 258
Cdd:PRK11160 164 LTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAE----DRYRQQLEQTEQQWLAAQRR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 259 -SFMAGAVPGTLLAVT--TSGVILYGGYQIIEGTMSIGTLVAFMAYQSrlFSPIQVLM---GLVSGLSSARVSLARIFEL 332
Cdd:PRK11160 240 qANLTGLSQALMILANglTVVLMLWLAAGGVGGNAQPGALIALFVFAA--LAAFEALMpvaGAFQHLGQVIASARRINEI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 333 FDTPAEVLEGSSARAFPGlSEAIRFEDVALAHDGRA--VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGR 410
Cdd:PRK11160 318 TEQKPEVTFPTTSTAAAD-QVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 411 ILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERlPQGLATPAGERGLA 490
Cdd:PRK11160 397 ILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQ 475
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 491 LSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQ 550
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
41-569 |
1.78e-57 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 202.25 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 41 VLLVSLISTaLNLAQPYLSKMLID--------NALLPRDMGALVAIGLAmigVTIGNYALNIL---ASYRyistsadMLF 109
Cdd:PRK10789 1 VALLIIIAM-LQLIPPKVVGIIVDgvteqhmtTGQILMWIGTMVLIAVV---VYLLRYVWRVLlfgASYQ-------LAV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 110 DIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMltgGVAIML----WLDWKLFLLAivL 185
Cdd:PRK10789 70 ELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVM---GCAVLIvmstQISWQLTLLA--L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 186 LPACVgLFVVFQRKLDRLTRTMRERGSDLGSL---LVDTIMGMRVVSSLNAAAHETERFRArnSAFVEAMLRMQVASFMA 262
Cdd:PRK10789 145 LPMPV-MAIMIKRYGDQLHERFKLAQAAFSSLndrTQESLTSIRMIKAFGLEDRQSALFAA--DAEDTGKKNMRVARIDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 263 GAVPGTLLAVTTSGVILYGG--YQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFDTPAEVL 340
Cdd:PRK10789 222 RFDPTIYIAIGMANLLAIGGgsWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 341 EGS-SARAFPG-LSEAIRfeDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPL 418
Cdd:PRK10789 302 DGSePVPEGRGeLDVNIR--QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 419 SAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQR 498
Cdd:PRK10789 380 TKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQR 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 499 IALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHR-PALAEvADRIITIEEGRAHMR 569
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRlSALTE-ASEILVMQHGHIAQR 530
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
38-329 |
2.93e-57 |
|
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: 193.79 E-value: 2.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVT----IGNYALNILASYryisTSADMLFDIRV 113
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFllrgLASYLQTYLMAY----VGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 114 ALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLF 193
Cdd:cd18552 77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 194 VVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVT 273
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 274 TSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18552 237 IALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
38-329 |
6.80e-57 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis 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: 349990 [Multi-domain] Cd Length: 292 Bit Score: 192.70 E-value: 6.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLR 117
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQ 197
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 198 RKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVAsfMAGAVPGTLL--AVTTS 275
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRL--VAIYFPGVELlgNLATA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 276 GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18546 239 AVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
354-565 |
3.38e-56 |
|
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: 188.57 E-value: 3.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDG--RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVI 431
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 432 LLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDV 511
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 512 LILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGR 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
168-568 |
1.15e-55 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 196.89 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 168 VAIMLWLDWKLFLLAIVLLPACVGLFVVFQRK----LDRLTRTMRERGSDLGSLL--VDTI--MGMrvvssLNAAAhetE 239
Cdd:COG4618 147 LAVLFLFHPLLGLLALVGALVLVALALLNERLtrkpLKEANEAAIRANAFAEAALrnAEVIeaMGM-----LPALR---R 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 240 RFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGL 319
Cdd:COG4618 219 RWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQF 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 320 SSARVSLARIFELFDT-PAEvlegSSARAFPGLSEAIRFEDVALAHDG--RAVLKGFTLEIPRGSFCAVLGPSGVGKSTL 396
Cdd:COG4618 299 VSARQAYRRLNELLAAvPAE----PERMPLPRPKGRLSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 397 ADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAfaR-PEASEEAIRTAAHQAGLDPLLER 475
Cdd:COG4618 375 ARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA--RfGDADPEKVVAAAKLAGVHEMILR 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 476 LPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE-ATIIAITHRPALAEV 554
Cdd:COG4618 453 LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAA 532
|
410
....*....|....
gi 1730203856 555 ADRIITIEEGRAHM 568
Cdd:COG4618 533 VDKLLVLRDGRVQA 546
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
38-329 |
7.72e-55 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 187.36 E-value: 7.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALL-PRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALL 116
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIgSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 117 RHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVF 196
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 197 QRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRmqVASFMAGAVPGTLLAVTTSG 276
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLR--AMKLWAIFHPLMEFLTSLGT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 277 VI--LYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18778 239 VLvlGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
355-565 |
2.73e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 183.09 E-value: 2.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLD 434
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFNDTIGANIAF----ARPEASEEAIRTAAHQAGLDPLLerlpqgLATPAGErglaLSAGERQRIALARVLLRRPD 510
Cdd:COG4619 81 QEPALWGGTVRDNLPFpfqlRERKFDRERALELLERLGLPPDI------LDKPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 511 VLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAE-VADRIITIEEGR 565
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHDPEQIErVADRVLTLEAGR 208
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
355-565 |
5.67e-54 |
|
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: 183.06 E-value: 5.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRA---VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVI 431
Cdd:cd03248 12 VKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 432 LLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDV 511
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 512 LILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
355-565 |
6.27e-52 |
|
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: 177.52 E-value: 6.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALA-HDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILL 433
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTP--YLFNDTIGANIAFArPEA---SEEAIRTAAHQA----GLDPLLERLPQglatpagerglALSAGERQRIALARV 504
Cdd:COG1122 81 FQNPddQLFAPTVEEDVAFG-PENlglPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 505 LLRRPDVLILDEPTSALDPKTERHIAQTLRQvLPEA--TIIAITHRPALA-EVADRIITIEEGR 565
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKR-LNKEgkTVIIVTHDLDLVaELADRVIVLDDGR 211
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
40-329 |
6.89e-52 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 179.60 E-value: 6.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 40 LVLLvsLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLRHL 119
Cdd:cd18576 2 LILL--LLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 120 QTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRK 199
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 200 LDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGVIL 279
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 280 YGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18576 240 YGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
38-316 |
2.10e-51 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. 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: 349993 [Multi-domain] Cd Length: 295 Bit Score: 178.41 E-value: 2.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLR 117
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVT----ADTMLSVLsnllMLTGGVAIMLWLDWKLFLLAIVLLPACVGLF 193
Cdd:cd18549 84 HLQKLSFSFFDNNKTGQLMSRITNDLFDISELAhhgpEDLFISII----TIIGSFIILLTINVPLTLIVFALLPLMIIFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 194 VVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRM--QVASFMAGAvpGTLLA 271
Cdd:cd18549 160 IYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAykAMAYFFSGM--NFFTN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1730203856 272 VTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLV 316
Cdd:cd18549 238 LLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFT 282
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
38-329 |
1.77e-50 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis 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: 349987 [Multi-domain] Cd Length: 291 Bit Score: 175.75 E-value: 1.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLR 117
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLsVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQ 197
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPF-LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 198 RKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAmlRMQVASFMA--GAVPGTLLAVTTS 275
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRAT--RLRAARLRArfWPLLEALPELGLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 276 GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18543 238 AVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
31-568 |
2.69e-49 |
|
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: 179.08 E-value: 2.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 31 LRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADmlFD 110
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEK--LD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 111 IRVAllrhlqtlSPRFYSRFRLGdlMSRINSD----VSDIQRVTAdtmlsvlsnllMLTGGVAIMLW-LDW-KLFLLAIV 184
Cdd:TIGR01842 79 GALN--------QPIFAASFSAT--LRRGSGDglqaLRDLDQLRQ-----------FLTGPGLFAFFdAPWmPIYLLVCF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 185 LLPACVGLFVVF----------------QRKLDRLTRTMRERGSDLGSLL----VDTIMGMRvvsslnaaAHETERFRAR 244
Cdd:TIGR01842 138 LLHPWIGILALGgavvlvglallnnratKKPLKEATEASIRANNLADSALrnaeVIEAMGMM--------GNLTKRWGRF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 245 NSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARV 324
Cdd:TIGR01842 210 HSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 325 SLARIFELFdtpAEVLEGSSARAFPGLSEAIRFEDVALAHDG--RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVR 402
Cdd:TIGR01842 290 AYKRLNELL---ANYPSRDPAMPLPEPEGHLSVENVTIVPPGgkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 403 YLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLAT 482
Cdd:TIGR01842 367 IWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 483 PAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQV-LPEATIIAITHRPALAEVADRIITI 561
Cdd:TIGR01842 447 VIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVL 526
|
....*..
gi 1730203856 562 EEGRAHM 568
Cdd:TIGR01842 527 QDGRIAR 533
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
38-329 |
3.64e-49 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 172.25 E-value: 3.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMlfDIRVAL-- 115
Cdd:cd18570 4 LILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKL--DIRLILgy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 116 LRHLQTLSPRFYSRFRLGDLMSRINsDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVV 195
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 196 FQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTS 275
Cdd:cd18570 161 FNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 276 GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18570 241 LILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
355-565 |
3.79e-49 |
|
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: 170.36 E-value: 3.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH--DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVIL 432
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVL 512
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 513 ILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGR 213
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
24-565 |
6.59e-49 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 178.93 E-value: 6.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 24 YARLLPYLRPYLGRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMgalvaigLAMIGVTIGNYALNILAsYRYIST 103
Cdd:TIGR01192 7 YVRALSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSDV-------LPTLALWAGFGVFNTIA-YVLVAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 104 SADMLFDIRVALL---------------RHLQTLSPRFYSRFRLGDLMSRInsdvsdiqrvTADTMLSVLSNLLMLTGGV 168
Cdd:TIGR01192 79 EADRLAHGRRATLlteafgriismplswHQQRGTSNALHTLLRATETLFGL----------WLEFMRQHLATFVALFLLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 169 AIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRArnsaF 248
Cdd:TIGR01192 149 PTAFAMDWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQ----F 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 249 VEAMLRMQ--VASFMAGAVPGTLLAVTTS--GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARV 324
Cdd:TIGR01192 225 TNNLLSAQypVLDWWALASGLNRMASTISmmCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 325 SLARIFELFDTPAEVLEGSSARAFPGLSEAIRFEDVA--LAHDGRAVlKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVR 402
Cdd:TIGR01192 305 KLEDFFDLEDSVFQREEPADAPELPNVKGAVEFRHITfeFANSSQGV-FDVSFEAKAGQTVAIVGPTGAGKTTLINLLQR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 403 YLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLAT 482
Cdd:TIGR01192 384 VYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDT 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 483 PAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIE 562
Cdd:TIGR01192 464 LVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLD 543
|
...
gi 1730203856 563 EGR 565
Cdd:TIGR01192 544 QGR 546
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
356-565 |
4.76e-48 |
|
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: 166.49 E-value: 4.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 356 RFEDVALAHDG--RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILL 433
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTP--YLFNDTIGANIAFA------RPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVL 505
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 506 LRRPDVLILDEPTSALDPKTERHIAQTLRQvLPEA--TIIAITHRPA-LAEVADRIITIEEGR 565
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
38-329 |
1.62e-47 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. 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: 349995 [Multi-domain] Cd Length: 289 Bit Score: 167.61 E-value: 1.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIglaMIGVTIGNYALNILASYRYISTSADMLFDIRVALLR 117
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLAL---LVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQ 197
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 198 RKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRAR-NSAFveaMLRMQVASFMAGAVPGTLLAVTTS- 275
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAaERLY---RAGLKAAKIEALIGPLMGLAVQLAl 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 276 -GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18551 235 lVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
38-329 |
1.97e-47 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-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. 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: 349985 [Multi-domain] Cd Length: 293 Bit Score: 167.59 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDN-ALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALL 116
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDAlTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 117 RHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVF 196
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 197 QRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSG 276
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 277 VILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18541 241 VLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
40-329 |
6.52e-47 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima 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, 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: 349992 [Multi-domain] Cd Length: 292 Bit Score: 166.03 E-value: 6.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 40 LVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLRHL 119
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 120 QTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKL---FLLAIVLLPACVG----- 191
Cdd:cd18548 83 QSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLaliLLVAIPILALVVFlimkk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 192 ---LFVVFQRKLDRLTRTMRERgsdlgsllvdtIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRmqVASFMAGAVPGT 268
Cdd:cd18548 163 aipLFKKVQKKLDRLNRVVREN-----------LTGIRVIRAFNREDYEEERFDKANDDLTDTSLK--AGRLMALLNPLM 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 269 LLAV--TTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18548 230 MLIMnlAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
355-568 |
6.95e-46 |
|
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: 159.40 E-value: 6.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRA--VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTlGSLREKVIL 432
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFNDTIGANIafarpeaseeairtaahqagldpllerlpqglatpagerGLALSAGERQRIALARVLLRRPDVL 512
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 513 ILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGRAHM 568
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
355-565 |
2.01e-45 |
|
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: 159.97 E-value: 2.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH--DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVIL 432
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFNDTIGANIAfarP--EASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPD 510
Cdd:cd03244 83 IPQDPVLFSGTIRSNLD---PfgEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 511 VLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRpaLAEVA--DRIITIEEGR 565
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHR--LDTIIdsDRILVLDKGR 214
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
38-329 |
4.87e-43 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima 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, 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: 349991 [Multi-domain] Cd Length: 298 Bit Score: 156.02 E-value: 4.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPR------DMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDI 111
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 112 RVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVG 191
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 192 LFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRmqvASFMAGAVPGTLLA 271
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK---AQFYSGLLMPIMNF 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 272 VTTSG---VILYGGYQIIEGTMSIGTLVAFMAYqSRLFS-PIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18547 238 INNLGyvlVAVVGGLLVINGALTVGVIQAFLQY-SRQFSqPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
42-329 |
9.48e-43 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 154.64 E-value: 9.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 42 LLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLRHLQT 121
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 122 LSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLD 201
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 202 RLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGVILYG 281
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1730203856 282 GYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18557 242 GYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
38-309 |
3.85e-42 |
|
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: 152.80 E-value: 3.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMG--ALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVAL 115
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 116 LRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVV 195
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 196 FQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTS 275
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1730203856 276 GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPI 309
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
286-576 |
2.16e-41 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 157.66 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 286 IEGTMSIGTLV----AFMAYQSRLFSPIQVLmglvSGLSSARVSLARIFELFD--TPAEVLEGSSARAFPGLSEAIRFED 359
Cdd:COG4178 292 FAGEITLGGLMqaasAFGQVQGALSWFVDNY----QSLAEWRATVDRLAGFEEalEAADALPEAASRIETSEDGALALED 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 360 VALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTL----ADL-------LVRyldPDAGRILFdqaplsaftlgslr 427
Cdd:COG4178 368 LTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLlraiAGLwpygsgrIAR---PAGARVLF-------------- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 428 ekvilLDQTPYLFNDTIGANIAFARPEA--SEEAIRTAAHQAGLDPLLERLPQGLAtpageRGLALSAGERQRIALARVL 505
Cdd:COG4178 431 -----LPQRPYLPLGTLREALLYPATAEafSDAELREALEAVGLGHLAERLDEEAD-----WDQVLSLGEQQRLAFARLL 500
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 506 LRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGRAHMRTAASLAP 576
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
355-565 |
7.07e-41 |
|
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: 146.85 E-value: 7.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRA-----VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRIlfdqaplsaftlgSLREK 429
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 VILLDQTPYLFNDTIGANIAFARP---EASEEAIRTAAhqagLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLL 506
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfdeERYEKVIKACA----LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 507 RRPDVLILDEPTSALDPKTERHIAQT-LRQVLPE-ATIIAITHRPALAEVADRIITIEEGR 565
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNnKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
329-565 |
1.94e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 155.00 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 329 IFELFDTPAEVLEGSSARAFPGLSEAIRFED-VALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLdPD 407
Cdd:PRK11174 324 LVTFLETPLAHPQQGEKELASNDPVTIEAEDlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 408 AGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGER 487
Cdd:PRK11174 403 QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQ 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 488 GLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK11174 483 AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
37-329 |
2.38e-40 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 148.40 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 37 RLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNyALNILASYRYIST-SADMLFDIRVAL 115
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQ-ALSVFLFIRLAGKiEMGVSYDLRKKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 116 LRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVV 195
Cdd:cd18540 82 FEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 196 FQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAaahETERFRarnsAFVEAMLRMQVASFMAG-------AVPGT 268
Cdd:cd18540 162 FQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVR---EEKNLR----EFKELTEEMRRASVRAArlsalflPIVLF 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 269 LLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18540 235 LGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
354-565 |
9.21e-40 |
|
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: 145.57 E-value: 9.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILL 433
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTPYL-FNDTIGANIAFAR----------PEASEEAIRTAAHQAGLDPLLERlpqglatPAGErglaLSAGERQRIALA 502
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRyphlglfgrpSAEDREAVEEALERTGLEHLADR-------PVDE----LSGGERQRVLIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALA-EVADRIITIEEGR 565
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAaRYADRLVLLKDGR 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
355-565 |
4.24e-39 |
|
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: 142.70 E-value: 4.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLD-----PDAGRILFDQAPLSA--FTLGSLR 427
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 428 EKVILLDQTPYLFNDTIGANIAFA---RPEASEEAIRTAAHQAgldplLER--LPQGLATPAGerGLALSAGERQRIALA 502
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGlrlHGIKLKEELDERVEEA-----LRKaaLWDEVKDRLH--ALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAE-VADRIITIEEGR 565
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGR 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
369-565 |
1.37e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.33 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT---LGSLR-EKVILLDQTPYLFND-T 443
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLRrRHIGFVFQFFNLLPElT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 444 IGANIAFA------RPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:COG1136 103 ALENVALPlllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 518 TSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAEVADRIITIEEGR 565
Cdd:COG1136 172 TGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGR 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
355-566 |
1.57e-38 |
|
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: 139.66 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDG--RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVIL 432
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFNDTIGANIafarpeaseeairtaahqagldpllerlpqglatpagerglaLSAGERQRIALARVLLRRPDVL 512
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 513 ILDEPTSALDPKTERHIAQTLRQV-LPEATIIAITHRPALAEVADRIITIEEGRA 566
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
355-567 |
2.05e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.05 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAvlKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAftLGSLREKVILLD 434
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA--LPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFND-TIGANIAFA-RP-----EASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLR 507
Cdd:COG3840 78 QENNLFPHlTVAQNIGLGlRPglkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAE-VADRIITIEEGRAH 567
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRErgLTVLMVTHDPEDAArIADRVLLVADGRIA 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
355-565 |
9.90e-38 |
|
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: 138.81 E-value: 9.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSafTLGSLREKVILLD 434
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLF-NDTIGANIAFA--RPEASEEAIRTAAHQA----GLDPLLERLPqglatpagergLALSAGERQRIALARVLLR 507
Cdd:cd03259 79 QDYALFpHLTVAENIAFGlkLRGVPKAEIRARVRELlelvGLEGLLNRYP-----------HELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEAlALADRIAVMNEGR 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
356-565 |
3.22e-37 |
|
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: 135.45 E-value: 3.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 356 RFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQ 435
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 436 tpylfndtiganiafarpeaseeairtaahqagldpllerlpqglatpagerglaLSAGERQRIALARVLLRRPDVLILD 515
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 516 EPTSALDPKTERHIAQTLRQVLPE-ATIIAITHRPALAE-VADRIITIEEGR 565
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
354-565 |
1.58e-36 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 136.26 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT---LGSLREKV 430
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 431 ILLDQTPYLFND-TIGANIAFA---RPEASEEAIRTAA----HQAGLDPLLERLPqglatpaGErglaLSAGERQRIALA 502
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVleklELVGLPGAADKMP-------SE----LSGGMRKRVALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTERHIAQ---TLRQVLPeATIIAITHR-PALAEVADRIITIEEGR 565
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDElirELRDELG-LTSVVVTHDlDSAFAIADRVAVLADGK 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-565 |
4.05e-36 |
|
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: 142.24 E-value: 4.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 31 LRPYLGRLTLVLLVSLISTALNLAqpylSKMLIDNALLpRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFD 110
Cdd:COG4615 8 LRESRWLLLLALLLGLLSGLANAG----LIALINQALN-ATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 111 IRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTAdTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACV 190
Cdd:COG4615 83 LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 191 GLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSsLNaaaheterfRARNSAFVEAML----------RMQVASF 260
Cdd:COG4615 162 AGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELK-LN---------RRRRRAFFDEDLqptaeryrdlRIRADTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 261 MAGAVP-GTLLAVTTSGVILYGGYQIieGTMSIGTLVAF---MAYqsrLFSPIQVLMGLVSGLSSARVSLARIFEL---F 333
Cdd:COG4615 232 FALANNwGNLLFFALIGLILFLLPAL--GWADPAVLSGFvlvLLF---LRGPLSQLVGALPTLSRANVALRKIEELelaL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 334 DTPAEVLEGSSARAFPGLSEAIRFEDVALAHDGRAVLKGFT-----LEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDA 408
Cdd:COG4615 307 AAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEGFTlgpidLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPES 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 409 GRILFDQAPLSAFTLGSLREK--VILLDQtpYLFNDTIGAniafaRPEASEEAIRtaahqagldPLLERLpqGLATPAGE 486
Cdd:COG4615 387 GEILLDGQPVTADNREAYRQLfsAVFSDF--HLFDRLLGL-----DGEADPARAR---------ELLERL--ELDHKVSV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 487 RG-----LALSAGERQRIALARVLLRRPDVLILDEPTSALDPkTERHIaqTLRQVLPE-----ATIIAITHRPALAEVAD 556
Cdd:COG4615 449 EDgrfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDP-EFRRV--FYTELLPElkargKTVIAISHDDRYFDLAD 525
|
....*....
gi 1730203856 557 RIITIEEGR 565
Cdd:COG4615 526 RVLKMDYGK 534
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
358-565 |
6.96e-36 |
|
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: 132.56 E-value: 6.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQtp 437
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 438 ylfndtiganiafarpeaseeairtAAHQAGLDPLLERlpqglatPAGErglaLSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:cd03214 81 -------------------------ALELLGLAHLADR-------PFNE----LSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 518 TSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALA-EVADRIITIEEGR 565
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAaRYADRVILLKDGR 175
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
369-565 |
8.83e-36 |
|
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: 133.38 E-value: 8.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSL----REKVILLDQTPYLFND-T 443
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFNLLPDlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 444 IGANIAFA------RPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:cd03255 99 ALENVELPlllagvPKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 518 TSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALAEVADRIITIEEGR 565
Cdd:cd03255 168 TGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
355-565 |
9.17e-36 |
|
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: 133.78 E-value: 9.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT---LGSLREKVI 431
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 432 LLDQTPYLFND-TIGANIAF---ARPEASEEAIRTAA----HQAGLDPLLERLPqglatpaGErglaLSAGERQRIALAR 503
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFplrEHTRLSEEEIREIVleklEAVGLRGAEDLYP-------AE----LSGGMKKRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 504 VLLRRPDVLILDEPTSALDPKTERHIAQ---TLRQVLPeATIIAITHR-PALAEVADRIITIEEGR 565
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDlirSLKKELG-LTSIMVTHDlDTAFAIADRIAVLYDGK 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
363-565 |
9.69e-36 |
|
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: 134.16 E-value: 9.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 363 AHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYL-FN 441
Cdd:COG1124 14 GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAsLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 442 ------DTIGANIAFARPEASEEAIRTAAHQAGLDP-LLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLIL 514
Cdd:COG1124 94 prhtvdRILAEPLRIHGLPDREERIAELLEQVGLPPsFLDRYPH-----------QLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 515 DEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAE-VADRIITIEEGR 565
Cdd:COG1124 163 DEPTSALDVSVQAEILNLLKDLREErgLTYLFVSHDLAVVAhLCDRVAVMQNGR 216
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
41-301 |
1.07e-35 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 135.30 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 41 VLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIgnyALNILASYRY--ISTSADMLF-DIRVALLR 117
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVAL---VLALASALRFylVSWLGERVVaDLRKAVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQ 197
Cdd:cd18575 78 HLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 198 RKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRAR-NSAFVEAMLRMQVASFMAGAVpgTLLAVTTSG 276
Cdd:cd18575 158 RRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAvEAAFAAALRRIRARALLTALV--IFLVFGAIV 235
|
250 260
....*....|....*....|....*.
gi 1730203856 277 VILY-GGYQIIEGTMSIGTLVAFMAY 301
Cdd:cd18575 236 FVLWlGAHDVLAGRMSAGELSQFVFY 261
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
355-568 |
1.27e-35 |
|
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: 134.89 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALA-HDG----RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQ---APLSAFTLGSL 426
Cdd:TIGR04521 1 IKLKNVSYIyQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrdiTAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 427 REKVILLDQTP--YLFNDTIGANIAF------ARPEASEEAIRTAAHQAGLDP-LLERLPqglatpagergLALSAGERQ 497
Cdd:TIGR04521 81 RKKVGLVFQFPehQLFEETVYKDIAFgpknlgLSEEEAEERVKEALELVGLDEeYLERSP-----------FELSGGQMR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 498 RIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPA-LAEVADRIITIEEGRAHM 568
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEdVAEYADRVIVMHKGKIVL 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
354-565 |
5.55e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 135.23 E-value: 5.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSaftlgslrekvill 433
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTPY------------LF-NDTIGANIAF---ARpEASEEAIRTAAHQA----GLDPLLERLPQglatpagerglALSA 493
Cdd:COG3842 71 GLPPEkrnvgmvfqdyaLFpHLTVAENVAFglrMR-GVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 494 GERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRP--ALAeVADRIITIEEGR 565
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElgITFIYVTHDQeeALA-LADRIAVMNDGR 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
355-565 |
6.81e-35 |
|
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: 131.47 E-value: 6.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRA----VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF---DQAPLSAFTLGSLR 427
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 428 EKVILLDQTPYL-FND--TIGANIA----FARPEASEEAIRTAAHQA----GLDP-LLERLPQglatpagerglALSAGE 495
Cdd:cd03257 82 KEIQMVFQDPMSsLNPrmTIGEQIAeplrIHGKLSKKEARKEAVLLLlvgvGLPEeVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 496 RQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLR--QVLPEATIIAITHRPAL-AEVADRIITIEEGR 565
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVvAKIADRVAVMYAGK 223
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
38-329 |
8.51e-35 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 133.10 E-value: 8.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLR 117
Cdd:cd18782 4 LIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRInSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQ 197
Cdd:cd18782 84 HLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 198 RKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGV 277
Cdd:cd18782 163 PILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 278 ILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18782 243 LWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
326-565 |
9.26e-35 |
|
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: 137.73 E-value: 9.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 326 LARIFELFDTPAEVLEGSSARAFPGLSE-AIRFEDVALAHDGRA-----VLKGFTLEIPRGSFCAVLGPSGVGKSTLADL 399
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEpLLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 400 LVRYLDPDAGRILFDQAPLSAFTLGSLRE---KVILLDQTPYL-FN--DTIGANIAFA-------RPEASEEAIRTAAHQ 466
Cdd:COG1123 311 LLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQDPYSsLNprMTVGDIIAEPlrlhgllSRAERRERVAELLER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 467 AGLDP-LLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TII 543
Cdd:COG1123 391 VGLPPdLADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYL 459
|
250 260
....*....|....*....|...
gi 1730203856 544 AITHRPALA-EVADRIITIEEGR 565
Cdd:COG1123 460 FISHDLAVVrYIADRVAVMYDGR 482
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
355-569 |
1.33e-34 |
|
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: 130.28 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRA----VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAftlgsLREKV 430
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 431 ILLDQTPYLFN-DTIGANIAF-------ARPEASEEAIRtAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALA 502
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALglelqgvPKAEARERAEE-LLELVGLSGFENAYPH-----------QLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHrpALAE---VADRIITIEEGRAHMR 569
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtgKTVLLVTH--DIDEavfLADRVVVLSARPGRIV 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
355-565 |
5.48e-34 |
|
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: 129.22 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREkviLL 433
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQ---LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTPYLFND-------TIGANIAFARPEA-----------SEEAIRTAAHqagldpLLERLpqGLATPAGERGLALSAGE 495
Cdd:cd03256 78 RQIGMIFQQfnlierlSVLENVLSGRLGRrstwrslfglfPKEEKQRALA------ALERV--GLLDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 496 RQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLArEYADRIVGLKDGR 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
354-565 |
6.60e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.02 E-value: 6.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLRE---K 429
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 VILLDQTPYLFND-TIGANI------------AFARPEASEEaiRTAAHQAgldplLERLpqGLATPAGERGLALSAGER 496
Cdd:COG3638 82 IGMIFQQFNLVPRlSVLTNVlagrlgrtstwrSLLGLFPPED--RERALEA-----LERV--GLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 497 QRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdgITVVVNLHQVDLArRYADRIIGLRDGR 224
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
42-329 |
7.59e-34 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 130.62 E-value: 7.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 42 LLVSLISTALNLAQPYLSKMLIDNALLPRDMGA-------LVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVA 114
Cdd:cd18554 5 IVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLdekvyklFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 115 LLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFV 194
Cdd:cd18554 85 LFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 195 VFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTT 274
Cdd:cd18554 165 YFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAP 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 275 SGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18554 245 LLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
42-329 |
1.20e-33 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 130.38 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 42 LLVSLISTALNLAQPYLSKMLID--------------NALLPRD-MGALVAIGLAMIGVTIGNYALNILASYRYISTSAD 106
Cdd:cd18565 5 LLASILNRLFDLAPPLLIGVAIDavfngeasflplvpASLGPADpRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 107 MLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLL 186
Cdd:cd18565 85 VQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 187 PACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAmlRMQVASFMAGAVP 266
Cdd:cd18565 165 PLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDA--NWRAIRLRAAFFP 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 267 GTLLAVTTS--GVILYGGYQIIEG------TMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18565 243 VIRLVAGAGfvATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
355-565 |
1.45e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.87 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLgSLREKVILLD 434
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFND-TIGANIAFA------RPEASEEAIRTAAHQAGLDPLLERlpqglatPAGErglaLSAGERQRIALARVLLR 507
Cdd:COG1131 80 QEPALYPDlTVRENLRFFarlyglPRKEARERIDELLELFGLTDAADR-------KVGT----LSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLRQ-VLPEATIIAITHRPALAE-VADRIITIEEGR 565
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAErLCDRVAIIDKGR 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
73-564 |
2.62e-33 |
|
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: 136.23 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 73 GAL-VAIGLAMIGVTIGNYALNILASYRyistsadmlfdIRVALLrHLQTLSPR-FYSRFRLGDLMSRINSDVSDIQRVT 150
Cdd:TIGR00957 1012 GALgILQGFAVFGYSMAVSIGGIQASRV-----------LHQDLL-HNKLRSPMsFFERTPSGNLVNRFSKELDTVDSMI 1079
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 151 ADTMLSVLSNLLMLTGGVAIMLwLDWKLFllAIVLLPACVGLFVVFQ------RKLDRLTRTMRergSDLGSLLVDTIMG 224
Cdd:TIGR00957 1080 PPVIKMFMGSLFNVIGALIVIL-LATPIA--AVIIPPLGLLYFFVQRfyvassRQLKRLESVSR---SPVYSHFNETLLG 1153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 225 MRVVSSLNaaahETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGVILYGG-YQII-EGTMSIGTLVAFMAYQ 302
Cdd:TIGR00957 1154 VSVIRAFE----EQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAAlFAVIsRHSLSAGLVGLSVSYS 1229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 303 SRLFSPIQVLMGLVSGLSSARVSLARIFELFDT----PAEVLEGSSARAFPGLSEaIRFEDVALAH--DGRAVLKGFTLE 376
Cdd:TIGR00957 1230 LQVTFYLNWLVRMSSEMETNIVAVERLKEYSETekeaPWQIQETAPPSGWPPRGR-VEFRNYCLRYreDLDLVLRHINVT 1308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 377 IPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANI-AFArpEA 455
Cdd:TIGR00957 1309 IHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS--QY 1386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 456 SEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQ 535
Cdd:TIGR00957 1387 SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT 1466
|
490 500 510
....*....|....*....|....*....|.
gi 1730203856 536 VLPEATIIAITHRpaLAEVAD--RIITIEEG 564
Cdd:TIGR00957 1467 QFEDCTVLTIAHR--LNTIMDytRVIVLDKG 1495
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
354-565 |
4.68e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.41 E-value: 4.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDG--RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVI 431
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 432 LLDQTPYlfNDTIGA----NIAFA------RPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIAL 501
Cdd:PRK13632 87 IIFQNPD--NQFIGAtvedDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 502 ARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGK 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
78-565 |
4.79e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 135.49 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 78 IGLAMIGVTIGNyalnilaSYRYISTSADMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSV 157
Cdd:PLN03232 959 LGFGQVAVTFTN-------SFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMF 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 158 LSNLLMLTGGVAIMLWLD----WKLFLLAIVLLPAcvglFVVFQ------RKLDRLTRtmrergSDLGSLLVDTIMGMRV 227
Cdd:PLN03232 1032 MNQLWQLLSTFALIGTVStislWAIMPLLILFYAA----YLYYQstsrevRRLDSVTR------SPIYAQFGEALNGLSS 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 228 VSSLNAaaheTERFRARNSAFVEAMLRMQVASFMAG--------AVPGTLLAVTTS-GVILYGGYQIIEGTMSIGTLVaf 298
Cdd:PLN03232 1102 IRAYKA----YDRMAKINGKSMDNNIRFTLANTSSNrwltirleTLGGVMIWLTATfAVLRNGNAENQAGFASTMGLL-- 1175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 299 MAYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFDTPAE---VLEGSSARAFPGLSEAIRFEDVALAHDGR--AVLKGF 373
Cdd:PLN03232 1176 LSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEataIIENNRPVSGWPSRGSIKFEDVHLRYRPGlpPVLHGL 1255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 374 TLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANI-AFAr 452
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFS- 1334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 453 pEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQT 532
Cdd:PLN03232 1335 -EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
490 500 510
....*....|....*....|....*....|...
gi 1730203856 533 LRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:PLN03232 1414 IREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQ 1446
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
355-565 |
6.93e-33 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 125.33 E-value: 6.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSA--FTLGSLREKVIL 432
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLF-NDTIGANIAFA----RPEASEEAIRTAAHqagldpLLERLpqGLATPAGERGLALSAGERQRIALARVLLR 507
Cdd:cd03262 81 VFQQFNLFpHLTVLENITLApikvKGMSKAEAEERALE------LLEKV--GLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALA-EVADRIITIEEGR 565
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEMGFArEVADRVIFMDDGR 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
355-565 |
9.48e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.16 E-value: 9.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSaftlgSLREKVIll 433
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-----RLKRREI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 dqtPYL-------FND-------TIGANIAFA------RPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSA 493
Cdd:COG2884 75 ---PYLrrrigvvFQDfrllpdrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 494 GERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQV-LPEATIIAITHRPAL-AEVADRIITIEEGR 565
Cdd:COG2884 141 GEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELvDRMPKRVLELEDGR 214
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
41-329 |
1.68e-32 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 126.52 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 41 VLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLRHLQ 120
Cdd:cd18568 7 ILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 121 TLSPRFYSRFRLGDLMSRINSDvSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKL 200
Cdd:cd18568 87 SLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 201 DRLTRTMRERGSDLGSLLVDTIMGMRVVSSLnaAAHETERFRARN--SAFVEAMLRMQVASFMAGAVPGTLLAVTTSGVI 278
Cdd:cd18568 166 KRNSREIFQANAEQQSFLVEALTGIATIKAL--AAERPIRWRWENkfAKALNTRFRGQKLSIVLQLISSLINHLGTIAVL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 279 LYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18568 244 WYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
354-565 |
1.78e-32 |
|
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: 131.18 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFED--VALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDA---GRILFDQAPLSAFTLGSLRE 428
Cdd:COG1123 4 LLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 429 KVILLDQTPY--LFNDTIGANIAFA-------RPEASEEAIRtAAHQAGLDPLLERLPQglatpagerglALSAGERQRI 499
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEAlenlglsRAEARARVLE-LLEAVGLERRLDRYPH-----------QLSGGQRQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 500 ALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPAL-AEVADRIITIEEGR 565
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVvAEIADRVVVMDDGR 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
354-567 |
2.28e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.82 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLsaftlGSLREKVILL 433
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTPYLFNDT------------IGANIAFARPEASE-EAIRTAAHQAGLDPLLERlpqglatPAGErglaLSAGERQRIA 500
Cdd:COG1121 81 PQRAEVDWDFpitvrdvvlmgrYGRRGLFRRPSRADrEAVDEALERVGLEDLADR-------PIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 501 LARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQvLPEA--TIIAITHRP-ALAEVADRIITIEEGRAH 567
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRE-LRREgkTILVVTHDLgAVREYFDRVLLLNRGLVA 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
354-565 |
2.69e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.50 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTL----ADLLvrylDPDAGRILFDQAPLSA--------- 420
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiAGLE----DPTSGEILIGGRDVTDlppkdrnia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 421 --FtlgslrekvilldQTPYLF-NDTIGANIAFA-----RPEAS-EEAIRTAAHQAGLDPLLERLPQglatpagerglAL 491
Cdd:COG3839 79 mvF-------------QSYALYpHMTVYENIAFPlklrkVPKAEiDRRVREAAELLGLEDLLDRKPK-----------QL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 492 SAGERQRIALARVLLRRPDVLILDEPTSALDPK----TERHIAQTLRQVlpEATIIAITHRP--ALAeVADRIITIEEGR 565
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDAKlrveMRAEIKRLHRRL--GTTTIYVTHDQveAMT-LADRIAVMNDGR 211
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
38-329 |
7.07e-32 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 124.88 E-value: 7.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLR 117
Cdd:cd18567 4 LLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRINSdVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQ 197
Cdd:cd18567 84 HLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 198 RKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGV 277
Cdd:cd18567 163 PPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 278 ILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18567 243 IYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKLFELRMLRLHLERL 294
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
370-519 |
8.90e-32 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 120.06 E-value: 8.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFND-TIGANI 448
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 449 AFArpeASEEAIRTAAHQAGLDPLLERLPQG--LATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTS 519
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
355-565 |
8.98e-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: 8.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSA--FTLGSLREKVIL 432
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLF-NDTIGANIAFArpeaseeairtaahqagldpllerlpqglatpagerglaLSAGERQRIALARVLLRRPDV 511
Cdd:cd03229 81 VFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 512 LILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALAE-VADRIITIEEGR 565
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAArLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
354-559 |
9.67e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 123.66 E-value: 9.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALA----HDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAftlgsLREK 429
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 VILLDQTPYLFN-DTIGANIAFA------RPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALA 502
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITH--RPALAeVADRII 559
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTHdvDEAVF-LADRVV 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
355-565 |
9.71e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 121.82 E-value: 9.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLgSLREKVILLD 434
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFND-TIGANIAFAR----PEASEEAIRTAAHQAGLDPLLERlpqglatPAGErglaLSAGERQRIALARVLLRRP 509
Cdd:COG4133 82 HADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLADL-------PVRQ----LSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 510 DVLILDEPTSALDPKTERHIAQTLRQVLPE-ATIIAITHRPALAEvADRIITIEEGR 565
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARgGAVLLTTHQPLELA-AARVLDLGDFK 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
355-565 |
1.57e-31 |
|
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: 122.27 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLD 434
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFNDTIGANIAFARP------EASEEAIRTAAHQAGLDPLLERLPQGLatpagerglalSAGERQRIALARVLLRR 508
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAElyglfdEELKKRIEELIELLGLEEFLDRRVGEL-----------STGMKKKVALARALVHD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 509 PDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAI-THRPALAE-VADRIITIEEGR 565
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFsSHIMQEVEaLCDRVVILHKGK 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
355-565 |
3.64e-31 |
|
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: 120.21 E-value: 3.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVAL--AHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVIL 432
Cdd:cd03369 7 IEVENLSVryAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFNDTIGANIAfARPEASEEAIRTAAhqagldplleRLPQGlatpagerGLALSAGERQRIALARVLLRRPDVL 512
Cdd:cd03369 87 IPQDPTLFSGTIRSNLD-PFDEYSDEEIYGAL----------RVSEG--------GLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 513 ILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRpaLAEVA--DRIITIEEGR 565
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFTNSTILTIAHR--LRTIIdyDKILVMDAGE 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
369-565 |
5.55e-31 |
|
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: 120.52 E-value: 5.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSafTLGSLREKVILLDQTPYLF-NDTIGAN 447
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 448 IAFA-------RPEASEEAIRTAAhQAGLDPLLERLPqglatpagergLALSAGERQRIALARVLLRRPDVLILDEPTSA 520
Cdd:cd03299 92 IAYGlkkrkvdKKEIERKVLEIAE-MLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 521 LDPKTERHIAQTLRQVLPEA--TIIAITHrpALAEV---ADRIITIEEGR 565
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFgvTVLHVTH--DFEEAwalADKVAIMLNGK 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
355-565 |
1.10e-30 |
|
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: 119.65 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAftLGSLREKVILLD 434
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFND-TIGANIAFA-----RPEAS-EEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLR 507
Cdd:cd03300 79 QNYALFPHlTVFENIAFGlrlkkLPKAEiKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITH--RPALAeVADRIITIEEGR 565
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHdqEEALT-MSDRIAVMNKGK 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
355-567 |
1.50e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.89 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDG--RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVIL 432
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYlfNDTIGA----NIAFA-------RPEASEEaIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIAL 501
Cdd:PRK13635 86 VFQNPD--NQFVGAtvqdDVAFGlenigvpREEMVER-VDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 502 ARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAEVADRIITIEEGRAH 567
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
355-565 |
3.28e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.41 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTL----ADLLvrylDPDAGRILFDQAPLsaFTLGSLRE-K 429
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLlriiAGLE----TPDSGRIVLNGRDL--FTNLPPRErR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 VILLDQTPYLF-NDTIGANIAFA---RPeASEEAIRTAAHQ----AGLDPLLERLP-QglatpagerglaLSAGERQRIA 500
Cdd:COG1118 77 VGFVFQHYALFpHMTVAENIAFGlrvRP-PSKAEIRARVEEllelVQLEGLADRYPsQ------------LSGGQRQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 501 LARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHDQEEAlELADRVVVMNQGR 211
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
38-329 |
5.25e-30 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 119.54 E-value: 5.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLR 117
Cdd:cd18555 4 LISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 118 HLQTLSPRFYSRFRLGDLMSRINSDVSdIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQ 197
Cdd:cd18555 84 HLLKLPYSFFENRSSGDLLFRANSNVY-IRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 198 RKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAaahETERFRARNSAFVEAMLRMQVASFMA---GAVPGTLLAVTT 274
Cdd:cd18555 163 KKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGS---EKNIYKKWENLFKKQLKAFKKKERLSnilNSISSSIQFIAP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 275 SGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18555 240 LLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
356-563 |
6.32e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.81 E-value: 6.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 356 RFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDA---GRILFDQAPLSafTLGSLREKVIL 432
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLT--ALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLF-NDTIGANIAFARPE-----ASEEAIRTAAHQAGLDPLLERLPqglATpagerglaLSAGERQRIALARVLL 506
Cdd:COG4136 81 LFQDDLLFpHLSVGENLAFALPPtigraQRRARVEQALEEAGLAGFADRDP---AT--------LSGGQRARVALLRALL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 507 RRPDVLILDEPTSALDPKTErhiAQTLRQVLPEAT---IIAI--THRPALAEVADRIITIEE 563
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALR---AQFREFVFEQIRqrgIPALlvTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
355-565 |
6.99e-30 |
|
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: 115.57 E-value: 6.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLgSLREKVILLD 434
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFND-TIGANiafarpeaseeairtaahqagldpllerlpqglatpagergLALSAGERQRIALARVLLRRPDVLI 513
Cdd:cd03230 80 EEPSLYENlTVREN-----------------------------------------LKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 514 LDEPTSALDPKTERHIAQTLRQVLPE-ATIIAITHRPALAE-VADRIITIEEGR 565
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAErLCDRVAILNNGR 172
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
364-564 |
1.22e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 115.82 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 364 HDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAftlGSLREKVILLDQTP--YLFN 441
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQDVdyQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 442 DTIGANIAFARPEASEEAIRTAAhqagldpLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSAL 521
Cdd:cd03226 87 DSVREELLLGLKELDAGNEQAET-------VLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1730203856 522 DPKTERHIAQTLRQVLPEA-TIIAITHRPA-LAEVADRIITIEEG 564
Cdd:cd03226 158 DYKNMERVGELIRELAAQGkAVIVITHDYEfLAKVCDRVLLLANG 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
355-565 |
1.36e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 116.63 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSA--FTLGSLREKVIL 432
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFND-TIGANIAFA--------RPEASEEAIRtaahqagldpLLERLpqGLATPAGERGLALSAGERQRIALAR 503
Cdd:COG1126 82 VFQQFNLFPHlTVLENVTLApikvkkmsKAEAEERAME----------LLERV--GLADKADAYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 504 VLLRRPDVLILDEPTSALDPKTERHIAQTLRQVlpeA----TIIAITHRPALA-EVADRIITIEEGR 565
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDL---AkegmTMVVVTHEMGFArEVADRVVFMDGGR 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
356-559 |
1.40e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 116.09 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 356 RFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFtlgslREKVILLDQ 435
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 436 TPYL---FNDTI---------GANIAFARPEASEEAIRTAAHQA-GLDPLLERlpqglatPAGErglaLSAGERQRIALA 502
Cdd:cd03235 76 RRSIdrdFPISVrdvvlmglyGHKGLFRRLSKADKAKVDEALERvGLSELADR-------QIGE----LSGGQQQRVLLA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE-ATIIAITH-RPALAEVADRII 559
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHdLGLVLEYFDRVL 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
355-565 |
5.21e-29 |
|
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: 115.48 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALA-HDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILL 433
Cdd:cd03295 1 IEFENVTKRyGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTPYLF-NDTIGANIAFArP---EASEEAIRTAAHQA----GLDP--LLERLPQglatpagerglALSAGERQRIALAR 503
Cdd:cd03295 81 IQQIGLFpHMTVEENIALV-PkllKWPKEKIRERADELlalvGLDPaeFADRYPH-----------ELSGGQQQRVGVAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 504 VLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAfRLADRIAIMKNGE 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
370-565 |
5.51e-29 |
|
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: 114.31 E-value: 5.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIP---RGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPL----SAFTLGSLREKVILLDQTPYLF-N 441
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 442 DTIGANIAFARPEASEEAIRTAAHQA----GLDPLLERLPQGLatpagerglalSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRISVDELldllGLDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 518 TSALDPKTERHIAQTLRQVLPEATI--IAITHRPALAE-VADRIITIEEGR 565
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIpvIFVTHDLSEAEyLADRIVVMEDGR 209
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
352-571 |
1.27e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 113.66 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 352 SEAIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVI 431
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 432 LLDQTPYLFNDTIGANIAFA------RPEasEEAIRTAAHQAGLDplLERLPQGLAtpagerglALSAGERQRIALARVL 505
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPwqirnqQPD--PAIFLDDLERFALP--DTILTKNIA--------ELSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 506 LRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAI--THRPALAEVADRIITIEEGRAHMRTA 571
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITLQPHAGEMQEA 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
407-559 |
1.45e-28 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 121.67 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 407 DAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGE 486
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGP 1354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 487 RGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALAEVADRII 559
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIV 1429
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
373-565 |
1.49e-28 |
|
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: 112.97 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 373 FTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAftLGSLREKVILLDQTPYLFND-TIGANIAFA 451
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLFAHlTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 452 RP------EASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEPTSALDPKT 525
Cdd:cd03298 95 LSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1730203856 526 ERHIAQTLRQVLPEA--TIIAITHRPALAE-VADRIITIEEGR 565
Cdd:cd03298 164 RAEMLDLVLDLHAETkmTVLMVTHQPEDAKrLAQRVVFLDNGR 206
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
42-322 |
2.62e-28 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 114.56 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 42 LLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLRHL-- 119
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 120 QTLSprFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRK 199
Cdd:cd18572 82 QDIA--FFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 200 LDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGVIL 279
Cdd:cd18572 160 YRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLF 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1730203856 280 YGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSA 322
Cdd:cd18572 240 YGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQA 282
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
355-565 |
3.02e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.67 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSL---R---- 427
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarrRavlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 428 -----------EKVILLDQTPYlfndtiganiaFARPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGER 496
Cdd:COG4559 82 qhsslafpftvEEVVALGRAPH-----------GSSAAQDRQIVREALALVGLAHLAGRSYQ-----------TLSGGEQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 497 QRIALARVL--LRRPD-----VLILDEPTSALDPKTERHIAQTLRQVLPE-ATIIAITHRPAL-AEVADRIITIEEGR 565
Cdd:COG4559 140 QRVQLARVLaqLWEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLARRgGGVVAVLHDLNLaAQYADRILLLHQGR 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
353-567 |
3.43e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.33 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 353 EAIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSL-REKVI 431
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 432 LLDQTPYLFNDTIGANIAFAR------PEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVL 505
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRaphglsRAEDDALVAAALAQVDLAHLAGRDYP-----------QLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 506 --LRRPD----VLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAEV-ADRIITIEEGRAH 567
Cdd:PRK13548 150 aqLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNLAARyADRIVLLHQGRLV 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
355-565 |
4.49e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 118.24 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRI---------LFDQAplsaftLGS 425
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgetvkigYFDQH------QEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 426 LREkvillDQTPYlfnDTIGAniafARPEASEEAIRTaahqagldpLLERL---PQGLATPAGerglALSAGERQRIALA 502
Cdd:COG0488 390 LDP-----DKTVL---DELRD----GAPGGTEQEVRG---------YLGRFlfsGDDAFKPVG----VLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTerhiaqtlRQVLPEA------TIIAITH-RPALAEVADRIITIEEGR 565
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIET--------LEALEEAlddfpgTVLLVSHdRYFLDRVATRILEFEDGG 506
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
355-565 |
6.58e-28 |
|
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: 111.90 E-value: 6.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDV----ALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLadllVRYLD----PDAGRIL---FDQAPLSAFTL 423
Cdd:cd03258 2 IELKNVskvfGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINglerPTSGSVLvdgTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 424 GSLREKVILLDQTPYLFND-TIGANIAF----ARPEASEEAIRtaahqagLDPLLERLpqGLATPAGERGLALSAGERQR 498
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSSrTVFENVALpleiAGVPKAEIEER-------VLELLELV--GLEDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 499 IALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHR-PALAEVADRIITIEEGR 565
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElgLTIVLITHEmEVVKRICDRVAVMEKGE 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
354-565 |
9.96e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 111.66 E-value: 9.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLgslREKVI-L 432
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERNVgF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFND-TIGANIAF---ARPEA---SEEAIRTAAHQ----AGLDPLLERLPQglatpagerglALSAGERQRIAL 501
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFglrVKPRSerpPEAEIRAKVHEllklVQLDWLADRYPA-----------QLSGGQRQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 502 ARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElhVTTVFVTHDQEEAlEVADRVVVMNKGR 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
325-565 |
1.22e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 118.69 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 325 SLARIFELFDTPAEV-LEGSSARAFPG--LSEAIRFEDVALAH--DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADL 399
Cdd:PLN03130 1205 AVERVGTYIDLPSEApLVIENNRPPPGwpSSGSIKFEDVVLRYrpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNA 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 400 LVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANI-AFArpEASEEAIRTAAHQAGLDPLLERLPQ 478
Cdd:PLN03130 1285 LFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdPFN--EHNDADLWESLERAHLKDVIRRNSL 1362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 479 GLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRI 558
Cdd:PLN03130 1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRI 1442
|
....*..
gi 1730203856 559 ITIEEGR 565
Cdd:PLN03130 1443 LVLDAGR 1449
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
41-329 |
1.31e-27 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 112.59 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 41 VLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSA--DMLFDIRvaLLRH 118
Cdd:cd18588 7 VLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNriDAELGAR--LFRH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 119 LQTLSPRFYSRFRLGDLMSRINsDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQR 198
Cdd:cd18588 85 LLRLPLSYFESRQVGDTVARVR-ELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 199 KLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGVI 278
Cdd:cd18588 164 ILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAIL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 279 LYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18588 244 WFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
369-566 |
1.38e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 110.45 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT---LGSLRE------KVILLDQTPYl 439
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrIGYLPEerglypKMKVIDQLVY- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 440 FNDTIGANIAFARPEAseeairtaahqaglDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTS 519
Cdd:cd03269 94 LAQLKGLKKEEARRRI--------------DEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1730203856 520 ALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAE-VADRIITIEEGRA 566
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGkTVILSTHQMELVEeLCDRVLLLNKGRA 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
355-565 |
2.83e-27 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 109.65 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSafTLGSLREKVILLD 434
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLF-NDTIGANIAF------ARPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLR 507
Cdd:cd03301 79 QNYALYpHMTVYDNIAFglklrkVPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAE-VADRIITIEEGR 565
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHDQVEAMtMADRIAVMNDGQ 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
355-565 |
2.90e-27 |
|
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: 110.47 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQ---APLSAFTLGSLREKV 430
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtdiTKLRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 431 ILLDQTPYLF-NDTIGANIAFARpEASEEAIRT-------AAHQAGLDpLLERLpqGLATPAGERGLALSAGERQRIALA 502
Cdd:TIGR02315 82 GMIFQHYNLIeRLTVLENVLHGR-LGYKPTWRSllgrfseEDKERALS-ALERV--GLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAIT--HRPALA-EVADRIITIEEGR 565
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIInlHQVDLAkKYADRIVGLKAGE 223
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
36-329 |
2.98e-27 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 111.87 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 36 GRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVAL 115
Cdd:cd18779 2 GLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 116 LRHLQTLSPRFYSRFRLGDLMSRINSdVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVV 195
Cdd:cd18779 82 LEHLLRLPYRFFQQRSTGDLLMRLSS-NATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 196 FQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTS 275
Cdd:cd18779 161 TRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 276 GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18779 241 VLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
373-567 |
5.84e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 109.29 E-value: 5.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 373 FTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAfTLGSLReKVILLDQTPYLFND-TIGANIAFA 451
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT-TPPSRR-PVSMLFQENNLFSHlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 452 -RP-----EASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEPTSALDPKT 525
Cdd:PRK10771 96 lNPglklnAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1730203856 526 ERHIAQTLRQVLPEA--TIIAITHRPA-LAEVADRIITIEEGRAH 567
Cdd:PRK10771 165 RQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIA 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
355-564 |
5.98e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.23 E-value: 5.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRA--VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVIL 432
Cdd:PRK13648 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYlfNDTIGANIAFarpeasEEAIRTAAHQAGLDPLLERLPQGLA-----TPAGERGLALSAGERQRIALARVLLR 507
Cdd:PRK13648 88 VFQNPD--NQFVGSIVKY------DVAFGLENHAVPYDEMHRRVSEALKqvdmlERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAEVADRIITIEEG 564
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKG 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
308-565 |
8.04e-27 |
|
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: 116.20 E-value: 8.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 308 PIQVLMGLVSGLSSARVSLARIfELFDTPAEV----LEGSSARAFPGLSEAIRFEDVALAHDGRAVLKGFTLEIPRGSFC 383
Cdd:TIGR00957 589 PLNILPMVISSIVQASVSLKRL-RIFLSHEELepdsIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALV 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 384 AVLGPSGVGKSTLADLLVRYLDPDAGRIlfdqaplsaftlgSLREKVILLDQTPYLFNDTIGANIAFARPeASEEAIRTA 463
Cdd:TIGR00957 668 AVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFGKA-LNEKYYQQV 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 464 AHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTL---RQVLPEA 540
Cdd:TIGR00957 734 LEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNK 813
|
250 260
....*....|....*....|....*
gi 1730203856 541 TIIAITHRPALAEVADRIITIEEGR 565
Cdd:TIGR00957 814 TRILVTHGISYLPQVDVIIVMSGGK 838
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
365-552 |
9.99e-27 |
|
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: 107.12 E-value: 9.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPL--SAFTLGSLREKVILLDQTP--YLF 440
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQRVGLVFQDPddQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 441 NDTIGANIAFA------RPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLIL 514
Cdd:TIGR01166 83 AADVDQDVAFGplnlglSEAEVERRVREALTAVGASGLRERPTH-----------CLSGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 1730203856 515 DEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALA 552
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAEGmTVVISTHDVDLA 190
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
354-565 |
1.19e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.89 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAH--DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDA---GRILFDQAPLSAFTLGSLRE 428
Cdd:PRK13640 5 IVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 429 KVILLDQTP--YLFNDTIGANIAFA-------RPEAsEEAIRTAAHQAGLDPLLERLPQGLatpagerglalSAGERQRI 499
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGlenravpRPEM-IKIVRDVLADVGMLDYIDSEPANL-----------SGGQKQRV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 500 ALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGK 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
80-564 |
1.46e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 115.46 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 80 LAMIGVTIGnyalnILASYRYISTSADMLFDIR----VALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRV------ 149
Cdd:PLN03232 346 LIFFGVTFG-----VLCESQYFQNVGRVGFRLRstlvAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIaeqlhg 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 150 --TADTMLSVLSNLLMLTGGVAimlwldwKLF--LLAIVLLPacvgLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGM 225
Cdd:PLN03232 421 lwSAPFRIIVSMVLLYQQLGVA-------SLFgsLILFLLIP----LQTLIVRKMRKLTKEGLQWTDKRVGIINEILASM 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 226 RVVSSLnaAAHETERFRA---RN---SAFVEAMLRMQVASFMAGAVPgtlLAVTtsgVILYGGYQIIEGTMSIGTLVAFM 299
Cdd:PLN03232 490 DTVKCY--AWEKSFESRIqgiRNeelSWFRKAQLLSAFNSFILNSIP---VVVT---LVSFGVFVLLGGDLTPARAFTSL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 300 AYQSRLFSPIQVLMGLVSGLSSARVSLARIFELFDTPAEVLEGSSARAfPGlSEAIRFEDVALAHDGRA---VLKGFTLE 376
Cdd:PLN03232 562 SLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQ-PG-APAISIKNGYFSWDSKTskpTLSDINLE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 377 IPRGSFCAVLGPSGVGKSTLADLLVRYLDPdagrilfdqaplSAFTLGSLREKVILLDQTPYLFNDTIGANIAFA---RP 453
Cdd:PLN03232 640 IPVGSLVAIVGGTGEGKTSLISAMLGELSH------------AETSSVVIRGSVAYVPQVSWIFNATVRENILFGsdfES 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 454 EASEEAIRTAAHQAGLDplleRLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQT- 532
Cdd:PLN03232 708 ERYWRAIDVTALQHDLD----LLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSc 783
|
490 500 510
....*....|....*....|....*....|..
gi 1730203856 533 LRQVLPEATIIAITHRPALAEVADRIITIEEG 564
Cdd:PLN03232 784 MKDELKGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
365-566 |
1.50e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.55 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPL--SAFTLGSLREKVILLDQTP--YLF 440
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMVFQDPdnQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 441 NDTIGANIAFAR-----PEAS-EEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLIL 514
Cdd:PRK13636 97 SASVYQDVSFGAvnlklPEDEvRKRVDNALKRTGIEHLKDKPTH-----------CLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 515 DEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHR-PALAEVADRIITIEEGRA 566
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDiDIVPLYCDNVFVMKEGRV 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
355-565 |
1.70e-26 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 107.49 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAF---TLGSLREKV 430
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 431 -ILLDQTPYLFNDTIGANIAFARpEASEEAIRTAAHQagLDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRP 509
Cdd:cd03292 81 gVVFQDFRLLPDRNVYENVAFAL-EVTGVPPREIRKR--VPAALELV--GLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 510 DVLILDEPTSALDPKTERHIAQTLRQV-LPEATIIAITHRPALAE-VADRIITIEEGR 565
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDtTRHRVIALERGK 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
354-557 |
2.08e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.20 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLD--PDA---GRILFDQAPLSAFT--LGSL 426
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIYDPDvdVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 427 REKVILLDQTPYLFNDTIGANIAFA-------RPEASEEAIRTAAHQAGL-DPLLERLpqglatpaGERGLALSAGERQR 498
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEESLRKAALwDEVKDRL--------KKSALGLSGGQQQR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 499 IALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALA-EVADR 557
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAaRVSDY 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
343-565 |
2.46e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 108.23 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 343 SSARAFPGLSEAIrfEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAft 422
Cdd:PRK11247 3 NTARLNQGTPLLL--NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 423 lgsLREKVILLDQTPYLFN-----DTIGANIafarpeasEEAIRTAAHQAgldplLERLpqGLATPAGERGLALSAGERQ 497
Cdd:PRK11247 79 ---AREDTRLMFQDARLLPwkkviDNVGLGL--------KGQWRDAALQA-----LAAV--GLADRANEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 498 RIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALA-EVADRIITIEEGR 565
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAvAMADRVLLIEEGK 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
355-562 |
2.92e-26 |
|
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: 104.93 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTL----ADL-------LVRyldPDAGRILF-DQAPLsaF 421
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLfralAGLwpwgsgrIGM---PEGEDLLFlPQRPY--L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 422 TLGSLREKVIlldqtpYLFNDTiganiafarpeaseeairtaahqagldpllerlpqglatpagerglaLSAGERQRIAL 501
Cdd:cd03223 76 PLGTLREQLI------YPWDDV-----------------------------------------------LSGGEQQRLAF 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 502 ARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLpeATIIAITHRPALAEVADRIITIE 562
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHRPSLWKFHDRVLDLD 161
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
373-565 |
1.08e-25 |
|
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: 104.94 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 373 FTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAplSAFTLGSLREKVILLDQTPYLFND-TIGANIAFA 451
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFAHlTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 452 -RP-----EASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEPTSALDPKT 525
Cdd:TIGR01277 95 lHPglklnAEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1730203856 526 ERHIAQTLRQVLPEA--TIIAITHRPA-LAEVADRIITIEEGR 565
Cdd:TIGR01277 164 REEMLALVKQLCSERqrTLLMVTHHLSdARAIASQIAVVSQGK 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
355-565 |
2.59e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.09 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDV--ALAHDGRAV--LKGFTLEIPRGSFCAVLGPSGVGKSTLA---DLLVRyldPDAGRILFDQAPLSAFTLGSLR 427
Cdd:COG1135 2 IELENLskTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 428 EK-----VI-----LLDQTpylfndTIGANIAFarP----EASEEAIRTAAhqaglDPLLERLpqGLAtpagERGLA--- 490
Cdd:COG1135 79 AArrkigMIfqhfnLLSSR------TVAENVAL--PleiaGVPKAEIRKRV-----AELLELV--GLS----DKADAyps 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 491 -LSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITH-----RpalaEVADRIITIE 562
Cdd:COG1135 140 qLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElgLTIVLITHemdvvR----RICDRVAVLE 215
|
...
gi 1730203856 563 EGR 565
Cdd:COG1135 216 NGR 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
366-564 |
3.43e-25 |
|
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: 103.95 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 366 GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF----DQAPLSAFTLGSLREKVILLDQTPYLFN 441
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 442 DTIGANIAFARPeASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSAL 521
Cdd:cd03290 93 ATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1730203856 522 DPKTERHIAQT-LRQVLPE--ATIIAITHRPALAEVADRIITIEEG 564
Cdd:cd03290 172 DIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
369-565 |
6.90e-25 |
|
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: 100.97 E-value: 6.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDqaplsaftlgslrekvilldqtpylfndtiGANI 448
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------------------------------GKEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 449 AFARPEASEEA-IRTAaHQagldpllerlpqglatpagerglaLSAGERQRIALARVLLRRPDVLILDEPTSALDPKTER 527
Cdd:cd03216 65 SFASPRDARRAgIAMV-YQ------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1730203856 528 HIAQTLRQVLPE-ATIIAITHRPA-LAEVADRIITIEEGR 565
Cdd:cd03216 120 RLFKVIRRLRAQgVAVIFISHRLDeVFEIADRVTVLRDGR 159
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
357-565 |
7.57e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.74 E-value: 7.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 357 FEDVALAHdgravlkgFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLS--AFTLGSLREKVILLD 434
Cdd:PRK13637 18 FEKKALDN--------VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTP--YLFNDTIGANIAFArPE---ASEEAIRTAAHQA----GLD--PLLERLPqglatpagergLALSAGERQRIALAR 503
Cdd:PRK13637 90 QYPeyQLFEETIEKDIAFG-PInlgLSEEEIENRVKRAmnivGLDyeDYKDKSP-----------FELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 504 VLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHR-PALAEVADRIITIEEGR 565
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEynMTIILVSHSmEDVAKLADRIIVMNKGK 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
352-565 |
9.16e-25 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 103.24 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 352 SEAIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGR--ILFDQaplsafTLGS---- 425
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGE------RRGGedvw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 426 -LREKV-----ILLDQTPYL----------FNDTIGaniafaRPEASEEAIRTAAHQagldpLLERLpqGLATPAGERGL 489
Cdd:COG1119 75 eLRKRIglvspALQLRFPRDetvldvvlsgFFDSIG------LYREPTDEQRERARE-----LLELL--GLAHLADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 490 ALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQV--LPEATIIAITHRP--ALAEVaDRIITIEEGR 565
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVeeIPPGI-THVLLLKDGR 220
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
40-321 |
1.54e-24 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. 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.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 103.75 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 40 LVLLvsLISTALNLAQPYLSKMLID----NALLPRDMGA-LVAIGLAMIGV----TIGNYALNIL---ASYRYIStsadm 107
Cdd:cd18573 2 LALL--LVSSAVTMSVPFAIGKLIDvaskESGDIEIFGLsLKTFALALLGVfvvgAAANFGRVYLlriAGERIVA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 108 lfDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLP 187
Cdd:cd18573 75 --RLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 188 ACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVAS--FMAGAv 265
Cdd:cd18573 153 PIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASglFFGST- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 266 pGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYqsrlfspiQVLMGL-VSGLSS 321
Cdd:cd18573 232 -GFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMY--------AVYVGSsVSGLSS 279
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
127-548 |
2.65e-24 |
|
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: 108.46 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 127 YSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLTRT 206
Cdd:TIGR01271 976 LNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQL 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 207 MRERGSDLGSLLVDTIMGMRVVSSLNAAAH-ETERFRARN----------SAFVEAMLRMQVAsFMAGAVPGTLLAVTTS 275
Cdd:TIGR01271 1056 ESEARSPIFSHLITSLKGLWTIRAFGRQSYfETLFHKALNlhtanwflylSTLRWFQMRIDII-FVFFFIAVTFIAIGTN 1134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 276 GvilyggyqiiEGTMSIGTLVAFM-----AYQSRLFSPIQVlmglvSGLSSarvSLARIFELFDTPAEVLEGSSARAFPG 350
Cdd:TIGR01271 1135 Q----------DGEGEVGIILTLAmnilsTLQWAVNSSIDV-----DGLMR---SVSRVFKFIDLPQEEPRPSGGGGKYQ 1196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 351 LSEAIRFED-------------------VALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDaGRI 411
Cdd:TIGR01271 1197 LSTVLVIENphaqkcwpsggqmdvqgltAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEI 1275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 412 LFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIafaRPEA--SEEAIRTAAHQAGLDPLLERLPQGLATPAGERGL 489
Cdd:TIGR01271 1276 QIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGY 1352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 490 ALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHR 548
Cdd:TIGR01271 1353 VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHR 1411
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
350-547 |
2.69e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.55 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 350 GLSEAIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLD--PDA---GRILFDQAPLSAFTLG 424
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 425 --SLREKVILLDQTPYLFNDTIGANIAFArpeaseeaIRTAAHQAGLDPLLER-LPQG-----LATPAGERGLALSAGER 496
Cdd:PRK14243 86 pvEVRRRIGMVFQKPNPFPKSIYDNIAYG--------ARINGYKGDMDELVERsLRQAalwdeVKDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 497 QRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITH 547
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
246-564 |
4.04e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 107.90 E-value: 4.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 246 SAFVEAMLRMQVASFMAGAVPgtlLAVTtsgVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVS 325
Cdd:PLN03130 514 SWFRKAQLLSAFNSFILNSIP---VLVT---VVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVS 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 326 LARIFELFDTPAEVLEGSSARAfPGLSeAIRFEDVALAHDG---RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVR 402
Cdd:PLN03130 588 LKRLEELLLAEERVLLPNPPLE-PGLP-AISIKNGYFSWDSkaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 403 YLDPDAGRILFdqaplsaftlgsLREKVILLDQTPYLFNDTIGANIAFARP---EASEEAIRTAAHQAGLDplleRLPQG 479
Cdd:PLN03130 666 ELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSPfdpERYERAIDVTALQHDLD----LLPGG 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 480 LATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQT-LRQVLPEATIIAITHRPALAEVADRI 558
Cdd:PLN03130 730 DLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRI 809
|
....*.
gi 1730203856 559 ITIEEG 564
Cdd:PLN03130 810 ILVHEG 815
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
354-565 |
5.07e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 101.37 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRI-----LFDQA-PLSAFT--LGS 425
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTArSLSQQKglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 426 LREKVILLDQTPYLF-NDTIGANI----AFARPEASEEAIRTAAHqagldpLLERLpqGLATPAGERGLALSAGERQRIA 500
Cdd:PRK11264 83 LRQHVGFVFQNFNLFpHRTVLENIiegpVIVKGEPKEEATARARE------LLAKV--GLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 501 LARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALA-EVADRIITIEEGR 565
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFArDVADRAIFMDQGR 221
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
369-567 |
5.65e-24 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 100.50 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT---LGSLREKVI-LLDQTPYLFND-T 443
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSsneRAKLRNKKLgFIYQFHHLLPDfT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 444 IGANIA-------FARPEASEEAIRtaahqagldpLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDE 516
Cdd:TIGR02211 100 ALENVAmplligkKSVKEAKERAYE----------MLEKV--GLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 517 PTSALDPKTERHIAQTLRQVLPEATI--IAITHRPALAEVADRIITIEEGRAH 567
Cdd:TIGR02211 168 PTGNLDNNNAKIIFDLMLELNRELNTsfLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
354-575 |
6.42e-24 |
|
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: 100.59 E-value: 6.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRA----VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT----LGS 425
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 426 LREKVILLDQTPYLfndtIGA-----NIAFARPEASEEAIRTAAHQagldpLLERLpqGLATPAGERGLALSAGERQRIA 500
Cdd:COG4181 88 RARHVGFVFQSFQL----LPTltaleNVMLPLELAGRRDARARARA-----LLERV--GLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 501 LARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAEVADRIITIEEGRAHMRTAASLA 575
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATAA 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
358-565 |
7.19e-24 |
|
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: 100.59 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT------LG------- 424
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpheiarLGigrtfqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 425 -------SLREKVIL--LDQTPYLFNdtiganiaFARPEASEEAIRTAAHQagldpLLERLpqGLA----TPAGErglaL 491
Cdd:cd03219 84 prlfpelTVLENVMVaaQARTGSGLL--------LARARREEREARERAEE-----LLERV--GLAdladRPAGE----L 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 492 SAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE-ATIIAITHR-PALAEVADRIITIEEGR 565
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDmDVVMSLADRVTVLDQGR 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
355-565 |
7.56e-24 |
|
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: 97.52 E-value: 7.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQaplsaftlgslrekvilld 434
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 qtpylfndtiGANIAFarpeaseeairtaahqagldpllerLPQglatpagerglaLSAGERQRIALARVLLRRPDVLIL 514
Cdd:cd03221 62 ----------TVKIGY-------------------------FEQ------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 515 DEPTSALDPKTERHIAQTLRQVlpEATIIAITH-RPALAEVADRIITIEEGR 565
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEY--PGTVILVSHdRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
355-564 |
7.58e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 7.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH------DGRAvLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT----LG 424
Cdd:PRK13634 3 ITFQKVEHRYqyktpfERRA-LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkkLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 425 SLREKVILLDQTP--YLFNDTIGANIAFArPE----ASEEAIRTAAHQ---AGLDP-LLERLPqglatpagergLALSAG 494
Cdd:PRK13634 82 PLRKKVGIVFQFPehQLFEETVEKDICFG-PMnfgvSEEDAKQKAREMielVGLPEeLLARSP-----------FELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 495 ERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHR-PALAEVADRIITIEEG 564
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSmEDAARYADQIVVMHKG 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
354-565 |
9.14e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.35 E-value: 9.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVIL 432
Cdd:PRK13647 4 IIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTP--YLFNDTIGANIAFA------RPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARV 504
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 505 LLRRPDVLILDEPTSALDPKTERhiaqTLRQVLPE-----ATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQE----TLMEILDRlhnqgKTVIVATHDVDLAaEWADQVIVLKEGR 215
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
363-561 |
1.12e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.46 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 363 AHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFtlgsLREKVILLDQTPYLFND 442
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY----VPQRSEVPDSLPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 TI-----GANIAFARPEASEEAIRTAAhqagldplLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:NF040873 77 LVamgrwARRGLWRRLTRDDRAAVDDA--------LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1730203856 518 TSALDPKTERHIAQTLRQVLPE-ATIIAITHRPALAEVADRIITI 561
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-565 |
1.17e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 100.37 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLD--PDA---GRILFDQAPLSAFTLGSLREK 429
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 VILLDQTPY-LFNDTIGANIAF---------ARPEAsEEAIRTAAHQAgldPLLERLPQGLATPAGErglaLSAGERQRI 499
Cdd:PRK14247 84 VQMVFQIPNpIPNLSIFENVALglklnrlvkSKKEL-QERVRWALEKA---QLWDEVKDRLDAPAGK----LSGGQQQRL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 500 ALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPA-LAEVADRIITIEEGR 565
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQqAARISDYVAFLYKGQ 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
365-565 |
1.24e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPL--SAFTLGSLREKVILLDQTP--YLF 440
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVFQNPddQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 441 NDTIGANIAFA------RPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLIL 514
Cdd:PRK13639 93 APTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 515 DEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAEV-ADRIITIEEGR 565
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGiTIIISTHDVDLVPVyADKVYVMSDGK 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
367-565 |
1.36e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 367 RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTP--YLFNDTI 444
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 445 GANIAFA------RPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEPT 518
Cdd:PRK13652 97 EQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 519 SALDPKTERHIAQTLRQvLPEA---TIIAITHRPAL-AEVADRIITIEEGR 565
Cdd:PRK13652 166 AGLDPQGVKELIDFLND-LPETygmTVIFSTHQLDLvPEMADYIYVMDKGR 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
357-565 |
6.80e-23 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 98.48 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 357 FEDVALAHDGRAVLKGF---------TLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLR 427
Cdd:cd03294 18 FKLLAKGKSKEEILKKTgqtvgvndvSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 428 E----KVILLDQTPYLF-NDTIGANIAF----------ARPEASEEAIrtaaHQAGLDPLLERLPQglatpagerglALS 492
Cdd:cd03294 98 ElrrkKISMVFQSFALLpHRTVLENVAFglevqgvpraEREERAAEAL----ELVGLEGWEHKYPD-----------ELS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 493 AGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALA-EVADRIITIEEGR 565
Cdd:cd03294 163 GGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELqkTIVFITHDLDEAlRLGDRIAIMKDGR 238
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
366-565 |
7.46e-23 |
|
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: 96.90 E-value: 7.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 366 GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAplSAFTLGSLREKVILLDQTPYLFNDTIG 445
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 446 aniafarpeasEEAIRTAAHQAGL-----DPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSA 520
Cdd:cd03268 90 -----------RENLRLLARLLGIrkkriDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 521 LDPKTERHIAQTLRqVLPE--ATIIAITHrpALAE---VADRIITIEEGR 565
Cdd:cd03268 157 LDPDGIKELRELIL-SLRDqgITVLISSH--LLSEiqkVADRIGIINKGK 203
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
355-565 |
9.74e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.47 E-value: 9.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTL------------ADLLVRYLDPDAGRIlfdqaplsafT 422
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcinkleeitsGDLIVDGLKVNDPKV----------D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 423 LGSLREKVILLDQTPYLFND-TIGANIAFArPEASEEAIRTAAHQAGLDpLLERLpqGLATPAGERGLALSAGERQRIAL 501
Cdd:PRK09493 72 ERLIRQEAGMVFQQFYLFPHlTALENVMFG-PLRVRGASKEEAEKQARE-LLAKV--GLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 502 ARVLLRRPDVLILDEPTSALDPKTeRHIAQTLRQVLPEA--TIIAITHRPALAE-VADRIITIEEGR 565
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPEL-RHEVLKVMQDLAEEgmTMVIVTHEIGFAEkVASRLIFIDKGR 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
340-564 |
1.42e-22 |
|
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: 97.29 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 340 LEGSSARAFPGLSEAIRFEDVALAHDG--RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAP 417
Cdd:cd03288 5 ISGSSNSGLVGLGGEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 418 LSAFTLGSLREKVILLDQTPYLFNDTIGANIafaRPE--ASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGE 495
Cdd:cd03288 85 ISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 496 RQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEG 564
Cdd:cd03288 162 RQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRG 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
366-565 |
1.78e-22 |
|
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: 95.31 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 366 GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDP--DAGRILFDQAPLSAFtlgSLREKVILLDQTPYLF-ND 442
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKR---SFRKIIGYVPQDDILHpTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 TIganiafarpeasEEAIRTAAHQAGLdpllerlpqglatpagerglalSAGERQRIALARVLLRRPDVLILDEPTSALD 522
Cdd:cd03213 98 TV------------RETLMFAAKLRGL----------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1730203856 523 PKTERHIAQTLRQVLPEA-TIIAITHRPA--LAEVADRIITIEEGR 565
Cdd:cd03213 144 SSSALQVMSLLRRLADTGrTIICSIHQPSseIFELFDKLLLLSQGR 189
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
36-329 |
2.10e-22 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 97.65 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 36 GRLTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVAL 115
Cdd:cd18566 2 PLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 116 LRHLQTLSPRFYSRFRLGDLMSRINsDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVV 195
Cdd:cd18566 82 FEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 196 FQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTS 275
Cdd:cd18566 161 LGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 276 GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18566 241 AVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
354-565 |
2.41e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRIL-----FD-QAPLSAFTLGSLR 427
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqFDfSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 428 EKVILLDQT----PYLfndTIGANIAFA--------RPEASEEAIRtaahqagldpLLERLpqGLATPAGERGLALSAGE 495
Cdd:COG4161 82 QKVGMVFQQynlwPHL---TVMENLIEApckvlglsKEQAREKAMK----------LLARL--RLTDKADRFPLHLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 496 RQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQvLPEATI--IAITHRPALA-EVADRIITIEEGR 565
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRE-LSQTGItqVIVTHEVEFArKVASQVVYMEKGR 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
369-565 |
3.54e-22 |
|
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: 95.19 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQApLSAFTLGSLREKVILldqtpYLFNDTIG--- 445
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHD-GGWVDLAQASPREIL-----ALRRRTIGyvs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 446 ---------------ANIAFARPEASEEAIRTAAHqagldpLLERL--PQGL--ATPAgerglALSAGERQRIALARVLL 506
Cdd:COG4778 100 qflrviprvsaldvvAEPLLERGVDREEARARARE------LLARLnlPERLwdLPPA-----TFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 507 RRPDVLILDEPTSALDPKTerhiAQTLRQVLPEA-----TIIAITHRPALAE-VADRIITIEEGR 565
Cdd:COG4778 169 ADPPLLLLDEPTASLDAAN----RAVVVELIEEAkargtAIIGIFHDEEVREaVADRVVDVTPFS 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
357-568 |
7.56e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 7.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 357 FEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQaplsaftlgslREKVILLDQT 436
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 437 PYLFND-TIGANI--AFAR---------------PEASEEAIRTAAHQAGLDP------------LLERLpqGLATPAGE 486
Cdd:COG0488 70 PPLDDDlTVLDTVldGDAElraleaeleeleaklAEPDEDLERLAELQEEFEAlggweaearaeeILSGL--GFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 487 RGLA-LSAGERQRIALARVLLRRPDVLILDEPTSALDPKT----ERHIAQTlrqvlpEATIIAITH-RPALAEVADRIIT 560
Cdd:COG0488 148 RPVSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNY------PGTVLVVSHdRYFLDRVATRILE 221
|
....*...
gi 1730203856 561 IEEGRAHM 568
Cdd:COG0488 222 LDRGKLTL 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
354-565 |
7.85e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.58 E-value: 7.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAH------DGRAvLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT----L 423
Cdd:PRK13649 2 GINLQNVSYTYqagtpfEGRA-LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 424 GSLREKVILLDQTP--YLFNDTIGANIAFArPE----ASEEAIRTAAHQAGL----DPLLERLPqglatpagergLALSA 493
Cdd:PRK13649 81 KQIRKKVGLVFQFPesQLFEETVLKDVAFG-PQnfgvSQEEAEALAREKLALvgisESLFEKNP-----------FELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 494 GERQRIALARVLLRRPDVLILDEPTSALDPKTERHIaQTLRQVLPEA--TIIAITH-RPALAEVADRIITIEEGR 565
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL-MTLFKKLHQSgmTIVLVTHlMDDVANYADFVYVLEKGK 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
365-578 |
7.87e-22 |
|
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: 95.69 E-value: 7.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDaGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTI 444
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 445 GANIAfARPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPK 524
Cdd:cd03289 94 RKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 525 TERHIAQTLRQVLPEATIIAITHR-PALAEvADRIITIEEGRahMRTAASLAPLV 578
Cdd:cd03289 173 TYQVIRKTLKQAFADCTVILSEHRiEAMLE-CQRFLVIEENK--VRQYDSIQKLL 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
367-522 |
8.74e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 96.72 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 367 RAVlKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLRE---KVILLDQTPYL-FND 442
Cdd:COG4608 32 KAV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDPYAsLNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 --TIGANIAF-------ARPEASEEAIRTAAHQAGLDP-LLERLPQglatpagerglALSAGERQRIALARVLLRRPDVL 512
Cdd:COG4608 111 rmTVGDIIAEplrihglASKAERRERVAELLELVGLRPeHADRYPH-----------EFSGGQRQRIGIARALALNPKLI 179
|
170
....*....|
gi 1730203856 513 ILDEPTSALD 522
Cdd:COG4608 180 VCDEPVSALD 189
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
355-565 |
1.33e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.41 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHD--GRAV--LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLRE-- 428
Cdd:PRK11153 2 IELKNISKVFPqgGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 429 -KVILLDQTPYLFND-TIGANIAFARPEA--SEEAIRtaahqAGLDPLLERLpqGLAT-----PAgerglALSAGERQRI 499
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVFDNVALPLELAgtPKAEIK-----ARVTELLELV--GLSDkadryPA-----QLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 500 ALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElgLTIVLITHEMDVVkRICDRVAVIDAGR 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
41-326 |
1.55e-21 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 95.28 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 41 VLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASY--RYISTSADMLFDIRValLRH 118
Cdd:cd18783 7 VAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYllLVATTRIDARLALRT--FDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 119 LQTLSPRFYSRFRLGDLMSRInSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAI---VLLPACVGLFV- 194
Cdd:cd18783 85 LLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLafsALIALIILAFLp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 195 VFQRKLDRLTRTMRERGSdlgsLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTT 274
Cdd:cd18783 164 PFRRRLQALYRAEGERQA----FLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 275 SGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSL 326
Cdd:cd18783 240 VGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSV 291
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
355-565 |
1.66e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT-LGSLREKVIL 432
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTP--YLFNDTIGANIAFAR------PEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARV 504
Cdd:PRK13644 82 VFQNPetQFVGRTVEEDLAFGPenlclpPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAGI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 505 LLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGK 212
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
38-329 |
1.89e-21 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 94.85 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYrYIstsadMLFDIRVAL-- 115
Cdd:cd18569 4 LLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQY-YL-----LRLETKLALss 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 116 ----LRHLQTLSPRFYSRFRLGDLMSRINSDvSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVG 191
Cdd:cd18569 78 ssrfFWHVLRLPVEFFSQRYAGDIASRVQSN-DRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 192 LFVVFQRKLDRLTRT-MRERGSDLGSllvdTIMGMRVVSSLNAAAHETERFR---ARNSAFVEAMLRMQVASFMAGAVPG 267
Cdd:cd18569 157 VLRLVSRKRVDLNRRlLQDSGKLTGT----TMSGLQMIETLKASGAESDFFSrwaGYQAKVLNAQQELGRTNQLLGALPT 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 268 TLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18569 233 LLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
359-565 |
2.77e-21 |
|
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: 95.55 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 359 DVALAHDgravLKGFTL----EIPRGSFCAVLGPSGVGKSTLADL---LVRyldPDAGRILFDQAPL--SAFTLGSLREK 429
Cdd:COG4148 4 EVDFRLR----RGGFTLdvdfTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLqdSARGIFLPPHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 --VILLDQTPYLFND-TIGANIAFARPEASEEAIRTAAHQA----GLDPLLERLPQglatpagerglALSAGERQRIALA 502
Cdd:COG4148 77 rrIGYVFQEARLFPHlSVRGNLLYGRKRAPRAERRISFDEVvellGIGHLLDRRPA-----------TLSGGERQRVAIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTERHIAQTLRQV-----LPeatIIAITHrpALAEV---ADRIITIEEGR 565
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILPYLERLrdeldIP---ILYVSH--SLDEVarlADHVVLLEQGR 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
355-565 |
3.63e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.40 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSafTLGSLREKVILLD 434
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLF-NDTIGANIAFA-----RPEAS-----EEAIRTAAhqagLDPLLERLPQglatpagerglALSAGERQRIALAR 503
Cdd:PRK09452 93 QSYALFpHMTVFENVAFGlrmqkTPAAEitprvMEALRMVQ----LEEFAQRKPH-----------QLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 504 VLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITH--RPALAeVADRIITIEEGR 565
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHdqEEALT-MSDRIVVMRDGR 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
356-565 |
3.98e-21 |
|
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: 92.33 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 356 RFEDVALAHDG----RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDA---GRILFDQAPLSAFTLgslRE 428
Cdd:cd03234 5 PWWDVGLKAKNwnkyARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQF---QK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 429 KVILLDQT----PYLfndTIGANIAF----ARPEASEEAIRTAAHQaglDPLLERLpqGLATPAGERGLALSAGERQRIA 500
Cdd:cd03234 82 CVAYVRQDdillPGL---TVRETLTYtailRLPRKSSDAIRKKRVE---DVLLRDL--ALTRIGGNLVKGISGGERRRVS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 501 LARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAIT-H--RPALAEVADRIITIEEGR 565
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGE 221
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
30-339 |
4.26e-21 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 94.44 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 30 YLRPYLGRLTLVLLVSLISTALNLAQPYL-SKML----IDNALLPRDMGALVAIGLAMIGVT--IGNYALNILASYryis 102
Cdd:cd18578 3 LNKPEWPLLLLGLIGAIIAGAVFPVFAILfSKLIsvfsLPDDDELRSEANFWALMFLVLAIVagIAYFLQGYLFGI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 103 TSADMLFDIRVALLRHL--QTLSprFYSRFR--LGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKL 178
Cdd:cd18578 79 AGERLTRRLRKLAFRAIlrQDIA--WFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 179 FLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRAR-NSAFVEAMLRMQV 257
Cdd:cd18578 157 ALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEAlEEPLKKGLRRALI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 258 ASFMAGAVPGTLLAVTtsGVIL-YGGYQIIEGTMSIGTLvaFMAYQSRLFSPIQV--LMGLVSGLSSARVSLARIFELFD 334
Cdd:cd18578 237 SGLGFGLSQSLTFFAY--ALAFwYGGRLVANGEYTFEQF--FIVFMALIFGAQSAgqAFSFAPDIAKAKAAAARIFRLLD 312
|
....*
gi 1730203856 335 TPAEV 339
Cdd:cd18578 313 RKPEI 317
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
358-575 |
6.25e-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: 91.73 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGS-LREKVILLDQT 436
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 437 PYLFND-TIGANI---AFARPEASEEAIrtaahqagLDPLLERLPQgLATPAGERGLALSAGERQRIALARVLLRRPDVL 512
Cdd:cd03224 84 RRIFPElTVEENLllgAYARRRAKRKAR--------LERVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 513 ILDEPTSALDPKTERHIAQTLRQVLPE-ATIIAITHRPALA-EVADRIITIEEGR-AHMRTAASLA 575
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFAlEIADRAYVLERGRvVLEGTAAELL 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-556 |
6.32e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 6.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 351 LSEAIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDA-----GRI-LFDQAPLSA-FTL 423
Cdd:PRK14258 4 LIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVeFFNQNIYERrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 424 GSLREKVILLDQTPYLFNDTIGANIAFA------RPEASEEAIRTAAHQAGldPLLERLPQGLATPAgergLALSAGERQ 497
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKDA--DLWDEIKHKIHKSA----LDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 498 RIALARVLLRRPDVLILDEPTSALDP----KTErHIAQTLRqVLPEATIIAITHR-PALAEVAD 556
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPiasmKVE-SLIQSLR-LRSELTMVIVSHNlHQVSRLSD 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
367-522 |
1.27e-20 |
|
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: 95.52 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 367 RAVlKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRyLDPDAGRILFDQAPLSAFT---LGSLREKVILLDQTPY-LFN- 441
Cdd:COG4172 300 KAV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPFgSLSp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 442 -----DTIGANIAFARPEASEEAIRTAAHQA----GLDP-LLERLPQglatpagerglALSAGERQRIALARVLLRRPDV 511
Cdd:COG4172 378 rmtvgQIIAEGLRVHGPGLSAAERRARVAEAleevGLDPaARHRYPH-----------EFSGGQRQRIAIARALILEPKL 446
|
170
....*....|.
gi 1730203856 512 LILDEPTSALD 522
Cdd:COG4172 447 LVLDEPTSALD 457
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
358-549 |
1.27e-20 |
|
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: 90.24 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLsAFTLGSLREKVILLDQTP 437
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 438 YLFND-TIGANIAFARPEASEEAIRTAAHQAGLDPLlERLPQGlatpagerglALSAGERQRIALARVLLRRPDVLILDE 516
Cdd:cd03231 83 GIKTTlSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|....
gi 1730203856 517 PTSALDPKTERHIAQTLRQVLPE-ATIIAITHRP 549
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARgGMVVLTTHQD 185
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-565 |
1.42e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.44 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLD--PDA---------GRILF--DQAPLSa 420
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArvegevrlfGRNIYspDVDPIE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 421 ftlgsLREKVILLDQTPYLF-NDTIGANIA-------FARPEAS-EEAIRTAAHQAGL-DPLLERLPQglaTPAGergla 490
Cdd:PRK14267 83 -----VRREVGMVFQYPNPFpHLTIYDNVAigvklngLVKSKKElDERVEWALKKAALwDEVKDRLND---YPSN----- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 491 LSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPA-LAEVADRIITIEEGR 565
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAqAARVSDYVAFLYLGK 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
349-565 |
1.46e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 349 PGLSEAIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSlRE 428
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 429 KVILLDQTPYLFND-TIGANI-AFARpeasEEAIRTAAHQAGLDPLLE--RLPQGLATPAGErglaLSAGERQRIALARV 504
Cdd:PRK13537 81 RVGVVPQFDNLDPDfTVRENLlVFGR----YFGLSAAAARALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 505 LLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAE-VADRIITIEEGR 565
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHFMEEAErLCDRLCVIEEGR 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-566 |
2.44e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.71 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTL---GSLRE-- 428
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrriGYLPEer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 429 ----KVILLDQTPYlfndtiganiaFAR------PEASEEAIRtaahqagldpLLERLpqGLATPAGERGLALSAGERQR 498
Cdd:COG4152 81 glypKMKVGEQLVY-----------LARlkglskAEAKRRADE----------WLERL--GLGDRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 499 IALARVLLRRPDVLILDEPTSALDPkterhIAQ-TLRQVLPE-----ATIIAITHRPALAE-VADRIITIEEGRA 566
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDP-----VNVeLLKDVIRElaakgTTVIFSSHQMELVEeLCDRIVIINKGRK 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
369-565 |
2.46e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.46 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLadllVRYLD----PDAGRI-----LFD-QAPLSAFTLGSLREKVILLDQT-- 436
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSL----LRVLNllemPRSGTLniagnHFDfSKTPSDKAIRELRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 437 --PYLfndTIGANI--------AFARPEASEEAirtaahqaglDPLLERLPqgLATPAGERGLALSAGERQRIALARVLL 506
Cdd:PRK11124 93 lwPHL---TVQQNLieapcrvlGLSKDQALARA----------EKLLERLR--LKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 507 RRPDVLILDEPTSALDPKTERHIAQTLRQvLPEATI--IAITHRPALA-EVADRIITIEEGR 565
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRE-LAETGItqVIVTHEVEVArKTASRVVYMENGH 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
370-565 |
3.04e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.95 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYlfNDTIGA--- 446
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPD--NQFVGAtve 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 447 -NIAFARPEA--SEEAIRTAAHQA----GLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEPTS 519
Cdd:PRK13650 101 dDVAFGLENKgiPHEEMKERVNEAlelvGMQDFKEREPA-----------RLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 520 ALDPKTERHIAQTLRQVLPE--ATIIAITHRpaLAEVA--DRIITIEEGR 565
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDyqMTVISITHD--LDEVAlsDRVLVMKNGQ 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
367-564 |
3.07e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.45 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 367 RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF---DQAPLSAftlgslRE-KVILLDQTPYLFND 442
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtDVSRLHA------RDrKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 -TIGANIAFA------RPEASEEAIRTAAHQ----AGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDV 511
Cdd:PRK10851 89 mTVFDNIAFGltvlprRERPNAAAIKAKVTQllemVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 512 LILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALA-EVADRIITIEEG 564
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAmEVADRVVVMSQG 213
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
370-565 |
3.16e-20 |
|
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: 91.30 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRilfdqaplsAFTLG--------SLREKVILLDQTPYLFN 441
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGT---------ARVAGydvvreprKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 442 D--------TIGANIAFARPEASEEAIRtaahqagldpLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLI 513
Cdd:TIGR01188 80 DltgrenleMMGRLYGLPKDEAEERAEE----------LLELF--ELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 514 LDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAE-VADRIITIEEGR 565
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWDYIRALKEEGvTILLTTHYMEEADkLCDRIAIIDHGR 201
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
80-329 |
3.56e-20 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 91.38 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 80 LAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLS 159
Cdd:cd18577 51 LYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 160 NLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETE 239
Cdd:cd18577 131 SLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 240 RFrarNSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGVIL---YGGYQIIEGTMSIGT-LVAFMAYQSRLFSpIQVLMGL 315
Cdd:cd18577 211 RY---SKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALafwYGSRLVRDGEISPGDvLTVFFAVLIGAFS-LGQIAPN 286
|
250
....*....|....
gi 1730203856 316 VSGLSSARVSLARI 329
Cdd:cd18577 287 LQAFAKARAAAAKI 300
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-561 |
4.04e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 95.10 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 78 IGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLRHLqtlsprFYS--RFRLGDLMSRINSDVS-DIQRVTADTM 154
Cdd:PTZ00265 99 IIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSV------FYQdgQFHDNNPGSKLTSDLDfYLEQVNAGIG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 155 LSVLSNLLMLTGGVAIMLWLDWK---LFLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSL 231
Cdd:PTZ00265 173 TKFITIFTYASAFLGLYIWSLFKnarLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 232 NAAAHETERFRARNSAFVEAMLRMQ-VASFMAGAVPGTLLAVTTSGviLYGGYQIIEGTMSigtlvafMAYQSRLF---S 307
Cdd:PTZ00265 253 CGEKTILKKFNLSEKLYSKYILKANfMESLHIGMINGFILASYAFG--FWYGTRIIISDLS-------NQQPNNDFhggS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 308 PIQVLMGLVSGLSSARVSLARI-------------FELFDTPAEVLEGSSARAFPGLSEaIRFEDVALAHDGRA---VLK 371
Cdd:PTZ00265 324 VISILLGVLISMFMLTIILPNIteymksleatnslYEIINRKPLVENNDDGKKLKDIKK-IQFKNVRFHYDTRKdveIYK 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 372 GFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF-DQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAF 450
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKY 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 451 ---------ARPEASEEaiRTAAHQAGLDP-------------------------------------------------- 471
Cdd:PTZ00265 483 slyslkdleALSNYYNE--DGNDSQENKNKrnscrakcagdlndmsnttdsneliemrknyqtikdsevvdvskkvlihd 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 472 LLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA---TIIaITHR 548
Cdd:PTZ00265 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnriTII-IAHR 639
|
570
....*....|...
gi 1730203856 549 PALAEVADRIITI 561
Cdd:PTZ00265 640 LSTIRYANTIFVL 652
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
385-565 |
6.03e-20 |
|
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: 91.02 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 385 VLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSafTLGSLREKVILLDQTPYLF-NDTIGANIAFA-RPEASEEAIRT 462
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT--NVPPHLRHINMVFQSYALFpHMTVEENVAFGlKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 463 AAHQAGLdplleRLPQgLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--A 540
Cdd:TIGR01187 79 PRVLEAL-----RLVQ-LEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlgI 152
|
170 180
....*....|....*....|....*..
gi 1730203856 541 TIIAITH--RPALAeVADRIITIEEGR 565
Cdd:TIGR01187 153 TFVFVTHdqEEAMT-MSDRIAIMRKGK 178
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
351-547 |
6.49e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.45 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 351 LSEAI-RFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRY--LDPD---AGRILFDQAPLSAFTLG 424
Cdd:PRK14239 1 MTEPIlQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 425 S--LREKVILLDQTPYLFNDTIGANIAFA-------RPEASEEAIRTAAHQAGL-DPLLERLpqglatpaGERGLALSAG 494
Cdd:PRK14239 81 TvdLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIwDEVKDRL--------HDSALGLSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 495 ERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITH 547
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
369-568 |
9.28e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.76 E-value: 9.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLS-AFTLGSLREKVILLDQTPylfNDTIGAN 447
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLWDIRNKAGMVFQNP---DNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 448 I-----AFArPE----ASEEaIRTAahqagLDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPT 518
Cdd:PRK13633 102 IveedvAFG-PEnlgiPPEE-IRER-----VDESLKKV--GMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 519 SALDPKTERHIAQTLRQVLPEA--TIIAITHRPALAEVADRIITIEEGRAHM 568
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVM 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
353-547 |
1.04e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.15 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 353 EAIRFEDVALAHDG----RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAftLGSLRE 428
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 429 KVI----LLdqtPYLfndTIGANIAFA-----RPEASEEAIrtaAHQagldpLLERLpqGLATPAGERGLALSAGERQRI 499
Cdd:COG4525 80 VVFqkdaLL---PWL---NVLDNVAFGlrlrgVPKAERRAR---AEE-----LLALV--GLADFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 500 ALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITH 547
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITH 193
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
355-565 |
1.19e-19 |
|
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: 87.63 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFcAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGsLREKVILLD 434
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 Q--------TPYLFNDTIGANIAFARPEASEEAIRtaahqagldpLLERLpqGLATPAGERGLALSAGERQRIALARVLL 506
Cdd:cd03264 79 QefgvypnfTVREFLDYIAWLKGIPSKEVKARVDE----------VLELV--NLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 507 RRPDVLILDEPTSALDPKtERHIAQT-LRQVLPEATIIAITHRPA-LAEVADRIITIEEGR 565
Cdd:cd03264 147 GDPSILIVDEPTAGLDPE-ERIRFRNlLSELGEDRIVILSTHIVEdVESLCNQVAVLNKGK 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
355-564 |
1.64e-19 |
|
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: 91.79 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLvRYLD---PDAGRILF------------------ 413
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVL-RGMDqyePTSGRIIYhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 414 DQAPLSAFTLGS---------------LREKV-ILLDQTPYLF-NDTIGANIAFARPEA---SEEAIRTAAHqagldpLL 473
Cdd:TIGR03269 80 EPCPVCGGTLEPeevdfwnlsdklrrrIRKRIaIMLQRTFALYgDDTVLDNVLEALEEIgyeGKEAVGRAVD------LI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 474 E--RLPQGLATPAGErglaLSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRP 549
Cdd:TIGR03269 154 EmvQLSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWP 229
|
250
....*....|....*.
gi 1730203856 550 -ALAEVADRIITIEEG 564
Cdd:TIGR03269 230 eVIEDLSDKAIWLENG 245
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
46-321 |
2.24e-19 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 88.85 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 46 LISTALNLAQPYLSKMLIDNALLPR------DMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLRHL 119
Cdd:cd18780 6 LVSSGTNLALPYFFGQVIDAVTNHSgsggeeALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 120 QTLSPRFYSRFRLGDLMSRINSDVSDIQRVtADTMLS-VLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQR 198
Cdd:cd18780 86 IAQEIAFFDVTRTGELLNRLSSDTQVLQNA-VTVNLSmLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 199 KLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERF-RARNSAF-VEAMLRMQVASFMagavpGTLLAVTTSG 276
Cdd:cd18780 165 YVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYsEKINESYlLGKKLARASGGFN-----GFMGAAAQLA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1730203856 277 VIL---YGGYQIIEGTMSIGTLVAFMAYQsrlfspIQVLMGLvSGLSS 321
Cdd:cd18780 240 IVLvlwYGGRLVIDGELTTGLLTSFLLYT------LTVAMSF-AFLSS 280
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
356-569 |
2.40e-19 |
|
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: 87.04 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 356 RFEDVAlahDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFD-----QAPLSAFT-LGSLREK 429
Cdd:cd03266 10 RFRDVK---KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvKEPAEARRrLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 VILLDQTpylfndTIGANIA-FAR-----PEASEEAIRTAAHQAGLDPLLERlpqglatpageRGLALSAGERQRIALAR 503
Cdd:cd03266 87 TGLYDRL------TARENLEyFAGlyglkGDELTARLEELADRLGMEELLDR-----------RVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 504 VLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHR-PALAEVADRIITIEEGRAHMR 569
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGkCILFSTHImQEVERLCDRVVVLHRGRVVYE 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-564 |
4.29e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.02 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLD------PDAGRILFDQAPLSAFTLGSLREKVILLDQTPY 438
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 439 LF-NDTIGANIAFarPEAS-------------EEAIRTAAhqagldpLLERLPQGLATPAGErglaLSAGERQRIALARV 504
Cdd:PRK14246 101 PFpHLSIYDNIAY--PLKShgikekreikkivEECLRKVG-------LWKEVYDRLNSPASQ----LSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 505 LLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRP-ALAEVADRIITIEEG 564
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPqQVARVADYVAFLYNG 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
369-558 |
4.43e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT-LGSLREKVILLDQTPYLFND-TIGA 446
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 447 NIAFARPEASEEAIRTAAHQAGLDPLLERLpqGL----ATPAGErglaLSAGERQRIALARVLLRRPDVLILDEPTSALD 522
Cdd:COG1129 99 NIFLGREPRRGGLIDWRAMRRRARELLARL--GLdidpDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1730203856 523 PK-TER--HIAQTLRQ--VlpeaTIIAITHRpaLAEV---ADRI 558
Cdd:COG1129 173 EReVERlfRIIRRLKAqgV----AIIYISHR--LDEVfeiADRV 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
367-559 |
4.57e-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: 88.19 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 367 RAVlKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDP---DAGRILFDQAPLSAFTLGSLREkvILLDQTPYLFND- 442
Cdd:COG0444 19 KAV-DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRK--IRGREIQMIFQDp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 --------TIGANIAFA--------RPEASEEAIRtaahqagldpLLERLpqGLATPAgERGLA----LSAGERQRIALA 502
Cdd:COG0444 96 mtslnpvmTVGDQIAEPlrihgglsKAEARERAIE----------LLERV--GLPDPE-RRLDRypheLSGGMRQRVMIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHR-PALAEVADRII 559
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElgLAILFITHDlGVVAEIADRVA 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
365-565 |
5.58e-19 |
|
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: 85.88 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVlKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRilfdqAPLSAFTL----GSLREKVILLDQTPYLF 440
Cdd:cd03265 12 DFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR-----ATVAGHDVvrepREVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 441 NDTIG-ANIA-FARPEASEEAIRTAAhqagLDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPT 518
Cdd:cd03265 86 DELTGwENLYiHARLYGVPGAERRER----IDELLDFV--GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 519 SALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAE-VADRIITIEEGR 565
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEfgMTILLTTHYMEEAEqLCDRVAIIDHGR 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
354-565 |
5.89e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.35 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAfTLGSLREKVILL 433
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTPYLFND-TIGAN-IAFARpeasEEAIRTAAHQAGLDPLLE--RLPQGLATPAGErglaLSAGERQRIALARVLLRRP 509
Cdd:PRK13536 120 PQFDNLDLEfTVRENlLVFGR----YFGMSTREIEAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDP 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 510 DVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAE-VADRIITIEEGR 565
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGkTILLTTHFMEEAErLCDRLCVLEAGR 249
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
355-565 |
6.03e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.68 E-value: 6.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLD 434
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYlFND--TIGANIAFAR-P-------EASEEAIRTAAHQAGLDPLLER-LPQglatpagerglaLSAGERQRIALAR 503
Cdd:COG4604 82 QENH-INSrlTVRELVAFGRfPyskgrltAEDREIIDEAIAYLDLEDLADRyLDE------------LSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 504 VLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALAEV-ADRIITIEEGR 565
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCyADHIVAMKDGR 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
370-565 |
7.03e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.19 E-value: 7.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT----LGSLREKVILLDQTP--YLFNDT 443
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknLKKLRKKVSLVFQFPeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 444 I-------GANIAFARPEASEEAIRTAaHQAGL-DPLLERLPqglatpagergLALSAGERQRIALARVLLRRPDVLILD 515
Cdd:PRK13641 103 VlkdvefgPKNFGFSEDEAKEKALKWL-KKVGLsEDLISKSP-----------FELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 516 EPTSALDPKTERHIAQTLRQVLPEA-TIIAITHR-PALAEVADRIITIEEGR 565
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGhTVILVTHNmDDVAEYADDVLVLEHGK 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
369-565 |
8.92e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 8.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTL------------ADLLVR--YLDPDAGRILFDQAPLSAF--TLGSLREKVIL 432
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLvthfnglikskyGTIQVGdiYIGDKKNNHELITNPYSKKikNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTP--YLFNDTIGANIAF---ARPEASEEAIRTAAH---QAGLD-PLLERLPQGLatpagerglalSAGERQRIALAR 503
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFgpvALGVKKSEAKKLAKFylnKMGLDdSYLERSPFGL-----------SGGQKRRVAIAG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 504 VLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHR-PALAEVADRIITIEEGR 565
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTmEHVLEVADEVIVMDKGK 253
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
355-564 |
9.00e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.10 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHD------GRAVLKgFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT----LG 424
Cdd:PRK13643 2 IKFEKVNYTYQpnspfaSRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 425 SLREKVILLDQTP--YLFNDTIGANIAFArPE----ASEEAIRTAAHQagldplLERLpqGLATPAGERG-LALSAGERQ 497
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFG-PQnfgiPKEKAEKIAAEK------LEMV--GLADEFWEKSpFELSGGQMR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 498 RIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITH-RPALAEVADRIITIEEG 564
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHlMDDVADYADYVYLLEKG 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
366-565 |
1.07e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 85.29 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 366 GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTL-GSLREKVILLDQTPYLFND-T 443
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 444 IGANIAFA---RPEASEEAIRTaahqagLDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSA 520
Cdd:cd03218 92 VEENILAVleiRGLSKKEREEK------LEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1730203856 521 LDPKTERHIaQTLRQVLPEATI-IAIT-H--RPALAeVADRIITIEEGR 565
Cdd:cd03218 164 VDPIAVQDI-QKIIKILKDRGIgVLITdHnvRETLS-ITDRAYIIYEGK 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
375-565 |
1.13e-18 |
|
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: 87.86 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 375 LEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAplsafTLGSLREKVILldqTP------YLFND------ 442
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-----TLFDSRKGIFL---PPekrrigYVFQEarlfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 -TIGANIAFA--RPEASEEAIRTAAHQA--GLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:TIGR02142 90 lSVRGNLRYGmkRARPSERRISFERVIEllGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 518 TSALDPKTERHIAQTLRQVLPEATI--IAITHRPA-LAEVADRIITIEEGR 565
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIpiLYVSHSLQeVLRLADRVVVLEDGR 209
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
358-565 |
1.56e-18 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 84.76 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLgslrEKVILLDQTP 437
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDL----HKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 438 YLFNdtigaNIAfARPEASEEAIRTAAHQAGLDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:TIGR03740 80 PLYE-----NLT-ARENLKVHTTLLGLPDSRIDEVLNIV--DLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 518 TSALDPKTerhiAQTLRQVL---PEATIIAITHRPALAEV---ADRIITIEEGR 565
Cdd:TIGR03740 152 TNGLDPIG----IQELRELIrsfPEQGITVILSSHILSEVqqlADHIGIISEGV 201
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
358-561 |
1.63e-18 |
|
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: 83.95 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAfTLGSLREKVILLDQTP 437
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 438 YLFND-TIGANIAFARP--EASEEAIRTAAHQAGLDPLlERLPQGlatpagerglALSAGERQRIALARVLLRRPDVLIL 514
Cdd:TIGR01189 83 GLKPElSALENLHFWAAihGGAQRTIEDALAAVGLTGF-EDLPAA----------QLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1730203856 515 DEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRIITI 561
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEARELRL 198
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
355-567 |
2.80e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.77 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF---DQAPLSAFTLGSLREKV 430
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsghDITRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 431 ILLDQTPYLFND-TIGANIAFAR--PEASEEAIRTAAhQAGLDPLlerlpqGLATPAGERGLALSAGERQRIALARVLLR 507
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIPLiiAGASGDDIRRRV-SAALDKV------GLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLRQV-LPEATIIAITHRPALAEVAD-RIITIEEGRAH 567
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
341-565 |
3.11e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.81 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 341 EGSSARAFPGLSEaIRfeDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSa 420
Cdd:PRK11607 9 QAKTRKALTPLLE-IR--NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 421 fTLGSLREKVILLDQTPYLF-NDTIGANIAFARPE---ASEEAIRTAAHQAGLDPLLERlpqglatpAGERGLALSAGER 496
Cdd:PRK11607 85 -HVPPYQRPINMMFQSYALFpHMTVEQNIAFGLKQdklPKAEIASRVNEMLGLVHMQEF--------AKRKPHQLSGGQR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 497 QRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAmTMAGRIAIMNRGK 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
329-564 |
3.60e-18 |
|
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: 88.81 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 329 IFELFDtpaEVLEGSSARAFPGLSEAIRFEDVALAhdGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDA 408
Cdd:TIGR01271 406 IGELFE---KIKQNNKARKQPNGDDGLFFSNFSLY--VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 409 GRILFDQaplsaftlgslreKVILLDQTPYLFNDTIGANIAFARpEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERG 488
Cdd:TIGR01271 481 GKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFGL-SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGG 546
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 489 LALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQT-LRQVLPEATIIAITHRPALAEVADRIITIEEG 564
Cdd:TIGR01271 547 ITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
355-547 |
4.19e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.30 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLD 434
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFND-TIGANIAFARP----------EASEEAIRTAAHQAGLDPLLERlpqglatpageRGLALSAGERQRIALAR 503
Cdd:PRK11231 83 QHHLTPEGiTVRELVAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLADR-----------RLTDLSGGQRQRAFLAM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1730203856 504 VLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITH 547
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGkTVVTVLH 196
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
369-565 |
4.91e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.98 E-value: 4.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFD--------------------QAPLSAfTLGSLre 428
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgkdvtklpeykrakyigrvfQDPMMG-TAPSM-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 429 kvilldqtpylfndTIGAN--IAFARPEASEEAIR-TAAHQAGLDPLLERLPQGL----ATPAGerglALSAGERQRIAL 501
Cdd:COG1101 98 --------------TIEENlaLAYRRGKRRGLRRGlTKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQRQALSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 502 ARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITH--RPALaEVADRIITIEEGR 565
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHnmEQAL-DYGNRLIMMHEGR 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
367-565 |
5.06e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 88.30 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 367 RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAplsaftlgslrekVILLDQTPYLFNDTIGA 446
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-------------IAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 447 NIAFARPEASE---EAIRTAAHQAGLdpllERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDP 523
Cdd:PTZ00243 740 NILFFDEEDAArlaDAVRVSQLEADL----AQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1730203856 524 KT-ERHIAQTLRQVLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:PTZ00243 816 HVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGR 858
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
370-575 |
1.88e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.46 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLS------AFTLG--------------SLREK 429
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdAIALGigmvhqhfmlvpnlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 VIL-LDQTPYLFNDTiganiafarpEASEEAIRTAAHQAGL--DPllerlpqglATPAGErglaLSAGERQRIALARVLL 506
Cdd:COG3845 101 IVLgLEPTKGGRLDR----------KAARARIRELSERYGLdvDP---------DAKVED----LSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 507 RRPDVLILDEPTSALDPKTERHIAQTLRQvLPEA--TIIAITHRpaLAEV---ADRIITIEEGR--AHMRTA----ASLA 575
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRR-LAAEgkSIIFITHK--LREVmaiADRVTVLRRGKvvGTVDTAetseEELA 234
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
366-564 |
1.92e-17 |
|
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: 82.98 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 366 GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQaplsaftlgslreKVILLDQTPYLFNDTIG 445
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 446 ANIAFARpEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKT 525
Cdd:cd03291 116 ENIIFGV-SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1730203856 526 ERHIAQT-LRQVLPEATIIAITHRPALAEVADRIITIEEG 564
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
366-567 |
2.88e-17 |
|
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: 84.99 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 366 GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLvryldpdAGrilFDQaPLSAFTLGSLREKVILLDQTPYL-FNDTI 444
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VDK-DFNGEARPQPGIKVGYLPQEPQLdPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 445 GANI-------------------AFARPEAS-----------EEAIRTA-AHQagLDPLLERLPQGLATPAGERGLA-LS 492
Cdd:TIGR03719 86 RENVeegvaeikdaldrfneisaKYAEPDADfdklaaeqaelQEIIDAAdAWD--LDSQLEIAMDALRCPPWDADVTkLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 493 AGERQRIALARVLLRRPDVLILDEPTSALDPKT----ERHIAQTlrqvlpEATIIAITH-RPALAEVADRIITIEEGRAH 567
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQEY------PGTVVAVTHdRYFLDNVAGWILELDRGRGI 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
357-564 |
3.02e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 357 FEDVALAHdgravlkgFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT----LGSLREKVIL 432
Cdd:PRK13646 18 YEHQAIHD--------VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRPVRKRIGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTP--YLFNDTIGANIAFArPE---ASEEAIRTAAHQAGLDPLLERLPQGLATpagergLALSAGERQRIALARVLLR 507
Cdd:PRK13646 90 VFQFPesQLFEDTVEREIIFG-PKnfkMNLDEVKNYAHRLLMDLGFSRDVMSQSP------FQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHR-PALAEVADRIITIEEG 564
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDmNEVARYADEVIVMKEG 222
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
357-564 |
3.10e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.99 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 357 FEDVALAH-DGRA-VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLD 434
Cdd:PTZ00243 1311 FEGVQMRYrEGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFNDTIGANI-AFArpEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLI 513
Cdd:PTZ00243 1391 QDPVLFDGTVRQNVdPFL--EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFI 1468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 514 L-DEPTSALDPKTERHIAQTLRQVLPEATIIAITHRpaLAEVA--DRIITIEEG 564
Cdd:PTZ00243 1469 LmDEATANIDPALDRQIQATVMSAFSAYTVITIAHR--LHTVAqyDKIIVMDHG 1520
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
373-522 |
3.55e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 82.70 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 373 FTLEipRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFD-QAPL--SAFTLGSLREKVILLDQTPY-LFN--DTIGA 446
Cdd:PRK11308 36 FTLE--RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQgQDLLkaDPEAQKLLRQKIQIVFQNPYgSLNprKKVGQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 447 --------NIAFARPEASEEAIRTAAhQAGLDP-LLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:PRK11308 114 ileeplliNTSLSAAERREKALAMMA-KVGLRPeHYDRYPH-----------MFSGGQRQRIAIARALMLDPDVVVADEP 181
|
....*
gi 1730203856 518 TSALD 522
Cdd:PRK11308 182 VSALD 186
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
355-567 |
4.29e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.74 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLD 434
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 Q-TPYLFNDTIGANIAFAR-PEASEEAIRTAAHQAGLDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVL 512
Cdd:PRK09536 84 QdTSLSFEFDVRQVVEMGRtPHRSRFDTWTETDRAAVERAMERT--GVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 513 ILDEPTSALDPKterHIAQTL----RQVLPEATIIAITHRPAL-AEVADRIITIEEGRAH 567
Cdd:PRK09536 162 LLDEPTASLDIN---HQVRTLelvrRLVDDGKTAVAAIHDLDLaARYCDELVLLADGRVR 218
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
41-551 |
4.38e-17 |
|
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: 84.80 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 41 VLLVSLISTALNlAQPYLSKMLIDNAllPRDMGALVAIGLAMIGVTIGNYALN-ILASY-----RYisTSADMLFDIRVA 114
Cdd:TIGR00954 95 TGLLILIAFLLV-SRTYLSVYVATLD--GQIESSIVRRSPRNFAWILFKWFLIaPPASFinsaiKY--LLKELKLRFRVR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 115 LLRHLQTLSPRFYSRFRLGDLMSRI-NSDVSDIQRVT--ADTMLSVLSNLL------------MLTGGVAIMLWLDWKLF 179
Cdd:TIGR00954 170 LTRYLYSKYLSGFTFYKVSNLDSRIqNPDQLLTQDVEkfCDSVVELYSNLTkpildvilysfkLLTALGSVGPAGLFAYL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 180 LLAIVLLPAcvglfvvFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVAS 259
Cdd:TIGR00954 250 FATGVVLTK-------LRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIKFR 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 260 FMAGAVPGTLLAVTTSGV-ILYGGYQII------EGTMSIGTLVAFMAYQSRLF----SPIQVLMGLVSGLSSARVSLAR 328
Cdd:TIGR00954 323 FSYGFLDNIVAKYTWSAVgLVAVSIPIFdkthpaFLEMSEEELMQEFYNNGRLLlkaaDALGRLMLAGRDMTRLAGFTAR 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 329 IFELFDT----------PAEVLEGSSARAFPGLSE-------------AIRFEDVALAH-DGRAVLKGFTLEIPRGSFCA 384
Cdd:TIGR00954 403 VDTLLQVlddvksgnfkRPRVEEIESGREGGRNSNlvpgrgiveyqdnGIKFENIPLVTpNGDVLIESLSFEVPSGNNLL 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 385 VLGPSGVGKSTLADLL---------VRYLDPDaGRILF-DQAPLsaFTLGSLREKVILLDQTPYLFNDTIGaniafarpE 454
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILgelwpvyggRLTKPAK-GKLFYvPQRPY--MTLGTLRDQIIYPDSSEDMKRRGLS--------D 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 455 ASEEAIRTAAHqagLDPLLERlpqglatpagERGLA--------LSAGERQRIALARVLLRRPDVLILDEPTSALDPKTE 526
Cdd:TIGR00954 552 KDLEQILDNVQ---LTHILER----------EGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
570 580
....*....|....*....|....*
gi 1730203856 527 RHIAQTLRQVlpEATIIAITHRPAL 551
Cdd:TIGR00954 619 GYMYRLCREF--GITLFSVSHRKSL 641
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
369-565 |
4.62e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 81.39 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTL---ADLLVrylDPDAGRILFD-------------QAPLSAFTLGSLREKVIL 432
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFlrcINLLE---TPDSGEIRVGgeeirlkpdrdgeLVPADRRQLQRIRTRLGM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTpylFN----DTIGANIAFA------RPEAseEAIRTAAHqagldpLLERLpqGLATPAGERGLALSAGERQRIALA 502
Cdd:COG4598 100 VFQS---FNlwshMTVLENVIEApvhvlgRPKA--EAIERAEA------LLAKV--GLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 503 RVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALA-EVADRIITIEEGR 565
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGrTMLVVTHEMGFArDVSSHVVFLHQGR 231
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
366-523 |
5.45e-17 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 80.40 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 366 GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTL-GSLREKVILLDQTPYLFND-T 443
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMhERARLGIGYLPQEASIFRKlT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 444 IGANIAFA---RPEASEEAIRtaahqAGLDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSA 520
Cdd:TIGR04406 93 VEENIMAVleiRKDLDRAERE-----ERLEALLEEF--QISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAG 165
|
...
gi 1730203856 521 LDP 523
Cdd:TIGR04406 166 VDP 168
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-565 |
6.79e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.30 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 338 EVLEGSSARA-FPGLSEAIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAG------- 409
Cdd:PRK14271 4 ERLGGQSGAAdVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 410 ----RILFDQAPLSAFtlgslREKVILLDQTPYLFNDTIGANI---AFARPEASEEAIRTAAH----QAGL-DPLLERLp 477
Cdd:PRK14271 84 llggRSIFNYRDVLEF-----RRRVGMLFQRPNPFPMSIMDNVlagVRAHKLVPRKEFRGVAQarltEVGLwDAVKDRL- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 478 qglatpaGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPA-LAEVAD 556
Cdd:PRK14271 158 -------SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISD 230
|
....*....
gi 1730203856 557 RIITIEEGR 565
Cdd:PRK14271 231 RAALFFDGR 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
370-573 |
8.49e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.91 E-value: 8.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYlfNDTIGANIa 449
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPD--NQFVGATV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 450 farpeasEEAIRTAAHQAGL--DPLLERLPQGLAT----------PAgerglALSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:PRK13642 100 -------EDDVAFGMENQGIprEEMIKRVDEALLAvnmldfktrePA-----RLSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 518 TSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAEVADRIITIEEGRAHMRTAAS 573
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPS 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
368-565 |
8.82e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.62 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 368 AVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLvRYLD-PDAG--RIL-FDQAPLSAFTLGSLR--------EKVILLDQ 435
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDkPTSGtyRVAgQDVATLDADALAQLRrehfgfifQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 436 TPYLFNDTIGANIAfarpeASEEAIRTAAHQAgldpLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILD 515
Cdd:PRK10535 101 LTAAQNVEVPAVYA-----GLERKQRLLRAQE----LLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 516 EPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGhTVIIVTHDPQVAAQAERVIEIRDGE 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
356-522 |
9.28e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 356 RFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILL-D 434
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLpQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFNDTIGANIAFAR----------PEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARV 504
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAML 161
|
170
....*....|....*...
gi 1730203856 505 LLRRPDVLILDEPTSALD 522
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALD 179
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-565 |
2.00e-16 |
|
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: 82.16 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 335 TPAEVlegsSARAFPGLSEAIRFEDVALAHD--------------GRAVLK---GFTLEIPRGSFCAVLGPSGVGKSTLA 397
Cdd:TIGR03269 252 TPDEV----VAVFMEGVSEVEKECEVEVGEPiikvrnvskryisvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 398 DLLVRYLDPDAGRILF-------DQAPLSAFTLGSLREKVILLDQTPYLF-NDTIGAN----IAFARPEasEEAIRTAAH 465
Cdd:TIGR03269 328 KIIAGVLEPTSGEVNVrvgdewvDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNlteaIGLELPD--ELARMKAVI 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 466 ---QAGLD-----PLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTL---R 534
Cdd:TIGR03269 406 tlkMVGFDeekaeEILDKYPD-----------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaR 474
|
250 260 270
....*....|....*....|....*....|..
gi 1730203856 535 QVLpEATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:TIGR03269 475 EEM-EQTFIIVSHDMDFVlDVCDRAALMRDGK 505
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
350-565 |
2.11e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.35 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 350 GLSEAIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT---LGSL 426
Cdd:PRK10419 8 GLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 427 REKVILLDQ-TPYLFN--DTIGANIA-----FARPEASEEAIRTAA--HQAGLDP-LLERLPQglatpagerglALSAGE 495
Cdd:PRK10419 88 RRDIQMVFQdSISAVNprKTVREIIReplrhLLSLDKAERLARASEmlRAVDLDDsVLDKRPP-----------QLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 496 RQRIALARVLLRRPDVLILDEPTSALDpkteRHI-AQTLRQV--LPEATIIA---ITHRPALAE-VADRIITIEEGR 565
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLD----LVLqAGVIRLLkkLQQQFGTAclfITHDLRLVErFCQRVMVMDNGQ 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
355-525 |
2.43e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.42 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSL---REKVI 431
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 432 LLDQTPYLFND-TIGANIAFARPEaseeairtaaHQAGLDPLLERLPQGLATPAGERGLA------LSAGERQRIALARV 504
Cdd:PRK11831 88 MLFQSGALFTDmNVFDNVAYPLRE----------HTQLPAPLLHSTVMMKLEAVGLRGAAklmpseLSGGMARRAALARA 157
|
170 180
....*....|....*....|.
gi 1730203856 505 LLRRPDVLILDEPTSALDPKT 525
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPIT 178
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
367-560 |
3.67e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.69 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 367 RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYL--DPDAGRILFDQAPLSaftlgslREKVILldqtpylfnDTI 444
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG-------REASLI---------DAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 445 GANIAFArpeaseEAIRtAAHQAGL-DPLLERlpqglATPAgerglALSAGERQRIALARVLLRRPDVLILDEPTSALDP 523
Cdd:COG2401 107 GRKGDFK------DAVE-LLNAVGLsDAVLWL-----RRFK-----ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1730203856 524 KTERHIAQTLRQVLPEA--TIIAITHRPALAEV--ADRIIT 560
Cdd:COG2401 170 QTAKRVARNLQKLARRAgiTLVVATHHYDVIDDlqPDLLIF 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
355-565 |
4.19e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLD 434
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFND-TIGANIA---------FARPEASEEAIRTAAHQAgldpllerlpQGLATPAGERGLALSAGERQRIALARV 504
Cdd:PRK10253 88 QNATTPGDiTVQELVArgryphqplFTRWRKEDEEAVTKAMQA----------TGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 505 LLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALA-EVADRIITIEEGR 565
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQAcRYASHLIALREGK 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
358-549 |
4.32e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQaplSAFTLGSLREkvilldQTP 437
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAE------ACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 438 YL-----FND--TIGANIAFARP--EASEEAIRTAAHQAGLDPLLERlpqglatPAGErglaLSAGERQRIALARVLL-R 507
Cdd:PRK13539 77 YLghrnaMKPalTVAENLEFWAAflGGEELDIAAALEAVGLAPLAHL-------PFGY----LSAGQKRRVALARLLVsN 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1730203856 508 RPdVLILDEPTSALDPKTERHIAQTLRQVLPE-ATIIAITHRP 549
Cdd:PRK13539 146 RP-IWILDEPTAALDAAAVALFAELIRAHLAQgGIVIAATHIP 187
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
39-312 |
4.53e-16 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 79.08 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 39 TLVLLVslISTALNLAQPYLSKMLID------NALLPRDMGALVAIGLAMIGVTIGNYALNILasYRYISTSAdmLFDIR 112
Cdd:cd18582 1 ALLLLV--LAKLLNVAVPFLLKYAVDalsapaSALLAVPLLLLLAYGLARILSSLFNELRDAL--FARVSQRA--VRRLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 113 VALLRHLQTLSPRFYSRFRLGDLmsrinsdVSDIQRVTA--DTMLSVLSNLLMLT----GGVAIMLW--LDWKLFLLAIV 184
Cdd:cd18582 75 LRVFRHLHSLSLRFHLSRKTGAL-------SRAIERGTRgiEFLLRFLLFNILPTilelLLVCGILWylYGWSYALITLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 185 LLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGA 264
Cdd:cd18582 148 TVALYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNI 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1730203856 265 VPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVL 312
Cdd:cd18582 228 GQALIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFL 275
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
363-565 |
4.57e-16 |
|
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: 78.31 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 363 AHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSL----REKVILLDQTPY 438
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRrafrRDVQLVFQDSPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 439 LFN--DTIGANIA-----FARPEASEEAIRTAA--HQAGLDP-LLERLPQglatpagerglALSAGERQRIALARVLLRR 508
Cdd:TIGR02769 100 AVNprMTVRQIIGeplrhLTSLDESEQKARIAEllDMVGLRSeDADKLPR-----------QLSGGQLQRINIARALAVK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 509 PDVLILDEPTSALDPKTERHIAQTLRQVLPEATI--IAITHRPALAE-VADRIITIEEGR 565
Cdd:TIGR02769 169 PKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQsFCQRVAVMDKGQ 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
359-564 |
6.90e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 359 DVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVI-LLDQTP 437
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIyLVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 438 YLF-NDTIGANIAFARPEASEEAIRTAAHQAGLDPLLErlpqgLATPAGerglALSAGERQRIALARVLLRRPDVLILDE 516
Cdd:PRK15439 96 LLFpNLSVKENILFGLPKRQASMQKMKQLLAALGCQLD-----LDSSAG----SLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 517 PTSALDP-KTERHIAQtLRQVLPEAT-IIAITHR-PALAEVADRIITIEEG 564
Cdd:PRK15439 167 PTASLTPaETERLFSR-IRELLAQGVgIVFISHKlPEIRQLADRISVMRDG 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
364-547 |
7.73e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 7.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 364 HDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSaftlGSLREKVILLDQTPYLFNDT 443
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE----GPGAERGVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 444 IGANIAFARPEA--SEEAIRTAAHQagldpLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSAL 521
Cdd:PRK11248 87 VQDNVAFGLQLAgvEKMQRLEIAHQ-----MLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*...
gi 1730203856 522 DPKTERHIAQTLRQVLPEA--TIIAITH 547
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETgkQVLLITH 187
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
358-580 |
9.25e-16 |
|
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: 76.03 E-value: 9.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLV---RYlDPDAGRILFDqaplsaftlgslreKVILLD 434
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKY-EVTEGEILFK--------------GEDITD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPY------LFndtiganIAFARPEASEEaIRTAAhqagldpLLERLPQGLatpagerglalSAGERQRIALARVLLRR 508
Cdd:cd03217 69 LPPEerarlgIF-------LAFQYPPEIPG-VKNAD-------FLRYVNEGF-----------SGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 509 PDVLILDEPTSALDPKTERHIAQTLRQVLPEAT-IIAITHRPALAE--VADRIITIEEGRAHMRTAASLAPLVEA 580
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKsVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKELALEIEK 197
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
355-564 |
1.38e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.98 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLadllVRYLdpdAGRILFDQAPLSAFTL----------- 423
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTL----LRHL---SGLITGDKSAGSHIELlgrtvqregrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 424 -----------GSLREKVILLDQTPYLFNDTIGA--NIAFAR-------PEASEEAIRTaahqagldplLERLpqGLATP 483
Cdd:PRK09984 78 ardirksrantGYIFQQFNLVNRLSVLENVLIGAlgSTPFWRtcfswftREQKQRALQA----------LTRV--GMVHF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 484 AGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIIT 560
Cdd:PRK09984 146 AHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYAlRYCERIVA 225
|
....
gi 1730203856 561 IEEG 564
Cdd:PRK09984 226 LRQG 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
355-565 |
1.44e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.53 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQA-----PLSAFTLGSLREK 429
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 VILLdqtPYLfndTIGANIAF----ARPEASEEAIRT--AAHQAGLDPLLERLPQglatpagerglALSAGERQRIALAR 503
Cdd:PRK11000 84 YALY---PHL---SVAENMSFglklAGAKKEEINQRVnqVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 504 VLLRRPDVLILDEPTSALDP----KTERHIAQTLRQVlpEATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAalrvQMRIEISRLHKRL--GRTMIYVTHDQVEAmTLADKIVVLDAGR 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
369-565 |
1.72e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGS---LREKVI-LLDQTPYLFND-T 443
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQKLgFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 444 IGANIAFarPEASEEAIRTAAHQAGLDPLLerlPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDP 523
Cdd:PRK11629 104 ALENVAM--PLLIGKKKPAEINSRALEMLA---AVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1730203856 524 KTERHIAQTLRQ--VLPEATIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK11629 179 RNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGR 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
369-565 |
2.14e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.05 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF---DQAPLS-AFTLGSLREKVILldQTPY------ 438
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKkTKEKEKVLEKLVI--QKTRfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 439 ------------------LFNDTIGANIAFA-------RPEASEEAiRTAAHQAGLD-PLLERLPqglatpagergLALS 492
Cdd:PRK13651 100 ikeirrrvgvvfqfaeyqLFEQTIEKDIIFGpvsmgvsKEEAKKRA-AKYIELVGLDeSYLQRSP-----------FELS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 493 AGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHR--PALaEVADRIITIEEGR 565
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDldNVL-EWTKRTIFFKDGK 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
370-564 |
2.49e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.15 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLRE-----------KVILLDQTPY 438
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkkiamvfqSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 439 LFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEPT 518
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1730203856 519 SALDP--KTERHIAQTLRQVLPEATIIAITHRPALA-EVADRIITIEEG 564
Cdd:PRK10070 193 SALDPliRTEMQDELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNG 241
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
111-322 |
3.61e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter 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.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 76.20 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 111 IRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACV 190
Cdd:cd18784 71 IRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 191 GLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNsaFVEAMLRMQVASFMAGAVPG--- 267
Cdd:cd18784 151 IVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKL--KDTYKLKIKEALAYGGYVWSnel 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 268 TLLAVTTSgVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSA 322
Cdd:cd18784 229 TELALTVS-TLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQA 282
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
368-565 |
3.93e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.82 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 368 AVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT---LGSLREKVILLDQTPYLFNDTI 444
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLRAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 445 GA--NI---AFARPEASEEAIRTAA---HQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDE 516
Cdd:PRK10584 104 NAleNVelpALLRGESSRQSRNGAKallEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 517 PTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
305-565 |
4.05e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.09 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 305 LFSPIQVLMGLVSGLSSARVSLARI--FELFDTPAEVlegSSARAFPGLSEaIRFEDVALA-HDGRAVLKGFTLEIPRGS 381
Cdd:PRK10522 275 LRTPLLSAVGALPTLLSAQVAFNKLnkLALAPYKAEF---PRPQAFPDWQT-LELRNVTFAyQDNGFSVGPINLTIKRGE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 382 FCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGaniafarPEAseeair 461
Cdd:PRK10522 351 LLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLG-------PEG------ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 462 TAAHQAGLDPLLERLP-QGLATPAGER--GLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLP 538
Cdd:PRK10522 418 KPANPALVEKWLERLKmAHKLELEDGRisNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQ 497
|
250 260
....*....|....*....|....*....
gi 1730203856 539 EA--TIIAITHRPALAEVADRIITIEEGR 565
Cdd:PRK10522 498 EMgkTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
369-565 |
6.47e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.30 E-value: 6.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLsafTLGSLREKVI-LLDQTPYLF-NDTIGA 446
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRDIcMVFQSYALFpHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 447 NIAFA-----RPEAS-EEAIRTAAHQAGLDPLLER-LPQglatpagerglaLSAGERQRIALARVLLRRPDVLILDEPTS 519
Cdd:PRK11432 98 NVGYGlkmlgVPKEErKQRVKEALELVDLAGFEDRyVDQ------------ISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1730203856 520 ALDPKTERHIAQTLRQVLPEATIIA--ITHRPALA-EVADRIITIEEGR 565
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSlyVTHDQSEAfAVSDTVIVMNKGK 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
369-565 |
8.78e-15 |
|
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: 73.91 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGR------ILFDQAPlsaftlGSLREKVILLDQTPYLFND 442
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEvrvaglVPWKRRK------KFLRRIGVVFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 -TIGANIAFARPEASEEAIRTAAHQAGLDPLLErLPQGLATPAGErglaLSAGERQRIALARVLLRRPDVLILDEPTSAL 521
Cdd:cd03267 110 lPVIDSFYLLAAIYDLPPARFKKRLDELSELLD-LEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1730203856 522 DPKTERHIAQTLRQVLPE--ATIIAITHR-PALAEVADRIITIEEGR 565
Cdd:cd03267 185 DVVAQENIRNFLKEYNRErgTTVLLTSHYmKDIEALARRVLVIDKGR 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
366-567 |
9.09e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.08 E-value: 9.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 366 GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLAdllvryldpdagRIL--FDQ-----APLSA-FTLGSL----------- 426
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMagVDKefegeARPAPgIKVGYLpqepqldpekt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 427 ---------REKVILLDQtpylFNDtIGAniAFARPEASEEAirTAAHQA------------GLDPLLERLPQGLATPAG 485
Cdd:PRK11819 87 vrenveegvAEVKAALDR----FNE-IYA--AYAEPDADFDA--LAAEQGelqeiidaadawDLDSQLEIAMDALRCPPW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 486 ERGLA-LSAGERQRIALARVLLRRPDVLILDEPTSALDPKT----ERHIAQTlrqvlpEATIIAITH-RPALAEVADRII 559
Cdd:PRK11819 158 DAKVTkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHDY------PGTVVAVTHdRYFLDNVAGWIL 231
|
....*...
gi 1730203856 560 TIEEGRAH 567
Cdd:PRK11819 232 ELDRGRGI 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
369-565 |
1.25e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.24 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFD----------QAPLSAF---TLGSLREKVILLDQ 435
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdkDGQLKVAdknQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 436 TPYLFND-TIGANI--------AFARPEASEEAIRTAAhQAGLDpllERlpqglatPAGERGLALSAGERQRIALARVLL 506
Cdd:PRK10619 100 HFNLWSHmTVLENVmeapiqvlGLSKQEARERAVKYLA-KVGID---ER-------AQGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 507 RRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAE-VADRIITIEEGR 565
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGkTMVVVTHEMGFARhVSSHVIFLHQGK 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
352-571 |
1.54e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.39 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 352 SEAIRFEDVALAHDGRAV-----------LKGFTL-----EIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDq 415
Cdd:PRK13409 321 PEPIEFEERPPRDESEREtlveypdltkkLGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 416 aplsaftlgslrEKVILLDQtpYLFND---TIGANIAFARPEASEEAIRTA-AHQAGLDPLLERlpqglatPAGErglaL 491
Cdd:PRK13409 400 ------------LKISYKPQ--YIKPDydgTVEDLLRSITDDLGSSYYKSEiIKPLQLERLLDK-------NVKD----L 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 492 SAGERQRIALARVLLRRPDVLILDEPTSALD-------PKTERHIAQTlrqvlPEATIIAITHRPALAE-VADRIITIE- 562
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE-----REATALVVDHDIYMIDyISDRLMVFEg 529
|
250
....*....|....*..
gi 1730203856 563 ----EGRAH----MRTA 571
Cdd:PRK13409 530 epgkHGHASgpmdMREG 546
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
359-565 |
1.79e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 359 DVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPL--SAFTLGSLREKVILLDQT 436
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 437 P--YLFNDTIGANIAFARPE---ASEEAIRtaahqagldplleRLPQGLATPAGERG-----LALSAGERQRIALARVLL 506
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNlgvPEAEITR-------------RVDEALTLVDAQHFrhqpiQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 507 RRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPA--LAEVADRIITIEEGR 565
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIdlIYEISDAVYVLRQGQ 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
365-565 |
2.50e-14 |
|
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: 72.15 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAfTLGSLREKV-------ILLDQ-T 436
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLgycpqfdALFDElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 437 PY---LFndtiganiaFAR----PEASEEAIRTAAHQA-GLDPLLERLPQglatpagerglALSAGERQRIALARVLLRR 508
Cdd:cd03263 92 VRehlRF---------YARlkglPKSEIKEEVELLLRVlGLTDKANKRAR-----------TLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 509 PDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEV-ADRIITIEEGR 565
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGK 209
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
370-562 |
2.88e-14 |
|
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: 72.83 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSF-----CAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLS-------AFTLGSLREkvILLDQTP 437
Cdd:cd03237 10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikADYEGTVRD--LLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 438 YLFNDtiganiAFARPEAseeairtaAHQAGLDPLLER-LPQglatpagerglaLSAGERQRIALARVLLRRPDVLILDE 516
Cdd:cd03237 88 DFYTH------PYFKTEI--------AKPLQIEQILDReVPE------------LSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1730203856 517 PTSALDPKTERHIAQTLRQVL--PEATIIAITHRPALAE-VADRIITIE 562
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAenNEKTAFVVEHDIIMIDyLADRLIVFE 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
365-535 |
4.56e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRyLDPDAGRILFDQAPLSAFT---LGSLREKVILLDQTPY-LF 440
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLR-LINSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPNsSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 441 N------DTIGANIAFARPEAS----EEAIRTAAHQAGLDPLL-ERLPQglatpagerglALSAGERQRIALARVLLRRP 509
Cdd:PRK15134 376 NprlnvlQIIEEGLRVHQPTLSaaqrEQQVIAVMEEVGLDPETrHRYPA-----------EFSGGQRQRIAIARALILKP 444
|
170 180
....*....|....*....|....*.
gi 1730203856 510 DVLILDEPTSALDPKTERHIAQTLRQ 535
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKS 470
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
370-565 |
5.08e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.73 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAF-----TLGSLREKVILLDQTP--YLFND 442
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikEVKRLRKEIGLVFQFPeyQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 TIGANIAFArP----EASEEAIRTAahqagldPLLERLPQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPT 518
Cdd:PRK13645 107 TIEKDIAFG-PvnlgENKQEAYKKV-------PELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 519 SALDPKTERHIAQTLRQVLPE--ATIIAITHR-PALAEVADRIITIEEGR 565
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEykKRIIMVTHNmDQVLRIADEVIVMHEGK 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
358-523 |
5.90e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGS-LREKVILLDQT 436
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 437 PYLFNDTIGANIAFARPEASEEaIRTAAHQAGLDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDE 516
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDD-LSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
....*..
gi 1730203856 517 PTSALDP 523
Cdd:PRK10895 164 PFAGVDP 170
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
42-312 |
6.81e-14 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 72.26 E-value: 6.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 42 LLVSLISTALNLAQPYLSKMLID------NALLPRDMGALVAIGLAMIGVTIGNYALNILasYRYISTSAdmLFDIRVAL 115
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNaltlakVKDLESAVTLILLYALLRFSSKLLKELRSLL--YRRVQQNA--YRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 116 LRHLQTLSPRFYSRFRLGDLMSRINSDVSdiqrvTADTMLSVLSNLLMLT----GGVAIMLWLDWKLFLLAIVLLpaCVG 191
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVVRIMDRGTE-----SANTLLSYLVFYLVPTllelIVVSVVFAFHFGAWLALIVFL--SVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 192 LFVVFQRKLD----RLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPG 267
Cdd:cd18560 151 LYGVFTIKVTewrtKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQ 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1730203856 268 TLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVL 312
Cdd:cd18560 231 LIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFL 275
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
354-566 |
7.25e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAV--LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTlgslREKVI 431
Cdd:PRK10261 14 AVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS----RQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 432 LLDQTPYLFNDTIGANIA--FARPEAS-----------EEAIRTAAHQAGLDPLLE--RLPQGLATPAGERGLA-----L 491
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAmiFQEPMTSlnpvftvgeqiAESIRLHQGASREEAMVEakRMLDQVRIPEAQTILSryphqL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 492 SAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEAT--IIAITH-RPALAEVADRIITIEEGRA 566
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHdMGVVAEIADRVLVMYQGEA 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
358-525 |
1.10e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRI---------LFDQaplsaftlgsLRE 428
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevaYFDQ----------HRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 429 KvilLDqtPylfNDTIGANIAfarpEASEEAIRTAAHQAGLDPLLERL--PQGLATPAGerglALSAGERQRIALARVLL 506
Cdd:PRK11147 393 E---LD--P---EKTVMDNLA----EGKQEVMVNGRPRHVLGYLQDFLfhPKRAMTPVK----ALSGGERNRLLLARLFL 456
|
170
....*....|....*....
gi 1730203856 507 RRPDVLILDEPTSALDPKT 525
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVET 475
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
360-565 |
1.51e-13 |
|
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: 73.18 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 360 VALAHDGRA--VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDA----GRILFDQAPLSAFTLGSLRE----K 429
Cdd:COG4172 14 VAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGLSERELRRirgnR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 VILLDQTPY-----LFndTIGANIAfarpeaseEAI-------RTAAHQAGLDpLLERLpqGLATPagERGLA-----LS 492
Cdd:COG4172 94 IAMIFQEPMtslnpLH--TIGKQIA--------EVLrlhrglsGAAARARALE-LLERV--GIPDP--ERRLDayphqLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 493 AGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPAL-AEVADRIITIEEGR 565
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElgMALLLITHDLGVvRRFADRVAVMRQGE 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
351-522 |
1.90e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 351 LSEAIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAplsaFTLGSLREKv 430
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----LRIGYVPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 431 ILLDQTPYLfndTIGAniaFARpeaseeaIRTAAHQAGLDPLLERLPQG--LATPAGErglaLSAGERQRIALARVLLRR 508
Cdd:PRK09544 76 LYLDTTLPL---TVNR---FLR-------LRPGTKKEDILPALKRVQAGhlIDAPMQK----LSGGETQRVLLARALLNR 138
|
170
....*....|....
gi 1730203856 509 PDVLILDEPTSALD 522
Cdd:PRK09544 139 PQLLVLDEPTQGVD 152
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
168-329 |
2.33e-13 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 70.93 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 168 VAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSA 247
Cdd:cd18587 132 LAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 248 FVEAMLRMQVASFMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLA 327
Cdd:cd18587 212 LARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALK 291
|
..
gi 1730203856 328 RI 329
Cdd:cd18587 292 SL 293
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
107-300 |
2.66e-13 |
|
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: 70.59 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 107 MLFDIRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQ----RVtadtMLSVLSNLLMLTGGVAIMLWLDWKL-FLL 181
Cdd:cd18585 66 LLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDnlylRV----LSPPVVALLVILATILFLAFFSPALaLIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 182 AIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFM 261
Cdd:cd18585 142 LAGLLLAGVVIPLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGL 221
|
170 180 190
....*....|....*....|....*....|....*....
gi 1730203856 262 AGAVPGTLLAVTTSGVILYGGYQIIEGTMSiGTLVAFMA 300
Cdd:cd18585 222 SQALMILLSGLTVWLVLWLGAPLVQNGALD-GALLAMLV 259
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
375-565 |
2.68e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.44 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 375 LEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRI------LFDQaplsaftlgslrEKVILLdqTP------YLFND 442
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDA------------EKGICL--PPekrrigYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 -------TIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPqglatpagergLALSAGERQRIALARVLLRRPDVLILD 515
Cdd:PRK11144 85 arlfphyKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 516 EPTSALD--------PKTERhIAQTLRqvLPeatIIAITHrpALAEV---ADRIITIEEGR 565
Cdd:PRK11144 154 EPLASLDlprkrellPYLER-LAREIN--IP---ILYVSH--SLDEIlrlADRVVVLEQGK 206
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
365-561 |
2.78e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAftlgsLREKviLLDQTPYL----- 439
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDE--YHQDLLYLghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 440 FNDTIGA--NIAFARP---EASEEAIRTAAHQAGLDPLlERLPQGlatpagerglALSAGERQRIALARVLLRRPDVLIL 514
Cdd:PRK13538 85 IKTELTAleNLRFYQRlhgPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 515 DEPTSALDPKT----ERHIAQTLRQvlpEATIIAITHRPaLAEVADRIITI 561
Cdd:PRK13538 154 DEPFTAIDKQGvarlEALLAQHAEQ---GGMVILTTHQD-LPVASDKVRKL 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
366-565 |
3.71e-13 |
|
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: 67.84 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 366 GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGslrekvilldqtpylfnDTIG 445
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR-----------------DAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 446 ANIAFArPEaseeairtaahqagldpllERLPQGLATPAGER-----GLALSAGERQRIALARVLLRRPDVLILDEPTSA 520
Cdd:cd03215 75 AGIAYV-PE-------------------DRKREGLVLDLSVAenialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1730203856 521 LDPKTERHIAQTLRQVLPE--ATIIAITHRPALAEVADRIITIEEGR 565
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAgkAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
370-571 |
5.43e-13 |
|
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: 71.74 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSF-----CAVLGPSGVGKSTLADLLVRYLDPDAGrilfdqaplsaftlgSLREKVILLDQTPYLFNDTI 444
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEG---------------EVDEDLKISYKPQYISPDYD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 445 GANIAFARpEASEEAIRTAAHQA------GLDPLLERlpqglatPAGErglaLSAGERQRIALARVLLRRPDVLILDEPT 518
Cdd:COG1245 416 GTVEEFLR-SANTDDFGSSYYKTeiikplGLEKLLDK-------NVKD----LSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 519 SALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAE-VADRIITIE-----EGRAH----MRTA 571
Cdd:COG1245 484 AHLDVEQRLAVAKAIRRFAENrgKTAMVVDHDIYLIDyISDRLMVFEgepgvHGHASgpmdMREG 548
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
370-559 |
7.61e-13 |
|
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: 68.80 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLA-DLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTP----------- 437
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLInDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 438 Y--LFnDTI-----------------------GANIA-------------FARPEASEEAIRTAaHQAGLDPLleRLPQG 479
Cdd:cd03271 91 YtgVF-DEIrelfcevckgkrynretlevrykGKSIAdvldmtveealefFENIPKIARKLQTL-CDVGLGYI--KLGQP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 480 LATpagerglaLSAGERQRIALARVLLRR---PDVLILDEPTSALDPKTERHIAQTLrQVLPEA--TIIAITHRPALAEV 554
Cdd:cd03271 167 ATT--------LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVL-QRLVDKgnTVVVIEHNLDVIKC 237
|
....*
gi 1730203856 555 ADRII 559
Cdd:cd03271 238 ADWII 242
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
346-565 |
7.66e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.97 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 346 RAFPGLSEAIRFEDVALAHD--GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAfTL 423
Cdd:TIGR01257 920 RELPGLVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NL 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 424 GSLREKVILLDQTPYLFND-TIGANIAF---ARPEASEEAirtaahQAGLDPLLErlPQGLATPAGERGLALSAGERQRI 499
Cdd:TIGR01257 999 DAVRQSLGMCPQHNILFHHlTVAEHILFyaqLKGRSWEEA------QLEMEAMLE--DTGLHHKRNEEAQDLSGGMQRKL 1070
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 500 ALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEV-ADRIITIEEGR 565
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGR 1137
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
366-523 |
1.04e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.13 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 366 GRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAF------TLGslrekVILLDQTPYL 439
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkraRLG-----IGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 440 FND-TIGANIA----FARPEASEEAIRtaahqagLDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLIL 514
Cdd:COG1137 90 FRKlTVEDNILavleLRKLSKKEREER-------LEELLEEF--GITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
....*....
gi 1730203856 515 DEPTSALDP 523
Cdd:COG1137 161 DEPFAGVDP 169
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
126-312 |
1.16e-12 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 68.90 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 126 FYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLTR 205
Cdd:cd18590 86 FFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 206 TMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFrarnSAFVEAMLRMQVASFMAGAVPGTLLAVTTSGV----ILYG 281
Cdd:cd18590 166 AVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRY----SEALERTYNLKDRRDTVRAVYLLVRRVLQLGVqvlmLYCG 241
|
170 180 190
....*....|....*....|....*....|.
gi 1730203856 282 GYQIIEGTMSIGTLVAFMAYQSRLFSPIQVL 312
Cdd:cd18590 242 RQLIQSGHLTTGSLVSFILYQKNLGSYVRTL 272
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
373-547 |
1.45e-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: 67.78 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 373 FTLEIPR-GSFCAVLGPSGVGKSTLADLLVRYLDPDAGRilFDQAP-----LSAFTLGSLRE--------------KVIL 432
Cdd:cd03236 18 HRLPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRGSELQNyftkllegdvkvivKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFNDTIGANIafarpEASEE--AIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPD 510
Cdd:cd03236 96 VDLIPKAVKGKVGELL-----KKKDErgKLDELVDQLELRHVLDRNID-----------QLSGGELQRVAIAAALARDAD 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1730203856 511 VLILDEPTSALDPKTERHIAQTLRQVL-PEATIIAITH 547
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAeDDNYVLVVEH 197
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
126-313 |
1.59e-12 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 68.27 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 126 FYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLTR 205
Cdd:cd18589 86 FFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 206 TMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARnsafVEAMLRMQ-------VASFMAGAVPGTLLAVttsGVI 278
Cdd:cd18589 166 QVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQR----LQKTYRLNkkeaaayAVSMWTSSFSGLALKV---GIL 238
|
170 180 190
....*....|....*....|....*....|....*
gi 1730203856 279 LYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLM 313
Cdd:cd18589 239 YYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLL 273
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
38-329 |
2.29e-12 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 67.85 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASY--RYIST--SADMLFDIRV 113
Cdd:cd18571 4 ILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWilLHISSriNISIISDFLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 114 ALLRhlqtLSPRFYSRFRLGDLMSRINsDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLF 193
Cdd:cd18571 84 KLMR----LPISFFDTKMTGDILQRIN-DHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYILWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 194 VVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAH---ETERFRARNSAFVEAMLRM-QVASfmAGAVpgTL 269
Cdd:cd18571 159 LLFLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQkrwEWERIQAKLFKINIKSLKLdQYQQ--IGAL--FI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 270 LAVTTSGVILYGGYQIIEGTMSIGTLVA--FMAYQsrLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18571 235 NQLKNILITFLAAKLVIDGEITLGMMLAiqYIIGQ--LNSPIEQLIGFIQSLQDAKISLERL 294
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
372-565 |
3.59e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.55 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 372 GFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSL-REKVILLDQTPYLFND-TIGANI- 448
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFREmTVIENLl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 449 -------------------AFARPEAseEAIRTAAH---QAGLDPLLERlpqglatPAGErglaLSAGERQRIALARVLL 506
Cdd:PRK11300 103 vaqhqqlktglfsgllktpAFRRAES--EALDRAATwleRVGLLEHANR-------QAGN----LAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 507 RRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIITIEEGR 565
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLVmGISDRIYVVNQGT 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
355-565 |
6.03e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVAlAHDGR-AVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAF-TLGSLREKVIL 432
Cdd:PRK11614 6 LSFDKVS-AHYGKiQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFND-TIGANIA----FARPEASEEAIRTAAhqaGLDP-LLERLPQglatpageRGLALSAGERQRIALARVLL 506
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAmggfFAERDQFQERIKWVY---ELFPrLHERRIQ--------RAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 507 RRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPA--LAEVADRIITIEEGR 565
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGH 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
367-566 |
6.53e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 367 RAVlKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF---DQAPLSAFTLGSLREKVILLDQTPYL-FND 442
Cdd:PRK15079 35 KAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDPLAsLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 --TIGANIA----FARPEAS----EEAIRTAAHQAGLDP-LLERLPQglatpagerglALSAGERQRIALARVLLRRPDV 511
Cdd:PRK15079 114 rmTIGEIIAeplrTYHPKLSrqevKDRVKAMMLKVGLLPnLINRYPH-----------EFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 512 LILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALAE-VADRIITIEEGRA 566
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKhISDRVLVMYLGHA 240
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
354-566 |
1.80e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.02 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRA-VLKGFTLEIPRGSFCAVLGPSGVGKSTLAdllvryldpdagRILfdqAPLSAFTLGSLR--EKV 430
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLL------------RMV---AGLERITSGEIWigGRV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 431 IlldqtpylfND---------------------TIGANIA-------FARPEAsEEAIRTAAHQAGLDPLLERLPQglat 482
Cdd:PRK11650 68 V---------NElepadrdiamvfqnyalyphmSVRENMAyglkirgMPKAEI-EERVAEAARILELEPLLDRKPR---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 483 pagerglALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHI---AQTLRQVLpEATIIAITHRPALA-EVADRI 558
Cdd:PRK11650 134 -------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMrleIQRLHRRL-KTTSLYVTHDQVEAmTLADRV 205
|
....*...
gi 1730203856 559 ITIEEGRA 566
Cdd:PRK11650 206 VVMNGGVA 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
373-577 |
2.05e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 373 FTLEiPRGSFcAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLS--AFTLGSLREKVILLDQTPYLF-NDTIGANIA 449
Cdd:PRK15112 34 FTLR-EGQTL-AIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDPSTSLNpRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 450 FA-------RPEASEEAIRTAAHQAGLdpllerlpqgLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALD 522
Cdd:PRK15112 112 FPlrlntdlEPEQREKQIIETLRQVGL----------LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 523 PKTERHIAQTLRQVLPEATI--IAIT-HRPALAEVADRIITIEEGRAHMR--TAASLA-PL 577
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGIsyIYVTqHLGMMKHISDQVLVMHQGEVVERgsTADVLAsPL 242
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
375-559 |
2.83e-11 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 63.33 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 375 LEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSA--FTLGSLREK-------VILLDQTpyLFNDTIG 445
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKgwRHIGYVPQRhefawdfPISVAHT--VMSGRTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 446 ANIAFARP-EASEEAIRTAAHQAGLDPLLERlpqglatPAGErglaLSAGERQRIALARVLLRRPDVLILDEPTSALDPK 524
Cdd:TIGR03771 79 HIGWLRRPcVADFAAVRDALRRVGLTELADR-------PVGE----LSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1730203856 525 TERHIAQTLRQVLPEA-TIIAITHR-PALAEVADRII 559
Cdd:TIGR03771 148 TQELLTELFIELAGAGtAILMTTHDlAQAMATCDRVV 184
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
352-547 |
3.32e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 352 SEAIRFEDVALAH-DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAftlgSLREKV 430
Cdd:PRK15056 4 QAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 431 I-LLDQT-------PYLFNDTI-----GANIAFARPEASEEAIRTAAhQAGLDPLLERLPQglatpAGErglaLSAGERQ 497
Cdd:PRK15056 80 VaYVPQSeevdwsfPVLVEDVVmmgryGHMGWLRRAKKRDRQIVTAA-LARVDMVEFRHRQ-----IGE----LSGGQKK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 498 RIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITH 547
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGkTMLVSTH 200
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
97-312 |
3.82e-11 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 64.09 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 97 SYRYISTSAdmlfdirvalLRHLQTLSPRFYSRFRLGDLMSRIN--SDVSDIqrvtADTML-SVLSNLLMLTggVAImlW 173
Cdd:cd18583 68 SYRALSTAA----------FNHVMNLSMDFHDSKKSGEVLKAIEqgSSINDL----LEQILfQIVPMIIDLV--IAI--V 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 174 LDWKLFLLAIVLLPACVG-LFVVFQRKLD----RLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAF 248
Cdd:cd18583 130 YLYYLFDPYMGLIVAVVMvLYVWSTIKLTswrtKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNY 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 249 VEAMLRMQVASFMAGAVPGTLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVL 312
Cdd:cd18583 210 QKAERKYLFSLNLLNAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFF 273
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
367-565 |
5.69e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 367 RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPD--AGRILFDQAPLSAFTL---GSLREKVILLdqtPYLfn 441
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILkrtGFVTQDDILY---PHL-- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 442 dTIGANIAFAR----PEASEEAIRTAAHQAGLDPL-LERLPQGLATPAGERGLalSAGERQRIALARVLLRRPDVLILDE 516
Cdd:PLN03211 156 -TVRETLVFCSllrlPKSLTKQEKILVAESVISELgLTKCENTIIGNSFIRGI--SGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 517 PTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPA--LAEVADRIITIEEGR 565
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGkTIVTSMHQPSsrVYQMFDSVLVLSEGR 284
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
373-531 |
5.89e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.03 E-value: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 373 FTLEIPRGSFCAVLGPSGVGKSTL----ADLLvryldPDAGRILFDQAPLSAFTLGSL-REKVILLDQTPYLFNDTIGAN 447
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLlarmAGLL-----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 448 IAFARP-----EASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLR-RPDV------LILD 515
Cdd:PRK03695 90 LTLHQPdktrtEAVASALNEVAEALGLDDKLGRSVN-----------QLSGGEWQRVRLAAVVLQvWPDInpagqlLLLD 158
|
170
....*....|....*.
gi 1730203856 516 EPTSALDpkterhIAQ 531
Cdd:PRK03695 159 EPMNSLD------VAQ 168
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
370-561 |
1.22e-10 |
|
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: 60.41 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLadlLVRYLDPDAGRILFDQAPLSAftlgslREKVILLDQTPYLFNdtigania 449
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---VNEGLYASGKARLISFLPKFS------RNKLIFIDQLQFLID-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 450 farpeaseeairtaahqAGLDPLleRLPQGLATpagerglaLSAGERQRIALARVLLRRPD--VLILDEPTSALDPKTER 527
Cdd:cd03238 74 -----------------VGLGYL--TLGQKLST--------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*
gi 1730203856 528 HIAQTLRQVLPEA-TIIAITHRPALAEVADRIITI 561
Cdd:cd03238 127 QLLEVIKGLIDLGnTVILIEHNLDVLSSADWIIDF 161
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
370-565 |
1.46e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.91 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPD---AGRILFDQAPL--------SAFT------LGSL--REKV 430
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIdakemraiSAYVqqddlfIPTLtvREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 431 IlldqtpylfndtIGANIAFARPEASEEairtaaHQAGLDPLLERLpqGLATPA------GERGLALSAGERQRIALARV 504
Cdd:TIGR00955 121 M------------FQAHLRMPRRVTKKE------KRERVDEVLQAL--GLRKCAntrigvPGRVKGLSGGERKRLAFASE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 505 LLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAIT-HRPA--LAEVADRIITIEEGR 565
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSseLFELFDKIILMAEGR 244
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
370-565 |
1.48e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.83 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLAdLLVRYLDPDAGRILFDQAPLSA------FTLGSLR------EKVILLDQTP 437
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCAnrralrRTIG*HRpvr*grRESFSGRENL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 438 YLfndtIGANIAFARPEASEEAirtaahqaglDPLLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:NF000106 108 YM----IGR*LDLSRKDARARA----------DELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 518 TSALDPKTERHIAQTLRQVLPE-ATIIAITHRPALAE-VADRIITIEEGR 565
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEqLAHELTVIDRGR 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
354-566 |
1.76e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDG--RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPD-----AGRILFDQAPL---SAFTL 423
Cdd:PRK15134 7 AIENLSVAFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLlhaSEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 424 GSLR-EKVILLDQTPYL-FNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLpqGLATPAGErgLA-----LSAGER 496
Cdd:PRK15134 87 RGVRgNKIAMIFQEPMVsLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRV--GIRQAAKR--LTdyphqLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 497 QRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALA-EVADRIITIEEGRA 566
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVrKLADRVAVMQNGRC 235
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
65-324 |
1.91e-10 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 62.18 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 65 NALLPRDMGALVAIGLAMIGVTIGNY-------ALNILASY--------RYIST----SADMLFDIRVALLRHLQTLSPR 125
Cdd:cd18574 12 NIQIPLLLGDLVNVISRSLKETNGDFiedlkkpALKLLGLYllqslltfAYISLlsvvGERVAARLRNDLFSSLLRQDIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 126 FYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLTR 205
Cdd:cd18574 92 FFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 206 TMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRA--RNSAFVEAMLRMQVASFMAG---AVPGTLLavttsGVILY 280
Cdd:cd18574 172 RAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEevEKAAKLNEKLGLGIGIFQGLsnlALNGIVL-----GVLYY 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1730203856 281 GGYQIIEGTMSIGTLVAFM-AYQS--RLFSPIQVLMG-LVSGLSS-ARV 324
Cdd:cd18574 247 GGSLVSRGELTAGDLMSFLvATQTiqRSLAQLSVLFGqYVKGKSAgARV 295
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
373-547 |
2.07e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 373 FTLEIPR-GSFCAVLGPSGVGKSTLADLLVRYLDPDAGRilFDQAP-----LSAFTlGS--------LRE---KVIL--- 432
Cdd:PRK13409 91 YGLPIPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPswdevLKRFR-GTelqnyfkkLYNgeiKVVHkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 -LDQTPYLFNDTIGaniafarpeaseEAIRTAAHQAGLDPLLERLpqGLaTPAGERGL-ALSAGERQRIALARVLLRRPD 510
Cdd:PRK13409 168 yVDLIPKVFKGKVR------------ELLKKVDERGKLDEVVERL--GL-ENILDRDIsELSGGELQRVAIAAALLRDAD 232
|
170 180 190
....*....|....*....|....*....|....*...
gi 1730203856 511 VLILDEPTSALDPKtER-HIAQTLRQVLPEATIIAITH 547
Cdd:PRK13409 233 FYFFDEPTSYLDIR-QRlNVARLIRELAEGKYVLVVEH 269
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
355-576 |
3.62e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDA--------GRILFDQAPLSAFTLGSL 426
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 427 -REKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGL-DPLLERlpQGLATPAGERGLALSAGERQRIALARV 504
Cdd:PRK13547 82 aRLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIaWQALAL--AGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 505 L---------LRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATI--IAITHRPAL-AEVADRIITIEEGR--AHMRT 570
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNLaARHADRIAMLADGAivAHGAP 239
|
....*.
gi 1730203856 571 AASLAP 576
Cdd:PRK13547 240 ADVLTP 245
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
38-328 |
6.30e-10 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 60.73 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNAL--LPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVAL 115
Cdd:cd18556 4 FFSILFISLLSSILISISPVILAKITDLLTssSSDSYNYIVVLAALYVITISATKLLGFLSLYLQSSLRVELIISISSSY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 116 LRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLW-LDWklFLLAIVLLPAcvGLFV 194
Cdd:cd18556 84 FRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSsGDY--FVAALFLLYA--VLFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 195 V----FQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRA-----RNS--AFVEAMLRMQVASfmag 263
Cdd:cd18556 160 InntiFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEAtltndRNSqkRYWKLTFKMLILN---- 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 264 avpgTLLAVTTSGVI-LYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLAR 328
Cdd:cd18556 236 ----SLLNVILFGLSfFYSLYGVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSVHSLAG 297
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
380-565 |
7.52e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 380 GSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQA---PLSAFTLGSLREKVILLDQTPYLFND---TIGANIAfaRP 453
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYASLDprqTVGDSIM--EP 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 454 EASEEAIRTAAHQAGLDPLLERLpqGLATPAGER-GLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQT 532
Cdd:PRK10261 428 LRVHGLLPGKAAAARVAWLLERV--GLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINL 505
|
170 180 190
....*....|....*....|....*....|....*.
gi 1730203856 533 LRQVLPEATI--IAITHRPALAE-VADRIITIEEGR 565
Cdd:PRK10261 506 LLDLQRDFGIayLFISHDMAVVErISHRVAVMYLGQ 541
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
369-568 |
7.84e-10 |
|
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: 59.08 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRIlfdqaplsaftlgSLREKVILLdqtpylfndtIGANI 448
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-------------TVRGRVSSL----------LGLGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 449 AFaRPEAS-EEAIRTAAHQAGLDP-----LLER------LPQGLATPAGErglaLSAGERQRIALARVLLRRPDVLILDE 516
Cdd:cd03220 94 GF-NPELTgRENIYLNGRLLGLSRkeideKIDEiiefseLGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 517 PTSALDP----KTERHIAQTLRQvlpEATIIAITHRP-ALAEVADRIITIEEGRAHM 568
Cdd:cd03220 169 VLAVGDAafqeKCQRRLRELLKQ---GKTVILVSHDPsSIKRLCDRALVLEKGKIRF 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
355-567 |
9.81e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF---------DQAplsaftlgs 425
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvDQS--------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 426 lREKvilLDQTPYLF------NDTI--GANIAFARPEASEEAIRTAAHQagldpllerlpqglaTPAGErglaLSAGERQ 497
Cdd:TIGR03719 394 -RDA---LDPNKTVWeeisggLDIIklGKREIPSRAYVGRFNFKGSDQQ---------------KKVGQ----LSGGERN 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 498 RIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLrQVLPEATIIaITH-RPALAEVADRIITIeEGRAH 567
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL-LNFAGCAVV-ISHdRWFLDRIATHILAF-EGDSH 518
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
354-565 |
1.08e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRI---------LFDQAPLSAFtlg 424
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigYYAQDHAYDF--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 425 slrekvillDQTPYLFnDTIGaniAFARPEASEEAIRTAahqagldplLERLPQGlATPAGERGLALSAGERQRIALARV 504
Cdd:PRK15064 396 ---------ENDLTLF-DWMS---QWRQEGDDEQAVRGT---------LGRLLFS-QDDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 505 LLRRPDVLILDEPTSALDPKTERHIAQTLRQVlpEATIIAITH-RPALAEVADRIITIEEGR 565
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EGTLIFVSHdREFVSSLATRIIEITPDG 512
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
355-564 |
1.28e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFT--------LGSL 426
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklaaqlgIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 427 REKVILLDQTPYLFNDTIG---------ANI---AFARPEASEeairtaahqagldpLLERLpqGLATPAGERGLALSAG 494
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGrhltkkvcgVNIidwREMRVRAAM--------------MLLRV--GLKVDLDEKVANLSIS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 495 ERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEAT-IIAITHRPA-LAEVADRIITIEEG 564
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAeIRRICDRYTVMKDG 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
379-565 |
1.36e-09 |
|
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: 60.61 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 379 RGSFCAVLGPSGVGKSTLADLLV-RYLDPDAGRILFDQAPLSAFT-LGSLREKVILLDQ-------TPYLfndTIGANIA 449
Cdd:TIGR02633 285 RGEILGVAGLVGAGRTELVQALFgAYPGKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEdrkrhgiVPIL---GVGKNIT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 450 FA--RPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGlALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTER 527
Cdd:TIGR02633 362 LSvlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKY 440
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1730203856 528 HIAQTLRQVLPE--ATIIAITHRPALAEVADRIITIEEGR 565
Cdd:TIGR02633 441 EIYKLINQLAQEgvAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
482-565 |
1.86e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 482 TPAGER--GLaLSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHR-PALAEVADR 557
Cdd:PRK10762 386 TPSMEQaiGL-LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGlSIILVSSEmPEVLGMSDR 464
|
....*...
gi 1730203856 558 IITIEEGR 565
Cdd:PRK10762 465 ILVMHEGR 472
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
354-523 |
2.19e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 354 AIRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLL----------VRYLDPD----------AGRIlf 413
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagarkiqqgrVEVLGGDmadarhrravCPRI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 414 dqaplsAF-----------TLgSLREkvilldqtpylfndtigaNIAF-AR---PEASEEAIRTAA--HQAGLDPLLERl 476
Cdd:NF033858 79 ------AYmpqglgknlypTL-SVFE------------------NLDFfGRlfgQDAAERRRRIDEllRATGLAPFADR- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1730203856 477 pqglatPAGErglaLSAGERQRIALARVLLRRPDVLILDEPTSALDP 523
Cdd:NF033858 133 ------PAGK----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
43-312 |
2.27e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC 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. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. 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: 350005 [Multi-domain] Cd Length: 289 Bit Score: 58.83 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 43 LVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDIRVALLRHLQTL 122
Cdd:cd18561 3 LLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 123 SPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWklflLAIVLLPACVGLFVVFQRKLDR 202
Cdd:cd18561 83 GPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDP----LVALILLVFALLIPLSPALWDR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 203 LtrtMRERG-------SDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTLLAVTTS 275
Cdd:cd18561 159 L---AKDTGrrhwaayGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTA 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 1730203856 276 GVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVL 312
Cdd:cd18561 236 LALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDL 272
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-565 |
2.56e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.95 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 349 PGLSEAIR------FEDValahdgRAVlKGFTLEIPRGSFCAVLGPSGVGKST----LADLLVryldPDAGRILFdqapl 418
Cdd:COG4586 18 PGLKGALKglfrreYREV------EAV-DDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILV----PTSGEVRV----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 419 saftlgslrekvilLDQTPYLfndtigANIAFAR-----------------PEASEEAIR------TAAHQAGLDPLLER 475
Cdd:COG4586 82 --------------LGYVPFK------RRKEFARrigvvfgqrsqlwwdlpAIDSFRLLKaiyripDAEYKKRLDELVEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 476 LPQG--LATPAGErglaLSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPA- 550
Cdd:COG4586 142 LDLGelLDTPVRQ----LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErgTTILLTSHDMDd 217
|
250
....*....|....*
gi 1730203856 551 LAEVADRIITIEEGR 565
Cdd:COG4586 218 IEALCDRVIVIDHGR 232
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
387-562 |
3.67e-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: 56.85 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 387 GPSGVGKSTLADLLVRYLDPDAGRILFDQAPL-SAFTLGSLREKVILLdqtpylFNDTIGANIAFAR-PEASEEAIRTaa 464
Cdd:cd03240 29 GQNGAGKTTIIEALKYALTGELPPNSKGGAHDpKLIREGEVRAQVKLA------FENANGKKYTITRsLAILENVIFC-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 465 HQAGLDPLLERlpqglatpagERGlALSAGERQ------RIALARVLLRRPDVLILDEPTSALDpktERHIAQTLRQVLP 538
Cdd:cd03240 101 HQGESNWPLLD----------MRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIE 166
|
170 180 190
....*....|....*....|....*....|
gi 1730203856 539 EAT------IIAITHRPALAEVADRIITIE 562
Cdd:cd03240 167 ERKsqknfqLIVITHDEELVDAADHIYRVE 196
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
358-565 |
4.85e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILF---DQAPLSAFTLGSLREKviLLD 434
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERR--RLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLF-----------NDTIGANIAfARPEASEE----AIRTAAHQagldpLLERLPQGLA----TPAgerglALSAGE 495
Cdd:PRK11701 88 RTEWGFvhqhprdglrmQVSAGGNIG-ERLMAVGArhygDIRATAGD-----WLERVEIDAAriddLPT-----TFSGGM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 496 RQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE---ATIIaITHRPALAEV-ADRIITIEEGR 565
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElglAVVI-VTHDLAVARLlAHRLLVMKQGR 229
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
379-559 |
4.85e-09 |
|
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: 55.46 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 379 RGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVILldqtpylfndtiganiafarpeasee 458
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 459 airtaahqagldpllerlpqglatpaGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVL- 537
Cdd:smart00382 55 --------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLl 108
|
170 180 190
....*....|....*....|....*....|....
gi 1730203856 538 ------PEATIIAITHRP------ALAEVADRII 559
Cdd:smart00382 109 lllkseKNLTVILTTNDEkdlgpaLLRRRFDRRI 142
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
369-568 |
7.01e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.63 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 369 VLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQ--APLSAFTLG-----SLREKVIL--------L 433
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvSALLELGAGfhpelTGRENIYLngrllglsR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTPYLFNDtIganIAFarpeaseeairtaahqAGLDPLLErlpqglaTPAGerglALSAGERQRIALARVLLRRPDVLI 513
Cdd:COG1134 121 KEIDEKFDE-I---VEF----------------AELGDFID-------QPVK----TYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 514 LDEPTSALDP----KTERHIAQTLRQvlpEATIIAITH-RPALAEVADRIITIEEGRAHM 568
Cdd:COG1134 170 VDEVLAVGDAafqkKCLARIRELRES---GRTVIFVSHsMGAVRRLCDRAIWLEKGRLVM 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
349-566 |
7.59e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 349 PGLSeAIRFEDVALAHDGRAVL-KGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRIlFDQAPLSAFTLGSLR 427
Cdd:PLN03073 504 PGPP-IISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRMAVFSQHH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 428 EKVILLDQTPYLFndtiganIAFARPEASEEAIRTAAHQAGLDPLLERLPQglatpagergLALSAGERQRIALARVLLR 507
Cdd:PLN03073 582 VDGLDLSSNPLLY-------MMRCFPGVPEQKLRAHLGSFGVTGNLALQPM----------YTLSGGQKSRVAFAKITFK 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 508 RPDVLILDEPTSALDPKTERHIAQTLrqVLPEATIIAITHRPAL-AEVADRIITIEEGRA 566
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLiSGSVDELWVVSEGKV 702
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
42-308 |
7.81e-09 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 57.26 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 42 LLVSLISTALNLAQPYLSKMLIDnALLPRDMGALVAIGLAMIGVTIGNYAL-----------NILASYRYISTSADMLFD 110
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVD-SLTPDSADSPLAFPWALILLYVFLKFLqgggsgsvgllSNLRSFLWIPVQQFTTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 111 IRVALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQrvtadtmlSVLSNLLMLTG------GVAIMLWLDWKLFLLAIV 184
Cdd:cd18581 81 ISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSIN--------SLLSYVLFNIGptiadiIIAIIYFAIAFNPWFGLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 185 LLpACVGLFVV-----------FQRKLDRLTRTMRERGsdlgsllVDTIMGMRVVSSLNAAAHETERFRarnsafvEAML 253
Cdd:cd18581 153 VF-VTMALYLIltiiitewrtkFRREMNKLDNEKRAKA-------VDSLLNFETVKYYNAERFEVERYR-------RAID 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 254 RMQVASFMAGAVPgTLLAVTTSGVI--------LYGGYQIIEGTMSIGTLVAFMAYQSRLFSP 308
Cdd:cd18581 218 DYQVAEWKSNASL-NLLNTAQNLIItigllagsLLCAYFVVEGKLTVGDFVLFLTYIIQLYAP 279
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
355-542 |
1.52e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRI-LFDQAPLSAFTLGSLreKVILL 433
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQL--EFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 434 DQTPYlfndtigANIAFARPEASEEAIRTAAHQAGLdpllerlpQG-LATPAGERglaLSAGERQRIALARVLLRRPDVL 512
Cdd:PRK10636 391 DESPL-------QHLARLAPQELEQKLRDYLGGFGF--------QGdKVTEETRR---FSGGEKARLVLALIVWQRPNLL 452
|
170 180 190
....*....|....*....|....*....|
gi 1730203856 513 ILDEPTSALDpkterhiaQTLRQVLPEATI 542
Cdd:PRK10636 453 LLDEPTNHLD--------LDMRQALTEALI 474
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
492-565 |
1.78e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.27 E-value: 1.78e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 492 SAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRpaLAEVA---DRIITIEEGR 565
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHD--LGVVAgicDKVLVMYAGR 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
359-564 |
2.04e-08 |
|
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: 54.56 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 359 DVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLvryldpdAGRilfdqaplsafTLGSLREKVILLD--QT 436
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-------AGR-----------KTAGVITGEILINgrPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 437 PYLFNDTIGaniaFAR------PEAS-EEAIRTAAhqagldpLLerlpqglatpageRGLalSAGERQRIALARVLLRRP 509
Cdd:cd03232 74 DKNFQRSTG----YVEqqdvhsPNLTvREALRFSA-------LL-------------RGL--SVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 510 DVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRP--ALAEVADRIITIEEG 564
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGqAILCTIHQPsaSIFEKFDRLLLLKRG 185
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
365-579 |
2.19e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYldPD----AGRILFDQAPLSAFT------LGslrekVILLD 434
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEpeerahLG-----IFLAF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 435 QTPYLFNDTigANIAFARpeASEEAIRTAAHQAGLDPL------LERLPQ-GLATPAGERGL--ALSAGERQRIALARVL 505
Cdd:CHL00131 91 QYPIEIPGV--SNADFLR--LAYNSKRKFQGLPELDPLefleiiNEKLKLvGMDPSFLSRNVneGFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 506 LRRPDVLILDEPTSALDPKTERHIAQTLRQVL-PEATIIAITHRPALAE--VADRIITIEEGRAHMRTAASLAPLVE 579
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQRLLDyiKPDYVHVMQNGKIIKTGDAELAKELE 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
375-523 |
3.46e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 375 LEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRI-LFDQaPLSAFTLgSLREKVILLDQTPYLFND-TIGANIAF-A 451
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFGQ-PVDAGDI-ATRRRVGYMSQAFSLYGElTVRQNLELhA 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 452 R-----PEASEEAIRTAAHQAGLDPLLERLPQglatpagerglALSAGERQRIALARVLLRRPDVLILDEPTSALDP 523
Cdd:NF033858 365 RlfhlpAAEIAARVAEMLERFDLADVADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
491-561 |
4.02e-08 |
|
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: 52.75 E-value: 4.02e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 491 LSAGERQRIALARVL----LRRPDVLILDEPTSALDPKTERHIAQTL-RQVLPEATIIAITHRPALAEVADRIITI 561
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
364-531 |
5.29e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 364 HDgRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAfTLGSLREKVILLDQ----TPYL 439
Cdd:PRK13540 12 HD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHrsgiNPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 440 fndTIGANIAFArpeaseeaIRTAAHQAGLDPL--LERLPQGLATPAGerglALSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:PRK13540 90 ---TLRENCLYD--------IHFSPGAVGITELcrLFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180
....*....|....*....|..
gi 1730203856 518 TSALD--------PKTERHIAQ 531
Cdd:PRK13540 155 LVALDelslltiiTKIQEHRAK 176
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
370-577 |
5.97e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLS-AFTLGSLREKVILLDQTPYLFND-TIGAN 447
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVPEmTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 448 IAFAR-PEA-----SEEAIRTAAHQagldplLERLPQGL--ATPAGErglaLSAGERQRIALARVLLRRPDVLILDEPTS 519
Cdd:PRK11288 100 LYLGQlPHKggivnRRLLNYEAREQ------LEHLGVDIdpDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 520 ALDPKTERHIAQTLRQVLPEAT-IIAITHRpaLAEV---ADRIITIEEGRaHMRTAASLAPL 577
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEGRvILYVSHR--MEEIfalCDAITVFKDGR-YVATFDDMAQV 228
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
489-562 |
6.99e-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: 6.99e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 489 LALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA--TIIAITHRPALAE-VADRIITIE 562
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkkTALVVEHDLAVLDyLSDRIHVFE 146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
373-547 |
7.39e-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: 55.18 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 373 FTLEIPR-GSFCAVLGPSGVGKSTLADLLVRYLDPDAGRilFDQAP-----LSAFT-------LGSLREKVI-------L 432
Cdd:COG1245 91 YGLPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGD--YDEEPswdevLKRFRgtelqdyFKKLANGEIkvahkpqY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQTPYLFNDTIGaniafarpeaseEAIRTAAHQAGLDPLLERLpqGLaTPAGERGLA-LSAGERQRIALARVLLRRPDV 511
Cdd:COG1245 169 VDLIPKVFKGTVR------------ELLEKVDERGKLDELAEKL--GL-ENILDRDISeLSGGELQRVAIAAALLRDADF 233
|
170 180 190
....*....|....*....|....*....|....*..
gi 1730203856 512 LILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITH 547
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEEGkYVLVVEH 270
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
370-564 |
1.09e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSaFT---------LGSLREKVILLDQTpylf 440
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNgpkssqeagIGIIHQELNLIPQL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 441 ndTIGANIAFAR-PEASEEAIRTAAHQAGLDPLLERL--PQGLATPAGErglaLSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:PRK10762 95 --TIAENIFLGReFVNRFGRIDWKKMYAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 518 TSAL-DPKTErhiaqTLRQVLPE-----ATIIAITHR-PALAEVADRIITIEEG 564
Cdd:PRK10762 169 TDALtDTETE-----SLFRVIRElksqgRGIVYISHRlKEIFEICDDVTVFRDG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
390-565 |
1.30e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.25 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 390 GVGKSTLADLLVRYLDPDAGRILFDQAPLsafTLGSLREKV---------------ILLDQTpylfndtIGANIAFARPE 454
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPV---RIRSPRDAIragiayvpedrkgegLVLDLS-------IRENITLASLD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 455 A-------SEEAIRTAAhqaglDPLLERL---PQGLATPAGErglaLSAGERQRIALARVLLRRPDVLILDEPTSALDPK 524
Cdd:COG1129 358 RlsrggllDRRRERALA-----EEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVG 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 525 TERHIAQTLRQV-------------LPEatiiaithrpaLAEVADRIITIEEGR 565
Cdd:COG1129 429 AKAEIYRLIRELaaegkavivisseLPE-----------LLGLSDRILVMREGR 471
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
355-565 |
1.56e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDgRAVLKGFTLEIPRGSFCAVLGPSGVGKS----TLADLLVRYLDPDAGRILFDQAPLSAftlGSLR-EK 429
Cdd:PRK10418 5 IELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP---CALRgRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 VILLDQTP-YLFN--DTIGAN-----IAFARPeASEEAIRTAAHQAGL-DPllERLPQGLAtpagergLALSAGERQRIA 500
Cdd:PRK10418 81 IATIMQNPrSAFNplHTMHTHaretcLALGKP-ADDATLTAALEAVGLeNA--ARVLKLYP-------FEMSGGMLQRMM 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 501 LARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEAT--IIAITH-RPALAEVADRIITIEEGR 565
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHdMGVVARLADDVAVMSHGR 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
376-580 |
1.60e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.59 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 376 EIPRGSFCAVLGPSGVGKStLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREKVilldqtpylFNDTIGANIA--FARP 453
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKS-VSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE---------RRNLVGAEVAmiFQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 454 EAS-----------EEAIRTaaHQAG-----LDPLLERLPQ-GLATPAGERGL---ALSAGERQRIALARVLLRRPDVLI 513
Cdd:PRK11022 99 MTSlnpcytvgfqiMEAIKV--HQGGnkktrRQRAIDLLNQvGIPDPASRLDVyphQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 514 LDEPTSALDPKTERHIAQTL--RQVLPEATIIAITHRPAL-AEVADRIIT------IEEGRAHMRTAASLAPLVEA 580
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLleLQQKENMALVLITHDLALvAEAAHKIIVmyagqvVETGKAHDIFRAPRHPYTQA 252
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
358-547 |
1.68e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 358 EDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLvryldpdAGRILFDqaplsaFTLGSLREK-VILLDQT 436
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATL-------AGREDYE------VTGGTVEFKgKDLLELS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 437 PylfNDTIGANI--AFARP------------EASEEAIRTAAHQAGLDPL-----------LERLPQGLATPAGERGlaL 491
Cdd:PRK09580 72 P---EDRAGEGIfmAFQYPveipgvsnqfflQTALNAVRSYRGQEPLDRFdfqdlmeekiaLLKMPEDLLTRSVNVG--F 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 492 SAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQ---TLRQvlPEATIIAITH 547
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRD--GKRSFIIVTH 203
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
370-561 |
2.24e-07 |
|
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: 51.87 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLA-DLLV-----RYLD---------------PDAGRI------------LFDQA 416
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfDTIYaegqrRYVEslsayarqflgqmdkPDVDSIeglspaiaidqkTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 417 PLSafTLGSLREkviLLDQTPYLF-NDTIGANIAFARpeaseeairtaahQAGLDPL-LERlpqglATPAgerglaLSAG 494
Cdd:cd03270 91 PRS--TVGTVTE---IYDYLRLLFaRVGIRERLGFLV-------------DVGLGYLtLSR-----SAPT------LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 495 ERQRIALARVL-LRRPDVL-ILDEPTSALDPKTERHIAQTLrQVLPEA--TIIAITHRPALAEVADRIITI 561
Cdd:cd03270 142 EAQRIRLATQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETL-KRLRDLgnTVLVVEHDEDTIRAADHVIDI 211
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
180-329 |
3.52e-07 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 52.22 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 180 LLAIVLLPACVGLFVVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLRmqvAS 259
Cdd:cd18586 142 WVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIR---AS 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730203856 260 FMAGAVPG---TLLAVTTSGVILYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18586 219 DLAGAISAigkTLRMALQSLILGVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQAYERL 291
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
370-572 |
4.34e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLL---VRYLDPDaGRILFDQAPLSAFTLGSLREKVIL-----LDQTPYLfn 441
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvYPHGTYE-GEIIFEGEELQASNIRDTERAGIAiihqeLALVKEL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 442 dTIGANIAFARPEASEEAIRTAAHQAGLDPLLERLPQGL--ATPAGERGLalsaGERQRIALARVLLRRPDVLILDEPTS 519
Cdd:PRK13549 98 -SVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDInpATPVGNLGL----GQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 520 ALdpkTERHIAQTLRQV--LPEATI--IAITHR-PALAEVADRIITIEEGRaHMRTAA 572
Cdd:PRK13549 173 SL---TESETAVLLDIIrdLKAHGIacIYISHKlNEVKAISDTICVIRDGR-HIGTRP 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
444-565 |
6.48e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 444 IGANIAFA--RPEASEEAIRTAAHQAGLDPLLERLPQGLATPAGERGlALSAGERQRIALARVLLRRPDVLILDEPTSAL 521
Cdd:PRK13549 358 VGKNITLAalDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 522 D--PKTE--RHIAQTLRQVLpeaTIIAITHRpaLAEV---ADRIITIEEGR 565
Cdd:PRK13549 437 DvgAKYEiyKLINQLVQQGV---AIIVISSE--LPEVlglSDRVLVMHEGK 482
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
355-527 |
7.26e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRIlfdqaplsafTLGslrEKVIL-- 432
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI----------KIG---ETVKLay 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 433 LDQtpylFNDTIGAN-------------IAFARPEASEEAIRTAAHQAGLDpllerlpQGlaTPAGErglaLSAGERQRI 499
Cdd:PRK11819 392 VDQ----SRDALDPNktvweeisggldiIKVGNREIPSRAYVGRFNFKGGD-------QQ--KKVGV----LSGGERNRL 454
|
170 180
....*....|....*....|....*...
gi 1730203856 500 ALARVLLRRPDVLILDEPTSALDPKTER 527
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVETLR 482
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
360-565 |
7.95e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 360 VALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGSLREK---------- 429
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedrl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 430 ---VILldqtpylfNDTIGANIA---FARPEAS------EEAIRTAAHQagldpLLERL---PQGLATPAGerglALSAG 494
Cdd:COG3845 344 grgLVP--------DMSVAENLIlgrYRRPPFSrggfldRKAIRAFAEE-----LIEEFdvrTPGPDTPAR----SLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 495 ERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE-ATIIAIThrPALAEV---ADRIITIEEGR 565
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLIS--EDLDEIlalSDRIAVMYEGR 479
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
50-327 |
9.20e-07 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350006 [Multi-domain] Cd Length: 289 Bit Score: 50.70 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 50 ALNLAQPYLSKMLIDNALLPRDMGALVAIGLAMIGVTIGNYALnilasyryISTSADML-FDIRVALLR----HLQTLSP 124
Cdd:cd18562 13 GVQFAEPVLFGRVVDALSSGGDAFPLLALWAALGLFSILAGVL--------VALLADRLaHRRRLAVMAsyfeHVITLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 125 RFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLT 204
Cdd:cd18562 85 SFHSQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLALLLVVLAAVYAALNRLVMRRTKAGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 205 RTMRERGSDLGSLLVDTIMGMRVVSSLNAAAHETERFRarnsAFVEAMLRMQ--VASFMAGAVPGTLLAVTTS--GVILY 280
Cdd:cd18562 165 AAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALR----GITRRLLAAQypVLNWWALASVLTRAASTLTmvAIFAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1730203856 281 GGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLA 327
Cdd:cd18562 241 GAWLVQRGELTVGEIVSFVGFATLLIGRLDQLSGFINRLFMQAPKLQ 287
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
490-566 |
1.03e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 490 ALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPALAEVADRIITIEEGRA 566
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdkGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
40-329 |
1.04e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 50.56 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 40 LVLLVSLISTALNLAQPYLSKMLID--NALLPRDMGALVAIGLAMIGVTIgnyaLNILASYRYISTSADMLFDIRVALL- 116
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISylSSYPDEPLSEGYLLALALFLVSL----LQSLLLHQYFFLSFRLGMRVRSALSs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 117 ---RHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVtADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLF 193
Cdd:cd18579 77 liyRKALRLSSSARQETSTGEIVNLMSVDVQRIEDF-FLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 194 VVFQRKLDRLTRTMRERGSDLGSLLVDTIMGMRVVSsLNA----AAHETERFRARNSAFVEAMLRMQVASFMAGAVPGTL 269
Cdd:cd18579 156 AFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIK-LYAwekpFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 270 LAVTTsgvilYGGYQIIEGTMSIGTLVAFMAYQSRLFSPIQVLMGLVSGLSSARVSLARI 329
Cdd:cd18579 235 VSLAT-----FATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
367-563 |
1.53e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 367 RAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAplsaFTLGSLREKVILLDQTPY-------- 438
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN----WQLAWVNQETPALPQPALeyvidgdr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 439 ----LFNDTIGANI-----AFARPEASEEAIRTAAHQAGLDPLLERLpqGLATPAGERGL-ALSAGERQRIALARVLLRR 508
Cdd:PRK10636 90 eyrqLEAQLHDANErndghAIATIHGKLDAIDAWTIRSRAASLLHGL--GFSNEQLERPVsDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 509 PDVLILDEPTSALDPKTERHIAQTLRQVlpEATIIAITH-RPALAEVADRIITIEE 563
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILISHdRDFLDPIVDKIIHIEQ 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
365-572 |
1.74e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.59 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 365 DGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLL--VRYLDPDAGRILFDQAPLSAFTLGSLREK-VILLDQTPYLFN 441
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsgVYPHGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 442 D-TIGANIaFARPEASEEAIRTAahqaglDPLLERLPQGL-----------ATPAGERGLalsaGERQRIALARVLLRRP 509
Cdd:TIGR02633 92 ElSVAENI-FLGNEITLPGGRMA------YNAMYLRAKNLlrelqldadnvTRPVGDYGG----GQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 510 DVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHR-PALAEVADRIITIEEGRaHMRTAA 572
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGvACVYISHKlNEVKAVCDTICVIRDGQ-HVATKD 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
491-565 |
1.99e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 1.99e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 491 LSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAI--THRPALAEVADRIITIEEGR 565
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMvsSELPEIITVCDRIAVFCEGR 486
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
487-565 |
3.03e-06 |
|
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: 48.03 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 487 RGLalSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHRPA--LAEVADRIITIE 562
Cdd:cd03233 117 RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlkTTTFVSLYQASdeIYDLFDKVLVLY 194
|
...
gi 1730203856 563 EGR 565
Cdd:cd03233 195 EGR 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
375-536 |
4.14e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 375 LEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRIL--FDQ-APLSAFTLGSLREKVILLDQTPYL--FNDTIGANIA 449
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqFSHiTRLSFEQLQKLVSDEWQRNNTDMLspGEDDTGRTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 450 FARPEASEEAIRTA--AHQAGLDPLLERlpqglatpageRGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTER 527
Cdd:PRK10938 104 EIIQDEVKDPARCEqlAQQFGITALLDR-----------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
....*....
gi 1730203856 528 HIAQTLRQV 536
Cdd:PRK10938 173 QLAELLASL 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
490-564 |
4.31e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 4.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 490 ALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTerhiAQTLRQVLPE--ATIIAITH-RPALAEVADRIITIEEG 564
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTfqGSIIFISHdRSFIRNMATRIVDLDRG 229
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
387-547 |
4.41e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 387 GPSGVGKSTLADLLVRYLDPDAGRILFDqaplSAFTLGSLREkvillDQTPYLFNDTIGANIA---------------FA 451
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLD----PNERLGKLRQ-----DQFAFEEFTVLDTVIMghtelwevkqerdriYA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 452 RPEASEE-AIR--------------TAAHQAGlDPLLerlpqGLATPAGER-GL--ALSAGERQRIALARVLLRRPDVLI 513
Cdd:PRK15064 105 LPEMSEEdGMKvadlevkfaemdgyTAEARAG-ELLL-----GVGIPEEQHyGLmsEVAPGWKLRVLLAQALFSNPDILL 178
|
170 180 190
....*....|....*....|....*....|....
gi 1730203856 514 LDEPTSALDPKTERHIAQTLRQVlpEATIIAITH 547
Cdd:PRK15064 179 LDEPTNNLDINTIRWLEDVLNER--NSTMIIISH 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
486-562 |
4.65e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 486 ERGLA-LSAGERQ------RIALARVLLRRPDVLILDEPTSALDPKTERH----IAQTLRQVlPEatIIAITHRPALAEV 554
Cdd:PRK03918 783 ERPLTfLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKlvdiMERYLRKI-PQ--VIIVSHDEELKDA 859
|
....*...
gi 1730203856 555 ADRIITIE 562
Cdd:PRK03918 860 ADYVIRVS 867
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
359-523 |
5.10e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 359 DVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLsafTLGSLREKVILLDQTPY 438
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGDRSRFMAYLGHLPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 439 LFND-TIGANIAFARPEASEEAIRTAAHQAGLdpllerlpQGLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEP 517
Cdd:PRK13543 93 LKADlSTLENLHFLCGLHGRRAKQMPGSALAI--------VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*.
gi 1730203856 518 TSALDP 523
Cdd:PRK13543 165 YANLDL 170
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
370-559 |
1.16e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLA-DLLVRYLD---------PDAGR-----------ILFDQAPL---------- 418
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLInDTLYPALAnrlngaktvPGRYTsieglehldkvIHIDQSPIgrtprsnpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 419 --SAFTLgsLREkviLLDQTP-----------YLFN---------------------------------------DTI-- 444
Cdd:TIGR00630 704 ytGVFDE--IRE---LFAETPeakvrgytpgrFSFNvkggrceacqgdgvikiemhflpdvyvpcevckgkrynrETLev 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 445 ---GANIA----FARPEASE--EAIRTAAH--QAGLDPLLERLPqgLATPAgergLALSAGERQRIALARVLLRR---PD 510
Cdd:TIGR00630 779 kykGKNIAdvldMTVEEAYEffEAVPSISRklQTLCDVGLGYIR--LGQPA----TTLSGGEAQRIKLAKELSKRstgRT 852
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1730203856 511 VLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAEVADRII 559
Cdd:TIGR00630 853 LYILDEPTTGLHFDDIKKLLEVLQRLVDKGnTVVVIEHNLDVIKTADYII 902
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
38-262 |
1.95e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 46.73 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 38 LTLVLLVSLISTALNLAQPYLSKMLIDNALLPRDMGA---LVAIGLAMIGVTIGNYALNILASYRYISTSADMLFDirvA 114
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSgyyLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHD---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 115 LLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWklflLAIVLLPACVGLFV 194
Cdd:cd18580 78 LLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYY 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 195 VFQRKLDRLTRTMR----ERGSDLGSLLVDTIMGMRVVSSLNAaaheTERFRARNSAFVEAMLRMQVASFMA 262
Cdd:cd18580 154 LLQRYYLRTSRQLRrlesESRSPLYSHFSETLSGLSTIRAFGW----QERFIEENLRLLDASQRAFYLLLAV 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
485-564 |
2.58e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 485 GERGLALSAGERQRIALARVLLRRPDVLI-LDEPTSALDPKTERHIAQTLRQvLPEA--TIIAITHRPA--LAEVADRII 559
Cdd:TIGR00956 896 GVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRK-LADHgqAILCTIHQPSaiLFEEFDRLL 974
|
....*
gi 1730203856 560 TIEEG 564
Cdd:TIGR00956 975 LLQKG 979
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
492-522 |
3.63e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 3.63e-05
10 20 30
....*....|....*....|....*....|.
gi 1730203856 492 SAGERQRIALARVLLRRPDVLILDEPTSALD 522
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
372-565 |
5.01e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.20 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 372 GF---TLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPDAGRILFDQAPLSAFTLGS-LREKVILLD---QTPYLFND-- 442
Cdd:PRK15439 278 GFrniSLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYLDap 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 443 --------TIGANIAFARPeASEEAIRTAAHQAgLDPLLERLPQGLATpagerglaLSAGERQRIALARVLLRRPDVLIL 514
Cdd:PRK15439 358 lawnvcalTHNRRGFWIKP-ARENAVLERYRRA-LNIKFNHAEQAART--------LSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1730203856 515 DEPTSALDPKTERHIAQTLRQVLPEAT-IIAITHRpaLAEV---ADRIITIEEGR 565
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSD--LEEIeqmADRVLVMHQGE 480
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
370-565 |
5.36e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLADLLV------RYldpdAGRILFDQAPLSAFTL-GSLREKVILLDQ----TPY 438
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgSY----EGEILFDGEVCRFKDIrDSEALGIVIIHQelalIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 439 LfndTIGANIAFARPEASEEAI---RTAAHQAGLdplLERLpqGLATPAGERGLALSAGERQRIALARVLLRRPDVLILD 515
Cdd:NF040905 93 L---SIAENIFLGNERAKRGVIdwnETNRRAREL---LAKV--GLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 516 EPTSALDPKTERHIAQTLRQVLPEA-TIIAITHR-PALAEVADRIITIEEGR 565
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLELKAQGiTSIIISHKlNEIRRVADSITVLRDGR 216
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
471-564 |
5.43e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 471 PLLERLPQGLA-TPAGERGLALSAGERQRIALARVLL---RRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAI 545
Cdd:PRK00635 1679 PLQALIDNGLGyLPLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGhSVIYI 1758
|
90
....*....|....*....
gi 1730203856 546 THRPALAEVADRIITIEEG 564
Cdd:PRK00635 1759 DHDPALLKQADYLIEMGPG 1777
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
479-564 |
9.28e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 479 GLATPAGERGLA-LSAGERQRIALARVLLRRPD--VLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAEV 554
Cdd:PRK00635 464 GLPYLTPERALAtLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGnTVLLVEHDEQMISL 543
|
90
....*....|
gi 1730203856 555 ADRIITIEEG 564
Cdd:PRK00635 544 ADRIIDIGPG 553
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
482-565 |
1.15e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 482 TPAGERGL-ALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQvLPEATIIAITHRPALAEV---ADR 557
Cdd:PRK11288 387 TPSREQLImNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYE-LAAQGVAVLFVSSDLPEVlgvADR 465
|
....*...
gi 1730203856 558 IITIEEGR 565
Cdd:PRK11288 466 IVVMREGR 473
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
490-559 |
1.25e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 1.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 490 ALSAGERQRIALARVL---LRRPDVL-ILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRII 559
Cdd:pfam02463 1077 LLSGGEKTLVALALIFaiqKYKPAPFyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
491-565 |
1.68e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 1.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 491 LSAGERQRIALARVLLRRPDVLILDEPTSALD--PKTErhIAQTLRQVLPEA-TIIAITHR-PALAEVADRIITIEEGR 565
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgAKYE--IYTIINELAAEGkGVIVISSElPELLGMCDRIYVMNEGR 481
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
491-558 |
1.73e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 1.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730203856 491 LSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPE--ATIIAITHR-PALAEVADRI 558
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDlQMLSQWADKI 229
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
490-563 |
3.10e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.07 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 490 ALSAGERQRIALARV--LLR-RPDVL-ILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRII--TIEE 563
Cdd:cd03278 113 LLSGGEKALTALALLfaIFRvRPSPFcVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLYgvTMQE 192
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
370-437 |
3.37e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 3.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLA-DLLVRYLdpdAGRILFDQAPLSAFTlgSLR-----EKVILLDQTP 437
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVnDILYPAL---ARKLNGAKEKPGPHD--SIEglehiDKVIDIDQSP 689
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
483-559 |
3.63e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 483 PAGERGLALSAGERQRIALARVLL---RRPDVLILDEPTSAL---DPKTERHIAQTLRQVlpEATIIAITHRPALAEVAD 556
Cdd:PRK00635 802 PLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQ--GHTVVIIEHNMHVVKVAD 879
|
...
gi 1730203856 557 RII 559
Cdd:PRK00635 880 YVL 882
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
491-561 |
4.57e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 4.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730203856 491 LSAGERQRIALARVL-LRRPDVL-ILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALAEVADRIITI 561
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGnTLIVVEHDEDTIRAADYVIDI 562
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
370-397 |
6.04e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 6.04e-04
10 20
....*....|....*....|....*...
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLA 397
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSLA 43
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
490-563 |
7.32e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 490 ALSAGERQ------RIALARVLLRRPDVLILDEPTSALDpkTERH------IAQTLRQ--VLPEatIIAITHRPALAEVA 555
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLD--EDRRtnlkdiIEYSLKDssDIPQ--VIMISHHRELLSVA 876
|
....*...
gi 1730203856 556 DRIITIEE 563
Cdd:PRK01156 877 DVAYEVKK 884
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
400-551 |
9.57e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 400 LVRYLDPDAGRILFDQAPLSAFTLGSLREKVILLDQTPYLFNDTIGANIAFARPEASEEAIRTAAHQAGLDPLLERlPQG 479
Cdd:pfam13304 151 LSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLEN-GGG 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730203856 480 LATPAGErglaLSAGERQRIALARVLLRR---PDVLILDEPTSALDPKTERHIAQTLRQVLPE-ATIIAITHRPAL 551
Cdd:pfam13304 230 GELPAFE----LSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRLLELLKELSRNgAQLILTTHSPLL 301
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
491-558 |
1.16e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 40.71 E-value: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730203856 491 LSAGERQRIALARVL-LRRPD---VLILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRI 558
Cdd:cd03272 159 LSGGQKSLVALALIFaIQKCDpapFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKF 230
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
39-282 |
1.16e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 41.30 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 39 TLVLLVSLISTALNLAQPYL-----SKMLIDNALLPRD------MGALVAIGLAMIGVTIGNYALNILASYRyistSADM 107
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWlgiwaSAYETSSALPPSEvsvlyyLGIYALISLLSVLLGTLRYLLFFFGSLR----ASRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 108 LFDirvALLRHLQTLSPRFYSRFRLGDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLP 187
Cdd:cd18604 78 LHE---RLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 188 ACVGLFVVF---QRKLDRLTRTMRergSDLGSLLVDTIMGMRVVSSLNAaaheTERFRARNSAFVEAMLRMQVASFMAG- 263
Cdd:cd18604 155 LYVYIGRLYlraSRELKRLESVAR---SPILSHFGETLAGLVTIRAFGA----EERFIEEMLRRIDRYSRAFRYLWNLNr 227
|
250 260
....*....|....*....|....*
gi 1730203856 264 ------AVPGTLLAVTTSGVILYGG 282
Cdd:cd18604 228 wlsvriDLLGALFSFATAALLVYGP 252
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
372-416 |
1.30e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 1.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1730203856 372 GFTLEIPRGSFCAVLGPSGVGKSTLADLLVRYLDPdAGRILFDQA 416
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP-AKRARFNKA 57
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
41-265 |
1.32e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC 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. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. 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: 350028 [Multi-domain] Cd Length: 290 Bit Score: 40.86 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 41 VLLVSLISTALNLAQPYLSKMLIDNALLPRDMGALVAIGLAM-IGVTIGNYALNILASYRYISTSADMLFDIRVALLRHL 119
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLlLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 120 QTLSPRFYSRFRLGDLMSRINSDVSDIQRVTAD----TMLSVLSNLLMLtggvAIMLWLDWKLFLLAIVLLPacvgLFVV 195
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARylpqLVLAAIVPLLIL----VAVFPLDWVSALILLVTAP----LIPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 196 F------------QRKLDRLTRtmrergsdLGSLLVDTIMGMRVVSSLNAAAHETERFRARNSAFVEAMLR-MQVAsFMA 262
Cdd:cd18584 153 FmiligkaaqaasRRQWAALSR--------LSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKvLRVA-FLS 223
|
...
gi 1730203856 263 GAV 265
Cdd:cd18584 224 SAV 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
479-546 |
1.34e-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: 41.92 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730203856 479 GLATPAGERGLALSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEATIIAIT 546
Cdd:TIGR01257 2059 GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT 2126
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
355-523 |
1.42e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 355 IRFEDVALAHDGRAVLKGFTLEIPRGSFCAVLGPSGVGKSTLADLLVRylDPDAGR----ILFDQAPLSAFTLGSLREKV 430
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGYsndlTLFGRRRGSGETIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 431 ILLDQTPYL---------------FNDTIGANiafarpEASEEAIRTAAHQagldpLLERLpqGLATPAGERGL-ALSAG 494
Cdd:PRK10938 339 GYVSSSLHLdyrvstsvrnvilsgFFDSIGIY------QAVSDRQQKLAQQ-----WLDIL--GIDKRTADAPFhSLSWG 405
|
170 180 190
....*....|....*....|....*....|
gi 1730203856 495 ErQRIAL-ARVLLRRPDVLILDEPTSALDP 523
Cdd:PRK10938 406 Q-QRLALiVRALVKHPTLLILDEPLQGLDP 434
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
370-404 |
1.55e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLA-DLLVRYL 404
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLInETLYKAL 660
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
483-562 |
2.18e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 39.21 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 483 PAGERGLALSAGERQRIALARVL----LRRPDVLILDEPTSALDPKTERHIAQTL-RQVLPEATIIAITHRPALAEVADR 557
Cdd:cd03239 87 LQGKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIkEMAKHTSQFIVITLKKEMFENADK 166
|
....*
gi 1730203856 558 IITIE 562
Cdd:cd03239 167 LIGVL 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
491-563 |
2.29e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 2.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730203856 491 LSAGERQRIALARV---LLRRPDVL-ILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPALAEVADRI--ITIEE 563
Cdd:TIGR02168 1090 LSGGEKALTALALLfaiFKVKPAPFcILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLygVTMQE 1168
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
491-564 |
2.81e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 2.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730203856 491 LSAGERQRIALARVLLRRPDVLILDEPTSALDPKTERHIAQTLRQVLPEA-TIIAITHRPALA--EVADRIITIEEG 564
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGrTVVCTIHQPSIDifEAFDELLLMKRG 1096
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
491-521 |
3.05e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 3.05e-03
10 20 30
....*....|....*....|....*....|....
gi 1730203856 491 LSAGERQRIALARVLLRRPD---VLILDEPTSAL 521
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGL 864
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
133-296 |
3.82e-03 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 39.57 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 133 GDLMSRINSDVSDIQRVTADTMLSVLSNLLMLTGGVAIMLWLDWKLFLLAIVLLPACVGLFVVFQRKLDRLTRTMRERGS 212
Cdd:cd18558 116 GELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 213 DLGSLLVDTIMGMRVVSSLNAAAHETERF-RARNSAFVEAMLRMQVASFMAGAVPgTLLAVTTSGVILYGGYQIIEGTMS 291
Cdd:cd18558 196 KAGAVAEEVLEAFRTVIAFGGQQKEETRYaQNLEIAKRNGIKKAITFNISMGAAF-LLIYASYALAFWYGTYLVTQQEYS 274
|
....*
gi 1730203856 292 IGTLV 296
Cdd:cd18558 275 IGEVL 279
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
370-397 |
6.65e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 6.65e-03
10 20
....*....|....*....|....*...
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLA 397
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSLA 39
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
479-562 |
7.91e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 38.34 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730203856 479 GLATPAGERGLAL----SAGERQRIALA--RVLLRRPDV--LILDEPTSALDPKTERHIAQTLRQVLPEATIIAITHRPA 550
Cdd:cd03241 155 LFSTNPGEPLKPLakiaSGGELSRLMLAlkAILARKDAVptLIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCITHLPQ 234
|
90
....*....|..
gi 1730203856 551 LAEVADRIITIE 562
Cdd:cd03241 235 VAAMADNHFLVE 246
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
370-397 |
9.67e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 9.67e-03
10 20
....*....|....*....|....*...
gi 1730203856 370 LKGFTLEIPRGSFCAVLGPSGVGKSTLA 397
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSLA 43
|
|
| |
