|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-590 |
2.55e-148 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 439.99 E-value: 2.55e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 20 ASTTQTVHALIALLRPRGRALALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWST 99
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 100 QLLANVAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWR 179
Cdd:COG1132 83 YLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 180 FTVAIVAVAPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVR 259
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 260 LRTNFFAQLNGAELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARLIGVTAMPG 339
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 340 RPASIPASARSAPI--GVDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGT 417
Cdd:COG1132 323 EIPDPPGAVPLPPVrgEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 418 PIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKA-QWIHELPDGLETRVGAGGYQLTAAQA 496
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAhEFIEALPDGYDTVVGERGVNLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 497 QHIALVRLALLDPPVVILDEATAEagttaaglLDQAAELAV--------TGRTAVVIAHRLSQAVRADRILVMSGGRVVE 568
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSA--------LDTETEALIqealerlmKGRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
570 580
....*....|....*....|..
gi 532492226 569 SGTHDELIGADGSYAALWEAWS 590
Cdd:COG1132 555 QGTHEELLARGGLYARLYRLQF 576
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-587 |
5.45e-102 |
|
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: 324.48 E-value: 5.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 12 PAASALPIASTTQTVHALIALLRPRGRALALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAG 91
Cdd:COG2274 130 PTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 92 VALTWWSTQLLANVAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSgDVEAVNTVIARVLPATVSALFMISLTLV 171
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 172 GVGVIDWRFTVAIVAVAPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAI 251
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 252 SFDMQAVRLRTNFFAQLNGAELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:COG2274 369 NARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 332 IGVTAMP-GRPASIPASARSAPIG-VDVKRVSYSYD-NSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG 408
Cdd:COG2274 449 DDILDLPpEREEGRSKLSLPRLKGdIELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 409 DGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKA-QWIHELPDGLETRVGAG 487
Cdd:COG2274 529 SGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLhDFIEALPMGYDTVVGEG 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 488 GYQLTAAQAQHIALVRLALLDPPVVILDEATAEagttaaglLDQAAELAVT--------GRTAVVIAHRLSQAVRADRIL 559
Cdd:COG2274 609 GSNLSGGQRQRLAIARALLRNPRILILDEATSA--------LDAETEAIILenlrrllkGRTVIIIAHRLSTIRLADRII 680
|
570 580
....*....|....*....|....*...
gi 532492226 560 VMSGGRVVESGTHDELIGADGSYAALWE 587
Cdd:COG2274 681 VLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
29-587 |
2.87e-81 |
|
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: 265.86 E-value: 2.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 29 LIALLRPRGRALALTTVVLLSATACGLSTPALLGLMVDAvtegkpfvSLLRITAFMLSAAAAGV-------ALTWWSTQL 101
Cdd:COG4987 6 LLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAA--------AALAPPILNLFVPIVGVrafaigrTVFRYLERL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 102 LA-NVAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRF 180
Cdd:COG4987 78 VShDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 181 --------TVAIVAVAPIHYFALRHFLRRsgpvyrrSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAIS 252
Cdd:COG4987 158 alvlalglLLAGLLLPLLAARLGRRAGRR-------LAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 253 FDMQAVRL--RTNFFAQLngAELLGLAAVLSVGYWLVTTGSVSigAATAAALYFHSL-----FSPIAVFLSnidELQDAG 325
Cdd:COG4987 231 AQRRLARLsaLAQALLQL--AAGLAVVAVLWLAAPLVAAGALS--GPLLALLVLAALalfeaLAPLPAAAQ---HLGRVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 326 ASLARLIGVTAMPgRPASIPASARSAPIGVD--VKRVSYSYDNST-PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIA 402
Cdd:COG4987 304 AAARRLNELLDAP-PAVTEPAEPAPAPGGPSleLEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 403 GIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMK-AQWIHELPDGLE 481
Cdd:COG4987 383 RFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGlGDWLAALPDGLD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 482 TRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEagttaaglLDQAAELAV--------TGRTAVVIAHRLSQAV 553
Cdd:COG4987 463 TWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEG--------LDAATEQALladllealAGRTVLLITHRLAGLE 534
|
570 580 590
....*....|....*....|....*....|....
gi 532492226 554 RADRILVMSGGRVVESGTHDELIGADGSYAALWE 587
Cdd:COG4987 535 RMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
29-580 |
3.95e-81 |
|
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: 265.47 E-value: 3.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 29 LIALLRPRGRALALTTVVLLSATACGLSTPALLGLMVDAV-TEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQ 107
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLiIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 108 NVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAV 187
Cdd:COG4988 88 RVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 188 AP--------IHYFAL----RHFLRRSgpvyrrsraaqaRRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEhaisfdm 255
Cdd:COG4988 168 APliplfmilVGKGAAkasrRQWRALA------------RLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASE------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 256 qAVRLRTnffaqlngAELLGLA----AVLSvgywLVTTGSVSIGAATAAALYFH---SLFSPIAV------FLSNIDEL- 321
Cdd:COG4988 229 -DFRKRT--------MKVLRVAflssAVLE----FFASLSIALVAVYIGFRLLGgslTLFAALFVlllapeFFLPLRDLg 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 322 ------QDAGASLARLIGV--TAMPGRPASIPASARSAPIGVDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAG 393
Cdd:COG4988 296 sfyharANGIAAAEKIFALldAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 394 KTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKA-QW 472
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLdEF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 473 IHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEagttaaglLDQAAELAVT--------GRTAVV 544
Cdd:COG4988 456 VAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAH--------LDAETEAEILqalrrlakGRTVIL 527
|
570 580 590
....*....|....*....|....*....|....*.
gi 532492226 545 IAHRLSQAVRADRILVMSGGRVVESGTHDELIGADG 580
Cdd:COG4988 528 ITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
29-585 |
6.55e-68 |
|
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: 230.76 E-value: 6.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 29 LIALLRPRGRALALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQN 108
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 109 VLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVL------PATVSALFMISLTLvgvgviDWRFTV 182
Cdd:TIGR02203 85 VVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFivlvreTLTVIGLFIVLLYY------SWQLTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 183 AIVAVAPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRT 262
Cdd:TIGR02203 159 IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 263 NF--FAQLNGAelLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVfLSNID-ELQDAGASLARLIGVTAMPG 339
Cdd:TIGR02203 239 ISspITQLIAS--LALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKS-LTNVNaPMQRGLAAAESLFTLLDSPP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 340 RPASIPASARSAPIGVDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTP 418
Cdd:TIGR02203 316 EKDTGTRAIERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 419 IDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDS-DDAKITEAVETMKAQ-WIHELPDGLETRVGAGGYQLTAAQA 496
Cdd:TIGR02203 396 LADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQaDRAEIERALAAAYAQdFVDKLPLGLDTPIGENGVLLSGGQR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 497 QHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELI 576
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
....*....
gi 532492226 577 GADGSYAAL 585
Cdd:TIGR02203 556 ARNGLYAQL 564
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
28-585 |
1.22e-65 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 224.58 E-value: 1.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 28 ALIALLRP-RGRALAlTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVA 106
Cdd:TIGR02204 8 ALWPFVRPyRGRVLA-ALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 107 QNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIArvlpATVSALFMISLTLVG----VGVIDWRFTV 182
Cdd:TIGR02204 87 ERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIG----SSLSMALRNALMCIGglimMFITSPKLTS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 183 AIVAVAPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRT 262
Cdd:TIGR02204 163 LVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 263 NFFAQLNGAELLGLAAVLSVGYWLVTTGSVSigAATAAALYFHSLFSPIAV-FLSNI-DELQDAGASLARLIGV------ 334
Cdd:TIGR02204 243 LLTAIVIVLVFGAIVGVLWVGAHDVIAGKMS--AGTLGQFVFYAVMVAGSIgTLSEVwGELQRAAGAAERLIELlqaepd 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 335 TAMPGRPASIPASARSApIGVDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITV 414
Cdd:TIGR02204 321 IKAPAHPKTLPVPLRGE-IEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 415 DGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKA-QWIHELPDGLETRVGAGGYQLTA 493
Cdd:TIGR02204 400 DGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAhEFISALPEGYDTYLGERGVTLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 494 AQAQHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHD 573
Cdd:TIGR02204 480 GQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHA 559
|
570
....*....|..
gi 532492226 574 ELIGADGSYAAL 585
Cdd:TIGR02204 560 ELIAKGGLYARL 571
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
355-580 |
2.18e-62 |
|
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: 205.54 E-value: 2.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLV 434
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKA-QWIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVI 513
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAhDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 514 LDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADG 580
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
355-586 |
2.80e-61 |
|
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: 202.85 E-value: 2.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDN-STPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKA-QWIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVV 512
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAhEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 513 ILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADGSYAALW 586
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
355-588 |
1.02e-59 |
|
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: 198.92 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDN--STPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVV 432
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVHVFVGTIADDLRLCAPDSDDakiTEAVETMKAQWIHE----LPDGLETRVGAGGYQLTAAQAQHIALVRLALLD 508
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD---EEVEEAAKKANIHDfimsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 509 PPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADGSYAALWEA 588
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-582 |
1.10e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 206.11 E-value: 1.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 25 TVHALIALLRPRGRALALTTVVLLSATACGLSTPALLGLMVDAVTEGKPF----VSLLRITAFMLSAAAAgvALTWWSTQ 100
Cdd:PRK10790 10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLplglVAGLAAAYVGLQLLAA--GLHYAQSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 101 LLANVAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRF 180
Cdd:PRK10790 88 LFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 181 TVAIVAVAPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRL 260
Cdd:PRK10790 168 ALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 261 R-------TNFFAQLNGAELLGLaavlsvgYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARLIG 333
Cdd:PRK10790 248 DgfllrplLSLFSALILCGLLML-------FGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 334 VTAMP----GRPASIPASARsapigVDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGD 409
Cdd:PRK10790 321 LMDGPrqqyGNDDRPLQSGR-----IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 410 GRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLcAPDSDDAKITEAVETMK-AQWIHELPDGLETRVGAGG 488
Cdd:PRK10790 396 GEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTL-GRDISEEQVWQALETVQlAELARSLPDGLYTPLGEQG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 489 YQLTAAQAQHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVE 568
Cdd:PRK10790 475 NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
570
....*....|....
gi 532492226 569 SGTHDELIGADGSY 582
Cdd:PRK10790 555 QGTHQQLLAAQGRY 568
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
39-561 |
5.31e-57 |
|
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: 200.21 E-value: 5.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 39 ALALTTVVLLSATACGLStpallGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVF 118
Cdd:TIGR02857 10 LLGVLGALLIIAQAWLLA-----RVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 119 AATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHF 198
Cdd:TIGR02857 85 EAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 199 LRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLrtnffAQLNGAeLLGLAA 278
Cdd:TIGR02857 165 GWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRI-----AFLSSA-VLELFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 279 VLSVGYWLVTTG------SVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARLIGVTAMPGRPASIPASARSAP 352
Cdd:TIGR02857 239 TLSVALVAVYIGfrllagDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 353 I-GVDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKV 431
Cdd:TIGR02857 319 AsSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 432 VLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVE-TMKAQWIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPP 510
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAENIRLARPDASDAEIREALErAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 532492226 511 VVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVM 561
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
355-588 |
3.92e-55 |
|
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: 186.67 E-value: 3.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLV 434
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVGTIADDLRLCAPDSDDAKITEAVetmKAQWIHE----LPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPP 510
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAA---KAAQIHDkimrFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 511 VVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADGSYAALWEA 588
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
29-585 |
8.23e-55 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 197.86 E-value: 8.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 29 LIALLRPRGRALALTTVVLLSA----TACGLSTPALLGLMVDAV-TEGKPfvSLLR-ITAFMLSAAAAGVALTWWSTQLL 102
Cdd:TIGR03796 141 LLRALWRRLRGSRGALLYLLLAglllVLPGLVIPAFSQIFVDEIlVQGRQ--DWLRpLLLGMGLTALLQGVLTWLQLYYL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 103 ANVAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDvEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTV 182
Cdd:TIGR03796 219 RRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 183 AIVAVAPIHYFALRHFLRR-----------SGPVYRRSRAaqarrGQQLIETLGGAGTvtalrrTDEHIGRIAETSEHAI 251
Cdd:TIGR03796 298 IGIAFAAINVLALQLVSRRrvdanrrlqqdAGKLTGVAIS-----GLQSIETLKASGL------ESDFFSRWAGYQAKLL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 252 SfDMQAVRLRTNFFAQL-NGAELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLAR 330
Cdd:TIGR03796 367 N-AQQELGVLTQILGVLpTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNR 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 331 LIGVTAMPGRPA---SIPASARSAPIG-----VDVKRVSYSYDNS-TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLI 401
Cdd:TIGR03796 446 LDDVLRNPVDPLleePEGSAATSEPPRrlsgyVELRNITFGYSPLePPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLV 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 402 AGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRL---CAPDSD------DAKITEAVETMkaqw 472
Cdd:TIGR03796 526 AGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLwdpTIPDADlvrackDAAIHDVITSR---- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 473 ihelPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEagttaaglLDQAAELAVT------GRTAVVIA 546
Cdd:TIGR03796 602 ----PGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSA--------LDPETEKIIDdnlrrrGCTCIIVA 669
|
570 580 590
....*....|....*....|....*....|....*....
gi 532492226 547 HRLSQAVRADRILVMSGGRVVESGTHDELIGADGSYAAL 585
Cdd:TIGR03796 670 HRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-585 |
2.77e-52 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 190.70 E-value: 2.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 29 LIALLRPRGRALALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFM-----LSAAAAGValtwwSTQLLA 103
Cdd:TIGR00958 152 LLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMcllsiASSVSAGL-----RGGSFN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 104 NVAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVeavnTVIARVLPATVSaLFMISLTLVGVGVI-----DW 178
Cdd:TIGR00958 227 YTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDT----QTMSRSLSLNVN-VLLRNLVMLLGLLGfmlwlSP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 179 RFTVAIVAVAPIHYFALRHFlrrsGPVYRRSRA----AQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFD 254
Cdd:TIGR00958 302 RLTMVTLINLPLVFLAEKVF----GKRYQLLSEelqeAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLN 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 255 MQAVRLRTNFFAQLNGAELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDA-GASLArlig 333
Cdd:TIGR00958 378 KRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAvGASEK---- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 334 VTAMPGRPASIPASARSAPIG----VDVKRVSYSYDN--STPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPV 407
Cdd:TIGR00958 454 VFEYLDRKPNIPLTGTLAPLNleglIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 408 GDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKAQ-WIHELPDGLETRVGA 486
Cdd:TIGR00958 534 TGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHdFIMEFPNGYDTEVGE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 487 GGYQLTAAQAQHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAvtGRTAVVIAHRLSQAVRADRILVMSGGRV 566
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA--SRTVLLIAHRLSTVERADQILVLKKGSV 691
|
570
....*....|....*....
gi 532492226 567 VESGTHDELIGADGSYAAL 585
Cdd:TIGR00958 692 VEMGTHKQLMEDQGCYKHL 710
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
29-587 |
8.92e-52 |
|
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: 187.33 E-value: 8.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 29 LIALLRPRGRALALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLlritAFMLSAA-----AAGVALTWWSTQLLA 103
Cdd:COG5265 28 LPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVV----PVGLLLAygllrLLSVLFGELRDALFA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 104 NVAQNVLADLREDVFAATLAQPSSLVEDAGTGDL---ISRvsGdVEAVNTVIARVLPATVSALFMISLTLVGVGVI-DWR 179
Cdd:COG5265 104 RVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLsrdIER--G-TKGIEFLLRFLLFNILPTLLEIALVAGILLVKyDWW 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 180 FtVAIVAVAPIHYFAL-------RHFLRRsgpvyrRSRAAQARRGQQLIETLGGAGTV---TALRRTDEHIGRIAETSEH 249
Cdd:COG5265 181 F-ALITLVTVVLYIAFtvvvtewRTKFRR------EMNEADSEANTRAVDSLLNYETVkyfGNEAREARRYDEALARYER 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 250 AisfdmqAVRLRTNFFAqLNGAELL----GLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAvFLSNI-DELQDA 324
Cdd:COG5265 254 A------AVKSQTSLAL-LNFGQALiialGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLN-FLGFVyREIRQA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 325 GASLARLIGVTAMPGRPASIPAsARSAPIG---VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLI 401
Cdd:COG5265 326 LADMERMFDLLDQPPEVADAPD-APPLVVGggeVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 402 AGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVEtmKAQwIHE----LP 477
Cdd:COG5265 405 FRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAAR--AAQ-IHDfiesLP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 478 DGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEagttaaglLDQAAELAV--------TGRTAVVIAHRL 549
Cdd:COG5265 482 DGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA--------LDSRTERAIqaalrevaRGRTTLVIAHRL 553
|
570 580 590
....*....|....*....|....*....|....*...
gi 532492226 550 SQAVRADRILVMSGGRVVESGTHDELIGADGSYAALWE 587
Cdd:COG5265 554 STIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWA 591
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-549 |
3.60e-50 |
|
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: 181.79 E-value: 3.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 29 LIALLRPRGRALALTTVVLLSATACGLSTPALLGLMVDAVTEgKPFVSLLRITAFMLSAAAAGVALTWWSTQLLA-NVAQ 107
Cdd:TIGR02868 4 ILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAE-MPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGhDAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 108 NVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAV 187
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 188 APIHYFAL-RHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAIsfdmQAVRLRTNFFA 266
Cdd:TIGR02868 163 LLLAGFVApLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELT----RAERRAAAATA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 267 QLNGAELLGLAAVLSVGYWLVTTGSVS--IGAATAAALYFHSL--FSPIAVFLSNIDELQDAGASLARLIGVTAmPGRPA 342
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAVADgrLAPVTLAVLVLLPLaaFEAFAALPAAAQQLTRVRAAAERIVEVLD-AAGPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 343 SIPASARSAPIGVD-----VKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGT 417
Cdd:TIGR02868 318 AEGSAPAAGAVGLGkptleLRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 418 PIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMK-AQWIHELPDGLETRVGAGGYQLTAAQA 496
Cdd:TIGR02868 398 PVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGlADWLRALPDGLDTVLGEGGARLSGGER 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 532492226 497 QHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRL 549
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
355-570 |
2.94e-49 |
|
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: 170.46 E-value: 2.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNS-TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKA-QWIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVV 512
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVtDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 513 ILDEATAEagttaaglLDQAAELAV--------TGRTAVVIAHRLSQAVRADRILVMSGGRVVESG 570
Cdd:cd03245 163 LLDEPTSA--------MDMNSEERLkerlrqllGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
355-585 |
5.03e-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: 5.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVI-DSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKA-QWIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVV 512
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAhDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 513 ILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADGSYAAL 585
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
36-588 |
1.14e-47 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 175.92 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 36 RGRALALTTVVLLSATacgLSTPALLGLMVDAVTEGKPFVSLLRI-TAFMLSAAAAGVALTWWSTQLLANVAQNVLADlr 114
Cdd:PRK13657 20 LGILLAVANVLLAAAT---FAEPILFGRIIDAISGKGDIFPLLAAwAGFGLFNIIAGVLVARHADRLAHRRRLAVLTE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 115 edVFAATLAQPSSLVEDAGTGDLIsrvsgdveavntviaRVLPATVSALFMISL--------TLVGVGV-------IDWR 179
Cdd:PRK13657 95 --YFERIIQLPLAWHSQRGSGRAL---------------HTLLRGTDALFGLWLefmrehlaTLVALVVllplalfMNWR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 180 FTVAIVAVAPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDehigriAETSE-HAISFDMQAV 258
Cdd:PRK13657 158 LSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIE------AETQAlRDIADNLLAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 259 RLRT-NFFAQLNG----AELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARLI- 332
Cdd:PRK13657 232 QMPVlSWWALASVlnraASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFe 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 333 ---GVTAMPGRPASIPASARSApiGVDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGD 409
Cdd:PRK13657 312 vedAVPDVRDPPGAIDLGRVKG--AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 410 GRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKAQ-WIHELPDGLETRVGAGG 488
Cdd:PRK13657 390 GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHdFIERKPDGYDTVVGERG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 489 YQLTAAQAQHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVE 568
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
570 580
....*....|....*....|
gi 532492226 569 SGTHDELIGADGSYAALWEA 588
Cdd:PRK13657 550 SGSFDELVARGGRFAALLRA 569
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
12-585 |
1.28e-45 |
|
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: 171.85 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 12 PAASALPIASTTQTVHALIALLRPRGRALALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAG 91
Cdd:TIGR01193 130 PTPEYKPIKEKENSLLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQ 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 92 VALTWWSTQLLANVAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSgDVEAvntvIARVLPATVSALFMISLTLV 171
Cdd:TIGR01193 210 QILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASS----IIDALASTILSLFLDMWILV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 172 GVGVIDWR-----FTVAIVAVaPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIaeT 246
Cdd:TIGR01193 285 IVGLFLVRqnmllFLLSLLSI-PVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKI--D 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 247 SEHAISFDMQAVRLRTNFFAQL--NGAELLGLAAVLSVGYWLVTTGSVSIGAAtaaaLYFHSLFSPIAVFLSNI----DE 320
Cdd:TIGR01193 362 SEFGDYLNKSFKYQKADQGQQAikAVTKLILNVVILWTGAYLVMRGKLTLGQL----ITFNALLSYFLTPLENIinlqPK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 321 LQDAGASLARLIGVTAMPGR-PASIPASARSAPIG-VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLA 398
Cdd:TIGR01193 438 LQAARVANNRLNEVYLVDSEfINKKKRTELNNLNGdIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLA 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 399 KLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCA-PDSDDAKITEAVE--TMKAQwIHE 475
Cdd:TIGR01193 518 KLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEiaEIKDD-IEN 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 476 LPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEagttaaglLDQAAE-------LAVTGRTAVVIAHR 548
Cdd:TIGR01193 597 MPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSN--------LDTITEkkivnnlLNLQDKTIIFVAHR 668
|
570 580 590
....*....|....*....|....*....|....*..
gi 532492226 549 LSQAVRADRILVMSGGRVVESGTHDELIGADGSYAAL 585
Cdd:TIGR01193 669 LSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
355-585 |
2.44e-44 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 166.35 E-value: 2.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNS-TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVHVFVGTIADDLRLCAPDS-DDAKITEAVETMKA-QWIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPV 511
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAmDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 512 VILDEATAEagttaaglLDQAAELAVTG--------RTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADGSYA 583
Cdd:PRK11176 502 LILDEATSA--------LDTESERAIQAaldelqknRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
..
gi 532492226 584 AL 585
Cdd:PRK11176 574 QL 575
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
40-331 |
5.06e-44 |
|
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: 158.48 E-value: 5.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFA 119
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 120 ATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFL 199
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 200 RRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAV 279
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 280 LSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
355-565 |
5.22e-42 |
|
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: 149.07 E-value: 5.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNS-TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVHVFVGTIADDLrlcapdsddakiteavetmkaqwihelpdgletrvgaggyqLTAAQAQHIALVRLALLDPPVVI 513
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 514 LDEATAEagttaaglLDQAAELAVT--------GRTAVVIAHRLSQAVRADRILVMSGGR 565
Cdd:cd03228 120 LDEATSA--------LDPETEALILealralakGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
109-587 |
1.43e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 158.45 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 109 VLADLREDVFAATLaqPSSLVEDAG--TGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRF------ 180
Cdd:PRK11160 91 VLTHLRVFTFSKLL--PLSPAGLARyrQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLaltlgg 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 181 --TVAIVAVAPIHYFALRHF---LRRSGPVYRrsraaqarrgQQLIETLGGAGTVTALRRTDEHIGRIAETSEHaisfdM 255
Cdd:PRK11160 169 ilLLLLLLLPLLFYRLGKKPgqdLTHLRAQYR----------VQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQ-----W 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 256 QAVRLRTNFFAQLNGAELL---GLAAVLSVgyWLVT--TGSVSIGAATAAALYFHSLFS-----PIAVFLSNIDELQDAG 325
Cdd:PRK11160 234 LAAQRRQANLTGLSQALMIlanGLTVVLML--WLAAggVGGNAQPGALIALFVFAALAAfealmPVAGAFQHLGQVIASA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 326 ASLARLIGVTAMPGRPASIPASARSAPIgvDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGI 404
Cdd:PRK11160 312 RRINEITEQKPEVTFPTTSTAAADQVSL--TLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 405 IPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKAQWIHELPDGLETRV 484
Cdd:PRK11160 390 WDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDDKGLNAWL 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 485 GAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEagttaaglLDQAAE---LAV-----TGRTAVVIAHRLSQAVRAD 556
Cdd:PRK11160 470 GEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG--------LDAETErqiLELlaehaQNKTVLMITHRLTGLEQFD 541
|
490 500 510
....*....|....*....|....*....|.
gi 532492226 557 RILVMSGGRVVESGTHDELIGADGSYAALWE 587
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
355-566 |
2.76e-41 |
|
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: 149.16 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDN--STPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVV 432
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKAQ-WIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPV 511
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHsFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 512 VILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRV 566
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
45-582 |
5.18e-38 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 147.94 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 45 VVLLSATAC-GLSTPALLGLMVDAVTEGK-PFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAATL 122
Cdd:PRK10789 1 VALLIIIAMlQLIPPKVVGIIVDGVTEQHmTTGQILMWIGTMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 123 AQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGV-IDWRFTVAIVAVAPIHYFALRHFLRR 201
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMIKRYGDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 202 SGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAelLGLAAVLS 281
Cdd:PRK10789 161 LHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIA--IGMANLLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 282 V--GYWLVTTGSVSIGAATAAALYFHSLFSPIAV--FLSNIDELQDAGASLARLIGVTAMPGRPASIPASARSAPIGVDV 357
Cdd:PRK10789 239 IggGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLAlaWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 358 KRVSYSyDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQE 437
Cdd:PRK10789 319 RQFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 438 VHVFVGTIADDLRLCAPDSDDAKITEAVetmKAQWIHE----LPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVI 513
Cdd:PRK10789 398 PFLFSDTVANNIALGRPDATQQEIEHVA---RLASVHDdilrLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILI 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 514 LDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADGSY 582
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
355-571 |
2.57e-37 |
|
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: 138.01 E-value: 2.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVHVFVGTIADDLrlcAPDS--DDAKITEAVETMK-AQWIHELPDGLETRVGAGGYQLTAAQAQHIALVRlALL-DP 509
Cdd:cd03244 83 IPQDPVLFSGTIRSNL---DPFGeySDEELWQALERVGlKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR-ALLrKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 510 PVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGT 571
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
33-585 |
7.26e-36 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 142.79 E-value: 7.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 33 LRPRGRALALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLAD 112
Cdd:TIGR03797 131 LRGARRDLLAILAMGLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDAS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 113 LREDVFAATLAQPSSLVEDAGTGDLISRVSGdVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFT-----VAIVAV 187
Cdd:TIGR03797 211 LQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLAlvavaLALVAI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 188 APIHYFALRHfLRRSGPVyrrsraaQARRGQQLIETLGGAGTVTALRrtdehigrIAETSEHAISFDMQAVRLRTNFFAQ 267
Cdd:TIGR03797 290 AVTLVLGLLQ-VRKERRL-------LELSGKISGLTVQLINGISKLR--------VAGAENRAFARWAKLFSRQRKLELS 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 268 LNGAEllGLAAVLSVGYWLVTTGSVsigAATAAALYFHSLFSPiAVFLSNIDELQDAGASLARLIGvtAMPGRPASIPAS 347
Cdd:TIGR03797 354 AQRIE--NLLTVFNAVLPVLTSAAL---FAAAISLLGGAGLSL-GSFLAFNTAFGSFSGAVTQLSN--TLISILAVIPLW 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 348 ARSAPI-------------------GVDVKRVSYSYD-NSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPV 407
Cdd:TIGR03797 426 ERAKPIlealpevdeaktdpgklsgAIEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETP 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 408 GDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKAQWIHELPDGLETRVGAG 487
Cdd:TIGR03797 506 ESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEG 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 488 GYQLTAAQAQHIALVRLALLDPPVVILDEATAEagttaaglLD---QAAELAVTGR---TAVVIAHRLSQAVRADRILVM 561
Cdd:TIGR03797 586 GGTLSGGQRQRLLIARALVRKPRILLFDEATSA--------LDnrtQAIVSESLERlkvTRIVIAHRLSTIRNADRIYVL 657
|
570 580
....*....|....*....|....
gi 532492226 562 SGGRVVESGTHDELIGADGSYAAL 585
Cdd:TIGR03797 658 DAGRVVQQGTYDELMAREGLFAQL 681
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
374-585 |
8.75e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 141.91 E-value: 8.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 374 ISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVgDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCA 453
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 454 PDSDDAKITEAVETMKA-QWIHELPDGLETRVGAGGYQLTAAQAQHIALVRlALLDPP-VVILDEATAEAGTTAAGLLDQ 531
Cdd:PRK11174 448 PDASDEQLQQALENAWVsEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALAR-ALLQPCqLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 532492226 532 AAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADGSYAAL 585
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
355-576 |
9.95e-33 |
|
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: 125.52 E-value: 9.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLV 434
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQ--EVHVFVGTIADDL-----RLCAPDSD-DAKITEAVETMkaqwihelpdGLETRVGAGGYQLTAAQAQHIALVR-LA 505
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVafgpeNLGLPREEiRERVEEALELV----------GLEHLADRPPHELSGGQKQRVAIAGvLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 506 lLDPPVVI-------LDeataeaGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELI 576
Cdd:COG1122 151 -MEPEVLVldeptagLD------PRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
357-566 |
3.67e-31 |
|
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: 119.24 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVS 435
Cdd:cd03246 3 VENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 436 QEVHVFVGTIADDLrlcapdsddakiteavetmkaqwihelpdgletrvgaggyqLTAAQAQHIALVRLALLDPPVVILD 515
Cdd:cd03246 83 QDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 516 EATAEAGTTAAGLLDQA-AELAVTGRTAVVIAHRLSQAVRADRILVMSGGRV 566
Cdd:cd03246 122 EPNSHLDVEGERALNQAiAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
40-331 |
7.28e-31 |
|
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: 122.21 E-value: 7.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVD-AVTEGKPFVsLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVF 118
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDsGVRAGDLGV-LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 119 AATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHF 198
Cdd:cd18546 80 AHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 199 LRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAA 278
Cdd:cd18546 160 RRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 532492226 279 VLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18546 240 VLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
40-331 |
3.38e-30 |
|
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: 120.23 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLritAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFA 119
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLL---ALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 120 ATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFL 199
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 200 RRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAV 279
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 280 LSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18551 238 LGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
40-330 |
5.79e-30 |
|
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: 119.41 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDA--VTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDV 117
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDyiVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 118 FAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRH 197
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 198 FLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLA 277
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 532492226 278 AVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLAR 330
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAER 293
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
357-570 |
2.67e-29 |
|
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: 114.33 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAeLRHKVVLVS 435
Cdd:cd03247 3 INNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 436 QEVHVFVGTIADDLrlcapdsddakiteavetmkaqwihelpdgletrvgagGYQLTAAQAQHIALVRLALLDPPVVILD 515
Cdd:cd03247 82 QRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 516 EATAEagttaaglLDQAAELAV--------TGRTAVVIAHRLSQAVRADRILVMSGGRVVESG 570
Cdd:cd03247 124 EPTVG--------LDPITERQLlslifevlKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
357-565 |
2.69e-29 |
|
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: 115.26 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDNS-TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVS 435
Cdd:cd03225 2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 436 QEV-HVFVG-TIADDL-----RLCAPDSD-DAKITEAVETMkaqwihELPDGLETRVgaggYQLTAAQAQHIALVRLALL 507
Cdd:cd03225 82 QNPdDQFFGpTVEEEVafgleNLGLPEEEiEERVEEALELV------GLEGLRDRSP----FTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 508 DPPVVILDeataeagtTAAGLLDQAA---------ELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGR 565
Cdd:cd03225 152 DPDILLLD--------EPTAGLDPAGrrellellkKLKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-330 |
2.89e-29 |
|
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: 117.64 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVAL-TWWSTQLLANVAQNVLADLREDVF 118
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALlNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 119 AATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALfmisLTLVGVGVI----DWRFTVAIVAVAPIHYFA 194
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNV----LTLVGVAIIlfsiNPKLALLTLIPIPFLALG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 195 LRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELL 274
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 275 GLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLAR 330
Cdd:cd18778 237 GTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAER 292
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
40-330 |
2.17e-28 |
|
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: 115.19 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKP------FVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADL 113
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGggggvdFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 114 REDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYF 193
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 194 ALRHFLRRSGPVYRRSraaqarrgQQLI--------ETLGGAGTVTALRRTDEHIGRIAETSEhaisfDMQAVRLRTNFF 265
Cdd:cd18547 161 VTKFIAKRSQKYFRKQ--------QKALgelngyieEMISGQKVVKAFNREEEAIEEFDEINE-----ELYKASFKAQFY 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 266 AQL-----NGAELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLAR 330
Cdd:cd18547 228 SGLlmpimNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
40-331 |
4.24e-28 |
|
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: 114.07 E-value: 4.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFA 119
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 120 ATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFL 199
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 200 RRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAV 279
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 280 LSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
371-515 |
5.36e-28 |
|
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: 109.66 E-value: 5.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVG-TIADDL 449
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 450 R----LCAPDS--DDAKITEAVETMKaqwiheLPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILD 515
Cdd:pfam00005 81 RlgllLKGLSKreKDARAEEALEKLG------LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
92-581 |
1.43e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 118.54 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 92 VALTWWSTQLLANVAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLV 171
Cdd:PLN03232 964 VAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFA 1043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 172 GVGVIDwrfTVAIVAVAPI---HYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSE 248
Cdd:PLN03232 1044 LIGTVS---TISLWAIMPLlilFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMD 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 249 HAISFDMQAVrlrtnffaQLNGAELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDEL------- 321
Cdd:PLN03232 1121 NNIRFTLANT--------SSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITTLlsgvlrq 1192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 322 ----QDAGASLARLIGVTAMPGRPASIPASAR---SAPIGVDVK--RVSYSYDNS-TPVIDSISISIAPGERIAVVGSSG 391
Cdd:PLN03232 1193 askaENSLNSVERVGNYIDLPSEATAIIENNRpvsGWPSRGSIKfeDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTG 1272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 392 AGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCApDSDDAKITEAVETMKAQ 471
Cdd:PLN03232 1273 AGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALERAHIK 1351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 472 -WIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLS 550
Cdd:PLN03232 1352 dVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLN 1431
|
490 500 510
....*....|....*....|....*....|.
gi 532492226 551 QAVRADRILVMSGGRVVESGTHDELIGADGS 581
Cdd:PLN03232 1432 TIIDCDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
39-330 |
7.69e-27 |
|
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: 110.64 E-value: 7.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 39 ALALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVF 118
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 119 AATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIArvlpATVSALFMISLTLVGVGVI----DWRFTVAIVAVAPIHYFA 194
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLS----NGLINLIPDLLTLVGIVIImfslNVRLALVTLAVLPLLVLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 195 LRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELL 274
Cdd:cd18545 157 VFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISAL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 275 GLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIaVFLSNI-DELQDAGASLAR 330
Cdd:cd18545 237 GTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPI-RNLSNFyNQLQSAMASAER 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
355-585 |
1.11e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 113.84 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG---DGRITVDGTPIDDLSDAELRHK 430
Cdd:COG1123 5 LEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 431 VVLVSQE-----VHVFVGT-IADDLRLCAPDSDDAKiTEAVETMKAQwihelpdGLETRVGAGGYQLTAAQAQHIALVRL 504
Cdd:COG1123 85 IGMVFQDpmtqlNPVTVGDqIAEALENLGLSRAEAR-ARVLELLEAV-------GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 505 ALLDPPVVILD-EATAEAGTTAAGLLDQAAELAV-TGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELIGADGS 581
Cdd:COG1123 157 LALDPDLLIADePTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
....
gi 532492226 582 YAAL 585
Cdd:COG1123 237 LAAV 240
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
355-571 |
3.57e-26 |
|
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: 106.34 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVHVFVGTIADDLRLcAPDSDDAKITEAVetmkaqwihelpdgletRVGAGGYQLTAAQAQHIALVRLALLDPPVVI 513
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDP-FDEYSDEEIYGAL-----------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 514 LDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGT 571
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-311 |
6.93e-26 |
|
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: 107.98 E-value: 6.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKP---------------FVSLLRITAFMLSAAAAGVALTWWSTQLLAN 104
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPlpgllglapllgpdpLALLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 105 VAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALfmisLTLVG-VGV---IDWRF 180
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNL----LTLVGmLGVmfwLDWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 181 TVAIVAVAPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRL 260
Cdd:cd18564 157 ALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 532492226 261 RTNFFAQLNGAELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPI 311
Cdd:cd18564 237 QALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPV 287
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
39-331 |
7.73e-26 |
|
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: 107.51 E-value: 7.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 39 ALALTTVVLLSATacGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVF 118
Cdd:cd18552 2 ALAILGMILVAAT--TAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 119 AATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHF 198
Cdd:cd18552 80 DKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 199 ---LRRSGpvyRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLR--TNFFAQLNGAel 273
Cdd:cd18552 160 gkrLRKIS---RRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARalSSPLMELLGA-- 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 274 LGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18552 235 IAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-568 |
1.27e-25 |
|
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: 111.04 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 32 LLRPRGRALALttvVLLSATACGLSTPALLGLmVDAVTEGKPFVSLLRITAFMLSAAAAgVALTWWSTQLLANVAQNVLA 111
Cdd:COG4615 7 LLRESRWLLLL---ALLLGLLSGLANAGLIAL-INQALNATGAALARLLLLFAGLLVLL-LLSRLASQLLLTRLGQHAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 112 DLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVnTVIARVLPATVSALFMISLTLVGVGVIDWR-FTVAIVAVA-- 188
Cdd:COG4615 82 RLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPlFLLTLVLLGlg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 189 -PIHYFALRHFLRRsgpvYRRSRAAQARRGQQLIETLGGAGTVT--ALRRT---DEHIGRIAETSEHAIsfdmqaVRLRT 262
Cdd:COG4615 161 vAGYRLLVRRARRH----LRRAREAEDRLFKHFRALLEGFKELKlnRRRRRaffDEDLQPTAERYRDLR------IRADT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 263 NFFAQLNGAELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARLIGVTAMPGRPA 342
Cdd:COG4615 231 IFALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 343 SIPASARSAPIGVD-----VKRVSYSYDNSTP----VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRIT 413
Cdd:COG4615 311 PAAADAAAPPAPADfqtleLRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 414 VDGTPIDDLSDAELRHKVVLVSQEVHVFvgtiaDDLRLCAPDSDDAKITEAVETMKAQWIHELPDGLETRVgaggyQLTA 493
Cdd:COG4615 391 LDGQPVTADNREAYRQLFSAVFSDFHLF-----DRLLGLDGEADPARARELLERLELDHKVSVEDGRFSTT-----DLSQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 494 AQAQHIALVrLALL-DPPVVILDeataeagttaagllDQAA----------------ELAVTGRTAVVIAH--RLSQAvr 554
Cdd:COG4615 461 GQRKRLALL-VALLeDRPILVFD--------------EWAAdqdpefrrvfytellpELKARGKTVIAISHddRYFDL-- 523
|
570
....*....|....
gi 532492226 555 ADRILVMSGGRVVE 568
Cdd:COG4615 524 ADRVLKMDYGKLVE 537
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
313-578 |
1.36e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 110.76 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 313 VFLSNIDELQDAGASLARLIGVTAMPGRPAsiPASARSAPIgVDVKRVSYSYD----NSTPVIDSISISIAPGERIAVVG 388
Cdd:COG1123 222 VEDGPPEEILAAPQALAAVPRLGAARGRAA--PAAAAAEPL-LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 389 SSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDA---ELRHKVVLVSQevHVF--------VG-TIADDLRLCAPDS 456
Cdd:COG1123 299 ESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQ--DPYsslnprmtVGdIIAEPLRLHGLLS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 457 DDAKITEAVETMKAqwiHELPDGLETRVgagGYQLTAAQAQHIALVRLALLDPPVVI-------LDeataeaGTTAAGLL 529
Cdd:COG1123 377 RAERRERVAELLER---VGLPPDLADRY---PHELSGGQRQRVAIARALALEPKLLIldeptsaLD------VSVQAQIL 444
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 530 DQAAELAV-TGRTAVVIAHRLSqAVR--ADRILVMSGGRVVESGTHDELIGA 578
Cdd:COG1123 445 NLLRDLQReLGLTYLFISHDLA-VVRyiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
40-311 |
3.09e-25 |
|
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: 105.42 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGK--PFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDV 117
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGdpETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 118 FAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRH 197
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 198 FLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLA 277
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 532492226 278 AVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPI 311
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
40-331 |
4.00e-25 |
|
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: 105.64 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFA 119
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 120 ATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALfMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFL 199
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLL-TLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 200 RRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAV 279
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 280 LSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18543 240 LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
355-575 |
5.70e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.71 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEV-HVFVG-TIADD----LRLCAPDSDD--AKITEAVETMKAQ-WIHELPDGLetrvgAGGyqltaaQAQHIALVRL 504
Cdd:PRK13635 86 VFQNPdNQFVGaTVQDDvafgLENIGVPREEmvERVDQALRQVGMEdFLNREPHRL-----SGG------QKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 505 ALLDPPVVILDeataeagtTAAGLLDQA--AELAVTGR--------TAVVIAHRLSQAVRADRILVMSGGRVVESGTHDE 574
Cdd:PRK13635 155 LALQPDIIILD--------EATSMLDPRgrREVLETVRqlkeqkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
.
gi 532492226 575 L 575
Cdd:PRK13635 227 I 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
355-570 |
6.56e-25 |
|
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: 103.35 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDN---STPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL---R 428
Cdd:cd03257 2 LEVKNLSVSFPTgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 429 HKVVLVSQEVH-----VF-VGT-IADDLRLCAPDSDDAKITEAVETMKAQwiHELPDGLETRvgaggY--QLTAAQAQHI 499
Cdd:cd03257 82 KEIQMVFQDPMsslnpRMtIGEqIAEPLRIHGKLSKKEARKEAVLLLLVG--VGLPEEVLNR-----YphELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 500 ALVRLALLDPPVVILDEAT----AEAGTTAAGLLDQAAELavTGRTAVVIAHRLSqAVR--ADRILVMSGGRVVESG 570
Cdd:cd03257 155 AIARALALNPKLLIADEPTsaldVSVQAQILDLLKKLQEE--LGLTLLFITHDLG-VVAkiADRVAVMYAGKIVEEG 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
74-585 |
1.03e-24 |
|
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: 109.65 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 74 FVSLLRITAFM---LSAAAAGVALTWWSTQLLANVAQN-------------------------------VLAD--LREDV 117
Cdd:TIGR00957 965 FITFLSIFLFVcnhVSALASNYWLSLWTDDPMVNGTQNntslrlsvygalgilqgfavfgysmavsiggIQASrvLHQDL 1044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 118 FAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRH 197
Cdd:TIGR00957 1045 LHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRF 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 198 FLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTD--EHIG--RIAETSE----HAISFDMQAVRLR-------- 261
Cdd:TIGR00957 1125 YVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQErfIHQSdlKVDENQKayypSIVANRWLAVRLEcvgncivl 1204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 262 -TNFFAQLNGAELLGLAAVLSVGYWLvttgsvsigAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARLIGVTAMPGR 340
Cdd:TIGR00957 1205 fAALFAVISRHSLSAGLVGLSVSYSL---------QVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAP 1275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 341 PASIPASARsapigVDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPI 419
Cdd:TIGR00957 1276 PSGWPPRGR-----VEFRNYCLRYrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 420 DDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDaKITEAVETMKAQ-WIHELPDGLETRVGAGGYQLTAAQAQH 498
Cdd:TIGR00957 1351 AKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDE-EVWWALELAHLKtFVSALPDKLDHECAEGGENLSVGQRQL 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 499 IALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGA 578
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
....*..
gi 532492226 579 DGSYAAL 585
Cdd:TIGR00957 1510 RGIFYSM 1516
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-330 |
1.25e-24 |
|
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: 104.13 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAV----TEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLRE 115
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVliqlGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 116 DVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMIsltlVGVGV----IDWRFTVAIVAVAPIH 191
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMI----IGIGVvlfsLNWKLALLVLIPVPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 192 YFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGA 271
Cdd:cd18563 157 VWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 272 ELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLAR 330
Cdd:cd18563 237 TSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
355-576 |
2.73e-24 |
|
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: 101.99 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLV 434
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVG-TIADDLRLcAPdsddaKITEAVETMKAQWIHELPD--GLETRVGAGGY--QLTAAQAQHIALVRLALLDP 509
Cdd:cd03295 81 IQQIGLFPHmTVEENIAL-VP-----KLLKWPKEKIRERADELLAlvGLDPAEFADRYphELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 510 PVVILDEA-TAEAGTTAAGLLDQAAELAVT-GRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELI 576
Cdd:cd03295 155 PLLLMDEPfGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
356-570 |
3.41e-24 |
|
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: 99.82 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 356 DVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVS 435
Cdd:cd03214 1 EVENLSVGYGG-RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 436 QEVHVfVGtiaddlrlcapdsddakiteaVETMKAQWIHELPDGLETRVgaggyQLTAAQAQHialVRLALLDPPVVILD 515
Cdd:cd03214 80 QALEL-LG---------------------LAHLADRPFNELSGGERQRV-----LLARALAQE---PPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 516 eataeaGTTAAGLLDQAAELA-VTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:cd03214 130 ------IAHQIELLELLRRLArERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
342-585 |
4.02e-24 |
|
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: 101.91 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 342 ASIPASARSAPIG----VDVKRVSYSYDNS-TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDG 416
Cdd:cd03288 3 ASISGSSNSGLVGlggeIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 417 TPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDaKITEAVETMKAQ-WIHELPDGLETRVGAGGYQLTAAQ 495
Cdd:cd03288 83 IDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDD-RLWEALEIAQLKnMVKSLPGGLDAVVTEGGENFSVGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 496 AQHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDEL 575
Cdd:cd03288 162 RQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENL 241
|
250
....*....|.
gi 532492226 576 IG-ADGSYAAL 585
Cdd:cd03288 242 LAqEDGVFASL 252
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
355-576 |
6.43e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.52 E-value: 6.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSdAELRHKVVLV 434
Cdd:COG1131 1 IEVRGLTKRYGD-KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVG-TIADDLRLCA------PDSDDAKITEAVETMkaqwihELPDGLETRVGA--GGYQltaaqaQHIALVRlA 505
Cdd:COG1131 79 PQEPALYPDlTVRENLRFFArlyglpRKEARERIDELLELF------GLTDAADRKVGTlsGGMK------QRLGLAL-A 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 506 LL-DPPVVILDeata-eagTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELI 576
Cdd:COG1131 146 LLhDPELLILDeptsgldpEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
357-575 |
1.01e-23 |
|
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: 100.32 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDNStPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDaELRHKVVLVSQ 436
Cdd:COG4555 4 VENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 EVHVFVG-TIADDLRLCAP--DSDDAKITEAVEtmkaQWIH--ELPDGLETRVGaggyQLTAAQAQHIALVRLALLDPPV 511
Cdd:COG4555 82 ERGLYDRlTVRENIRYFAElyGLFDEELKKRIE----ELIEllGLEEFLDRRVG----ELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 512 VILDEATAEA-GTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDEL 575
Cdd:COG4555 154 LLLDEPTNGLdVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
356-575 |
1.24e-23 |
|
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: 99.43 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 356 DVKRVSYSYDNStPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE-LRHKVVLV 434
Cdd:cd03224 2 EVENLNAGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVG-TIADDLRLCAPDSDDAKITEAVEtmkaqWIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVI 513
Cdd:cd03224 81 PEGRRIFPElTVEENLLLGAYARRRAKRKARLE-----RVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 514 LDEATAEAG-TTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDEL 575
Cdd:cd03224 156 LDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-331 |
1.73e-23 |
|
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: 101.02 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFA 119
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 120 ATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFL 199
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 200 RRSGPVYRRSRAAQARRGQQLIETL--GGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLA 277
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 532492226 278 AVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
355-568 |
7.00e-23 |
|
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: 97.16 E-value: 7.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNS---TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIddlsdAELRHKV 431
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 432 VLVSQEVHVF-----VGTIAddLRLCAPDSDDAKITEAVEtmkaQWIHELpdGLETRVGAGGYQLTAAQAQHIALVRLAL 506
Cdd:cd03293 76 GYVFQQDALLpwltvLDNVA--LGLELQGVPKAEARERAE----ELLELV--GLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 507 LDPPVVILD-----EATAEAGTTAAGLLDQAAElavTGRTAVVIAHRLSQAVR-ADRILVMSG--GRVVE 568
Cdd:cd03293 148 VDPDVLLLDepfsaLDALTREQLQEELLDIWRE---TGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVA 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
356-567 |
7.37e-23 |
|
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: 96.56 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 356 DVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGtpiDDLSDAELRHKVVLVS 435
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 436 QEV--HVFVGTIADDLRLCAPDSDDaKITEAVETMKAQWIHELPDGLETrvgaggyQLTAAQAQHIALVRLALLDPPVVI 513
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDA-GNEQAETVLKDLDLYALKERHPL-------SLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 514 LDEATAEAGTTAAGLL-DQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVV 567
Cdd:cd03226 150 FDEPTSGLDYKNMERVgELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-330 |
1.12e-22 |
|
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: 98.79 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVS---------------LLRITAFMLSAAAAGVALTWWSTQLLAN 104
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLplvpaslgpadprgqLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 105 VAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNtviaRVLPATVSALFMISLTLVGVGVI----DWRF 180
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLE----RFLDDGANSIIRVVVTVLGIGAIlfylNWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 181 TVAIVAVAPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRL 260
Cdd:cd18565 157 ALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 261 RTNFFAQLNGAELLGLAAVLSVG-YWLVT-----TGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLAR 330
Cdd:cd18565 237 RAAFFPVIRLVAGAGFVATFVVGgYWVLDgpplfTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKR 312
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
355-575 |
1.71e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNST-PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:PRK13632 8 IKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEV-HVFVG-TIADDL------RLCAPDSDDAKITEAVEtmkaqwihelpdgletRVGAGGY------QLTAAQAQHI 499
Cdd:PRK13632 88 IFQNPdNQFIGaTVEDDIafglenKKVPPKKMKDIIDDLAK----------------KVGMEDYldkepqNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 500 ALVRLALLDPPVVILDeataeagtTAAGLLDQAA---------ELAVTG-RTAVVIAHRLSQAVRADRILVMSGGRVVES 569
Cdd:PRK13632 152 AIASVLALNPEIIIFD--------ESTSMLDPKGkreikkimvDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQ 223
|
....*.
gi 532492226 570 GTHDEL 575
Cdd:PRK13632 224 GKPKEI 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
357-565 |
1.93e-22 |
|
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: 93.85 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSq 436
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 evhvfvgtiaddlrlcapdsddakiteavetmkaqwihelpdgletrvgaggyQLTAAQAQHIALVRLALLDPPVVILD- 515
Cdd:cd00267 80 -----------------------------------------------------QLSGGQRQRVALARALLLNPDLLLLDe 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 532492226 516 EATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRA-DRILVMSGGR 565
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
44-327 |
3.17e-22 |
|
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: 97.17 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 44 TVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAATLA 123
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 124 QPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFLRRSG 203
Cdd:cd18576 82 LPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 204 PVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAVLSVG 283
Cdd:cd18576 162 KLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 532492226 284 YWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDA-GAS 327
Cdd:cd18576 242 GRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKAlGAS 286
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
40-331 |
3.48e-22 |
|
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: 97.10 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVS-LLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVF 118
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASqLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 119 AATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHF 198
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 199 LRRSGPVYRRSraaqarrgQQLI--------ETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNG 270
Cdd:cd18541 161 GKKIHKRFRKV--------QEAFsdlsdrvqESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 271 AELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAV--FLSNIdeLQDAGASLARL 331
Cdd:cd18541 233 LIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMAlgWVINL--IQRGAASLKRI 293
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
355-576 |
3.92e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.59 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSD-AELRHKVVL 433
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVHV-FVG-TIADDL-----RLCAPDSDDAKITEA--VETMKAQWIHELPDGLetrvgAGGyqltaaQAQHIALVRL 504
Cdd:PRK13644 82 VFQNPETqFVGrTVEEDLafgpeNLCLPPIEIRKRVDRalAEIGLEKYRHRSPKTL-----SGG------QGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 505 ALLDPPVVILDEATAEAG-TTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELI 576
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDpDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
355-570 |
8.53e-22 |
|
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: 93.74 E-value: 8.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDnSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSdAELRHkVVLV 434
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-PERRN-IGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVF-----VGTIADDLRLcapdsddAKITEAVETMKAQWIHELPdGLETRVGAGGYQLTAAQAQHIALVR------ 503
Cdd:cd03259 78 FQDYALFphltvAENIAFGLKL-------RGVPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARalarep 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 504 -LALLDPPVVILDeataeaGTTAAGLLDQAAEL-AVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:cd03259 150 sLLLLDEPLSALD------AKLREELREELKELqRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
356-578 |
1.53e-21 |
|
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: 93.80 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 356 DVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL---RHKVV 432
Cdd:cd03258 6 NVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVHVF-----VGTIADDLRLCApdSDDAKITEAVEtmkaqwihELPD--GLETRVGAGGYQLTAAQAQHIALVRLA 505
Cdd:cd03258 86 MIFQHFNLLssrtvFENVALPLEIAG--VPKAEIEERVL--------ELLElvGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 506 LLDPPVVILDEATAE-----AGTTAAGLLDQAAELavtGRTAVVIAHRLsQAVR--ADRILVMSGGRVVESGTHDELIGA 578
Cdd:cd03258 156 ANNPKVLLCDEATSAldpetTQSILALLRDINREL---GLTIVLITHEM-EVVKriCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
369-581 |
2.76e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 99.04 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 369 PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADD 448
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 449 LRlcaP--DSDDAKITEAVETMKAQ-WIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEAGTTA 525
Cdd:PLN03130 1333 LD---PfnEHNDADLWESLERAHLKdVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 526 AGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADGS 581
Cdd:PLN03130 1410 DALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
355-566 |
8.45e-21 |
|
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: 91.01 E-value: 8.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY---DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL---- 427
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 428 RHKVVLVSQEVHVFVG-TIADDLRLCA------PDSDDAKITEAVETMKaqwiheLPDGLETRVGaggyQLTAAQAQHIA 500
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLllagvpKKERRERAEELLERVG------LGDRLNHYPS----ELSGGQQQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 501 LVRlALL-DPPVVI-------LDeaTAEAGTTAAGLLDQAAElavTGRTAVVIAHRLSQAVRADRILVMSGGRV 566
Cdd:cd03255 151 IAR-ALAnDPKIILadeptgnLD--SETGKEVMELLRELNKE---AGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
44-331 |
2.00e-20 |
|
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: 91.85 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 44 TVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAATLA 123
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 124 QPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFLRRSG 203
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 204 PVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAVLSVG 283
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 532492226 284 YWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18557 242 GYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
355-575 |
3.75e-20 |
|
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: 89.55 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG-----DGRITVDGTPIDDLSDA--EL 427
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 428 RHKVVLVSQEVHVFVGTIADDLRL------CAPDSDDAKITEAVETMKAqwiheLPDGLETRVGAGGyqLTAAQAQHIAL 501
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYglrlhgIKLKEELDERVEEALRKAA-----LWDEVKDRLHALG--LSGGQQQRLCL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 502 VRLALLDPPVVILDEATAEagttaaglLDQAA---------ELAVTgRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGT 571
Cdd:cd03260 153 ARALANEPEVLLLDEPTSA--------LDPIStakieeliaELKKE-YTIVIVTHNMQQAARvADRTAFLLNGRLVEFGP 223
|
....
gi 532492226 572 HDEL 575
Cdd:cd03260 224 TEQI 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
355-579 |
7.62e-20 |
|
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: 88.71 E-value: 7.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDnSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRH---KV 431
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 432 VLVSQEVHVFVG-TIADD--------LRLcapdsDDAKITEAVetmkAQWIHELpdGLETRVGAGGYQLTAAQAQHIALV 502
Cdd:cd03261 80 GMLFQSGALFDSlTVFENvafplrehTRL-----SEEEIREIV----LEKLEAV--GLRGAEDLYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 503 RLALLDPPVVILDEATA-----EAGTTAAGLLDQAAELavtGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELI 576
Cdd:cd03261 149 RALALDPELLLYDEPTAgldpiASGVIDDLIRSLKKEL---GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELR 225
|
...
gi 532492226 577 GAD 579
Cdd:cd03261 226 ASD 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
356-575 |
9.01e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 88.50 E-value: 9.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 356 DVKRVSYSYDNStPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL-RHKVVLV 434
Cdd:COG0410 5 EVENLHAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVG-TIADDLRL-CAPDSDDAKITEAVEtmkaqWIHEL-PDgLETRVGAGGYQLTAAQAQHIALVR-------L 504
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLgAYARRDRAEVRADLE-----RVYELfPR-LKERRRQRAGTLSGGEQQMLAIGRalmsrpkL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 505 ALLD-P-----PVVILDeataeagttaagLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDEL 575
Cdd:COG0410 158 LLLDePslglaPLIVEE------------IFEIIRRLNREGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAEL 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
357-576 |
1.62e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.53 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQ 436
Cdd:PRK11231 5 TENLTVGYGT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 EVHVFVGTIADDL-------------RLcaPDSDDAKITEAVETMKaqwIHELPDGLETRVGAGGYQ---LTAAQAQHIA 500
Cdd:PRK11231 84 HHLTPEGITVRELvaygrspwlslwgRL--SAEDNARVNQAMEQTR---INHLADRRLTDLSGGQRQrafLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 501 LVrlaLLDPPVVILDEATAEAgttaagLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELI 576
Cdd:PRK11231 159 VV---LLDEPTTYLDINHQVE------LMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
359-576 |
4.24e-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: 88.57 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 359 RVSY-SYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG---DGRITVDGTPIDDLSDAELRH----K 430
Cdd:COG0444 8 KVYFpTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKirgrE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 431 VVLVSQE-------VHVfVGT-IADDLRLCAPDSDDAKITEAVETMKA-----------QWIHELpdgletrvgAGGyql 491
Cdd:COG0444 88 IQMIFQDpmtslnpVMT-VGDqIAEPLRIHGGLSKAEARERAIELLERvglpdperrldRYPHEL---------SGG--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 492 taaQAQHIALVRlAL-LDPPVVILDeataeagttaaglLD---QA------AELAVTGRTAVV-IAHRLSqAVR--ADRI 558
Cdd:COG0444 155 ---MRQRVMIAR-ALaLEPKLLIADept--------taLDvtiQAqilnllKDLQRELGLAILfITHDLG-VVAeiADRV 221
|
250
....*....|....*...
gi 532492226 559 LVMSGGRVVESGTHDELI 576
Cdd:COG0444 222 AVMYAGRIVEEGPVEELF 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
355-567 |
5.97e-19 |
|
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: 84.02 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE-LRHKVVL 433
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VsqevhvfvgtiaddlrlcapdsddakiteavetmkaqwihelpdgletrvgaggYQLTAAQAQHIALVRLALLDPPVVI 513
Cdd:cd03216 80 V------------------------------------------------------YQLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 514 LD-EATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVV 567
Cdd:cd03216 106 LDePTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
357-575 |
8.69e-19 |
|
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: 86.08 E-value: 8.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL---RHKVVL 433
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVH----------VFVGTIADD--LRLCA---PDSDDAKITEAVETMkaqwihELPDGLETRVGaggyQLTAAQAQH 498
Cdd:cd03256 83 IFQQFNlierlsvlenVLSGRLGRRstWRSLFglfPKEEKQRALAALERV------GLLDKAYQRAD----QLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 499 IALVR-------LALLDPPVVILDeaTAEAGTTAAGLLDQAAELavtGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:cd03256 153 VAIARalmqqpkLILADEPVASLD--PASSRQVMDLLKRINREE---GITVIVSLHQVDLAREyADRIVGLKDGRIVFDG 227
|
....*
gi 532492226 571 THDEL 575
Cdd:cd03256 228 PPAEL 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
356-571 |
1.47e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.59 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 356 DVKRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL-RHKVVLv 434
Cdd:PRK13548 4 EARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELaRRRAVL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHV-FVGTIADDLRL------CAPDSDDAKITEA-----VETMKAQWIHELPDGLETRVgaggyQLTAAQAQhIALV 502
Cdd:PRK13548 82 PQHSSLsFPFTVEEVVAMgraphgLSRAEDDALVAAAlaqvdLAHLAGRDYPQLSGGEQQRV-----QLARVLAQ-LWEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 503 ----RLALLDPPVVILDeataeaGTTAAGLLDQAAELAVTGRTAV-VIAHRLSQAVR-ADRILVMSGGRVVESGT 571
Cdd:PRK13548 156 dgppRWLLLDEPTSALD------LAHQHHVLRLARQLAHERGLAViVVLHDLNLAARyADRIVLLHQGRLVADGT 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
351-575 |
4.16e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.92 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 351 APIGVDVKRVSYSYDnSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSdAELRHk 430
Cdd:COG3842 2 AMPALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-PEKRN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 431 VVLVSQEV----HVfvgTIAD------DLRLCAPDSDDAKITEAVEtmkaqwihelpdgletRVGAGGY------QLTAA 494
Cdd:COG3842 79 VGMVFQDYalfpHL---TVAEnvafglRMRGVPKAEIRARVAELLE----------------LVGLEGLadryphQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 495 QAQHIALVRlAL-LDPPVVILDeataeagttaaglLDqaAELAV------------TGRTAVVIAHRLSQAVR-ADRILV 560
Cdd:COG3842 140 QQQRVALAR-ALaPEPRVLLLDepl--------saLD--AKLREemreelrrlqreLGITFIYVTHDQEEALAlADRIAV 208
|
250
....*....|....*
gi 532492226 561 MSGGRVVESGTHDEL 575
Cdd:COG3842 209 MNDGRIEQVGTPEEI 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
357-581 |
7.55e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.88 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDNSTPvidSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAElRhKVVLVSQ 436
Cdd:COG3840 4 LDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 EVHVF--------VGT-IADDLRLCAPDSddAKITEAVEtmkaqwihelpdgletRVGAGGY------QLTAAQAQHIAL 501
Cdd:COG3840 79 ENNLFphltvaqnIGLgLRPGLKLTAEQR--AQVEQALE----------------RVGLAGLldrlpgQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 502 VRLALLDPPVVILDEATAEagttaaglLDQA---------AELAV-TGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSA--------LDPAlrqemldlvDELCReRGLTVLMVTHDPEDAARiADRVLLVADGRIAADG 212
|
250
....*....|.
gi 532492226 571 THDELIGADGS 581
Cdd:COG3840 213 PTAALLDGEPP 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
355-575 |
8.17e-18 |
|
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: 82.67 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDnSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLV 434
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEV--HVFVG-TIADDLRLCAPDSDD--AKITEAVETMKAqwihelpDGLETRVGAggyQLTAAQAQHIALVRLALLDP 509
Cdd:cd03300 80 NYALfpHLTVFeNIAFGLRLKKLPKAEikERVAEALDLVQL-------EGYANRKPS---QLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 510 PVVILDEATAEagttaaglLDQA------AELA----VTGRTAVVIAHRLSQA-VRADRILVMSGGRVVESGTHDEL 575
Cdd:cd03300 150 KVLLLDEPLGA--------LDLKlrkdmqLELKrlqkELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
290-564 |
1.14e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 290 GSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARLIG----VTAMPGRPASIPASARSAPIGVDVKRVSYSYD 365
Cdd:COG4178 294 GEITLGGLMQAASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGfeeaLEAADALPEAASRIETSEDGALALEDLTLRTP 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 366 NSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVdgtPIDDlsdaelrhKVVLVSQEVHVFVGTi 445
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---PAGA--------RVLFLPQRPYLPLGT- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 446 addLR--LCAPDS----DDAKITEAVEtmKAQwIHELPDGLET-----RVGAGGYQltaaqaQHIALVRLALLDPPVVIL 514
Cdd:COG4178 442 ---LReaLLYPATaeafSDAELREALE--AVG-LGHLAERLDEeadwdQVLSLGEQ------QRLAFARLLLHKPDWLFL 509
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 515 DEATAEagttaaglLDQAAELAV--------TGRTAVVIAHRLSQAVRADRILVMSGG 564
Cdd:COG4178 510 DEATSA--------LDEENEAALyqllreelPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
355-566 |
1.18e-17 |
|
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: 80.90 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDlSDAELRHKVVLV 434
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFvgtiaDDLRlcapdsddakiteAVETMKaqwiheLPDGLETRVGAGgyqltaaqaqhIALV---RLALLDPPV 511
Cdd:cd03230 79 PEEPSLY-----ENLT-------------VRENLK------LSGGMKQRLALA-----------QALLhdpELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 512 VILDeataeaGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRV 566
Cdd:cd03230 124 SGLD------PESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
355-575 |
1.73e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.93 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGII---PVGDGRITVDGTPIDDLSDAELRHK 430
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 431 VVLVSQEV-HVFVG-TIADDLRL-----CAPDSDDAKITEAVetmkaqwiheLPDgletrVGAGGYQ------LTAAQAQ 497
Cdd:PRK13640 86 VGIVFQNPdNQFVGaTVGDDVAFglenrAVPRPEMIKIVRDV----------LAD-----VGMLDYIdsepanLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 498 HIALVRLALLDPPVVILDeataeagtTAAGLLDQAAELAV----------TGRTAVVIAHRLSQAVRADRILVMSGGRVV 567
Cdd:PRK13640 151 RVAIAGILAVEPKIIILD--------ESTSMLDPAGKEQIlklirklkkkNNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
....*...
gi 532492226 568 ESGTHDEL 575
Cdd:PRK13640 223 AQGSPVEI 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
355-570 |
2.58e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.48 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLV 434
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEV--HVFVGTIADD-------LRLcAPDSDDAKITEAVETMKAQWIHELPDgletrvgaggYQLTAAQAQHIALVRLA 505
Cdd:PRK13647 85 FQDPddQVFSSTVWDDvafgpvnMGL-DKDEVERRVEEALKAVRMWDFRDKPP----------YHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 506 LLDPPVVILDE-ATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:PRK13647 154 AMDPDVIVLDEpMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
355-575 |
2.89e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.11 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTP-VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEV-HVFVGTI-----ADDLRLCAPDSDD--AKITEAVE--TMKAQWIHElPDGLetrvgAGGyqltaaQAQHIALVR 503
Cdd:PRK13648 88 VFQNPdNQFVGSIvkydvAFGLENHAVPYDEmhRRVSEALKqvDMLERADYE-PNAL-----SGG------QKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 504 LALLDPPVVILDEATAEAG-TTAAGLLDQAAELAVTGR-TAVVIAHRLSQAVRADRILVMSGGRVVESGTHDEL 575
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDpDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
357-570 |
6.31e-17 |
|
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: 79.88 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIddlsdAELRHKVVLVSQ 436
Cdd:cd03235 2 VEDLTVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 EVHV---FVGTIAD--------DLRLCAPDS--DDAKITEAVEtmkaqwihelpdgletRVGAGGY------QLTAAQAQ 497
Cdd:cd03235 76 RRSIdrdFPISVRDvvlmglygHKGLFRRLSkaDKAKVDEALE----------------RVGLSELadrqigELSGGQQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 498 HI----ALV---RLALLDPPVVILDeataeaGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMsGGRVVES 569
Cdd:cd03235 140 RVllarALVqdpDLLLLDEPFAGVD------PKTQEDIYELLRELRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVAS 212
|
.
gi 532492226 570 G 570
Cdd:cd03235 213 G 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
355-579 |
6.91e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 80.52 E-value: 6.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIddlsdAELRHKVVLV 434
Cdd:COG1121 7 IELENLTVSYGG-RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHV----------FV--GTIADDLRLCAPDSDD-AKITEAVETMKAQwihelpdGLETR-VGA--GGyQLtaaQ--- 495
Cdd:COG1121 81 PQRAEVdwdfpitvrdVVlmGRYGRRGLFRRPSRADrEAVDEALERVGLE-------DLADRpIGElsGG-QQ---Qrvl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 496 -AQhiALV---RLALLDPPVVILDeataeaGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSgGRVVESG 570
Cdd:COG1121 150 lAR--ALAqdpDLLLLDEPFAGVD------AATEEALYELLRELRREGKTILVVTHDLGAVREyFDRVLLLN-RGLVAHG 220
|
....*....
gi 532492226 571 THDELIGAD 579
Cdd:COG1121 221 PPEEVLTPE 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
357-515 |
2.12e-16 |
|
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: 77.90 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDlSDAELRHKVVLVSQ 436
Cdd:COG4133 5 AENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 EVHVFVG-TIADDLRLCA----PDSDDAKITEAVETMkaqwihELPDGLETRVGaggyQLTAAQAQHIALVRLALLDPPV 511
Cdd:COG4133 83 ADGLKPElTVRENLRFWAalygLRADREAIDEALEAV------GLAGLADLPVR----QLSAGQKRRVALARLLLSPAPL 152
|
....
gi 532492226 512 VILD 515
Cdd:COG4133 153 WLLD 156
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
371-575 |
2.37e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.52 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVV---------LVSQEVHVF 441
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSdiqmifqdpLASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 442 VG-TIADDLRLCAPDSDDAKITEAVETMKAQwIHELPDgLETRVgagGYQLTAAQAQHIALVRLALLDPPVVILDEATAE 520
Cdd:PRK15079 117 IGeIIAEPLRTYHPKLSRQEVKDRVKAMMLK-VGLLPN-LINRY---PHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 521 agttaaglLDQAAELAVT----------GRTAVVIAHRLSqAVR--ADRILVMSGGRVVESGTHDEL 575
Cdd:PRK15079 192 --------LDVSIQAQVVnllqqlqremGLSLIFIAHDLA-VVKhiSDRVLVMYLGHAVELGTYDEV 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
109-566 |
2.67e-16 |
|
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: 83.04 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 109 VLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVeavnTVIARVLPATVSALfmISLTLVGVGVIdwrFTVAI---- 184
Cdd:TIGR01271 956 VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDM----AIIDDMLPLTLFDF--IQLTLIVLGAI---FVVSVlqpy 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 185 --VAVAPIH--YFALR-HFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTD--EHIGRIAETSEHAISFDMQA 257
Cdd:TIGR01271 1027 ifIAAIPVAviFIMLRaYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSyfETLFHKALNLHTANWFLYLS 1106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 258 VrLRTnFFAQLNGAELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARLIGVTAM 337
Cdd:TIGR01271 1107 T-LRW-FQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQE 1184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 338 PGRPASI--------------PASARSAPIG--VDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKL 400
Cdd:TIGR01271 1185 EPRPSGGggkyqlstvlvienPHAQKCWPSGgqMDVQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSA 1264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 401 IAGIIPVgDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDA--KITEAVeTMKAQwIHELPD 478
Cdd:TIGR01271 1265 LLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEiwKVAEEV-GLKSV-IEQFPD 1341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 479 GLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRI 558
Cdd:TIGR01271 1342 KLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQF 1421
|
....*...
gi 532492226 559 LVMSGGRV 566
Cdd:TIGR01271 1422 LVIEGSSV 1429
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
372-578 |
3.35e-16 |
|
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: 81.65 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 372 DSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGdGRITVDGTPIDDLSDAELRHkvvLVSQEVHVF---------- 441
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRP---LRRRMQVVFqdpfgslspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 442 --VG-TIADDLRLCAPDSDDAKITEAV----------ETMKAQWIHELpdgletrvgAGGyqltaaQAQHIALVRlAL-L 507
Cdd:COG4172 379 mtVGqIIAEGLRVHGPGLSAAERRARVaealeevgldPAARHRYPHEF---------SGG------QRQRIAIAR-ALiL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 508 DPPVVILDEATAEagttaaglLD---QA------AELAVT-GRTAVVIAHRLSqAVRA--DRILVMSGGRVVESGTHDEL 575
Cdd:COG4172 443 EPKLLVLDEPTSA--------LDvsvQAqildllRDLQREhGLAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPTEQV 513
|
...
gi 532492226 576 IGA 578
Cdd:COG4172 514 FDA 516
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
355-575 |
3.53e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.98 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY-----DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDA-ELR 428
Cdd:PRK13633 5 IKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 429 HKVVLVSQEV-HVFVGTIADDLRLCAPDS---DDAKITEAVEtmkaqwihelpDGLEtRVGAGGYQ------LTAAQAQH 498
Cdd:PRK13633 85 NKAGMVFQNPdNQIVATIVEEDVAFGPENlgiPPEEIRERVD-----------ESLK-KVGMYEYRrhaphlLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 499 IALVRLALLDPPVVILDEATAeagttaagLLDQAAELAVT----------GRTAVVIAHRLSQAVRADRILVMSGGRVVE 568
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTA--------MLDPSGRREVVntikelnkkyGITIILITHYMEEAVEADRIIVMDSGKVVM 224
|
....*..
gi 532492226 569 SGTHDEL 575
Cdd:PRK13633 225 EGTPKEI 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
355-570 |
4.72e-16 |
|
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: 77.30 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAElrHKVVLV 434
Cdd:cd03301 1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEV----HVFV-GTIADDLRL--CAPDSDDAKITEAVETMKaqwIHELPDGLETrvgaggyQLTAAQAQHIALVRLALL 507
Cdd:cd03301 78 FQNYalypHMTVyDNIAFGLKLrkVPKDEIDERVREVAELLQ---IEHLLDRKPK-------QLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 508 DPPVVILDEATAEagttaaglLDqaAELAVT------------GRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:cd03301 148 EPKVFLMDEPLSN--------LD--AKLRVQmraelkrlqqrlGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
379-570 |
6.66e-16 |
|
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: 76.95 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 379 APGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDlSDAEL-----RHKVVLVSQEVHVF-----VGTIADD 448
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKInlppqQRKIGLVFQQYALFphlnvRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 449 LRLCAPDSDDAKITEAVETMkaqwihelpdGLETRVGAGGYQLTAAQAQHIALVR-------LALLDPPVVILDeaTAEA 521
Cdd:cd03297 100 LKRKRNREDRISVDELLDLL----------GLDHLLNRYPAQLSGGEKQRVALARalaaqpeLLLLDEPFSALD--RALR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 532492226 522 GTTAAGLLDQAAELavtGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:cd03297 168 LQLLPELKQIKKNL---NIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
295-582 |
9.40e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.23 E-value: 9.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 295 GAATAAALYFHSLFsPIAVFLSNIDELQDAGAslaRLIGVTAMPGRpasipasarsapigVDVKRVSYSYDN--STPVID 372
Cdd:PTZ00265 1124 GDSENAKLSFEKYY-PLIIRKSNIDVRDNGGI---RIKNKNDIKGK--------------IEIMDVNFRYISrpNVPIYK 1185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 373 SISISIAPGERIAVVGSSGAGKTTLAKLI-----------------------------------AGIIPVGD-------- 409
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgdeeqnVGMKNVNEfsltkegg 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 410 -----------GRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKA-QWIHELP 477
Cdd:PTZ00265 1266 sgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIdEFIESLP 1345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 478 DGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQA-AELA-VTGRTAVVIAHRLSQAVRA 555
Cdd:PTZ00265 1346 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTiVDIKdKADKTIITIAHRIASIKRS 1425
|
330 340 350
....*....|....*....|....*....|...
gi 532492226 556 DRILVM-----SGGRVVESGTHDELIGA-DGSY 582
Cdd:PTZ00265 1426 DKIVVFnnpdrTGSFVQAHGTHEELLSVqDGVY 1458
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
355-565 |
1.02e-15 |
|
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: 75.30 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSD--AELRHKVV 432
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVHVFVG-TIADDLRLcapdsddakiteavetmkaqwihelpdGLetrvgAGGyqltaaQAQHIALVRLALLDPPV 511
Cdd:cd03229 80 MVFQDFALFPHlTVLENIAL---------------------------GL-----SGG------QQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 512 VILDEATAEA-GTTAAGLLDQAAEL-AVTGRTAVVIAHRLSQAVR-ADRILVMSGGR 565
Cdd:cd03229 122 LLLDEPTSALdPITRREVRALLKSLqAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
355-565 |
1.05e-15 |
|
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: 75.97 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYD----NSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTpiddlsdaelrhk 430
Cdd:cd03250 1 ISVEDASFTWDsgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 431 VVLVSQEVHVFVGTIADD---------------LRLCAPDSDdakiteavetmkaqwIHELPDGLETRVGAGGYQLTAAQ 495
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENilfgkpfdeeryekvIKACALEPD---------------LEILPDGDLTEIGEKGINLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 496 AQHIALVRLALLDPPVVILD-EATAEAGTTAAGLLDQA-AELAVTGRTAVVIAHRLSQAVRADRILVMSGGR 565
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDdPLSAVDAHVGRHIFENCiLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
368-576 |
1.07e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 368 TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE-LRHKVVLVSQEVHVFVG-TI 445
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 446 ADDLRLCAPDS-----DDAKITEAVETMKAQWihELPDGLETRVGaggyQLTAAQAQHIALVRlAL-LDPPVVILDeata 519
Cdd:COG1129 97 AENIFLGREPRrggliDWRAMRRRARELLARL--GLDIDPDTPVG----DLSVAQQQLVEIAR-ALsRDARVLILDepta 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 520 e-agttAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG-----THDELI 576
Cdd:COG1129 170 sltereVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELV 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
355-570 |
1.26e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 75.78 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIddlsDAELRHKVVLV 434
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVG-TIADDLRLCApDSDDAKITEAvetmkAQWIHELpdgLEtRVGAGGY------QLTAAQAQHIALVRLALL 507
Cdd:cd03269 76 PEERGLYPKmKVIDQLVYLA-QLKGLKKEEA-----RRRIDEW---LE-RLELSEYankrveELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 508 DPPVVILDEATAEAGTTAAGLLDQA-AELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDViRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
358-429 |
1.73e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.86 E-value: 1.73e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 358 KRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRH 429
Cdd:COG2884 5 ENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPY 76
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
355-576 |
1.75e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 76.28 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDD--LSDAELRHKVV 432
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVHVFVGTIADDLRLCAPdsddakitEAVETMKAQWIHELPDGLETRVG----AGGY--QLTAAQAQHIALVR--- 503
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGP--------LRVRGASKEEAEKQARELLAKVGlaerAHHYpsELSGGQQQRVAIARala 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 504 ----LALLDPPVVILDeataeaGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELI 576
Cdd:PRK09493 153 vkpkLMLFDEPTSALD------PELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
355-575 |
1.85e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.19 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAElRHkVVLV 434
Cdd:COG3839 4 LELENVSKSYGG-VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RN-IAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEV----HVfvgTIADD----LRLCAPDSD--DAKITEAVETMKaqwIHELpdgLETRVGaggyQLTAAQAQHIALVRl 504
Cdd:COG3839 81 FQSYalypHM---TVYENiafpLKLRKVPKAeiDRRVREAAELLG---LEDL---LDRKPK----QLSGGQRQRVALGR- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 505 AL-LDPPVVILDeataeagttaaglLDqaAELAV------------TGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:COG3839 147 ALvREPKVFLLDepl--------snLD--AKLRVemraeikrlhrrLGTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVG 216
|
....*
gi 532492226 571 THDEL 575
Cdd:COG3839 217 TPEEL 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
355-566 |
2.25e-15 |
|
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: 76.82 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVgDGRITVDGTPIDDLSDAELRHKVVL 433
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKAQWIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVI 513
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 532492226 514 LDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRV 566
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
355-575 |
2.57e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.69 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNST--PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVV 432
Cdd:PRK13650 5 IEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEV-HVFVG-TIADDLrlcAPDSDDAKIteAVETMKAQWIHELP----DGLETRVGAggyQLTAAQAQHIALVRLAL 506
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDV---AFGLENKGI--PHEEMKERVNEALElvgmQDFKEREPA---RLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 507 LDPPVVILDeataeagtTAAGLLDQAAELAVT----------GRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDEL 575
Cdd:PRK13650 157 MRPKIIILD--------EATSMLDPEGRLELIktikgirddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
47-303 |
2.69e-15 |
|
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: 76.78 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 47 LLSATACGLSTPALLGLMVDAVTEGKPF-----VSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAAT 121
Cdd:cd18573 5 LLVSSAVTMSVPFAIGKLIDVASKESGDieifgLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 122 LAQPSSLVEDAGTGDLISRVSGDV----EAVNTVIARVLPATVSA------LFMISLTLVGVGVIdwrfTVAIVAVAPIH 191
Cdd:cd18573 85 LRQDAAFFDKNKTGELVSRLSSDTsvvgKSLTQNLSDGLRSLVSGvggigmMLYISPKLTLVMLL----VVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 192 YfalRHFLRRsgpVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGA 271
Cdd:cd18573 161 Y---GRYVRK---LSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFS 234
|
250 260 270
....*....|....*....|....*....|..
gi 532492226 272 ELLGLAAVLSVGYWLVTTGSVSIGAATAAALY 303
Cdd:cd18573 235 GNLSLLSVLYYGGSLVASGELTVGDLTSFLMY 266
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
355-575 |
4.05e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.88 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPI--DDLSDAELRHKVV 432
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQ--EVHVFVGTIADD-----LRLCAPDSD-DAKITEAVEtmkaqwihelpdgletRVGAGGYQ------LTAAQAQH 498
Cdd:PRK13639 82 IVFQnpDDQLFAPTVEEDvafgpLNLGLSKEEvEKRVKEALK----------------AVGMEGFEnkpphhLSGGQKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 499 IALVRLALLDPPVVILDE-ATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQA-VRADRILVMSGGRVVESGTHDEL 575
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEpTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
354-575 |
4.37e-15 |
|
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: 75.07 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 354 GVDVKRVSYSYDNStPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGtpiDDLSDAELRHKVV- 432
Cdd:cd03296 2 SIEVRNVSKRFGDF-VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQERNVg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVHVFVG-TIADDL--------RLCAPDSD--DAKITEAVETMKAQWihelpdgLETRVGAggyQLTAAQAQHIAL 501
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVafglrvkpRSERPPEAeiRAKVHELLKLVQLDW-------LADRYPA---QLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 502 VRLALLDPPVVILDEATAEagttaaglLDQAA--ELAV--------TGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGA--------LDAKVrkELRRwlrrlhdeLHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVG 219
|
....*
gi 532492226 571 THDEL 575
Cdd:cd03296 220 TPDEV 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
355-428 |
5.07e-15 |
|
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: 75.02 E-value: 5.07e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 355 VDVKRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELR 428
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
370-570 |
8.50e-15 |
|
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: 73.56 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGtpIDDLSD-AELRHKVVLVS-----------QE 437
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEpAEARRRLGFVSdstglydrltaRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 438 VHVFVGtiadDLRLCAPDSDDAKITEAVETMkaqwihELPDGLETRVGAggyqLTAAQAQHIALVRLALLDPPVVILDEA 517
Cdd:cd03266 98 NLEYFA----GLYGLKGDELTARLEELADRL------GMEELLDRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 518 TAEA-GTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:cd03266 164 TTGLdVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
355-578 |
8.76e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAeLRHK--VV 432
Cdd:PRK15439 12 LCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQlgIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVHVFVG-TIADD--LRLCAPDSDDAKITEAVETMKAQwihelpdgLETRVGAGgyQLTAAQAQHIALVRLALLDP 509
Cdd:PRK15439 90 LVPQEPLLFPNlSVKENilFGLPKRQASMQKMKQLLAALGCQ--------LDLDSSAG--SLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 510 PVVILDE-ATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQaVR--ADRILVMSGGRVVESG-----THDELIGA 578
Cdd:PRK15439 160 RILILDEpTASLTPAETERLFSRIRELLAQGVGIVFISHKLPE-IRqlADRISVMRDGTIALSGktadlSTDDIIQA 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
355-566 |
1.04e-14 |
|
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: 73.33 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDA--ELRHKVV 432
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVHVFVG-TIADDlrlcapdsddakITEA---VETMKAQWIHELPDGLETRVG----AGGY--QLTAAQAQHIALV 502
Cdd:cd03262 80 MVFQQFNLFPHlTVLEN------------ITLApikVKGMSKAEAEERALELLEKVGladkADAYpaQLSGGQQQRVAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 503 R-LAL-------------LDPPVVildeataeagttaAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRV 566
Cdd:cd03262 148 RaLAMnpkvmlfdeptsaLDPELV-------------GEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
355-575 |
1.10e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.74 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPV--IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVV 432
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEV-HVFVGTIADDLRLCAPDSDDAKITEAVETMKAQWIHELPDGLETRVGAggyQLTAAQAQHIALVRLALLDPPV 511
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPA---RLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 512 VILDeataeagttaagllDQAAELAVTGRTAVV----------------IAHRLSQAVRADRILVMSGGRVVESGTHDEL 575
Cdd:PRK13642 162 IILD--------------ESTSMLDPTGRQEIMrviheikekyqltvlsITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
357-574 |
1.14e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.70 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDNSTP----VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDD--LSDAELRHK 430
Cdd:PRK13637 5 IENLTHIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 431 VVLVSQ--EVHVFVGTIADDL-----RLCAPDSD-DAKITEAVETMKAQWihelpDGLETRvgaGGYQLTAAQAQHIALV 502
Cdd:PRK13637 85 VGLVFQypEYQLFEETIEKDIafgpiNLGLSEEEiENRVKRAMNIVGLDY-----EDYKDK---SPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 503 RLALLDPPVVILDeataeagttaagllDQAAELAVTGR----------------TAVVIAHRLSQAVR-ADRILVMSGGR 565
Cdd:PRK13637 157 GVVAMEPKILILD--------------EPTAGLDPKGRdeilnkikelhkeynmTIILVSHSMEDVAKlADRIIVMNKGK 222
|
....*....
gi 532492226 566 VVESGTHDE 574
Cdd:PRK13637 223 CELQGTPRE 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
339-579 |
1.98e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.87 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 339 GRPASIPASARS-APIGVDVKRVSYSYDNStPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGT 417
Cdd:PRK13536 25 GISEAKASIPGSmSTVAIDLAGVSKSYGDK-AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 418 PIDDLSDAElRHKVVLVSQevhvfvgtiADDLRLCAPDSDDAKITEAVETMKAQWIHE-LPD-----GLETRVGAGGYQL 491
Cdd:PRK13536 104 PVPARARLA-RARIGVVPQ---------FDNLDLEFTVRENLLVFGRYFGMSTREIEAvIPSllefaRLESKADARVSDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 492 TAAQAQHIALVRLALLDPPVVILDEATAEAGTTAAGLL-DQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGR-VVE 568
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGRkIAE 253
|
250
....*....|....
gi 532492226 569 SGTH---DELIGAD 579
Cdd:PRK13536 254 GRPHaliDEHIGCQ 267
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
40-299 |
2.09e-14 |
|
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: 73.97 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFA 119
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 120 ATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFL 199
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 200 RRSGPVYRRSraaqarrgQQLI--------ETLGGAGTVTALRRTDEHIGRIAETSEhaisfDMQAVRLRTN-FFAQLNG 270
Cdd:cd18548 161 KKAIPLFKKV--------QKKLdrlnrvvrENLTGIRVIRAFNREDYEEERFDKAND-----DLTDTSLKAGrLMALLNP 227
|
250 260 270
....*....|....*....|....*....|...
gi 532492226 271 AELL----GLAAVLSVGYWLVTTGSVSIGAATA 299
Cdd:cd18548 228 LMMLimnlAIVAILWFGGHLINAGSLQVGDLVA 260
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
355-575 |
2.57e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.74 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSdAELRHkVVLV 434
Cdd:PRK10851 3 IEIANIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-ARDRK-VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVG-TIADDL--------RLCAPDSD--DAKITEAVETMkaQWIHelpdgLETRVGAggyQLTAAQAQHIALVR 503
Cdd:PRK10851 80 FQHYALFRHmTVFDNIafgltvlpRRERPNAAaiKAKVTQLLEMV--QLAH-----LADRYPA---QLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 504 -LA------LLDPPVVILDEATAEAGTTAAGLLDQaaELAVTGrtaVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDEL 575
Cdd:PRK10851 150 aLAvepqilLLDEPFGALDAQVRKELRRWLRQLHE--ELKFTS---VFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
343-414 |
2.99e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.49 E-value: 2.99e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 343 SIPASARSAPIGVDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITV 414
Cdd:COG0488 304 RFPPPERLGKKVLELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
354-575 |
4.31e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.64 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 354 GVDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTpiddlsDAELRHKVvl 433
Cdd:COG1118 2 SIEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR------DLFTNLPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 vsQEVHV-FVG---------TIADD----LRLCAPDSddAKITEAVEtmkaQWIHELP-DGLETRvgaggY--QLTAAQA 496
Cdd:COG1118 73 --RERRVgFVFqhyalfphmTVAENiafgLRVRPPSK--AEIRARVE----ELLELVQlEGLADR-----YpsQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 497 QHIALVR-LA------LLDPPVVILDEATaeagttaaglldqAAEL--------AVTGRTAVVIAHRLSQAVR-ADRILV 560
Cdd:COG1118 140 QRVALARaLAvepevlLLDEPFGALDAKV-------------RKELrrwlrrlhDELGGTTVFVTHDQEEALElADRVVV 206
|
250
....*....|....*
gi 532492226 561 MSGGRVVESGTHDEL 575
Cdd:COG1118 207 MNQGRIEQVGTPDEV 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
373-574 |
6.22e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 373 SISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPvGDGRITVDGTPIDDLSDAEL-RHKVVLVSQEVHVFVGTIADDLRL 451
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 452 CAPDSDDAKITEAVETMKAQWIhELPDGLETRVGaggyQLTAAQAQHIALV--------------RLALLDPPVVILDea 517
Cdd:PRK03695 93 HQPDKTRTEAVASALNEVAEAL-GLDDKLGRSVN----QLSGGEWQRVRLAavvlqvwpdinpagQLLLLDEPMNSLD-- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 518 taeagTTAAGLLDQ-AAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDE 574
Cdd:PRK03695 166 -----VAQQAALDRlLSELCQQGIAVVMSSHDLNHTLRhADRVWLLKQGKLLASGRRDE 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
370-568 |
6.23e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.03 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE---LRHKVVLVSQEV-------H 439
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDSisavnprK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 440 VFVGTIADDLRLCAPDSDDAKITEAVETMKAQwihELPDGLETRVGAggyQLTAAQAQHIALVRLALLDPPVVILDEATA 519
Cdd:PRK10419 107 TVREIIREPLRHLLSLDKAERLARASEMLRAV---DLDDSVLDKRPP---QLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 520 EA-GTTAAGLLDQAAELAVTGRTA-VVIAHRLSQAVR-ADRILVMSGGRVVE 568
Cdd:PRK10419 181 NLdLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
369-570 |
9.16e-14 |
|
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: 70.32 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 369 PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAeLRHKVVLVsqEVHVFVG--TIA 446
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-LRRIGALI--EAPGFYPnlTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 447 DDLRL--CAPDSDDAKITEAVETMkaqwihelpdGLETR--VGAGGYQLTAAQAQHIAlvrLALL-DPPVVILDEATAEa 521
Cdd:cd03268 91 ENLRLlaRLLGIRKKRIDEVLDVV----------GLKDSakKKVKGFSLGMKQRLGIA---LALLgNPDLLILDEPTNG- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 522 gttaaglLDQAA---------ELAVTGRTAVVIAHRLS--QAVrADRILVMSGGRVVESG 570
Cdd:cd03268 157 -------LDPDGikelrelilSLRDQGITVLISSHLLSeiQKV-ADRIGIINKGKLIEEG 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
304-583 |
1.20e-13 |
|
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: 74.60 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 304 FHSLFSPIAVFLSNIDELQDAGASLARL-IGVTAMPGRPASIPASARSAPIG--VDVKRVSYSYDNSTP-VIDSISISIA 379
Cdd:TIGR00957 583 FNILRFPLNILPMVISSIVQASVSLKRLrIFLSHEELEPDSIERRTIKPGEGnsITVHNATFTWARDLPpTLNGITFSIP 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 380 PGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTpiddlsdaelrhkVVLVSQEVHVFVGTIADDLRLCAPDSDD- 458
Cdd:TIGR00957 663 EGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKALNEKy 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 459 -AKITEAVETMKAQWIheLPDGLETRVGAGGYQLTAAQAQHIALVR-------LALLDPPVVILDEATAEAGTTAAGlld 530
Cdd:TIGR00957 730 yQQVLEACALLPDLEI--LPSGDRTEIGEKGVNLSGGQKQRVSLARavysnadIYLFDDPLSAVDAHVGKHIFEHVI--- 804
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 532492226 531 qAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADGSYA 583
Cdd:TIGR00957 805 -GPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFA 856
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
355-571 |
1.25e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.42 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY---DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL---R 428
Cdd:COG1135 2 IELENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 429 HKVVLVSQevH--------VFvGTIADDLRLCapDSDDAKITEAVEtmkaqwihELPD--GLETRVGAggY--QLTAAQA 496
Cdd:COG1135 82 RKIGMIFQ--HfnllssrtVA-ENVALPLEIA--GVPKAEIRKRVA--------ELLElvGLSDKADA--YpsQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 497 QHIALVRlAL-LDPPVV----------------ILDeataeagttaagLLDQA-AELavtGRTAVVIAHRLSqAVR--AD 556
Cdd:COG1135 147 QRVGIAR-ALaNNPKVLlcdeatsaldpettrsILD------------LLKDInREL---GLTIVLITHEMD-VVRriCD 209
|
250
....*....|....*
gi 532492226 557 RILVMSGGRVVESGT 571
Cdd:COG1135 210 RVAVLENGRIVEQGP 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
229-575 |
1.31e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 229 TVTALRRTDEHIGRIAE-----------TSEHAISFDMQAVRlrTNFFAQLNGAELLG------------LAAVLSVGYW 285
Cdd:PLN03232 468 TKEGLQWTDKRVGIINEilasmdtvkcyAWEKSFESRIQGIR--NEELSWFRKAQLLSafnsfilnsipvVVTLVSFGVF 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 286 LVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARLIGVTAMPGRP-ASIPASARSAPiGVDVKRVSYSY 364
Cdd:PLN03232 546 VLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERIlAQNPPLQPGAP-AISIKNGYFSW 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 365 DNST--PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPvgdgritvdgtPIDDLSdAELRHKVVLVSQEVHVFV 442
Cdd:PLN03232 625 DSKTskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-----------HAETSS-VVIRGSVAYVPQVSWIFN 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 443 GTIADDLrLCAPDSDDAKITEAVETMKAQwiHEL---PDGLETRVGAGGYQLTAAQAQHIALVR-------LALLDPPVV 512
Cdd:PLN03232 693 ATVRENI-LFGSDFESERYWRAIDVTALQ--HDLdllPGRDLTEIGERGVNISGGQKQRVSMARavysnsdIYIFDDPLS 769
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 513 ILDeataeaGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDEL 575
Cdd:PLN03232 770 ALD------AHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
355-515 |
1.66e-13 |
|
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: 69.74 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSD---AELRHKV 431
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraiPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 432 VLVSQEVHVFVG-TIADDLrlcapdsddAKITEAVETMKAQWIHELPD-----GLETRVGAGGYQLTAAQAQHIALVRLA 505
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENV---------AFALEVTGVPPREIRKRVPAalelvGLSHKHRALPAELSGGEQQRVAIARAI 151
|
170
....*....|
gi 532492226 506 LLDPPVVILD 515
Cdd:cd03292 152 VNSPTILIAD 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
355-562 |
1.90e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPV--IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITV-DGTPIDDLSDAELRHKV 431
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 432 VLVSQEVHVFVGTIADDLRL-----------------------------------CAPDSDDA----------------- 459
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqenknkrnscrakCAGDLNDMsnttdsneliemrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 460 --KITEAVETMKAQWIHE----LPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEagttaaglLDQAA 533
Cdd:PTZ00265 543 tiKDSEVVDVSKKVLIHDfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSS--------LDNKS 614
|
250 260 270
....*....|....*....|....*....|....*....
gi 532492226 534 ELAVT----------GRTAVVIAHRLSQAVRADRILVMS 562
Cdd:PTZ00265 615 EYLVQktinnlkgneNRITIIIAHRLSTIRYANTIFVLS 653
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
371-576 |
2.20e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.37 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRH----KVVLVSQEVHVFVG-TI 445
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 446 AD------DLRLCAPDSDDAKITEAVETMKAQ-WIHELPDgletrvgaggyQLTAAQAQHIALVRLALLDPPVVILDEA- 517
Cdd:PRK10070 124 LDntafgmELAGINAEERREKALDALRQVGLEnYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAf 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532492226 518 TAEAGTTAAGLLDQAAEL-AVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELI 576
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
355-585 |
3.03e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLV 434
Cdd:PRK09536 4 IDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVH----------VFVGTIADDLRLCAPDSDDAKITEavETMKAQWIHELPDGLETRVGAGGYQ---LTAAQAQHIAL 501
Cdd:PRK09536 83 PQDTSlsfefdvrqvVEMGRTPHRSRFDTWTETDRAAVE--RAMERTGVAQFADRPVTSLSGGERQrvlLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 502 VrlaLLDPPVVILDEATAEAGttaaglLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG------THDE 574
Cdd:PRK09536 161 L---LLDEPTASLDINHQVRT------LELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGppadvlTADT 231
|
250
....*....|.
gi 532492226 575 LIGADGSYAAL 585
Cdd:PRK09536 232 LRAAFDARTAV 242
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
355-586 |
3.51e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.19 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTP----VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPI-DDLSDAELRH 429
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 430 ---KVVLVSQ--EVHVFVGTIADDLrLCAPDSDDAKITEaVETMKAQWIHELpdGLETRV-GAGGYQLTAAQAQHIALVR 503
Cdd:PRK13646 83 vrkRIGMVFQfpESQLFEDTVEREI-IFGPKNFKMNLDE-VKNYAHRLLMDL--GFSRDVmSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 504 LALLDPPVVILDEATAEagttaaglLDQAAELAVT----------GRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTH 572
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAG--------LDPQSKRQVMrllkslqtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSP 230
|
250
....*....|....
gi 532492226 573 DELIGaDGSYAALW 586
Cdd:PRK13646 231 KELFK-DKKKLADW 243
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
47-332 |
4.00e-13 |
|
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: 70.56 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 47 LLSATACGLSTPA---LLGLMVDAVTEGKP--FVSLLRITAFMLSAAAAGVALTWW-STQLLANVAQNVLADLREDVFAA 120
Cdd:cd18578 15 LIGAIIAGAVFPVfaiLFSKLISVFSLPDDdeLRSEANFWALMFLVLAIVAGIAYFlQGYLFGIAGERLTRRLRKLAFRA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 121 TLAQPSSL--VEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVgVG-VIDWRFTVAIVAVAPIHYFALRH 197
Cdd:cd18578 95 ILRQDIAWfdDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLI-IAfVYGWKLALVGLATVPLLLLAGYL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 198 FLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLA 277
Cdd:cd18578 174 RMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYA 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 278 AVLSVGYWLVTTGSVSIG-----------AATAAAlyfhSLFSpiavFLSNIDELQDAGASLARLI 332
Cdd:cd18578 254 LAFWYGGRLVANGEYTFEqffivfmalifGAQSAG----QAFS----FAPDIAKAKAAAARIFRLL 311
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
370-576 |
4.20e-13 |
|
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: 69.29 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAelRHKVVLVSQEVHVF-----VGT 444
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFphmtvYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 445 IADDLRLCAPD--SDDAKITEAVETMK-AQWIHELPDGLetrvgAGGYQLTAAQAQhiALV---RLALLDPPVVILDEAT 518
Cdd:cd03299 92 IAYGLKKRKVDkkEIERKVLEIAEMLGiDHLLNRKPETL-----SGGEQQRVAIAR--ALVvnpKILLLDEPFSALDVRT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 519 AEAGTTaaglldqaaELAVTGR----TAVVIAHRLSQA-VRADRILVMSGGRVVESGTHDELI 576
Cdd:cd03299 165 KEKLRE---------ELKKIRKefgvTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
355-575 |
4.20e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.83 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLV 434
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQ--EVHVFVGTIADDLRL--CAPDSDDAKITEAVETMkaqwIHELpdGLETRVGAGGYQLTAAQAQHIALVRLALLDPP 510
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFgpINLGLDEETVAHRVSSA----LHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 511 VVILDE-ATAEAGTTAAGLLDQAAELAVT-GRTAVVIAHRLSQ-AVRADRILVMSGGRVVESGTHDEL 575
Cdd:PRK13652 158 VLVLDEpTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLvPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-567 |
4.70e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.34 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 366 NSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAElRHKvvLVSQevhVF---- 441
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAK--YIGR---VFqdpm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 442 VGT-----------IADD------LRLCAPDSDDAKITEAVETMKAQwiheLPDGLETRVGA--GGyqltaaQAQHIALV 502
Cdd:COG1101 91 MGTapsmtieenlaLAYRrgkrrgLRRGLTKKRRELFRELLATLGLG----LENRLDTKVGLlsGG------QRQALSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 503 rLALLDPPVVIldeataeagttaagLLD--------QAAE--LAVTGR-------TAVVIAHRLSQAVR-ADRILVMSGG 564
Cdd:COG1101 161 -MATLTKPKLL--------------LLDehtaaldpKTAAlvLELTEKiveennlTTLMVTHNMEQALDyGNRLIMMHEG 225
|
...
gi 532492226 565 RVV 567
Cdd:COG1101 226 RII 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
233-576 |
4.93e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.46 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 233 LRRTDEHIGRIAETSEhAI----------SFDMQAVRLRTNFFAQLNGAELLG------------LAAVLSVGYWLVTTG 290
Cdd:PLN03130 472 LQRTDKRIGLMNEVLA-AMdtvkcyawenSFQSKVQTVRDDELSWFRKAQLLSafnsfilnsipvLVTVVSFGVFTLLGG 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 291 SVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARLIGVTAMPGRPASIPASARSAPIGVDVKRVSYSYD--NST 368
Cdd:PLN03130 551 DLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGLPAISIKNGYFSWDskAER 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 369 PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIP-VGDGRITVDGTpiddlsdaelrhkVVLVSQEVHVFVGTIAD 447
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPpRSDASVVIRGT-------------VAYVPQVSWIFNATVRD 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 448 DLRLCAPdSDDAKITEAVETMKAQwiHE---LPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDE-ATAEAGT 523
Cdd:PLN03130 698 NILFGSP-FDPERYERAIDVTALQ--HDldlLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDpLSALDAH 774
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 532492226 524 TAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELI 576
Cdd:PLN03130 775 VGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS 827
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
371-575 |
5.45e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIP---VGDGRITVDGTPIddlsDAELRHKVVLVSQEVHVFVGTI-A 446
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPI----DAKEMRAISAYVQQDDLFIPTLtV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 447 DD-------LRLCAPDSDDAKItEAVEtmkaQWIHELpdGL----ETRVGAGGYQ--LTAAQAQHIALVRLALLDPPVVI 513
Cdd:TIGR00955 117 REhlmfqahLRMPRRVTKKEKR-ERVD----EVLQAL--GLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 514 LDEATAEAGTTAAGLLDQA-AELAVTGRTAVVIAHRLSQAVRA--DRILVMSGGRVVESGTHDEL 575
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVlKGLAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
370-574 |
6.95e-13 |
|
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: 68.62 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL-RHKVVLVSQEVHVFVG-TIAD 447
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 448 DLRLCA----PDSDDAKITEAVETMKAQWIHELpdgLEtRVGAGGY------QLTAAQAQHIALVRLALLDPPVVILDEA 517
Cdd:cd03219 95 NVMVAAqartGSGLLLARARREEREARERAEEL---LE-RVGLADLadrpagELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 518 TA-EAGTTAAGLLDQAAELAVTGRTAVVIAHRLSqAVR--ADRILVMSGGRVVESGTHDE 574
Cdd:cd03219 171 AAgLNPEETEELAELIRELRERGITVLLVEHDMD-VVMslADRVTVLDQGRVIAEGTPDE 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
357-568 |
7.86e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.57 E-value: 7.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDnSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSdAE----LRHKVV 432
Cdd:PRK11248 4 ISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AErgvvFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVhvfVGTIADDLRLcAPDSDDAKITEAVETMKAQwihelpdGLEtrvGAGG---YQLTAAQAQHIALVR------ 503
Cdd:PRK11248 82 LPWRNV---QDNVAFGLQL-AGVEKMQRLEIAHQMLKKV-------GLE---GAEKryiWQLSGGQRQRVGIARalaanp 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 504 -LALLDPPVVILDEATAeagttaagllDQAAELAV-----TGRTAVVIAHRLSQAV--RADRILVMSG-GRVVE 568
Cdd:PRK11248 148 qLLLLDEPFGALDAFTR----------EQMQTLLLklwqeTGKQVLLITHDIEEAVfmATELVLLSPGpGRVVE 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
355-575 |
9.27e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLI-------AGIIPVGDgrITVDGT-PIDDLSDA- 425
Cdd:PRK11264 4 IEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVGD--ITIDTArSLSQQKGLi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 426 -ELRHKVVLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVETMKAQWIHELpdGLETRVGAGGYQLTAAQAQHIALVRL 504
Cdd:PRK11264 81 rQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 505 ALLDPPVVILDE-ATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDEL 575
Cdd:PRK11264 159 LAMRPEVILFDEpTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
42-331 |
9.95e-13 |
|
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: 69.01 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 42 LTTVVLLSA--TACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFA 119
Cdd:cd18570 4 LILILLLSLliTLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 120 ATLAQPSSLVEDAGTGDLISRVSgDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIH---YFALR 196
Cdd:cd18570 84 HLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYiliILLFN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 197 HFLRRsgpVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIaetsEHAISfDMQAVRLRTNFFAQLNGA----- 271
Cdd:cd18570 163 KPFKK---KNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKI----EKKFS-KLLKKSFKLGKLSNLQSSikgli 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 272 ELLGLAAVLSVGYWLVTTGSVSIG---AATAAALYFhslFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18570 235 SLIGSLLILWIGSYLVIKGQLSLGqliAFNALLGYF---LGPIENLINLQPKIQEAKVAADRL 294
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
370-576 |
1.21e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 71.35 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDL 449
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 450 RlcaP--DSDDAKITEAVET--MKAQWIHElPDGLETRVGAGGYQLTAAQAQHIALVRlALL--DPPVVILDEATAEAGT 523
Cdd:PTZ00243 1405 D---PflEASSAEVWAALELvgLRERVASE-SEGIDSRVLEGGSNYSVGQRQLMCMAR-ALLkkGSGFILMDEATANIDP 1479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 532492226 524 TAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELI 576
Cdd:PTZ00243 1480 ALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
368-575 |
1.60e-12 |
|
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: 68.34 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 368 TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGtpiddlsdaelrhKVVLVSQEVHVFVGTIAD 447
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 448 DLrLCAPDSDDAKITEAVETMKAQW-IHELPDGLETRVGAGGYQLTAAQAQHIALVR-------LALLDPPVVILDeata 519
Cdd:cd03291 117 NI-IFGVSYDEYRYKSVVKACQLEEdITKFPEKDNTVLGEGGITLSGGQRARISLARavykdadLYLLDSPFGYLD---- 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 520 eaGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDEL 575
Cdd:cd03291 192 --VFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
372-573 |
1.82e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 372 DSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTP--IDDLSDAeLRHKVVLVSQE---VHVFvgTIA 446
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrIRSPRDA-IALGIGMVHQHfmlVPNL--TVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 447 DDLRLCAPDSDDAKITEAVEtmkAQWIHELPD--GLE----TRVGaggyQLTAAQAQHIALVRLALLDPPVVILDeatae 520
Cdd:COG3845 99 ENIVLGLEPTKGGRLDRKAA---RARIRELSEryGLDvdpdAKVE----DLSVGEQQRVEILKALYRGARILILDept-- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 521 agttaagLLDQAAE--------LAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVesGTHD 573
Cdd:COG3845 170 -----avLTPQEADelfeilrrLAAEGKSIIFITHKLREVMAiADRVTVLRRGKVV--GTVD 224
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
45-327 |
1.96e-12 |
|
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: 67.95 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 45 VVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAATLAQ 124
Cdd:cd18572 3 VFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 125 PSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFLRRSGP 204
Cdd:cd18572 83 DIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 205 VYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAVLSVGY 284
Cdd:cd18572 163 LSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 532492226 285 WLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDA-GAS 327
Cdd:cd18572 243 HLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAvGAA 286
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
368-585 |
2.54e-12 |
|
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: 70.32 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 368 TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGtpiddlsdaelrhKVVLVSQEVHVFVGTIAD 447
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 448 DLrLCAPDSDDAKITEAVETMKAQW-IHELPDGLETRVGAGGYQLTAAQAQHIALVR-------LALLDPPVVILDeata 519
Cdd:TIGR01271 506 NI-IFGLSYDEYRYTSVIKACQLEEdIALFPEKDKTVLGEGGITLSGGQRARISLARavykdadLYLLDSPFTHLD---- 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 520 eaGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGADGSYAAL 585
Cdd:TIGR01271 581 --VVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
375-570 |
3.23e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 65.98 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 375 SISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAElrHKVVLVSQEVHVFVG-TIADD----- 448
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNvglgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 449 ---LRLCAPDSddakitEAVETMKAQwihELPDGLETRVGAggyQLTAAQAQHIALVRLALLDPPVVILDEA-TAEAGTT 524
Cdd:cd03298 96 spgLKLTAEDR------QAIEVALAR---VGLAGLEKRLPG---ELSGGERQRVALARVLVRDKPVLLLDEPfAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 532492226 525 AAGLLDQAAEL-AVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:cd03298 164 RAEMLDLVLDLhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
375-585 |
3.47e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.53 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 375 SISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGtpIDDLSDAELRHKVVLVSQEVHVFVG-TIADD----- 448
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG--QDHTTTPPSRRPVSMLFQENNLFSHlTVAQNiglgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 449 ---LRLcapdsdDAKITEAVETMKAQ-WIHELPDGLETrvgaggyQLTAAQAQHIALVR-------LALLDPPVVILDea 517
Cdd:PRK10771 97 npgLKL------NAAQREKLHAIARQmGIEDLLARLPG-------QLSGGQRQRVALARclvreqpILLLDEPFSALD-- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 518 tAEAGTTAAGLLDQAAElaVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELIGADGSYAAL 585
Cdd:PRK10771 162 -PALRQEMLTLVSQVCQ--ERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
370-574 |
3.53e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 66.60 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHK----------------V-- 431
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiartfqnprlfpeltVle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 432 -VLVSQEVHVFVGTIADDLRLCAPDSDDAKITEAVEtmkaQWIHELpdGLETRVGAGGYQLTAAQAQHIALVRLALLDPP 510
Cdd:COG0411 99 nVLVAAHARLGRGLLAALLRLPRARREEREARERAE----ELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532492226 511 VVILDeataeagttaAGLLDQAAEL-----AVTGRTAVVIAHRLSqAVR--ADRILVMSGGRVVESGTHDE 574
Cdd:COG0411 173 LLLLDepaa---glnPEETEELAELirrlrDERGITILLIEHDMD-LVMglADRIVVLDFGRVIAEGTPAE 239
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
355-575 |
3.74e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.18 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDA--ELRHKVV 432
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEV--HVFVGTIADD-----LRLCAPDSDdakITEAVE-TMKAQWIHELPDgletrvgAGGYQLTAAQAQHIALVRL 504
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDvsfgaVNLKLPEDE---VRKRVDnALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 505 ALLDPPVVILDEATA-----EAGTTAAGLLDQAAELavtGRTAVVIAHRLSQ-AVRADRILVMSGGRVVESGTHDEL 575
Cdd:PRK13636 156 LVMEPKVLVLDEPTAgldpmGVSEIMKLLVEMQKEL---GLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
334-579 |
4.11e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 334 VTAMPGRPASIPASARSAPIG---VDVKRVSysydnSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDG 410
Cdd:COG1129 233 VRLMVGRELEDLFPKRAAAPGevvLEVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 411 RITVDGTPID--DLSDAeLRHKVVLVSQEVH---VFVG-TIADDLRLCAPDS-------DDAKITEAVEtmkaQWIHEL- 476
Cdd:COG1129 308 EIRLDGKPVRirSPRDA-IRAGIAYVPEDRKgegLVLDlSIRENITLASLDRlsrggllDRRRERALAE----EYIKRLr 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 477 --PDGLETRVGA--GGYQltaaqaQHIALVRLALLDPPVVILDeataea-gttaagLLDQAAELAVTGRTAVVIAHRLSQ 551
Cdd:COG1129 383 ikTPSPEQPVGNlsGGNQ------QKVVLAKWLATDPKVLILDeptrgidvgakaeIYRLIRELAAEGKAVIVISSELPE 456
|
250 260
....*....|....*....|....*....
gi 532492226 552 AVR-ADRILVMSGGRVVesgthDELIGAD 579
Cdd:COG1129 457 LLGlSDRILVMREGRIV-----GELDREE 480
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
370-515 |
6.00e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 65.21 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDL 449
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 450 RLCAPDSDDAKITEAVETMKAQWIHELPDGletrvgaggyQLTAAQAQHIALVRLALLDPPVVILD 515
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILD 150
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
371-575 |
9.39e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.53 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPI---DDLSDAELRHKVVLVSQEVHVF------ 441
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPYGSlnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 442 VGTIADDLRLCAPDSDDAKITEAVETMKAqwihelpdgletRVG-----AGGY--QLTAAQAQHIALVRLALLDPPVVIL 514
Cdd:PRK11308 111 VGQILEEPLLINTSLSAAERREKALAMMA------------KVGlrpehYDRYphMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 515 DEATAEAGTTAAG-----LLDQAAELavtGRTAVVIAHRLSqAVR--ADRILVMSGGRVVESGTHDEL 575
Cdd:PRK11308 179 DEPVSALDVSVQAqvlnlMMDLQQEL---GLSYVFISHDLS-VVEhiADEVMVMYLGRCVEKGTKEQI 242
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
341-571 |
1.00e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.89 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 341 PASIPASARSAPIGVDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPID 420
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDG-KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 421 DLSdAELRHkVVLVSQEVHVFVG-TIADD----LRL--CAPDSDDAKITEAVETMKaqwihelpdgLETRVGAGGYQLTA 493
Cdd:PRK09452 80 HVP-AENRH-VNTVFQSYALFPHmTVFENvafgLRMqkTPAAEITPRVMEALRMVQ----------LEEFAQRKPHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 494 AQAQHIALVR-------LALLDPPVVILDEAtaeagttaaglLDQAAELAV------TGRTAVVIAHRLSQAVR-ADRIL 559
Cdd:PRK09452 148 GQQQRVAIARavvnkpkVLLLDESLSALDYK-----------LRKQMQNELkalqrkLGITFVFVTHDQEEALTmSDRIV 216
|
250
....*....|..
gi 532492226 560 VMSGGRVVESGT 571
Cdd:PRK09452 217 VMRDGRIEQDGT 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
358-515 |
1.31e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 358 KRVSYSYDnSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQE 437
Cdd:PRK10247 11 QNVGYLAG-DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 438 VHVFVGTIADDL------RLCAPD----SDDAKITEAVETMKAQWIHELpdgletrvgAGGyqltaaQAQHIALVRLALL 507
Cdd:PRK10247 90 PTLFGDTVYDNLifpwqiRNQQPDpaifLDDLERFALPDTILTKNIAEL---------SGG------EKQRISLIRNLQF 154
|
....*...
gi 532492226 508 DPPVVILD 515
Cdd:PRK10247 155 MPKVLLLD 162
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
336-575 |
1.43e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.40 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 336 AMPgRPAsiPASARSAPIGVDVKRVSYSYDNStPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVD 415
Cdd:PRK11607 4 AIP-RPQ--AKTRKALTPLLEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 416 GT----------PIDDL--SDAELRHKVVlvsqEVHVFVGTIADDLrlcapdsDDAKITEAVETMKAqWIHelpdgLETR 483
Cdd:PRK11607 80 GVdlshvppyqrPINMMfqSYALFPHMTV----EQNIAFGLKQDKL-------PKAEIASRVNEMLG-LVH-----MQEF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 484 VGAGGYQLTAAQAQHIALVR-------LALLDPPVVILDEAtaeagttaaglLDQAAELAVT------GRTAVVIAHRLS 550
Cdd:PRK11607 143 AKRKPHQLSGGQRQRVALARslakrpkLLLLDEPMGALDKK-----------LRDRMQLEVVdilervGVTCVMVTHDQE 211
|
250 260
....*....|....*....|....*.
gi 532492226 551 QAVR-ADRILVMSGGRVVESGTHDEL 575
Cdd:PRK11607 212 EAMTmAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
355-576 |
2.27e-11 |
|
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: 64.34 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDG-RITVDGTPIDDLSDAELRHKVVL 433
Cdd:COG1119 4 LELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVHV---------------FVGTIAddlRLCAPDSDDAKITEavetmkaQWIHELpdGLETRVGAGGYQLTAAQAQH 498
Cdd:COG1119 83 VSPALQLrfprdetvldvvlsgFFDSIG---LYREPTDEQRERAR-------ELLELL--GLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 499 I----ALV---RLALLDPPVVILDeataeaGTTAAGLLDQAAELAVTGRTAVV-IAHRLSQAVRA-DRILVMSGGRVVES 569
Cdd:COG1119 151 VliarALVkdpELLILDEPTAGLD------LGARELLLALLDKLAAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
....*..
gi 532492226 570 GTHDELI 576
Cdd:COG1119 225 GPKEEVL 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
355-575 |
2.36e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.85 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPV----IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPID----DLSDAE 426
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 427 LRHKVVLVSQ--EVHVFVGTIADDLRLcAPDSDDAKITEAVETMKaQWIHELpdGLETRVGAGG-YQLTAAQAQHIALVR 503
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEF-GPKNFGFSEDEAKEKAL-KWLKKV--GLSEDLISKSpFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 504 LALLDPPVVILDE-ATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQ-AVRADRILVMSGGRVVESGTHDEL 575
Cdd:PRK13641 159 VMAYEPEILCLDEpAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
367-578 |
2.47e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 367 STPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSD---AELR-HKVVLVSQEVHVF- 441
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRnQKLGFIYQFHHLLp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 442 ----VGTIADDLRLCAPDSDDAKiTEAVETMKAQwihelpdGLETRVGAGGYQLTAAQAQHIALVR-------LALLDPP 510
Cdd:PRK11629 101 dftaLENVAMPLLIGKKKPAEIN-SRALEMLAAV-------GLEHRANHRPSELSGGERQRVAIARalvnnprLVLADEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 511 VVILDeataeaGTTAAGLLDQAAELAVTGRTA-VVIAHRLSQAVRADRILVMSGGRVVESGThdeLIGA 578
Cdd:PRK11629 173 TGNLD------ARNADSIFQLLGELNRLQGTAfLVVTHDLQLAKRMSRQLEMRDGRLTAELS---LMGA 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
357-416 |
2.61e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.24 E-value: 2.61e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDnSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDG 416
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK 59
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
43-313 |
3.24e-11 |
|
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: 64.22 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 43 TTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAATL 122
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 123 AQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFLRRS 202
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 203 GPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAVLSV 282
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270
....*....|....*....|....*....|.
gi 532492226 283 GYWLVTTGSVSIGAATAAALYFHSLFSPIAV 313
Cdd:cd18561 241 GALRVLGGQLTLSSLLLILFLSREFFRPLRD 271
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-575 |
3.29e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.91 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 347 SARSAPIGVDVKRVsYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVD------GTPID 420
Cdd:PRK14246 3 AGKSAEDVFNISRL-YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 421 DLSDAELRHKVVLVSQEVHVFVG-TIADDLRLCAPD---SDDAKITEAVET--MKAQWIHELPDgletRVGAGGYQLTAA 494
Cdd:PRK14246 82 QIDAIKLRKEVGMVFQQPNPFPHlSIYDNIAYPLKShgiKEKREIKKIVEEclRKVGLWKEVYD----RLNSPASQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 495 QAQHIALVRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHD 573
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSN 237
|
..
gi 532492226 574 EL 575
Cdd:PRK14246 238 EI 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
355-577 |
4.63e-11 |
|
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: 65.59 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNST-PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRIT-------VDGTPIDDLSDAE 426
Cdd:TIGR03269 283 RNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 427 LRHKVVLVSQEVHVF-----VGTIADDLRLCAPdsDDAKITEAVETMKAQWIHE---------LPDgletrvgaggyQLT 492
Cdd:TIGR03269 363 AKRYIGILHQEYDLYphrtvLDNLTEAIGLELP--DELARMKAVITLKMVGFDEekaeeildkYPD-----------ELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 493 AAQAQHIALVRLALLDPPVVILDEATAEagttaaglLDQAAELAVT----------GRTAVVIAHRLSQAVR-ADRILVM 561
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGT--------MDPITKVDVThsilkareemEQTFIIVSHDMDFVLDvCDRAALM 501
|
250
....*....|....*.
gi 532492226 562 SGGRVVESGTHDELIG 577
Cdd:TIGR03269 502 RDGKIVKIGDPEEIVE 517
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
45-331 |
6.09e-11 |
|
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: 63.66 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 45 VVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAATLAQ 124
Cdd:cd18575 3 IALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 125 PSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFLRRSGP 204
Cdd:cd18575 83 SPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 205 VYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAVLSVGY 284
Cdd:cd18575 163 LSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGA 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 532492226 285 WLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18575 243 HDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
370-417 |
6.32e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.79 E-value: 6.32e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGT 417
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR 88
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
370-418 |
6.97e-11 |
|
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: 62.16 E-value: 6.97e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTP 418
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV 85
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
353-571 |
7.35e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.22 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 353 IGVDVKRVSYSYDNSTP----VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSD---- 424
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 425 AELRHKVVLVSQ--EVHVFVGTIADDLRLcAPDSDDAKITEAVETMKAQWihELPDGLETRVGAGGYQLTAAQAQHIALV 502
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEETVLKDVAF-GPQNFGVSQEEAEALAREKL--ALVGISESLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532492226 503 RLALLDPPVVILDE-ATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQ-AVRADRILVMSGGRVVESGT 571
Cdd:PRK13649 158 GILAMEPKILVLDEpTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGK 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
355-417 |
8.08e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 60.15 E-value: 8.08e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 355 VDVKRVSYSYDNStPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGT 417
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST 62
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
362-564 |
9.36e-11 |
|
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: 61.96 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 362 YSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRI----TVDGTPIDDLSDAELRHKVVLVSQE 437
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 438 VHVFVGTIADDLRLCAPDSDD--AKITEAVETMKAqwIHELPDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILD 515
Cdd:cd03290 88 PWLLNATVEENITFGSPFNKQryKAVTDACSLQPD--IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 516 EATAEAGTTAAGLLDQAAELAV---TGRTAVVIAHRLSQAVRADRILVMSGG 564
Cdd:cd03290 166 DPFSALDIHLSDHLMQEGILKFlqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
372-573 |
9.94e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 372 DSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITV---DGTPID--DLSDAELRHkvvLVSQEVHVFVGTIA 446
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDlyALSEAERRR---LLRTEWGFVHQHPR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 447 DDLRLCApdSDDAKITE-----------AVETMKAQW----------IHELPdgletRVGAGGYQltaaQAQHIA--LV- 502
Cdd:PRK11701 100 DGLRMQV--SAGGNIGErlmavgarhygDIRATAGDWlerveidaarIDDLP-----TTFSGGMQ----QRLQIArnLVt 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 503 --RLALLDPPVVILDeataeaGTTAAGLLDQAAELAVTGRTAVVI-AHRLSQA-VRADRILVMSGGRVVESGTHD 573
Cdd:PRK11701 169 hpRLVFMDEPTGGLD------VSVQARLLDLLRGLVRELGLAVVIvTHDLAVArLLAHRLLVMKQGRVVESGLTD 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
360-575 |
1.05e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.72 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 360 VSYSYDNSTP----VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGII-------PVGDGRITVDGTPIDDLSDaeLR 428
Cdd:PRK13645 12 VSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgqtIVGDYAIPANLKKIKEVKR--LR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 429 HKVVLVSQ--EVHVFVGTIADDLRL----CAPDSDDA--KITEAVETMkaqwihELPDGLETRvgaGGYQLTAAQAQHIA 500
Cdd:PRK13645 90 KEIGLVFQfpEYQLFQETIEKDIAFgpvnLGENKQEAykKVPELLKLV------QLPEDYVKR---SPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 501 LVRLALLDPPVVILDEATAEagttaaglLDQAAELAVT----------GRTAVVIAHRLSQAVR-ADRILVMSGGRVVES 569
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGG--------LDPKGEEDFInlferlnkeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISI 232
|
....*.
gi 532492226 570 GTHDEL 575
Cdd:PRK13645 233 GSPFEI 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
355-575 |
2.10e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.43 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGtpiDDLSDAELRHK-VVL 433
Cdd:PRK11432 7 VVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEV----HVFVG-TIADDLRLCAPDSDDAK--ITEAVETMKAqwihelpDGLETRvgaggY--QLTAAQAQHIALVRL 504
Cdd:PRK11432 83 VFQSYalfpHMSLGeNVGYGLKMLGVPKEERKqrVKEALELVDL-------AGFEDR-----YvdQISGGQQQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 505 ALLDPPVVILDEATAEagttaaglLDqaAELAVTGR------------TAVVIAHRLSQAVR-ADRILVMSGGRVVESGT 571
Cdd:PRK11432 151 LILKPKVLLFDEPLSN--------LD--ANLRRSMRekirelqqqfniTSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGS 220
|
....
gi 532492226 572 HDEL 575
Cdd:PRK11432 221 PQEL 224
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
54-331 |
2.13e-10 |
|
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: 61.84 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 54 GLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAATLAQPSSLVEDAG 133
Cdd:cd18782 18 GLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 134 TGDLISRVSGDVEAVNTVIARVLPATVSALFMIsLTLVGVGVIDWRFTVAIVAVAPIHYF-------ALRHFLRRsgpvy 206
Cdd:cd18782 98 VGELSTRISELDTIRGFLTGTALTTLLDVLFSV-IYIAVLFSYSPLLTLVVLATVPLQLLltflfgpILRRQIRR----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 207 rrSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAVLSVGYWL 286
Cdd:cd18782 172 --RAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYL 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 532492226 287 VTTGSVSIGAATAaalyFHSL----FSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18782 250 VLRGELTLGQLIA----FRILsgyvTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
355-575 |
2.21e-10 |
|
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: 60.60 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY-DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGtpIDDLSDAELRHKVV- 432
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--YSIRTDRKAARQSLg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVHVFVG-TIADDLRLCA-----PDSDDAKITEAVETMKaqwihELPDGLETRVGA--GGYQ--LTAAqaqhIALV 502
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFYArlkglPKSEIKEEVELLLRVL-----GLTDKANKRARTlsGGMKrkLSLA----IALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 503 RlallDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQA-VRADRILVMSGGRVVESGTHDEL 575
Cdd:cd03263 150 G----GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
354-426 |
2.68e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 2.68e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 354 GVDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE 426
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD 75
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
355-570 |
2.82e-10 |
|
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: 60.28 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNsTPVIDSISISIAPGeRIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDaELRHKVVLV 434
Cdd:cd03264 1 LQLENLTKRYGK-KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVG-TIADDLRLCA-----PDSD-DAKITEAVETMkaqwihELPDGLETRVGaggyQLTAAQAQHIALVRLALL 507
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYIAwlkgiPSKEvKARVDEVLELV------NLGDRAKKKIG----SLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 508 DPPVVILDEATAEagttaaglLDQA---------AELAvTGRTAVVIAHRLSQ-AVRADRILVMSGGRVVESG 570
Cdd:cd03264 148 DPSILIVDEPTAG--------LDPEerirfrnllSELG-EDRIVILSTHIVEDvESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
360-568 |
2.82e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 360 VSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVH 439
Cdd:PRK10522 328 VTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 440 VFVGTIADDlrlcAPDSDDAKITEAVETMKAQWIHELPDGLETRVgaggyQLTAAQAQHIALVrLALLDP-PVVILDEAT 518
Cdd:PRK10522 408 LFDQLLGPE----GKPANPALVEKWLERLKMAHKLELEDGRISNL-----KLSKGQKKRLALL-LALAEErDILLLDEWA 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 519 AeagttaagllDQ------------AAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVE 568
Cdd:PRK10522 478 A----------DQdphfrrefyqvlLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
372-569 |
3.05e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 372 DSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG--DGRITVDGTPI--DDLSDAElRHKVVLVSQEVH-VFVGTIA 446
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCrfKDIRDSE-ALGIVIIHQELAlIPYLSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 447 DDLRLCAPDSD------DAKITEAVETMKAQWIHELPDGLETRVGAGGYQLTaaqaqHIAL-----VRLALLDPPVVILD 515
Cdd:NF040905 97 ENIFLGNERAKrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLV-----EIAKalskdVKLLILDEPTAALN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 516 eataeaGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVES 569
Cdd:NF040905 172 ------EEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIET 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
357-563 |
3.80e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 59.09 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRItvdGTPiddlsdaeLRHKVVLVSQ 436
Cdd:cd03223 3 LENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMP--------EGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 EVHVFVGTIADdlRLCAPdsddakiteavetmkaqWIHELPDGletrvgaggyqltaaQAQHIALVRLALLDPPVVILDE 516
Cdd:cd03223 72 RPYLPLGTLRE--QLIYP-----------------WDDVLSGG---------------EQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 532492226 517 ATAEagttaaglLDQAAE-----LAVTGRTAVV-IAHRLSQAVRADRILVMSG 563
Cdd:cd03223 118 ATSA--------LDEESEdrlyqLLKELGITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
47-190 |
5.49e-10 |
|
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: 60.95 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 47 LLSATACGLSTPA---LLGLMVDAVTE-------GKPFVSLLRITAFMLSAAAAGV-ALTWWSTQLLANVAQNVLADLRE 115
Cdd:cd18577 5 LLAAIAAGAALPLmtiVFGDLFDAFTDfgsgessPDEFLDDVNKYALYFVYLGIGSfVLSYIQTACWTITGERQARRIRK 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 116 DVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMIsLTLVGVG-VIDWRFTVAIVAVAPI 190
Cdd:cd18577 85 RYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTF-IAGFIIAfIYSWKLTLVLLATLPL 159
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
326-428 |
6.17e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.58 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 326 ASLARLigvtaMPGRPASIPASARSAPIG---VDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIA 402
Cdd:COG3845 231 EELAEL-----MVGREVLLRVEKAPAEPGevvLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALA 305
|
90 100
....*....|....*....|....*.
gi 532492226 403 GIIPVGDGRITVDGTPIDDLSDAELR 428
Cdd:COG3845 306 GLRPPASGSIRLDGEDITGLSPRERR 331
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
371-573 |
1.01e-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: 60.99 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG--DGRITVDGTPI--DDLSDAElRHKVVLVSQEV-------- 438
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLkaSNIRDTE-RAGIVIIHQELtlvpelsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 439 --HVFVGtiaDDLRLCAPDSDDAKITEAVETMKAQW-IHELPDGLETRVGAGGYQLTAAQAQhiAL---VRLALLDPPVV 512
Cdd:TIGR02633 96 aeNIFLG---NEITLPGGRMAYNAMYLRAKNLLRELqLDADNVTRPVGDYGGGQQQLVEIAK--ALnkqARLLILDEPSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 513 ILdeataeAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQaVRA--DRILVMSGGRVVesGTHD 573
Cdd:TIGR02633 171 SL------TEKETEILLDIIRDLKAHGVACVYISHKLNE-VKAvcDTICVIRDGQHV--ATKD 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
355-593 |
1.21e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.74 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIddlsDAELRHKV--- 431
Cdd:COG4152 2 LELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIgyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 432 -----------VLvsqEVHVFVGtiaddlRLCAPDSDDAKiteavetmkaQWIHELpdgLEtRVGAGGY------QLTAA 494
Cdd:COG4152 77 peerglypkmkVG---EQLVYLA------RLKGLSKAEAK----------RRADEW---LE-RLGLGDRankkveELSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 495 QAQHIALVrLALL-DPPVVILDeataea-gttaaGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGT 571
Cdd:COG4152 134 NQQKVQLI-AALLhDPELLILDepfsgldpvnveLLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
250 260 270
....*....|....*....|....*....|..
gi 532492226 572 HDEL----------IGADGSYAALWEAWSVRS 593
Cdd:COG4152 213 VDEIrrqfgrntlrLEADGDAGWLRALPGVTV 244
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
355-575 |
1.25e-09 |
|
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: 58.54 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPViDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGtpIDDLSDA-ELRHKVVL 433
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPrEVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVhvfvgTIADDL----------RLCAPDSDDAK--ITEAVETMkaqwihELPDGLETRVGA--GGYQ--LTAAQaq 497
Cdd:cd03265 78 VFQDL-----SVDDELtgwenlyihaRLYGVPGAERRerIDELLDFV------GLLEAADRLVKTysGGMRrrLEIAR-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 498 hiALV---RLALLDPPVVILDEATAEAGTTAAGLLDQAaelavTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHD 573
Cdd:cd03265 145 --SLVhrpEVLFLDEPTIGLDPQTRAHVWEYIEKLKEE-----FGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPE 217
|
..
gi 532492226 574 EL 575
Cdd:cd03265 218 EL 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
374-515 |
1.27e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.35 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 374 ISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRH--------KVVLvsqevhvfvgTI 445
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHylghrnamKPAL----------TV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 446 ADDLRLCAP--DSDDAKITEAVETMKAQWIHELPdgletrvgaGGYqLTAAQAQHIALVRLALLDPPVVILD 515
Cdd:PRK13539 91 AENLEFWAAflGGEELDIAAALEAVGLAPLAHLP---------FGY-LSAGQKRRVALARLLVSNRPIWILD 152
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
370-578 |
1.28e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.34 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKL-------IAGIIPVGDgrITVDGTPIDDLSDA-ELRHKVVLVSQEVHVF 441
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRYSGD--VLLGGRSIFNYRDVlEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 442 VGTIADDL------RLCAPDSDDAKITEAVETMKAQWihelpDGLETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILD 515
Cdd:PRK14271 114 PMSIMDNVlagvraHKLVPRKEFRGVAQARLTEVGLW-----DAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 516 EATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELIGA 578
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
365-578 |
1.41e-09 |
|
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: 60.85 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 365 DNSTPVIDSISISIAPGERIAVVGSSGAGK--TTLA--KLIAGIIPVGDGRITVDGTPIDDLSDAELRH----KVVLVSQ 436
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKsvTALSilRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 E-------VHVfVGT-IADDLRLCAPDSDDAKITEAVEtmkaqWIHE--LPDgLETRVGAGGYQLTAAQAQH--IALVrL 504
Cdd:COG4172 100 EpmtslnpLHT-IGKqIAEVLRLHRGLSGAAARARALE-----LLERvgIPD-PERRLDAYPHQLSGGQRQRvmIAMA-L 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 505 A----LL--DPP-----VV----ILDeataeagttaagLLdqaAELAVTGRTAVV-IAHRLSqAVR--ADRILVMSGGRV 566
Cdd:COG4172 172 AnepdLLiaDEPttaldVTvqaqILD------------LL---KDLQRELGMALLlITHDLG-VVRrfADRVAVMRQGEI 235
|
250
....*....|..
gi 532492226 567 VESGTHDELIGA 578
Cdd:COG4172 236 VEQGPTAELFAA 247
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
358-576 |
1.43e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 358 KRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE-LRHKVVLVSQ 436
Cdd:PRK11614 9 DKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 EVHVFVG-TIADDLRLCAPDSDDAKITEAVEtmkaqWIHEL-PDGLETRVGAGGyQLTAAQAQHIALVRLALLDPPVVIL 514
Cdd:PRK11614 88 GRRVFSRmTVEENLAMGGFFAERDQFQERIK-----WVYELfPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 515 DE-ATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELI 576
Cdd:PRK11614 162 DEpSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALL 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
355-571 |
2.02e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.43 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTPVI---DSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL---R 428
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 429 HKVVLVSQevH--------VFvGTIADDLRLCApdSDDAKITEAVEtmkaqwihELPD--GLETRVGAGGYQLTAAQAQH 498
Cdd:PRK11153 82 RQIGMIFQ--HfnllssrtVF-DNVALPLELAG--TPKAEIKARVT--------ELLElvGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 499 IALVRlAL---------------LDPPVV--ILDeataeagttaagLLDQA-AELavtGRTAVVIAHRLsQAVR--ADRI 558
Cdd:PRK11153 149 VAIAR-ALasnpkvllcdeatsaLDPATTrsILE------------LLKDInREL---GLTIVLITHEM-DVVKriCDRV 211
|
250
....*....|...
gi 532492226 559 LVMSGGRVVESGT 571
Cdd:PRK11153 212 AVIDAGRLVEQGT 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
355-515 |
2.03e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNStPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDdlsdaelrhKVVLV 434
Cdd:PRK13540 2 LDVIELDFDYHDQ-PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---------KDLCT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVG---TIADDLRL---CAPD----SDDAKITEAVETMKAQWIHELPDGLetrvgaggyqLTAAQAQHIALVR- 503
Cdd:PRK13540 72 YQKQLCFVGhrsGINPYLTLrenCLYDihfsPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRl 141
|
170
....*....|....*...
gi 532492226 504 ------LALLDPPVVILD 515
Cdd:PRK13540 142 wmskakLWLLDEPLVALD 159
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
44-327 |
2.38e-09 |
|
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: 58.80 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 44 TVVLLSATACGLSTPALLGLMVDAVT-----EGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVA-QNVLADLREDV 117
Cdd:cd18780 2 TIALLVSSGTNLALPYFFGQVIDAVTnhsgsGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAgERVVARLRKRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 118 FAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRH 197
Cdd:cd18780 82 FSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 198 FLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLA 277
Cdd:cd18780 162 YGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 278 AVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAvFLSNI--DELQDAGAS 327
Cdd:cd18780 242 LVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFA-FLSSLygDFMQAVGAS 292
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
355-575 |
2.96e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.24 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNStPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL---RHKV 431
Cdd:PRK11831 8 VDMRGVSFTRGNR-CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 432 VLVSQEVHVFVG-TIADDL--------RLCAPdsddakITEAVETMKAQWI------HELPDGLetrvgAGGYQLTAAQA 496
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVayplrehtQLPAP------LLHSTVMMKLEAVglrgaaKLMPSEL-----SGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 497 QHIAL-VRLALLDPPVVILDEATAEAGTTAAGLLDQAaelavTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDE 574
Cdd:PRK11831 156 RAIALePDLIMFDEPFVGQDPITMGVLVKLISELNSA-----LGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQA 230
|
.
gi 532492226 575 L 575
Cdd:PRK11831 231 L 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
358-575 |
3.26e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.49 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 358 KRVSYSYDNSTP----VIDSISISIAPGERIAVVGSSGAGKTT-------LAKLIAGIIPVGDGRITvDGTPIDDLSDae 426
Cdd:PRK13634 6 QKVEHRYQYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTllqhlngLLQPTSGTVTIGERVIT-AGKKNKKLKP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 427 LRHKVVLVSQ--EVHVFVGTIADDlrLC-APDSDDAKITEAVETMKaQWIHE--LPDGLETRvgaGGYQLTAAQAQHIAL 501
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKD--ICfGPMNFGVSEEDAKQKAR-EMIELvgLPEELLAR---SPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 502 VRLALLDPPVVILDeataeagttaagllDQAAELAVTGR----------------TAVVIAHRLSQAVR-ADRILVMSGG 564
Cdd:PRK13634 157 AGVLAMEPEVLVLD--------------EPTAGLDPKGRkemmemfyklhkekglTTVLVTHSMEDAARyADQIVVMHKG 222
|
250
....*....|.
gi 532492226 565 RVVESGTHDEL 575
Cdd:PRK13634 223 TVFLQGTPREI 233
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
39-190 |
3.74e-09 |
|
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: 58.19 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 39 ALALTTVVLLSATACGLSTpallgLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVF 118
Cdd:cd18584 3 LLGLLAALLIIAQAWLLAR-----IIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 119 AATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPI 190
Cdd:cd18584 78 ARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPL 149
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
371-576 |
5.80e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLS---DAELrhKVVLVSQEVHV------- 440
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQL--GIGIIYQELSVideltvl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 441 ---FVGTIADDLRLCAPDSDDAKITEAVETMKAqwIHELPDGLETRVGaggyQLTAAQAQHIALVRLALLDPPVVILDEA 517
Cdd:PRK09700 99 enlYIGRHLTKKVCGVNIIDWREMRVRAAMMLL--RVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 518 TAEAGTTAA----GLLDQaaeLAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG-----THDELI 576
Cdd:PRK09700 173 TSSLTNKEVdylfLIMNQ---LRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGmvsdvSNDDIV 238
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-575 |
6.89e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGII-----PVGDGRITVDGTPIDDLSDAELRH 429
Cdd:PRK14247 4 IEIRDLKVSFGQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 430 KVVLVSQ------EVHVFvGTIADDLRLCAPDSDDAKITEAVETM--KAQWIHELPDgletRVGAGGYQLTAAQAQHIAL 501
Cdd:PRK14247 83 RVQMVFQipnpipNLSIF-ENVALGLKLNRLVKSKKELQERVRWAleKAQLWDEVKD----RLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 502 VRLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDEL 575
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
370-570 |
7.32e-09 |
|
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: 56.00 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGiIP---VGDGRITVDGTPIDDLSDAE-LRHKVVLVSQEVHVFVG-T 444
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEIPGvK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 445 IADDLRlcapdsddakiteavetmkaqwihELPDGLetrvgAGGyqltaaQAQHIALVRLALLDPPVVILDEATAEAGTT 524
Cdd:cd03217 94 NADFLR------------------------YVNEGF-----SGG------EKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 532492226 525 AAGLL-DQAAELAVTGRTAVVIAH--RLSQAVRADRILVMSGGRVVESG 570
Cdd:cd03217 139 ALRLVaEVINKLREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
371-578 |
9.77e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 9.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPID--DLSDAELRHKVVL----VSQEVHVFVGT 444
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFqdpsTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 445 IAD-DLRLCAPDSDDAKITEAVETMKAqwIHELPDgletRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEA-G 522
Cdd:PRK15112 109 ILDfPLRLNTDLEPEQREKQIIETLRQ--VGLLPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLdM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 523 TTAAGLLDQAAELAVT-GRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELIGA 578
Cdd:PRK15112 183 SMRSQLINLMLELQEKqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLAS 240
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-579 |
1.15e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 56.74 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 351 APIgvDVKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSdAELRHK 430
Cdd:PRK13537 6 API--DFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 431 VVLVSQevhvfvgtiADDLRlcaPD---SDDAKITEAVETMKAQWIHELPDG------LETRVGAGGYQLTAAQAQHIAL 501
Cdd:PRK13537 82 VGVVPQ---------FDNLD---PDftvRENLLVFGRYFGLSAAAARALVPPllefakLENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 502 VRLALLDPPVVILDEATAEAGTTAAGLL-DQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELIGAD 579
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
42-331 |
1.47e-08 |
|
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: 56.40 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 42 LTTVVLLSA--TACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFA 119
Cdd:cd18779 4 LGQILLASLllQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 120 ATLAQPSSLVEDAGTGDLISRVSGdveavNTVIARVLPA-TVSALF---MISLTLVGVGVIDWRFTVAIVAVAPIHYFAL 195
Cdd:cd18779 84 HLLRLPYRFFQQRSTGDLLMRLSS-----NATIRELLTSqTLSALLdgtLVLGYLALLFAQSPLLGLVVLGLAALQVALL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 196 RHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLG 275
Cdd:cd18779 159 LATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 276 LAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18779 239 PLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
366-481 |
1.50e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 55.63 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 366 NSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLS-DAELRHKVVLVSQEVHVFVG- 443
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKl 90
|
90 100 110
....*....|....*....|....*....|....*...
gi 532492226 444 TIADDLRLcapdsddakITEAVETMKAQWIHELPDGLE 481
Cdd:cd03218 91 TVEENILA---------VLEIRGLSKKEREEKLEELLE 119
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
357-422 |
1.54e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.81 E-value: 1.54e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 357 VKRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDL 422
Cdd:COG1137 6 AENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL 70
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
370-566 |
1.80e-08 |
|
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: 54.36 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE-LRHKVVLVSQEVH---VFVG-T 444
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKregLVLDlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 445 IADDLRlcapdsddakiteavetmkaqwiheLPDGLetrvgAGGYQltaaqaQHIALVRLALLDPPVVILDEATAEagtt 524
Cdd:cd03215 95 VAENIA-------------------------LSSLL-----SGGNQ------QKVVLARWLARDPRVLILDEPTRG---- 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 525 aaglLDQAA---------ELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRV 566
Cdd:cd03215 135 ----VDVGAkaeiyrlirELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
352-570 |
2.73e-08 |
|
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: 54.09 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 352 PIGVDVKRVSYSYDNST-----PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAG-IIPVGD-GRITVDGTPIDDLSd 424
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPsksgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLINGRPLDKRS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 425 aeLRHKVVLVSQEVHVFvgtiaddlrlcapdsddAKITeAVETMK-AQWIHELPDGLETRVGAGgyqltaaqaqhialvr 503
Cdd:cd03213 80 --FRKIIGYVPQDDILH-----------------PTLT-VRETLMfAAKLRGLSGGERKRVSIA---------------- 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 504 LALL-DPPVVILDEATAEagttaaglLDQAAE---------LAVTGRTAVVIAHRLSQAV--RADRILVMSGGRVVESG 570
Cdd:cd03213 124 LELVsNPSLLFLDEPTSG--------LDSSSAlqvmsllrrLADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
371-570 |
4.17e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL---RHKVVLVSQEVHVfvgtiad 447
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQDPYA------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 448 dlrlcapdSDDAKITEAVETMKAQWIHELPDG---------LETRVG-----AGGY--QLTAAQAQHIALVRLALLDPPV 511
Cdd:PRK10261 413 --------SLDPRQTVGDSIMEPLRVHGLLPGkaaaarvawLLERVGllpehAWRYphEFSGGQRQRICIARALALNPKV 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 512 VILDEATAEAGTTAAG-----LLDQAAELavtGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:PRK10261 485 IIADEAVSALDVSIRGqiinlLLDLQRDF---GIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
355-575 |
4.23e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.09 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSYDNSTP----VIDSISISIAPGERIAVVGSSGAGKTTLAK-LIAGIIP----------------------V 407
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEhLNALLLPdtgtiewifkdeknkkktkekeK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 408 GDGRITVDGTPIDDLSDA-ELRHKVVLVSQ--EVHVFVGTIADDLrLCAPDSDDAKITEAVEtmKAQWIHELPDGLETRV 484
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIkEIRRRVGVVFQfaEYQLFEQTIEKDI-IFGPVSMGVSKEEAKK--RAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 485 GAGGYQLTAAQAQHIALVRLALLDPPVVILDE-ATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAV-RADRILVMS 562
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEpTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLeWTKRTIFFK 239
|
250
....*....|....
gi 532492226 563 GGRVVESG-THDEL 575
Cdd:PRK13651 240 DGKIIKDGdTYDIL 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
371-565 |
4.78e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG--DGRITVDGTPI--DDLSDAElRHKVVLVSQEVHVFVG-TI 445
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELqaSNIRDTE-RAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 446 ADDLRLCAPDS-----DDAKITEAVETMKAQWihELPDGLETRVG--AGGYQltaaQAQHIAL-----VRLALLDPPVVI 513
Cdd:PRK13549 100 LENIFLGNEITpggimDYDAMYLRAQKLLAQL--KLDINPATPVGnlGLGQQ----QLVEIAKalnkqARLLILDEPTAS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 532492226 514 LdeataeAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQ--AVrADRILVMSGGR 565
Cdd:PRK13549 174 L------TESETAVLLDIIRDLKAHGIACIYISHKLNEvkAI-SDTICVIRDGR 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
372-515 |
5.16e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 372 DSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELR------H----KVVLVSQEVHVF 441
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylgHqpgiKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 442 VGTIADDLrlcapdsDDAKITEAVEtmkaqwihelpdgletRVGAGGY------QLTAAQAQHIALVRLALLDPPVVILD 515
Cdd:PRK13538 98 YQRLHGPG-------DDEALWEALA----------------QVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILD 154
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
365-578 |
8.26e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.42 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 365 DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPvGDGRITVDGTPIDDLSDAEL----RHKVVLVSqevhv 440
Cdd:PRK15093 17 DGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDLLRLspreRRKLVGHN----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 441 fVGTIADDLRLCAPDSDDA--KITEAVE--TMKAQWIHEL------PDGLETRVG---------AGGYQLTAAQAQH--- 498
Cdd:PRK15093 91 -VSMIFQEPQSCLDPSERVgrQLMQNIPgwTYKGRWWQRFgwrkrrAIELLHRVGikdhkdamrSFPYELTEGECQKvmi 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 499 -IALV---RLALLDPPVVILDEATAEAGTTAAGLLDQAaelavTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHD 573
Cdd:PRK15093 170 aIALAnqpRLLIADEPTNAMEPTTQAQIFRLLTRLNQN-----NNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSK 244
|
....*
gi 532492226 574 ELIGA 578
Cdd:PRK15093 245 ELVTT 249
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
361-412 |
8.87e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 8.87e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 532492226 361 SYSYdnsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRI 412
Cdd:PRK11147 12 SFSD---APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI 60
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-416 |
9.42e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.94 E-value: 9.42e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDG 416
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
357-566 |
1.22e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.14 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 357 VKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIddlsdAELRHKVVLVSQ 436
Cdd:PRK11247 15 LNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 EVHVFV-GTIADDLRLCAPDSDDAKITEAVETMkaqwihelpdGLETRVGAGGYQLTAAQAQHIALVR-------LALLD 508
Cdd:PRK11247 89 DARLLPwKKVIDNVGLGLKGQWRDAALQALAAV----------GLADRANEWPAALSGGQKQRVALARalihrpgLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 509 PPVVILDEATAEAGTTAAGLLDQAaelavTGRTAVVIAHRLSQAVR-ADRILVMSGGRV 566
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQ-----HGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
365-570 |
1.31e-07 |
|
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: 52.66 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 365 DNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGD---GRITVDGTPiddLSDAELRHKVVLVSQEvHVF 441
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP---RKPDQFQKCVAYVRQD-DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 442 VG--TIADDLRLCAPDSDDAKITEAVETMKAqwihelPDGLETRVG---AGGY---QLTAAQAQHIALVRLALLDPPVVI 513
Cdd:cd03234 93 LPglTVRETLTYTAILRLPRKSSDAIRKKRV------EDVLLRDLAltrIGGNlvkGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 514 LDEATAEAGTTAAGLLDQA-AELAVTGRTAVVIAHR-LSQAVRA-DRILVMSGGRVVESG 570
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTlSQLARRNRIVILTIHQpRSDLFRLfDRILLLSSGEIVYSG 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
364-570 |
1.50e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.86 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 364 YDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLI---AGIIPvgdgRITVDGT----------PIDDlsDAELRHK 430
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNP----EVTITGSivynghniysPRTD--TVDLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 431 VVLVSQEVHVFVGTIADD----LRLcAPDSDDAKITEAVET-MKAQWIHelpDGLETRVGAGGYQLTAAQAQHIALVRLA 505
Cdd:PRK14239 88 IGMVFQQPNPFPMSIYENvvygLRL-KGIKDKQVLDEAVEKsLKGASIW---DEVKDRLHDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 506 LLDPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESG 570
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
370-576 |
1.53e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.59 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLS-DAELRHKVVLVSQEVHVF------- 441
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFrrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 442 ----VGTIADDLrlcapdSDDAKITEAVETMKAQWIHELPDGLetrvgagGYQLTAAQAQHIALVRLALLDPPVVILDEA 517
Cdd:PRK10895 98 nlmaVLQIRDDL------SAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532492226 518 TAEAGTTAAGLLDQAAE-LAVTGRTAVVIAHRLSQAVRA-DRILVMSGGRVVESGTHDELI 576
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEhLRDSGLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
355-412 |
1.83e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 1.83e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 532492226 355 VDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRI 412
Cdd:PRK15064 320 LEVENLTKGFDN-GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
325-570 |
1.87e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 325 GASLARLIGVTAMPGRPASIPASARSAPIGVDVKRVSYSYDNSTPVIDsISISIAPGERIAVVGSSGAGKTTLAKLIAGI 404
Cdd:PTZ00243 631 PSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFFELEPKVLLRD-VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQ 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 405 IPVGDGRITvdgtpiddlsdAElrHKVVLVSQEVHVFVGTIADDLrLCAPDSDDAKITEAVETMKAQW-IHELPDGLETR 483
Cdd:PTZ00243 710 FEISEGRVW-----------AE--RSIAYVPQQAWIMNATVRGNI-LFFDEEDAARLADAVRVSQLEAdLAQLGGGLETE 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 484 VGAGGYQLTAAQAQHIALVR-------LALLDPPVVILDEATAEAGTTAAGLLdqaaelAVTGRTAVVIAHRLSQAVRAD 556
Cdd:PTZ00243 776 IGEKGVNLSGGQKARVSLARavyanrdVYLLDDPLSALDAHVGERVVEECFLG------ALAGKTRVLATHQVHVVPRAD 849
|
250
....*....|....
gi 532492226 557 RILVMSGGRVVESG 570
Cdd:PTZ00243 850 YVVALGDGRVEFSG 863
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
366-515 |
2.01e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 366 NSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIddlSDAELRHKVVLVSQevhvfvgti 445
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGDRSRFMAYLGH--------- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 446 addLRLCAPDSDDAKITEAVETMKAQWIHELPDGLETRVGAGGY------QLTAAQAQHIALVRLALLDPPVVILD 515
Cdd:PRK13543 90 ---LPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLD 162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
371-575 |
2.59e-07 |
|
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: 53.29 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIP-VGDGRITVDGTPIDDLSDAE-LRHKVVLVSQEVH----VFVGT 444
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQaIRAGIAMVPEDRKrhgiVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 445 IADDLRLCAPDS-------DDAK----ITEAVETMKAQWIHelPDGLETRVgAGGYQltaaqaQHIALVRLALLDPPVVI 513
Cdd:TIGR02633 356 VGKNITLSVLKSfcfkmriDAAAelqiIGSAIQRLKVKTAS--PFLPIGRL-SGGNQ------QKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 514 LDEAT----AEAGTTAAGLLDQaaeLAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDEL 575
Cdd:TIGR02633 427 LDEPTrgvdVGAKYEIYKLINQ---LAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHAL 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
347-420 |
3.00e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 3.00e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 347 SARSAPIGVDVKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVdGTPID 420
Cdd:PRK11147 312 ASRSGKIVFEMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE 383
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
54-331 |
3.07e-07 |
|
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: 52.18 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 54 GLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAATLAQPSSLVEDAG 133
Cdd:cd18568 18 GLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 134 TGDLISRVSgdvEavNTVIARVLpaTVSALFMI--SLTLVGVGVI----DWRFTVAIVAVAPIH---YFALRHFLRRsgp 204
Cdd:cd18568 98 VGDIITRFQ---E--NQKIRRFL--TRSALTTIldLLMVFIYLGLmfyyNLQLTLIVLAFIPLYvllTLLSSPKLKR--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 205 VYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAVLSVGY 284
Cdd:cd18568 168 NSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 532492226 285 WLVTTGSVSIGAATAAALYFHSLFSPIaVFLSNI-DELQDAGASLARL 331
Cdd:cd18568 248 YLVISGQLTIGQLVAFNMLFGSVINPL-LALVGLwDELQETRISVERL 294
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
358-579 |
3.51e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 358 KRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQE 437
Cdd:PRK10253 11 EQLTLGYGKYT-VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 438 vhvfvgtiaddlrlcAPDSDDAKITEAV-------ETMKAQWIHELPDGLETRVGAGGYQ---------LTAAQAQH--I 499
Cdd:PRK10253 90 ---------------ATTPGDITVQELVargryphQPLFTRWRKEDEEAVTKAMQATGIThladqsvdtLSGGQRQRawI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 500 ALV-----RLALLDPPVVILDeataeaGTTAAGLLDQAAELAVT-GRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTH 572
Cdd:PRK10253 155 AMVlaqetAIMLLDEPTTWLD------ISHQIDLLELLSELNREkGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAP 228
|
....*..
gi 532492226 573 DELIGAD 579
Cdd:PRK10253 229 KEIVTAE 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
350-571 |
4.26e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.16 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 350 SAPIGVDVKRVSYSYDNSTP----VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDA 425
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 426 E----------------LRHKVVLVSQ--EVHVFVGTIADDL-----RLCAPDSDDAKITEA-VETMkaqwihelpdGL- 480
Cdd:PRK13631 97 HelitnpyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDImfgpvALGVKKSEAKKLAKFyLNKM----------GLd 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 481 ETRVGAGGYQLTAAQAQHIALVRLALLDPPVVILDEATAEA-----GTTAAGLLDQAAElavtGRTAVVIAHRLSQAVR- 554
Cdd:PRK13631 167 DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLdpkgeHEMMQLILDAKAN----NKTVFVITHTMEHVLEv 242
|
250
....*....|....*..
gi 532492226 555 ADRILVMSGGRVVESGT 571
Cdd:PRK13631 243 ADEVIVMDKGKILKTGT 259
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
370-570 |
4.51e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTT----LAKLIAgiipvGDGRITVDGTPIDDLSDAEL---RHKVVLVSQEVHVFV 442
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 443 G-------TIADDLRLCAPDSDDAKITEAVetmkAQWIHELPDGLETRVGAGGyQLTAAQAQHIALVRLALLDPPVVILD 515
Cdd:PRK15134 376 NprlnvlqIIEEGLRVHQPTLSAAQREQQV----IAVMEEVGLDPETRHRYPA-EFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 516 EATAEagttaaglLD---QAAELAV------TGRTA-VVIAHRLsQAVRA--DRILVMSGGRVVESG 570
Cdd:PRK15134 451 EPTSS--------LDktvQAQILALlkslqqKHQLAyLFISHDL-HVVRAlcHQVIVLRQGEVVEQG 508
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
50-311 |
6.26e-07 |
|
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: 51.30 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 50 ATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAATLAQPSSLV 129
Cdd:cd18549 14 IAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 130 EDAGTGDLISRVSGDVEAVNTViARVLPATvsaLFMISLTLVGVGV----IDWRFTVAIVAVAPIHYFALRHFLRRSGPV 205
Cdd:cd18549 94 DNNKTGQLMSRITNDLFDISEL-AHHGPED---LFISIITIIGSFIilltINVPLTLIVFALLPLMIIFTIYFNKKMKKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 206 YRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLGLAAVLSVGYW 285
Cdd:cd18549 170 FRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGY 249
|
250 260
....*....|....*....|....*.
gi 532492226 286 LVTTGSVSIGAATAAALYFHSLFSPI 311
Cdd:cd18549 250 FIIKGEITLGDLVAFLLYVNVFIKPI 275
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
354-571 |
7.11e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 354 GVDVKRVSYSYDNS-TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAeLRHKVV 432
Cdd:TIGR01257 928 GVCVKNLVKIFEPSgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA-VRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 LVSQEVHVFVG-TIADDL----RLCAPDSDDAKItEAVETMKAQWIHELPDGlETRVGAGGYQLTAAQAqhIALVRlall 507
Cdd:TIGR01257 1007 MCPQHNILFHHlTVAEHIlfyaQLKGRSWEEAQL-EMEAMLEDTGLHHKRNE-EAQDLSGGMQRKLSVA--IAFVG---- 1078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 508 DPPVVILDEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQA-VRADRILVMSGGRVVESGT 571
Cdd:TIGR01257 1079 DAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
358-574 |
7.82e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.26 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 358 KRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE---LRHKVVLV 434
Cdd:PRK10908 5 EHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 435 SQEVHVFVG-TIADD----LRLCAPDSDDA--KITEAVETMkaqwihelpdGLETRVGAGGYQLTAAQAQHIALVRlALL 507
Cdd:PRK10908 85 FQDHHLLMDrTVYDNvaipLIIAGASGDDIrrRVSAALDKV----------GLLDKAKNFPIQLSGGEQQRVGIAR-AVV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 508 DPPVVIL--DEATAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQ-AVRADRILVMSGGRVVEsGTHDE 574
Cdd:PRK10908 154 NKPAVLLadEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLiSRRSYRMLTLSDGHLHG-GVGGE 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
358-404 |
9.91e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 9.91e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 532492226 358 KRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGI 404
Cdd:PRK11819 10 NRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV 56
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
366-571 |
1.08e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 366 NSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAG-----IIpvgDGRITVDGTPIDDLsDAELRHK--VVLVSQ-E 437
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykIL---EGDILFKGESILDL-EPEERAHlgIFLAFQyP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 438 VHVFVGTIADDLRLC---------APDSDDAKITEAVETmKAQWIHELPDGLETRVGAGgyqLTAAQAQHIALVRLALLD 508
Cdd:CHL00131 94 IEIPGVSNADFLRLAynskrkfqgLPELDPLEFLEIINE-KLKLVGMDPSFLSRNVNEG---FSGGEKKRNEILQMALLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 509 PPVVILDEATAEagttaaglLDQAA---------ELAVTGRTAVVIAH--RLSQAVRADRILVMSGGRVVESGT 571
Cdd:CHL00131 170 SELAILDETDSG--------LDIDAlkiiaeginKLMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
367-416 |
1.09e-06 |
|
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: 50.02 E-value: 1.09e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 532492226 367 STPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDG 416
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG 82
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
370-577 |
1.43e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.97 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE-------------LRHKVVLVSQ 436
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 437 EVHVFVGTIADDLRLCAPDSDDAKITEAVETMKAQWIHELpdGLETRvGAGGY--QLTAAQAQHIALVRLALLDPPVVIL 514
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKV--GIDER-AQGKYpvHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 515 DEATAEAG-TTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELIG 577
Cdd:PRK10619 177 DEPTSALDpELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
354-575 |
1.54e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.41 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 354 GVDVKRVSYSYDNsTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAElrHKVVL 433
Cdd:PRK11000 3 SVTLRNVTKAYGD-VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEV----HVfvgTIADD----LRLCApdSDDAKITEAVEtmKAQWIHELPDGLETRVGAggyqLTAAQAQHIALVRLA 505
Cdd:PRK11000 80 VFQSYalypHL---SVAENmsfgLKLAG--AKKEEINQRVN--QVAEVLQLAHLLDRKPKA----LSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 506 LLDPPVVILDEATAEagttaaglLDQA------AELAV----TGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDE 574
Cdd:PRK11000 149 VAEPSVFLLDEPLSN--------LDAAlrvqmrIEISRlhkrLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLE 220
|
.
gi 532492226 575 L 575
Cdd:PRK11000 221 L 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
358-404 |
1.74e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.70 E-value: 1.74e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 532492226 358 KRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGI 404
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV 54
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
374-575 |
2.19e-06 |
|
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: 50.10 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 374 ISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPiddLSDAELR-----HK--VVLVSQEVHVF----- 441
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARGiflppHRrrIGYVFQEARLFphlsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 442 VGTIADDLRLCAPDSDDAKITEAVETMKaqwIHELpdgLETRVGaggyQLTAAQAQHIALVRlALL-DPPVVILDEATAE 520
Cdd:COG4148 95 RGNLLYGRKRAPRAERRISFDEVVELLG---IGHL---LDRRPA----TLSGGERQRVAIGR-ALLsSPRLLLMDEPLAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 521 agttaaglLDQA--AEL-----AVTGRTAVVI---AHRLSQAVR-ADRILVMSGGRVVESGTHDEL 575
Cdd:COG4148 164 --------LDLArkAEIlpyleRLRDELDIPIlyvSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
355-578 |
2.30e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.74 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 355 VDVKRVSYSY-DNSTP--VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIP----VGDGRITVDGTPIDDLSDAEL 427
Cdd:PRK11022 4 LNVDKLSVHFgDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 428 RHkvvLVSQEVHVF-------------VG-TIADDLRLCAPDSDDAKITEAVETMKAQWIhelPDGlETRVGAGGYQLTA 493
Cdd:PRK11022 84 RN---LVGAEVAMIfqdpmtslnpcytVGfQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI---PDP-ASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 494 AQAQH--IALV-----RLALLDPPVVILDEATAEAGTTAAGLLDQAAELAVtgrtaVVIAHRLSQ-AVRADRILVMSGGR 565
Cdd:PRK11022 157 GMSQRvmIAMAiacrpKLLIADEPTTALDVTIQAQIIELLLELQQKENMAL-----VLITHDLALvAEAAHKIIVMYAGQ 231
|
250
....*....|...
gi 532492226 566 VVESGTHDELIGA 578
Cdd:PRK11022 232 VVETGKAHDIFRA 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
368-578 |
2.33e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 368 TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDG----------TPIDDLSDAELRH----KVVL 433
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHvrgaDMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 VSQEVH-----VF-VG-TIADDLRLCAPDSDDAKITEA-----------VETMKAQWIHELPDGLETRVGAgGYQLTAAQ 495
Cdd:PRK10261 109 IFQEPMtslnpVFtVGeQIAESIRLHQGASREEAMVEAkrmldqvripeAQTILSRYPHQLSGGMRQRVMI-AMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 496 AQHIAlvrlallDPPVVILDEATAEAGTTAAGLLDQAAELAVtgrtaVVIAHRLS-QAVRADRILVMSGGRVVESGTHDE 574
Cdd:PRK10261 188 AVLIA-------DEPTTALDVTIQAQILQLIKVLQKEMSMGV-----IFITHDMGvVAEIADRVLVMYQGEAVETGSVEQ 255
|
....
gi 532492226 575 LIGA 578
Cdd:PRK10261 256 IFHA 259
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-575 |
2.71e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.26 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 354 GVDVKRVSYSYDnSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKL------IAGIIPVgDGRITVDGTPIDD--LSDA 425
Cdd:PRK14258 7 AIKVNNLSFYYD-TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKClnrmneLESEVRV-EGRVEFFNQNIYErrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 426 ELRHKVVLVSQEVHVFVGTIADDLRLCA------PDSDDAKITEAveTMKAQwihELPDGLETRVGAGGYQLTAAQAQHI 499
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVkivgwrPKLEIDDIVES--ALKDA---DLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 500 ALVRLALLDPPVVILDEATAEagttaaglLDQAAELAV----------TGRTAVVIAHRLSQAVR-ADRILVMSG----- 563
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFG--------LDPIASMKVesliqslrlrSELTMVIVSHNLHQVSRlSDFTAFFKGnenri 231
|
250
....*....|..
gi 532492226 564 GRVVESGTHDEL 575
Cdd:PRK14258 232 GQLVEFGLTKKI 243
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
374-579 |
7.75e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.86 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 374 ISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDL---- 449
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELvaig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 450 ---------RLCApdSDDAKITEAVETMKAQ-WIHELPDGLetrvgAGGYQLTAAQAQHIAL-VRLALLDPPVVILDEAT 518
Cdd:PRK10575 110 rypwhgalgRFGA--ADREKVEEAISLVGLKpLAHRLVDSL-----SGGERQRAWIAMLVAQdSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 519 AEAGTTAAGLLDQAaelavTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELIGAD 579
Cdd:PRK10575 183 QVDVLALVHRLSQE-----RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
357-403 |
8.39e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 8.39e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 532492226 357 VKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAG 403
Cdd:PRK10636 315 MEKVSAGYGDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG 360
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
370-571 |
1.21e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG--------DGRITVDGTP---IDDLSDAELRHKVVLVSQEV 438
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPlaaIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 439 HVF-------VGTIADDLRLCAPDSDDAKITEA------VETMKAQWIHELPDGLETRVgaggyQLTAAQAQ----HIAL 501
Cdd:PRK13547 96 FAFsareivlLGRYPHARRAGALTHRDGEIAWQalalagATALVGRDVTTLSGGELARV-----QFARVLAQlwppHDAA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 502 V--RLALLDPPVVILDeataeaGTTAAGLLDQAAELAVTGRTAVV-IAHRLSQAVR-ADRILVMSGGRVVESGT 571
Cdd:PRK13547 171 QppRYLLLDEPTAALD------LAHQHRLLDTVRRLARDWNLGVLaIVHDPNLAARhADRIAMLADGAIVAHGA 238
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
368-422 |
1.29e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.49 E-value: 1.29e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 368 TPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIP---------VGDGRITVDGTPIDDL 422
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtpvagcvdVPDNQFGREASLIDAI 106
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
40-310 |
1.42e-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: 47.11 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 40 LALTTVVLLSATACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFA 119
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 120 ATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFALRHFL 199
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 200 RRS-----------GPVYrrsraaqarrgQQLIETLGGAGTVTALRRTDehigRIAETSEHAISFDMQAvrlrtnFFAQL 268
Cdd:cd18580 161 RTSrqlrrlesesrSPLY-----------SHFSETLSGLSTIRAFGWQE----RFIEENLRLLDASQRA------FYLLL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 532492226 269 NGAELLGLaavlsvgyWLVTTGSVSIGAATAAALYFHSLFSP 310
Cdd:cd18580 220 AVQRWLGL--------RLDLLGALLALVVALLAVLLRSSISA 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
344-417 |
2.01e-05 |
|
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: 47.62 E-value: 2.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 344 IPASARSAPIGVDVKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGT 417
Cdd:TIGR03719 312 IPPGPRLGDKVIEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET 384
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
356-592 |
2.12e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.41 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 356 DVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL----RHKV 431
Cdd:PRK10535 9 DIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 432 VLVSQEVHVFVG-TIADDLRLCAPDSDDAKiteaveTMKAQWIHELPD--GLETRVGAGGYQLTAAQAQHIALVR----- 503
Cdd:PRK10535 89 GFIFQRYHLLSHlTAAQNVEVPAVYAGLER------KQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIARalmng 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 504 --LALLDPPVVILDeatAEAGTTAAGLLDQaaeLAVTGRTAVVIAHRLSQAVRADRILVMSGGRVV-ESGTHDELIGADG 580
Cdd:PRK10535 163 gqVILADEPTGALD---SHSGEEVMAILHQ---LRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVrNPPAQEKVNVAGG 236
|
250
....*....|..
gi 532492226 581 SYAALWEAWSVR 592
Cdd:PRK10535 237 TEPVVNTASGWR 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
367-437 |
2.17e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 2.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532492226 367 STPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE-LRHKVVLVSQE 437
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISED 335
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
354-579 |
2.65e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 354 GVDVKRVSYSYDNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDlsdaELRHKVVL 433
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 434 V---SQEVHVFVGTIADDLRLC-----------APDSDDAKITEAVETMkaqwihelpDGLETRVGAGGyQLTAAQAQHI 499
Cdd:PRK15056 82 YvpqSEEVDWSFPVLVEDVVMMgryghmgwlrrAKKRDRQIVTAALARV---------DMVEFRHRQIG-ELSGGQKKRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 500 ALVRLALLDPPVVILDEA-TAEAGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVRADRILVMSGGRVVESGTHDELIGA 578
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPfTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTA 231
|
.
gi 532492226 579 D 579
Cdd:PRK15056 232 E 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
369-578 |
2.82e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 369 PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG-----DGRITVDGTPIDDLSDAELRH----KVVLVSQE-- 437
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 438 -----VHVFVGTIADDLRLCAPDSDDAKITEAVETMKAQWIHELPdgleTRVGAGGYQLTAAQAQHIaLVRLALL----- 507
Cdd:PRK15134 103 vslnpLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAA----KRLTDYPHQLSGGERQRV-MIAMALLtrpel 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532492226 508 ---DPPVVILDEATAEAGTTAAGLLDQaaELavtGRTAVVIAHRLSqAVR--ADRILVMSGGRVVESGTHDELIGA 578
Cdd:PRK15134 178 liaDEPTTALDVSVQAQILQLLRELQQ--EL---NMGLLFITHNLS-IVRklADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
380-452 |
3.70e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 3.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 380 PGERIAVVGSSGAGKTTLAKLIAGIIPVGDGR-ITVDGTPIDDLSDAELRHKVVLVSQEVHVFVGTIADDLRLC 452
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
344-414 |
3.83e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 3.83e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532492226 344 IPASARSAPIGVDVKRVSYSYDNSTpVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITV 414
Cdd:PRK11819 314 IPPGPRLGDKVIEAENLSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
105-331 |
4.15e-05 |
|
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: 45.87 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 105 VAQNVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEA----VNTVIARVLPATVSALFMISLTLVGvgviDWRF 180
Cdd:cd18554 73 IANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQtkdfITTGLMNIWLDMITIIIAICIMLVL----NPKL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 181 TVAIVAVAPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRL 260
Cdd:cd18554 149 TFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRW 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532492226 261 RTNFFAQLNGAELLGLAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLARL 331
Cdd:cd18554 229 NAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
371-421 |
4.38e-05 |
|
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: 44.54 E-value: 4.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAG--IIPVGDGRITVDGTPIDD 421
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDK 75
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
366-419 |
5.87e-05 |
|
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: 46.55 E-value: 5.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 532492226 366 NSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPI 419
Cdd:TIGR01257 1950 TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI 2003
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
370-568 |
1.95e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 43.23 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPI---DDLSDAELRHKVVLVSQEVHVFVGTIA 446
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 447 --DDLRLCA---PDSDDAKITEAVETMKAQwihelpdGLETRVGAGGYQLTAAQAQHIALVR-------LALLDPPVVIL 514
Cdd:PRK10584 105 alENVELPAllrGESSRQSRNGAKALLEQL-------GLGKRLDHLPAQLSGGEQQRVALARafngrpdVLFADEPTGNL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 515 DEATAeagttaagllDQAAELAVT-----GRTAVVIAHRLSQAVRADRILVMSGGRVVE 568
Cdd:PRK10584 178 DRQTG----------DKIADLLFSlnrehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
378-453 |
2.10e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 378 IAPGERIAVVGSSGAGKTTLAKLIAG-----IIPVgDGRITVDGTPIDDLSDaELRHKVVLVSQ-EVHVFVGTIADDLRL 451
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASntdgfHIGV-EGVITYDGITPEEIKK-HYRGDVVYNAEtDVHFPHLTVGETLDF 161
|
..
gi 532492226 452 CA 453
Cdd:TIGR00956 162 AA 163
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
371-451 |
2.15e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE-LRHKVVLVSQEVH-VFVGTIADD 448
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNlVLQRSVMDN 93
|
...
gi 532492226 449 LRL 451
Cdd:PRK10982 94 MWL 96
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
48-176 |
2.20e-04 |
|
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: 43.30 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 48 LSATACGLSTPALLGLMVDAVTE-----GKPFVSLLRITAF-MLSAAAAGVALTWWSTQLLANVAQNVLADLREDVFAAT 121
Cdd:cd18574 6 LAAALVNIQIPLLLGDLVNVISRslketNGDFIEDLKKPALkLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 122 LAQPSSLVEDAGTGDLISRVSGDVEAVNT----VIARVLPAT------VSALFMIS--LTLVGVGVI 176
Cdd:cd18574 86 LRQDIAFFDTHRTGELVNRLTADVQEFKSsfkqCVSQGLRSVtqtvgcVVSLYLISpkLTLLLLVIV 152
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
371-575 |
2.25e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 43.05 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAEL-RHKVV----------------- 432
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVrtfqhvrlfremtvien 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 433 -LVSQEVHVFVGTIADDLRLcaPDSDDAKiTEAVETmKAQWihelpdgLEtRVG--------AGgyQLTAAQAQHIALVR 503
Cdd:PRK11300 101 lLVAQHQQLKTGLFSGLLKT--PAFRRAE-SEALDR-AATW-------LE-RVGllehanrqAG--NLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 504 LALLDPPVVILDEATAEAGTTAAGLLDQ-AAELAVTGRTAVV-IAHRLSQAVR-ADRILVMSGGRVVESGTHDEL 575
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDElIAELRNEHNVTVLlIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
369-592 |
2.28e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.46 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 369 PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDA--ELRHKVVLVSQ--EVHVFVGT 444
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQdpEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 445 IADDL-----RLCAPDSDDA-KITEAVETMKAQWIHELP-----DGLETRVGAGGYQLTAAqaqhialvRLALLDPPVVI 513
Cdd:PRK13638 95 IDSDIafslrNLGVPEAEITrRVDEALTLVDAQHFRHQPiqclsHGQKKRVAIAGALVLQA--------RYLLLDEPTAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 514 LDeataeaGTTAAGLLDQAAELAVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELIGADGSY--AALWEAWS 590
Cdd:PRK13638 167 LD------PAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAMeqAGLTQPWL 240
|
..
gi 532492226 591 VR 592
Cdd:PRK13638 241 VK 242
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
366-440 |
4.15e-04 |
|
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: 41.86 E-value: 4.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532492226 366 NSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG---DGRITVDGTPIDDLSDaELRHKVVLVSQE-VHV 440
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE-KYPGEIIYVSEEdVHF 95
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
341-515 |
4.52e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 341 PASIPASARSAPIgVDVKRVSYSYdNSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG---D----GRIT 413
Cdd:PRK10938 248 PSARHALPANEPR-IVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGysnDltlfGRRR 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 414 VDGTPIDDlsdaeLRHKVVLVSQEVHV--FVGTIADDLRLcapdS---DDAKITEAV---ETMKA-QWIHELpdGLETRV 484
Cdd:PRK10938 326 GSGETIWD-----IKKHIGYVSSSLHLdyRVSTSVRNVIL----SgffDSIGIYQAVsdrQQKLAqQWLDIL--GIDKRT 394
|
170 180 190
....*....|....*....|....*....|...
gi 532492226 485 GAGGYQ-LTAAQaQHIALVRLALLD-PPVVILD 515
Cdd:PRK10938 395 ADAPFHsLSWGQ-QRLALIVRALVKhPTLLILD 426
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
36-330 |
7.36e-04 |
|
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: 41.70 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 36 RGRALALTTVVLLSAtACGLSTPALLGLMVDAVTEGKPFVSLLRITAFMLSAAAAGVALTWWSTQLLANVAQNVLADLRE 115
Cdd:cd18540 1 KKLLILLIILMLLVA-LLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 116 DVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAVAPIHYFAL 195
Cdd:cd18540 80 KAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 196 RHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRLRTNFFAQLNGAELLG 275
Cdd:cd18540 160 IYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 276 LAAVLSVGYWLVTTGSVSIGAATAAALYFHSLFSPIAVFLSNIDELQDAGASLAR 330
Cdd:cd18540 240 TALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAER 294
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
369-584 |
8.01e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.61 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 369 PVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG----DGRITVDGTPIddlSDAELR-HKVVLVSQE------ 437
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPV---APCALRgRKIATIMQNprsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 438 -VHVFVGTIADDLRLCAPDSDDAKITEAVETMkaqwihelpdGLETR---VGAGGYQLTAAQAQH--IALVRLA-----L 506
Cdd:PRK10418 94 pLHTMHTHARETCLALGKPADDATLTAALEAV----------GLENAarvLKLYPFEMSGGMLQRmmIALALLCeapfiI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 507 LDPPVVILDeataeaGTTAAGLLDQAAEL-AVTGRTAVVIAHRLSQAVR-ADRILVMSGGRVVESGTHDELIGADGSYAA 584
Cdd:PRK10418 164 ADEPTTDLD------VVAQARILDLLESIvQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
371-416 |
1.23e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDG 416
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
355-431 |
1.80e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 1.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532492226 355 VDVKRVSYSYDnSTPVIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTpidDLSDAELRHKV 431
Cdd:NF033858 2 ARLEGVSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGG---DMADARHRRAV 74
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
371-417 |
1.90e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 1.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGT 417
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS 86
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
362-419 |
1.91e-03 |
|
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: 40.47 E-value: 1.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532492226 362 YSYDNSTPVIDSISISIAPG-----ERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPI 419
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV 63
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
370-570 |
2.32e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVG---DGRITVDGTPIDdlSDAELRHKVVlVSQEVHVFVGTIA 446
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGvitGGDRLVNGRPLD--SSFQRSIGYV-QQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 447 DDLRLCA--------PDSDDAKITEAVetMKaqwIHELPDGLETRVGAGGYQLTAAQAQHIAL-VRLA-------LLDPP 510
Cdd:TIGR00956 855 ESLRFSAylrqpksvSKSEKMEYVEEV--IK---LLEMESYADAVVGVPGEGLNVEQRKRLTIgVELVakpklllFLDEP 929
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532492226 511 VVILDEataeagttaaglldQAA--------ELAVTGRTAVVIAHRLSQAVRA--DRILVMS-GGRVVESG 570
Cdd:TIGR00956 930 TSGLDS--------------QTAwsicklmrKLADHGQAILCTIHQPSAILFEefDRLLLLQkGGQTVYFG 986
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
370-515 |
2.67e-03 |
|
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: 40.89 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 370 VIDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGtpiddlsdaelRHKVVLVSQEVHVFVGTIADdl 449
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRD-- 533
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532492226 450 RLCAPDS-DDAK---ITEAVETMKAQWIHeLPDGLETRVGAGGYQ-----LTAAQAQHIALVRLALLDPPVVILD 515
Cdd:TIGR00954 534 QIIYPDSsEDMKrrgLSDKDLEQILDNVQ-LTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILD 607
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
372-451 |
3.20e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 40.28 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 372 DSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE-LRHKVVLVSQEVH-VFVGTIADDL 449
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHlVPEMTVAENL 100
|
..
gi 532492226 450 RL 451
Cdd:PRK11288 101 YL 102
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
374-426 |
3.36e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 3.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 532492226 374 ISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAE 426
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ 334
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
378-405 |
3.65e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.18 E-value: 3.65e-03
10 20
....*....|....*....|....*...
gi 532492226 378 IAPGERIAVVGSSGAGKTTLAKLIAGII 405
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVL 389
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
371-420 |
4.50e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.99 E-value: 4.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 532492226 371 IDSISISIAPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPID 420
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT 69
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
364-437 |
4.95e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 4.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532492226 364 YDNSTPVIDSISISiaPGERIAVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPIDDLSDAELRHkvvLVSQE 437
Cdd:PRK10938 14 SDTKTLQLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LVSDE 82
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
384-470 |
6.58e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 38.73 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 384 IAVVGSSGAGKTTLAKLI---AGIIPvGDGRITvDGTPIDDLSDAELRHKvvlVSQEVHVfVGTIADDLRLCA---PDSD 457
Cdd:cd04170 2 IALVGHSGSGKTTLAEALlyaTGAID-RLGRVE-DGNTVSDYDPEEKKRK---MSIETSV-APLEWNGHKINLidtPGYA 75
|
90
....*....|...
gi 532492226 458 DAkITEAVETMKA 470
Cdd:cd04170 76 DF-VGETLSALRA 87
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
377-405 |
6.67e-03 |
|
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: 39.38 E-value: 6.67e-03
10 20
....*....|....*....|....*....
gi 532492226 377 SIAPGERIAVVGSSGAGKTTLAKLIAGII 405
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVL 390
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
108-314 |
7.17e-03 |
|
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: 38.62 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 108 NVLADLREDVFAATLAQPSSLVEDAGTGDLISRVSGDVEAVNTVIARVLPATVSALFMISLTLVGVGVIDWRFTVAIVAV 187
Cdd:cd18585 65 RLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 188 APIHYFALRH-FLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAIsfDMQAVRLRTNFFA 266
Cdd:cd18585 145 LLLAGVVIPLlFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALI--KEQRRLARLSGLS 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 532492226 267 Q-LNG-AELLGLAAVLSVGYWLVTTGsvSIGAATAAALYFHSLfspiAVF 314
Cdd:cd18585 223 QaLMIlLSGLTVWLVLWLGAPLVQNG--ALDGALLAMLVFAVL----ASF 266
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
380-426 |
7.46e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 38.70 E-value: 7.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 532492226 380 PGERI-AVVGSSGAGKTTLAKLIAGIIPVGDGRITVDGTPiddLSDAE 426
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV---LFDAE 66
|
|
| Dck |
COG1428 |
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism]; |
384-402 |
7.83e-03 |
|
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
Pssm-ID: 441037 [Multi-domain] Cd Length: 205 Bit Score: 37.84 E-value: 7.83e-03
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
113-303 |
1.00e-02 |
|
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: 38.47 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 113 LREDVFAATLAQPSSLVEDAGTGDLISRVSGDVeavnTVIARVLPATVSAL------------FMISLTlvgvgvidWRF 180
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDT----TLMSRSVALNANVLlrslvktlgmlgFMLSLS--------WQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532492226 181 TVAIVAVAPIHYFALRHFLRRSGPVYRRSRAAQARRGQQLIETLGGAGTVTALRRTDEHIGRIAETSEHAISFDMQAVRL 260
Cdd:cd18590 139 TLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTV 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 532492226 261 RTNFfaqLNGAELLGLA---AVLSVGYWLVTTGSVSIGAATAAALY 303
Cdd:cd18590 219 RAVY---LLVRRVLQLGvqvLMLYCGRQLIQSGHLTTGSLVSFILY 261
|
|
| |
