|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-578 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 663.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 1 MPRSPVNTdLLRSLRFMRRYRLVAAAAVLAVLGSSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQF 80
Cdd:COG1132 1 MSKSPRKL-LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 81 LQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAM 160
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 161 NWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLT 240
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 241 VRRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRLFEVLD 320
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 321 AETDVPERPGAIELTNARGRVEFRDVHLRYPGsDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVL 400
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 401 LDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLS 480
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 481 GGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTH 560
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558
|
570
....*....|....*...
gi 1309179971 561 EALLAESCVYAEIAASQL 578
Cdd:COG1132 559 EELLARGGLYARLYRLQF 576
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-578 |
1.16e-154 |
|
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: 460.84 E-value: 1.16e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 2 PRSPVNTDLLRSLRFMRRYRLVAAAAVLAVLGSSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFL 81
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 82 QGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLtSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMN 161
Cdd:COG2274 216 RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 162 WQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTV 241
Cdd:COG2274 295 PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 242 RRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRLFEVLDA 321
Cdd:COG2274 375 RRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 322 ETDVPERPGAIELTNARGRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLL 401
Cdd:COG2274 455 PPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 402 DDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSG 481
Cdd:COG2274 535 DGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSG 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 482 GQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHE 561
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHE 694
|
570
....*....|....*..
gi 1309179971 562 ALLAESCVYAEIAASQL 578
Cdd:COG2274 695 ELLARKGLYAELVQQQL 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
12-578 |
3.01e-143 |
|
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: 426.83 E-value: 3.01e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 12 RSLRFMRRYRLVAAAAVLAVLGSSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASH 91
Cdd:TIGR02203 4 RLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 92 GAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVA 171
Cdd:TIGR02203 84 KVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 172 IPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPL 251
Cdd:TIGR02203 164 LPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 252 LFSVGNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRLFEVLDAETDVPErpGA 331
Cdd:TIGR02203 244 TQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDT--GT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 332 IELTNARGRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTL 411
Cdd:TIGR02203 322 RAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 412 ASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADT-FIEQLSDGYDTRVGERGIKLSGGQRQRIAIA 490
Cdd:TIGR02203 402 ASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQdFVDKLPLGLDTPIGENGVLLSGGQRQRLAIA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 491 RALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVY 570
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
....*...
gi 1309179971 571 AEIAASQL 578
Cdd:TIGR02203 562 AQLHNMQF 569
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
10-578 |
1.61e-136 |
|
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: 409.47 E-value: 1.61e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 10 LLRSLRFMRRYRLVAAAAVLAVLGSSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKA 89
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 90 SHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVAL 169
Cdd:TIGR02204 86 GERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 170 VAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQ--QGLTVRRTVAN 247
Cdd:TIGR02204 166 LAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEaaRQRIRTRALLT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 248 AFPLLFSVGnlGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRLFEVLDAETDV-- 325
Cdd:TIGR02204 246 AIVIVLVFG--AIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIka 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 326 PERPGAIElTNARGRVEFRDVHLRYPG-SDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDH 404
Cdd:TIGR02204 324 PAHPKTLP-VPLRGEIEFEQVNFAYPArPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 405 DVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQR 484
Cdd:TIGR02204 403 DLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 485 QRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALL 564
Cdd:TIGR02204 483 QRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELI 562
|
570
....*....|....
gi 1309179971 565 AESCVYAEIAASQL 578
Cdd:TIGR02204 563 AKGGLYARLARLQF 576
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-583 |
8.67e-129 |
|
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: 390.72 E-value: 8.67e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 10 LLRSLRFMRRYRLVAAAAVLAVLGSSVADLIAPQILRRIIDQGITAGRREVITSGALLLigvaaAGGVAQFLQGFLS--- 86
Cdd:COG5265 24 LLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLL-----AYGLLRLLSVLFGelr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 87 ----AKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQL---ITRLTSDVDLVRDFvgggLVQAIAAA---IMLVgAVVL 156
Cdd:COG5265 99 dalfARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLsrdIERGTKGIEFLLRF----LLFNILPTlleIALV-AGIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 157 LLAMNWQLALVALVAIPLTILVLVRFVSKlgpmfR-GFQQRLSALNSilQENVAGI------RVVKAFAREPFEAARYRA 229
Cdd:COG5265 174 LVKYDWWFALITLVTVVLYIAFTVVVTEW-----RtKFRREMNEADS--EANTRAVdsllnyETVKYFGNEAREARRYDE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 230 ANESLLQQGLTVRRTVAnafplLFSVG-----NLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQT 304
Cdd:COG5265 247 ALARYERAAVKSQTSLA-----LLNFGqaliiALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYRE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 305 IARAGASASRLFEVLDAETDVPERPGAIELTNARGRVEFRDVHLRYpGSDAETLNGVSFVVEPGATIALVGSTGSGKTSV 384
Cdd:COG5265 322 IRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 385 VNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQL 464
Cdd:COG5265 401 ARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 465 SDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRAD 544
Cdd:COG5265 481 PDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDAD 560
|
570 580 590
....*....|....*....|....*....|....*....
gi 1309179971 545 EILVIEDGAVVARGTHEALLAESCVYAEIAASQLVGGEE 583
Cdd:COG5265 561 EILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEA 599
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
44-578 |
7.81e-113 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 348.93 E-value: 7.81e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 44 ILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLIT 123
Cdd:PRK11176 47 LLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 124 RLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLtILVLVRFVSKlgpMFR----GFQQRLSA 199
Cdd:PRK11176 127 RITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPI-VSIAIRVVSK---RFRniskNMQNTMGQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 200 LNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGRLTVG 279
Cdd:PRK11176 203 VTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 280 EL-VAFTSyLMLLLQPLFVLGFGAQTIARAGASASRLFEVLDAETDVPErpGAIELTNARGRVEFRDVHLRYPGSDAETL 358
Cdd:PRK11176 283 TItVVFSS-MIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDE--GKRVIERAKGDIEFRNVTFTYPGKEVPAL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 359 NGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAY 438
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 439 GKPD--ATPDAIAAAAQAAQADtFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESA 516
Cdd:PRK11176 440 ARTEqySREQIEEAARMAYAMD-FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERA 518
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 517 LRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEIAASQL 578
Cdd:PRK11176 519 IQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQF 580
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
34-315 |
2.64e-107 |
|
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: 324.38 E-value: 2.64e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYH 113
Cdd:cd18542 11 ATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGF 193
Cdd:cd18542 91 DKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 QQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAH 273
Cdd:cd18542 171 REQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVIN 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1309179971 274 GRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18542 251 GEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
341-572 |
1.16e-105 |
|
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: 318.02 E-value: 1.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVL 500
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 501 IMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAE 572
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
97-571 |
8.12e-105 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 331.69 E-value: 8.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 97 MREAIFERL--QTLSFsyHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPL 174
Cdd:TIGR00958 236 IREDLFRSLlrQDLGF--FDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 175 TILVLVRFVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQqgLTVRRTVANAFPLLFS 254
Cdd:TIGR00958 314 VFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQ--LNKRKALAYAGYLWTT 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 255 --VGNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRLFEVLDAETDVPErPGAI 332
Cdd:TIGR00958 392 svLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL-TGTL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 333 ELTNARGRVEFRDVHLRYPG-SDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTL 411
Cdd:TIGR00958 471 APLNLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 412 ASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIAR 491
Cdd:TIGR00958 551 HYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIAR 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 492 ALLIDPRVLIMDDSTSSVDAETESALRASLDRliGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYA 571
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
89-572 |
1.61e-104 |
|
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: 326.72 E-value: 1.61e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 89 ASHGAAY----DMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQL 164
Cdd:COG4987 78 VSHDATLrllaDLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 165 ALVALVAIPLTILVLVRFVSKLG-PMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRR 243
Cdd:COG4987 158 ALVLALGLLLAGLLLPLLAARLGrRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 244 TVANAFPLLFSVGNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRLFEVLDAET 323
Cdd:COG4987 238 LSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 324 DVPErPGAIELTNARGRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDD 403
Cdd:COG4987 318 AVTE-PAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 404 HDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQ 483
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 484 RQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEAL 563
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
....*....
gi 1309179971 564 LAESCVYAE 572
Cdd:COG4987 557 LAQNGRYRQ 565
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-577 |
2.21e-104 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 326.92 E-value: 2.21e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 12 RSLRFMRRYRLVAAAAVLAVLGSSVADLIAPQILRRIIDQgITAGrrevitSGALLLIGVAAAGGVAQFLQGFLSAKASH 91
Cdd:PRK13657 9 RVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDA-ISGK------GDIFPLLAAWAGFGLFNIIAGVLVARHAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 92 GAAYDMREAI----FERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALV 167
Cdd:PRK13657 82 RLAHRRRLAVlteyFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRLSLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 168 aLVAIPLTILVLVRFV-SKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVA 246
Cdd:PRK13657 162 -LVVLGIVYTLITTLVmRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 247 NAFPLLFSVGNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPL-FVLGFGAQTIARAgASASRLFEVLDAETDV 325
Cdd:PRK13657 241 LASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLdQVVAFINQVFMAA-PKLEEFFEVEDAVPDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 326 PERPGAIELTNARGRVEFRDVHLRYPGSdAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHD 405
Cdd:PRK13657 320 RDPPGAIDLGRVKGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 406 VRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQ 485
Cdd:PRK13657 399 IRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 486 RIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLA 565
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVA 558
|
570
....*....|..
gi 1309179971 566 ESCVYAEIAASQ 577
Cdd:PRK13657 559 RGGRFAALLRAQ 570
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
47-566 |
2.47e-104 |
|
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: 325.94 E-value: 2.47e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 47 RIIDQGITAGR-REVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRL 125
Cdd:COG4988 42 SLLAGLIIGGApLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 126 TSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTIL--VLVRFVSKlgPMFRGFQQRLSALNSI 203
Cdd:COG4988 122 TEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLVTAPLIPLfmILVGKGAA--KASRRQWRALARLSGH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 204 LQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRtVA--NAFPL-LFSVgnLGVALVvwagAVQVAHgRLTVGE 280
Cdd:COG4988 200 FLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLR-VAflSSAVLeFFAS--LSIALV----AVYIGF-RLLGGS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 281 LVAFTSYLMLLLQPLFVL---GFGAQTIARAG--ASASRLFEVLDAETDVPERPGAIELTNARGRVEFRDVHLRYPGsDA 355
Cdd:COG4988 272 LTLFAALFVLLLAPEFFLplrDLGSFYHARANgiAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPG-GR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 356 ETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAEN 435
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIREN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 436 IAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETES 515
Cdd:COG4988 431 LRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEA 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 516 ALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAE 566
Cdd:COG4988 511 EILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
341-577 |
9.46e-101 |
|
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: 305.62 E-value: 9.46e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPG-SDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIG 419
Cdd:cd03249 1 IEFKNVSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 VVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRV 499
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 500 LIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEIAASQ 577
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
35-573 |
6.64e-99 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 312.42 E-value: 6.64e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 35 SVADLIAPQILRRIIDqGITAGRrevITSGALLL-IGVAAAGGVAQFLQGFLSAKASHGAAY----DMREAIFERLQTLS 109
Cdd:PRK10789 8 AMLQLIPPKVVGIIVD-GVTEQH---MTTGQILMwIGTMVLIAVVVYLLRYVWRVLLFGASYqlavELREDFYRQLSRQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 110 FSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMlvGAVVLLL---AMNWQLALVALVAIPLTILVLVRFVSKL 186
Cdd:PRK10789 84 PEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVM--GCAVLIVmstQISWQLTLLALLPMPVMAIMIKRYGDQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 187 GPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWA 266
Cdd:PRK10789 162 HERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 267 GAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRLFEVLDAETDVPErpGAIELTNARGRVEFRDV 346
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKD--GSEPVPEGRGELDVNIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 347 HLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSV 426
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 427 LFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDST 506
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 507 SSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEI 573
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
341-577 |
9.84e-97 |
|
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: 294.91 E-value: 9.84e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSdAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVL 500
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 501 IMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEIAASQ 577
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
339-565 |
5.47e-91 |
|
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: 279.88 E-value: 5.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 339 GRVEFRDVHLRYpGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRI 418
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPR 498
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 499 VLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLA 565
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
39-577 |
3.00e-87 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 285.10 E-value: 3.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 39 LIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQT 118
Cdd:TIGR01846 156 LVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRV 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 119 GQLITRLtSDVDLVRDFVGGglvQAIAAAIMLVGAVVLLLAMNW---QLALVALVAIPLTILVLVrFVSklGPMFRGFQQ 195
Cdd:TIGR01846 236 GDTVARV-RELEQIRNFLTG---SALTVVLDLLFVVVFLAVMFFyspTLTGVVIGSLVCYALLSV-FVG--PILRKRVED 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 196 ---RLSALNSILQENVAGIRVVKAFAREPF-------EAARYRAANESLLQQGLTVRRTVAnafpllfSVGNLGVALVVW 265
Cdd:TIGR01846 309 kfeRSAAATSFLVESVTGIETIKATATEPQfqnrwdrQLAAYVAASFRVTNLGNIAGQAIE-------LIQKLTFAILLW 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 266 AGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRLFEVLDAETDvPERPGAIELTNARGRVEFRD 345
Cdd:TIGR01846 382 FGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTE-PRSAGLAALPELRGAITFEN 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 346 VHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDS 425
Cdd:TIGR01846 461 IRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 426 VLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDS 505
Cdd:TIGR01846 541 VLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEA 620
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 506 TSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEIAASQ 577
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
33-314 |
1.13e-84 |
|
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: 265.80 E-value: 1.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSY 112
Cdd:cd18548 10 LEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 113 HDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRG 192
Cdd:cd18548 90 IDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 193 FQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVA 272
Cdd:cd18548 170 VQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLIN 249
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1309179971 273 HGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASR 314
Cdd:cd18548 250 AGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKR 291
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
34-315 |
7.76e-83 |
|
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: 261.33 E-value: 7.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYH 113
Cdd:cd07346 11 ATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGF 193
Cdd:cd07346 91 DRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 QQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAH 273
Cdd:cd07346 171 RESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQ 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1309179971 274 GRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd07346 251 GSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
45-549 |
1.20e-75 |
|
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: 250.28 E-value: 1.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 45 LRRIIDQGITAGR-REVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLIT 123
Cdd:TIGR02857 26 LARVVDGLISAGEpLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELAT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 124 RLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSI 203
Cdd:TIGR02857 106 LALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 204 LQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRtVA--NAFPLLFsVGNLGVALVvwagAVQVAHgRLTVGEL 281
Cdd:TIGR02857 186 FLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLR-IAflSSAVLEL-FATLSVALV----AVYIGF-RLLAGDL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 282 VAFTSYLMLLLQPLFVL---GFGAQTIARAG--ASASRLFEVLDAETdVPERPGAIELTNARGRVEFRDVHLRYPGSDAe 356
Cdd:TIGR02857 259 DLATGLFVLLLAPEFYLplrQLGAQYHARADgvAAAEALFAVLDAAP-RPLAGKAPVTAAPASSLEFSGVSVAYPGRRP- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 357 TLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENI 436
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 437 AYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESA 516
Cdd:TIGR02857 417 RLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAE 496
|
490 500 510
....*....|....*....|....*....|...
gi 1309179971 517 LRASLDRLIGGRTTFIVAQRLSTVKRADEILVI 549
Cdd:TIGR02857 497 VLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
39-572 |
6.24e-75 |
|
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: 252.56 E-value: 6.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 39 LIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQT 118
Cdd:TIGR03796 171 LVIPAFSQIFVDEILVQGRQDWLRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 119 GQLITRLTSDvDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLS 198
Cdd:TIGR03796 251 GDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 199 ALNSILQENVAGIRVVKAFAREPFEAARYRAANESLL--QQGLTVRRTVANAFPLLFSvgNLGVALVVWAGAVQVAHGRL 276
Cdd:TIGR03796 330 KLTGVAISGLQSIETLKASGLESDFFSRWAGYQAKLLnaQQELGVLTQILGVLPTLLT--SLNSALILVVGGLRVMEGQL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 277 TVGELVAFTSYLMLLLQPLF-VLGFGaQTIARAGASASRLFEVLDAETD-VPERPGAIELTNA-----RGRVEFRDVHLR 349
Cdd:TIGR03796 408 TIGMLVAFQSLMSSFLEPVNnLVGFG-GTLQELEGDLNRLDDVLRNPVDpLLEEPEGSAATSEpprrlSGYVELRNITFG 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 350 YPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFS 429
Cdd:TIGR03796 487 YSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 430 GTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSV 509
Cdd:TIGR03796 567 GTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSAL 646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 510 DAETESALRASLDRLigGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAE 572
Cdd:TIGR03796 647 DPETEKIIDDNLRRR--GCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYAR 707
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-314 |
2.00e-74 |
|
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: 239.33 E-value: 2.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIID----QGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLS 109
Cdd:cd18563 11 GTALGLVPPYLTKILIDdvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 110 FSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPM 189
Cdd:cd18563 91 LSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 190 FRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAV 269
Cdd:cd18563 171 FHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGR 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1309179971 270 QVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASR 314
Cdd:cd18563 251 QVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
341-552 |
3.15e-74 |
|
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: 234.20 E-value: 3.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSGTIAENIaygkpdatpdaiaaaaqaaqadtfieqlsdgydtrvgergikLSGGQRQRIAIARALLIDPRVL 500
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 501 IMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDG 552
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
42-563 |
8.55e-73 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 244.03 E-value: 8.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 42 PQILRRIIDqGITAGRREVITsgALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQL 121
Cdd:TIGR01192 39 PILFGRIID-AISSKSDVLPT--LALWAGFGVFNTIAYVLVAREADRLAHGRRATLLTEAFGRIISMPLSWHQQRGTSNA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 122 ITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALN 201
Cdd:TIGR01192 116 LHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 202 SILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGRLTVGEL 281
Cdd:TIGR01192 196 KHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELSVGEV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 282 VAFTSYLMLLLQPLFVLGFGAQTIARAGASASRLFEVLDAETDVPERPGAIELTNARGRVEFRDVHLRYPGSdAETLNGV 361
Cdd:TIGR01192 276 IAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELPNVKGAVEFRHITFEFANS-SQGVFDV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 362 SFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKP 441
Cdd:TIGR01192 355 SFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGRE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 442 DATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASL 521
Cdd:TIGR01192 435 GATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAI 514
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1309179971 522 DRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEAL 563
Cdd:TIGR01192 515 DALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQEL 556
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
341-577 |
8.87e-73 |
|
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: 233.15 E-value: 8.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVL 500
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 501 IMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEIAASQ 577
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
33-315 |
9.95e-72 |
|
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: 232.37 E-value: 9.95e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSY 112
Cdd:cd18543 10 LATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 113 HDRIQTGQLITRLTSDVDLVRDFVGGGLvQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRG 192
Cdd:cd18543 90 HDRWQSGQLLSRATSDLSLVQRFLAFGP-FLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 193 FQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVA 272
Cdd:cd18543 169 AQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVA 248
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1309179971 273 HGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18543 249 NGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
45-573 |
4.67e-71 |
|
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: 242.34 E-value: 4.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 45 LRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITR 124
Cdd:TIGR01193 179 LQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSR 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 125 LTsDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSIL 204
Cdd:TIGR01193 259 FT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 205 QENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRT--VANAfplLFSVGNLGVALVV-WAGAVQVAHGRLTVGEL 281
Cdd:TIGR01193 338 IEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKAdqGQQA---IKAVTKLILNVVIlWTGAYLVMRGKLTLGQL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 282 VAFTSYLMLLLQPLFVLgFGAQTIARAGASAS-RLFEVLDAETDVPERPGAIELTNARGRVEFRDVHLRYpGSDAETLNG 360
Cdd:TIGR01193 415 ITFNALLSYFLTPLENI-INLQPKLQAARVANnRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSY-GYGSNILSD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 361 VSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYG- 439
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGa 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 440 KPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRA 519
Cdd:TIGR01193 573 KENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVN 652
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 520 SLDRLiGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEI 573
Cdd:TIGR01193 653 NLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
34-315 |
3.16e-70 |
|
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: 228.45 E-value: 3.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDqGITAGR--REVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFS 111
Cdd:cd18541 11 VDLLQLLIPRIIGRAID-ALTAGTltASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 112 YHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFR 191
Cdd:cd18541 90 FYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 192 GFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQV 271
Cdd:cd18541 170 KVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLV 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1309179971 272 AHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18541 250 IRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
34-314 |
1.71e-68 |
|
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: 223.80 E-value: 1.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREV--ITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFS 111
Cdd:cd18544 11 ATALELLGPLLIKRAIDDYIVPGQGDLqgLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 112 YHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFR 191
Cdd:cd18544 91 FFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 192 GFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQV 271
Cdd:cd18544 171 EVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1309179971 272 AHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASR 314
Cdd:cd18544 251 LSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAER 293
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
33-314 |
4.35e-68 |
|
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: 222.80 E-value: 4.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDQ-GITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFS 111
Cdd:cd18778 10 LSTLLGLVPPWLIRELVDLvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 112 YHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFR 191
Cdd:cd18778 90 YFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 192 GFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQV 271
Cdd:cd18778 170 KVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLV 249
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1309179971 272 AHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASR 314
Cdd:cd18778 250 LAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAER 292
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
39-578 |
6.07e-67 |
|
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: 230.61 E-value: 6.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 39 LIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQT 118
Cdd:TIGR03797 153 MLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYST 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 119 GQLITRlTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVL----VRFVSKLGPMFRGfQ 194
Cdd:TIGR03797 233 GDLASR-AMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALVAVALALVAIAVTlvlgLLQVRKERRLLEL-S 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 195 QRLSALNSILQENVAGIRV----VKAFAR--EPFEAARYRAANESLLQQGLTVRRTVanaFPLLFSvgnlgvALVVWAGA 268
Cdd:TIGR03797 311 GKISGLTVQLINGISKLRVagaeNRAFARwaKLFSRQRKLELSAQRIENLLTVFNAV---LPVLTS------AALFAAAI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 269 VQVAHGRLTVGELVAFTSYLMLLLQPLFVLgfgAQTIARAGASA---SRLFEVLDAETDVPE---RPGAIeltnaRGRVE 342
Cdd:TIGR03797 382 SLLGGAGLSLGSFLAFNTAFGSFSGAVTQL---SNTLISILAVIplwERAKPILEALPEVDEaktDPGKL-----SGAIE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 343 FRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVM 422
Cdd:TIGR03797 454 VDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 423 QDSVLFSGTIAENIAYGKPdATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIM 502
Cdd:TIGR03797 534 QNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLF 612
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 503 DDSTSSVDAETESALRASLDRLIGGRttFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEIAASQL 578
Cdd:TIGR03797 613 DEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQL 686
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
330-554 |
7.01e-66 |
|
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: 214.64 E-value: 7.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 330 GAIELTNARGRVEFRDVHLRYPG-SDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRD 408
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 409 LTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIA 488
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 489 IARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAV 554
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-594 |
7.59e-66 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 225.75 E-value: 7.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 10 LLRSLRFMRRYRLVAAAAVLAVLGSSVADLIAPQILRRIIDQGITAGRREV-ITSG---ALLLIGVAAAGgvAQFLQGFL 85
Cdd:PRK10790 11 LKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLgLVAGlaaAYVGLQLLAAG--LHYAQSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 86 SAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRD-FVGggLVQAIAAAIMLVGAvvLLLAM---N 161
Cdd:PRK10790 89 FNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDlYVT--VVATVLRSAALIGA--MLVAMfslD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 162 WQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREP------FEAAR--YRAANES 233
Cdd:PRK10790 165 WRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQArfgermGEASRshYMARMQT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 234 LLQQGLTVRrtvanafPLLfsvgNLGVALVVWAGAVQV---AHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGA 310
Cdd:PRK10790 245 LRLDGFLLR-------PLL----SLFSALILCGLLMLFgfsASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 311 SASRLFEVLDAETdvpERPGAIELTNARGRVEFRDVHLRYpGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPR 390
Cdd:PRK10790 314 AGERVFELMDGPR---QQYGNDDRPLQSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 391 FYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKpDATPDAIAAAAQAAQADTFIEQLSDGYDT 470
Cdd:PRK10790 390 YYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 471 RVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLdRLIGGRTTFIV-AQRLSTVKRADEILVI 549
Cdd:PRK10790 469 PLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVViAHRLSTIVEADTILVL 547
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1309179971 550 EDGAVVARGTHEALLAESCVYAEIAASQLVgGEELDLPESCMLEG 594
Cdd:PRK10790 548 HRGQAVEQGTHQQLLAAQGRYWQMYQLQLA-GEELAASVREEESL 591
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
33-314 |
1.14e-65 |
|
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: 216.57 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSY 112
Cdd:cd18545 11 LSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 113 HDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRG 192
Cdd:cd18545 91 FDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 193 FQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVA 272
Cdd:cd18545 171 VRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1309179971 273 HGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASR 314
Cdd:cd18545 251 GGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAER 292
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
33-315 |
4.11e-65 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 215.45 E-value: 4.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDQ---------------GITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDM 97
Cdd:cd18564 10 LETALRLLEPWPLKVVIDDvlgdkplpgllglapLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 98 REAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTIL 177
Cdd:cd18564 90 RRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 178 VLVRFVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGN 257
Cdd:cd18564 170 AARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 258 LGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18564 250 VGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
339-558 |
7.57e-65 |
|
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: 211.68 E-value: 7.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 339 GRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRI 418
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPR 498
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 499 VLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARG 558
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
34-314 |
1.30e-64 |
|
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: 213.80 E-value: 1.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQ------GITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQT 107
Cdd:cd18547 11 STLLSVLGPYLLGKAIDLiieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 108 LSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLG 187
Cdd:cd18547 91 LPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 188 PMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTvrrtvANAF-----PLLFSVGNLGVAL 262
Cdd:cd18547 171 KYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK-----AQFYsgllmPIMNFINNLGYVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 263 VVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASR 314
Cdd:cd18547 246 VAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
34-299 |
7.17e-64 |
|
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: 211.57 E-value: 7.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYH 113
Cdd:cd18576 8 SSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGF 193
Cdd:cd18576 88 HERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 QQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAH 273
Cdd:cd18576 168 QDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLA 247
|
250 260
....*....|....*....|....*.
gi 1309179971 274 GRLTVGELVAFTSYLMLLLQPLFVLG 299
Cdd:cd18576 248 GELTAGDLVAFLLYTLFIAGSIGSLA 273
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
64-537 |
3.67e-63 |
|
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: 216.84 E-value: 3.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 64 GALLLIGVAAAG--------GVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDF 135
Cdd:TIGR02868 47 PPVLYLSVAAVAvrafgigrAVFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 136 VGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRL-SALNSILQENVAGIRVV 214
Cdd:TIGR02868 127 YVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLrGELAAQLTDALDGAAEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 215 KAFAREPFEAARYRAANESLL--QQGLTVRRTVANAFPLLfsVGNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLL 292
Cdd:TIGR02868 207 VASGALPAALAQVEEADRELTraERRAAAATALGAALTLL--AAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 293 QPLFVLGFGAQTIARAGASASRLFEVLDAETDVPER--PGAIELTNARGRVEFRDVHLRYPGsDAETLNGVSFVVEPGAT 370
Cdd:TIGR02868 285 EAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGsaPAAGAVGLGKPTLELRDLSAGYPG-APPVLDGVSLDLPPGER 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 371 IALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAA 450
Cdd:TIGR02868 364 VAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 451 AAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTT 530
Cdd:TIGR02868 444 ALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV 523
|
....*..
gi 1309179971 531 FIVAQRL 537
Cdd:TIGR02868 524 VLITHHL 530
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
34-315 |
3.91e-63 |
|
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: 209.65 E-value: 3.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYH 113
Cdd:cd18546 11 DTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGF 193
Cdd:cd18546 91 ERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 QQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAH 273
Cdd:cd18546 171 RERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAA 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1309179971 274 GRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18546 251 GTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
33-315 |
3.92e-63 |
|
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: 209.59 E-value: 3.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSY 112
Cdd:cd18552 10 LVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 113 HDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRG 192
Cdd:cd18552 90 FDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 193 FQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVA 272
Cdd:cd18552 170 SQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVI 249
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1309179971 273 HGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18552 250 SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
60-566 |
7.41e-61 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 211.53 E-value: 7.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 60 VITSG--------ALLLIGVAAAGGVAQFLQGFLSAKAshGAAYDMREAifERLQTLSFSYHDRIQTGQLITRLtSDVDL 131
Cdd:COG4618 50 VLTSRsvdtllmlTLLALGLYAVMGLLDAVRSRILVRV--GARLDRRLG--PRVFDAAFRAALRGGGGAAAQAL-RDLDT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 132 VRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIplTILVLVRFVSKL--GPMFRGFQQRLSALNSILQENVA 209
Cdd:COG4618 125 LRQFLTGPGLFALFDLPWAPIFLAVLFLFHPLLGLLALVGA--LVLVALALLNERltRKPLKEANEAAIRANAFAEAALR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 210 GIRVVKAFAREPFEAARYRAAN-ESLLQQGLTVRRT-----VANAFPLLFSVGNLGValvvwaGAVQVAHGRLTVGELVA 283
Cdd:COG4618 203 NAEVIEAMGMLPALRRRWQRANaRALALQARASDRAggfsaLSKFLRLLLQSAVLGL------GAYLVIQGEITPGAMIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 284 fTSYLM-LLLQPlFVLGFGA-QTIARAGASASRLFEVLDAetdVPERPGAIELTNARGRVEFRDVHLRYPGSDAETLNGV 361
Cdd:COG4618 277 -ASILMgRALAP-IEQAIGGwKQFVSARQAYRRLNELLAA---VPAEPERMPLPRPKGRLSVENLTVVPPGSKRPILRGV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 362 SFVVEPGATIALVGSTGSGKTS----VVNLVPrfydVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIA 437
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTlarlLVGVWP----PTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 438 yGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESAL 517
Cdd:COG4618 428 -RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1309179971 518 RASLDRL-IGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAE 566
Cdd:COG4618 507 AAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-295 |
4.56e-57 |
|
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: 193.85 E-value: 4.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYH 113
Cdd:cd18550 11 SALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGF 193
Cdd:cd18550 91 TRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 QQRLSALNSILQE--NVAGIRVVKAFAREPFEAARYRAANESLlqQGLTVRRTVANA--FPLLFSVGNLGVALVVWAGAV 269
Cdd:cd18550 171 QEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSREL--RDLGVRQALAGRwfFAALGLFTAIGPALVYWVGGL 248
|
250 260
....*....|....*....|....*.
gi 1309179971 270 QVAHGRLTVGELVAFTSYLMLLLQPL 295
Cdd:cd18550 249 LVIGGGLTIGTLVAFTALLGRLYGPL 274
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
34-315 |
1.02e-55 |
|
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: 189.95 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDqgiTAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYH 113
Cdd:cd18551 11 GTAASLAQPLLVKNLID---ALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGF 193
Cdd:cd18551 88 DRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 QQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAH 273
Cdd:cd18551 168 QDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVAS 247
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1309179971 274 GRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18551 248 GALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
89-572 |
7.61e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 190.04 E-value: 7.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 89 ASHGAAY----DMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVrDFVGGGLVQAIAAAIMLVGAVVLLLA-MNWQ 163
Cdd:PRK11160 83 VSHDATFrvltHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTL-DHLYLRLISPLVAALVVILVLTIGLSfFDLT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 164 LALVaLVAIPLTILVLVRFV-SKLGpmfRGFQQRLSALNSILQENV-------AGIRVVKAfarepfeAARYRAANESLL 235
Cdd:PRK11160 162 LALT-LGGILLLLLLLLPLLfYRLG---KKPGQDLTHLRAQYRVQLtewlqgqAELTLFGA-------EDRYRQQLEQTE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 236 QQGLTVRRTVAN----AFPLLFSVGNLGVALVVW--AGAVQ--VAHGRLTVgeLVAFTSYLML-LLQPLFV----LGfga 302
Cdd:PRK11160 231 QQWLAAQRRQANltglSQALMILANGLTVVLMLWlaAGGVGgnAQPGALIA--LFVFAALAAFeALMPVAGafqhLG--- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 303 QTIAragaSASRLFEVLDAETDVpERPGAIELTNARGRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKT 382
Cdd:PRK11160 306 QVIA----SARRINEITEQKPEV-TFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 383 SVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIE 462
Cdd:PRK11160 381 TLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLE 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 463 QlSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKR 542
Cdd:PRK11160 461 D-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ 539
|
490 500 510
....*....|....*....|....*....|
gi 1309179971 543 ADEILVIEDGAVVARGTHEALLAESCVYAE 572
Cdd:PRK11160 540 FDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
34-315 |
2.89e-52 |
|
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: 180.83 E-value: 2.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYH 113
Cdd:cd18557 8 SSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGF 193
Cdd:cd18557 88 DKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 QQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQqgLTVRRTVANAFPLLFS--VGNLGVALVVWAGAVQV 271
Cdd:cd18557 168 QDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYR--LARKKALANALFQGITslLIYLSLLLVLWYGGYLV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1309179971 272 AHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18557 246 LSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
339-559 |
4.58e-52 |
|
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: 178.07 E-value: 4.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 339 GRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRI 418
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSGTIAENIA-YGKpdATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDP 497
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 498 RVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGT 559
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
65-566 |
9.19e-52 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 186.40 E-value: 9.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 65 ALLLIGVAAAGGVAQFLQGFLSAKASHgaayDMREAIFERLQTLSFSY---HDRIQTGQLITrltsDVDLVRDFV-GGGL 140
Cdd:TIGR01842 49 TVLALGLYLFLGLLDALRSFVLVRIGE----KLDGALNQPIFAASFSAtlrRGSGDGLQALR----DLDQLRQFLtGPGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 141 VQAIAAAIMLVGAVVLLLAMNW--QLALVALVAIPLTILVLVRFVSKlgpMFRGFQQRLSALNSILQENVAGIRVVKAFA 218
Cdd:TIGR01842 121 FAFFDAPWMPIYLLVCFLLHPWigILALGGAVVLVGLALLNNRATKK---PLKEATEASIRANNLADSALRNAEVIEAMG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 219 REPFEAARYRAANE-SLLQQGLTVRR-----TVANAFPLLFSVGNLGValvvwaGAVQVAHGRLTVGELVAFTSYLMLLL 292
Cdd:TIGR01842 198 MMGNLTKRWGRFHSkYLSAQSAASDRagmlsNLSKYFRIVLQSLVLGL------GAYLAIDGEITPGMMIAGSILVGRAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 293 QPLFVLGFGAQTIARAGASASRLFEVLDAetdVPERPGAIELTNARGRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIA 372
Cdd:TIGR01842 272 APIDGAIGGWKQFSGARQAYKRLNELLAN---YPSRDPAMPLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 373 LVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAA 452
Cdd:TIGR01842 349 IIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 453 QAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRL-IGGRTTF 531
Cdd:TIGR01842 429 KLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVV 508
|
490 500 510
....*....|....*....|....*....|....*
gi 1309179971 532 IVAQRLSTVKRADEILVIEDGAVVARGTHEALLAE 566
Cdd:TIGR01842 509 VITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
34-295 |
5.21e-51 |
|
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: 177.06 E-value: 5.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSG--ALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFS 111
Cdd:pfam00664 11 SGAISPAFPLVLGRILDVLLPDGDPETQALNvySLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 112 YHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFR 191
Cdd:pfam00664 91 FFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 192 GFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQV 271
Cdd:pfam00664 171 KEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLV 250
|
250 260
....*....|....*....|....
gi 1309179971 272 AHGRLTVGELVAFTSYLMLLLQPL 295
Cdd:pfam00664 251 ISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
34-298 |
4.89e-50 |
|
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: 174.95 E-value: 4.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGF----LSAKAShgaaYDMREAIFERLQTLS 109
Cdd:cd18549 14 IAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYwghvMGARIE----TDMRRDLFEHLQKLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 110 FSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPM 189
Cdd:cd18549 90 FSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 190 FRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAV 269
Cdd:cd18549 170 FRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGY 249
|
250 260
....*....|....*....|....*....
gi 1309179971 270 QVAHGRLTVGELVAFTSYLMLLLQPLFVL 298
Cdd:cd18549 250 FIIKGEITLGDLVAFLLYVNVFIKPIRRL 278
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
48-314 |
7.82e-49 |
|
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: 172.37 E-value: 7.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 48 IIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTS 127
Cdd:cd18565 40 VPASLGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 128 DVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQEN 207
Cdd:cd18565 120 DVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 208 VAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGR------LTVGEL 281
Cdd:cd18565 200 LSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPplftgtLTVGTL 279
|
250 260 270
....*....|....*....|....*....|...
gi 1309179971 282 VAFTSYLMLLLQPLFVLGFGAQTIARAGASASR 314
Cdd:cd18565 280 VTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKR 312
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
284-575 |
1.29e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 170.03 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 284 FTSYLMLLL-----QPLFVLGFGAQTIARAGASASRLFEVLDAETDVPERPGAIELTNARGRVEFRDVHLRYPgsDAETL 358
Cdd:PRK11174 288 FAGFFVLILapefyQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEILSP--DGKTL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 359 NG-VSFVVEPGATIALVGSTGSGKTSVVNLVPRF--YDvtgGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAEN 435
Cdd:PRK11174 366 AGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDN 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 436 IAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETES 515
Cdd:PRK11174 443 VLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 516 ALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEIAA 575
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
34-315 |
1.65e-45 |
|
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: 162.65 E-value: 1.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYH 113
Cdd:cd18575 8 AAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGF 193
Cdd:cd18575 88 ETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 QQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQqgLTVRRTVANAF--PLLFSVGNLGVALVVWAGAVQV 271
Cdd:cd18575 168 QDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFA--AALRRIRARALltALVIFLVFGAIVFVLWLGAHDV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1309179971 272 AHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18575 246 LAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
65-565 |
7.30e-45 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 171.75 E-value: 7.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 65 ALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERL--QTLSFSYHDRIQTGQLITRLTSDVDLVRDfvggGLVQ 142
Cdd:PTZ00265 869 SLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENIlyQEISFFDQDKHAPGLLSAHINRDVHLLKT----GLVN 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 143 AIAAAIMLVgaVVLLLAMNWQLALVALVAIPLTILVLVrfvsklgpMFRGF--QQRLSALNSILQENVAGIRVVKAFA-- 218
Cdd:PTZ00265 945 NIVIFTHFI--VLFLVSMVMSFYFCPIVAAVLTGTYFI--------FMRVFaiRARLTANKDVEKKEINQPGTVFAYNsd 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 219 ----REP---FEAARYRAANE----------SLLQQGLTV------RRTVANAFPLLFS-VGNLGV-ALVVWAGAVQVAH 273
Cdd:PTZ00265 1015 deifKDPsflIQEAFYNMNTViiygledyfcNLIEKAIDYsnkgqkRKTLVNSMLWGFSqSAQLFInSFAYWFGSFLIRR 1094
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 274 GRLTVGElvaftsYLMLLLQPLFVLGFGAQTIARAGASAS------RLFEVLDAETDVPERP-GAIELTNA---RGRVEF 343
Cdd:PTZ00265 1095 GTILVDD------FMKSLFTFLFTGSYAGKLMSLKGDSENaklsfeKYYPLIIRKSNIDVRDnGGIRIKNKndiKGKIEI 1168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 344 RDVHLRYPGS-DAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDV---------------------------- 394
Cdd:PTZ00265 1169 MDVNFRYISRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeq 1248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 395 --------------------------TGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPDATPDAI 448
Cdd:PTZ00265 1249 nvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDV 1328
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 449 AAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASL----DRl 524
Cdd:PTZ00265 1329 KRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDK- 1407
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1309179971 525 iGGRTTFIVAQRLSTVKRADEILVIED----GAVV-ARGTHEALLA 565
Cdd:PTZ00265 1408 -ADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAHGTHEELLS 1452
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-314 |
1.76e-44 |
|
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: 159.95 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYH 113
Cdd:cd18540 14 VALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRgf 193
Cdd:cd18540 94 DKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYR-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 qqRLSALNSIL----QENVAGIRVVKAFARE-----PFE--AARYRAAnesllqqglTVRRTVANA--FPLLFSVGNLGV 260
Cdd:cd18540 172 --KVRKINSRItgafNEGITGAKTTKTLVREeknlrEFKelTEEMRRA---------SVRAARLSAlfLPIVLFLGSIAT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 261 ALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLfvlgfgaQTIAR-------AGASASR 314
Cdd:cd18540 241 ALVLWYGGILVLAGAITIGTLVAFISYATQFFEPI-------QQLARvlaelqsAQASAER 294
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
342-554 |
4.28e-44 |
|
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: 154.68 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVV 421
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 422 MQDSVLFSGTIAENIaygkpdatpdaiaaaaqaaqadtfieqlsdgydtrvgergikLSGGQRQRIAIARALLIDPRVLI 501
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 502 MDDSTSSVDAETESALRASLDRL-IGGRTTFIVAQRLSTVKRADEILVIEDGAV 554
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
339-559 |
5.71e-41 |
|
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: 147.56 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 339 GRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRI 418
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSGTIAENIaygkpdatpdaiaaaaqaaqaDTFIEQLSDGYDT--RVGERGIKLSGGQRQRIAIARALLID 496
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNL---------------------DPFDEYSDEEIYGalRVSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 497 PRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGT 559
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
76-551 |
7.57e-40 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 156.34 E-value: 7.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 76 GVAQFLQGFLSAkashgaaYDMREAIFERLQTLSFSYHDRI--QTGQLI-----TRLTSDVDLVRDFVGGGL----VQAI 144
Cdd:PTZ00265 107 GIFQFILSFISS-------FCMDVVTTKILKTLKLEFLKSVfyQDGQFHdnnpgSKLTSDLDFYLEQVNAGIgtkfITIF 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 145 AAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGpmfrgFQQRLSALN-----SILQENVAGIRVVKAFA- 218
Cdd:PTZ00265 180 TYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVK-----INKKTSLLYnnntmSIIEEALVGIRTVVSYCg 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 219 ----------REPFEAARYRAAN--ESL---LQQGLTVrrtVANAFPLLFsvgnlGVALVVWAGAVQVAHGRLTVGELVa 283
Cdd:PTZ00265 255 ektilkkfnlSEKLYSKYILKANfmESLhigMINGFIL---ASYAFGFWY-----GTRIIISDLSNQQPNNDFHGGSVI- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 284 ftSYLMLLLQPLFVLGFGAQTIA---RAGASASRLFEVLDAETDVPERPGAIELTNARgRVEFRDVHLRYPG-SDAETLN 359
Cdd:PTZ00265 326 --SILLGVLISMFMLTIILPNITeymKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTrKDVEIYK 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 360 GVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDD-HDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAY 438
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKY 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 439 G--------------------------------------------KPDATPDAIAAAAQAAQADT-------------FI 461
Cdd:PTZ00265 483 SlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnTTDSNELIEMRKNYQTIKDSevvdvskkvlihdFV 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 462 EQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQRLST 539
Cdd:PTZ00265 563 SALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGneNRITIIIAHRLST 642
|
570
....*....|..
gi 1309179971 540 VKRADEILVIED 551
Cdd:PTZ00265 643 IRYANTIFVLSN 654
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
66-565 |
7.90e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 153.21 E-value: 7.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 66 LLLIGVAAAGGVA-QFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAI 144
Cdd:PLN03232 953 IVVYALLGFGQVAvTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFM 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 145 AAAIMLVGAVVLLlamnWQLALVALVAI-PLTILVLV---------RFVSKL-----GPMFRGFQQRLSALNSIlqenva 209
Cdd:PLN03232 1033 NQLWQLLSTFALI----GTVSTISLWAImPLLILFYAaylyyqstsREVRRLdsvtrSPIYAQFGEALNGLSSI------ 1102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 210 giRVVKAFAREPFEAARYRAANesllqqgltVRRTVANAFP---LLFSVGNLGvALVVWAGAVQVAHGRLTVGELVAFTS 286
Cdd:PLN03232 1103 --RAYKAYDRMAKINGKSMDNN---------IRFTLANTSSnrwLTIRLETLG-GVMIWLTATFAVLRNGNAENQAGFAS 1170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 287 YLMLLLQ-PLFVLGFGAQTIARAGASASRLFEVLDAET--DVPERPGAIELTN-------ARGRVEFRDVHLRYPGSDAE 356
Cdd:PLN03232 1171 TMGLLLSyTLNITTLLSGVLRQASKAENSLNSVERVGNyiDLPSEATAIIENNrpvsgwpSRGSIKFEDVHLRYRPGLPP 1250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 357 TLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENI 436
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 437 AYGKPDATPDAIAAAAQAAQADTfIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESA 516
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKDV-IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1309179971 517 LRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLA 565
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
341-552 |
4.28e-38 |
|
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: 139.53 E-value: 4.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAE---TLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVllddhdvrdltlaSLRGR 417
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 418 IGVVMQDSVLFSGTIAENIAYGKP----------DA---TPDaiaaaaqaaqadtfIEQLSDGYDTRVGERGIKLSGGQR 484
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfdeeryekviKAcalEPD--------------LEILPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 485 QRIAIARALLIDPRVLIMDDSTSSVDAETESALrasLDRLIGG-----RTTFIVAQRLSTVKRADEILVIEDG 552
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHI---FENCILGlllnnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-574 |
4.88e-37 |
|
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: 147.78 E-value: 4.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDQGITAGRREVITsgalLLIGVAAAGGVAQFLQGFLSAKA-SHG---AAYDMREAIFERLQTL 108
Cdd:TIGR00957 976 CNHVSALASNYWLSLWTDDPMVNGTQNNTS----LRLSVYGALGILQGFAVFGYSMAvSIGgiqASRVLHQDLLHNKLRS 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 109 SFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNwqlALVALVAIPLTILVLvrFVSKLgp 188
Cdd:TIGR00957 1052 PMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLAT---PIAAVIIPPLGLLYF--FVQRF-- 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 189 mFRGFQQRLSALNSI--------LQENVAGIRVVKAFAR-EPFEAARYRAANESllqQGLTVRRTVANAFpLLFSVGNLG 259
Cdd:TIGR00957 1125 -YVASSRQLKRLESVsrspvyshFNETLLGVSVIRAFEEqERFIHQSDLKVDEN---QKAYYPSIVANRW-LAVRLECVG 1199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 260 VALVVWAGAVQV-AHGRLTVGELVAFTSYLmllLQPLFVLGFGAQTIARAGA---SASRLFEVLDAETDVP---ERPGAI 332
Cdd:TIGR00957 1200 NCIVLFAALFAViSRHSLSAGLVGLSVSYS---LQVTFYLNWLVRMSSEMETnivAVERLKEYSETEKEAPwqiQETAPP 1276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 333 ELTNARGRVEFRDVHLRY-PGSDAeTLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTL 411
Cdd:TIGR00957 1277 SGWPPRGRVEFRNYCLRYrEDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGL 1355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 412 ASLRGRIGVVMQDSVLFSGTIAENI----AYGKPDAtpdaiAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRI 487
Cdd:TIGR00957 1356 HDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEEV-----WWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLV 1430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 488 AIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAES 567
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR 1510
|
....*..
gi 1309179971 568 CVYAEIA 574
Cdd:TIGR00957 1511 GIFYSMA 1517
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
341-558 |
7.93e-37 |
|
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: 135.13 E-value: 7.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGRIGV 420
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSGTIAENIaygkpdatpdaiaaaaqaaqadtfieqlsdgydtrvgerGIKLSGGQRQRIAIARALLIDPRVL 500
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 501 IMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARG 558
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
358-507 |
2.11e-36 |
|
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: 133.16 E-value: 2.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSG-TIAENI 436
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 437 AYGKPDATPDaiaAAAQAAQADTFIEQL--SDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTS 507
Cdd:pfam00005 81 RLGLLLKGLS---KREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
33-311 |
7.84e-36 |
|
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: 136.13 E-value: 7.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSY 112
Cdd:cd18572 7 VAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 113 HDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLV---RFVSKLGpm 189
Cdd:cd18572 87 FDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKvygRYYRKLS-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 190 fRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGltVRRTVANAFPLLFS--VGNLGVALVVWAG 267
Cdd:cd18572 165 -KEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLS--VRQALAYAGYVAVNtlLQNGTQVLVLFYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1309179971 268 AVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARA-GAS 311
Cdd:cd18572 242 GHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAvGAA 286
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
342-552 |
3.56e-35 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 131.82 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVV 421
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 422 MQ--DSVLFSGTIAENIAYG-----KPDATpdaiaaaaqaaqadtfIEQLSDGYDTRVGERGIK------LSGGQRQRIA 488
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGlenlgLPEEE----------------IEERVEEALELVGLEGLRdrspftLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 489 IARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIEDG 552
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
341-566 |
5.46e-35 |
|
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: 131.69 E-value: 5.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGsDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQ--DSVLFSGTIAENIAYG-----KPDATpdaiaaaaqaaqadtfIEQLSDGYDTRVG-----ERGI-KLSGGQRQRI 487
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAFGpenlgLPREE----------------IRERVEEALELVGlehlaDRPPhELSGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 488 AIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVA-QRLSTV-KRADEILVIEDGAVVARGTHEALLA 565
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
.
gi 1309179971 566 E 566
Cdd:COG1122 224 D 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
65-325 |
3.22e-34 |
|
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: 132.19 E-value: 3.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 65 ALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQ--TGQLITRLTSDVDLVRDFVGGGLVQ 142
Cdd:cd18578 55 ALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 143 AIAAAIMLVGAVVLLLAMNWQLALVALVAIPLtILVLVRFVSKlgpMFRGFQQR----LSALNSILQENVAGIRVVKAFA 218
Cdd:cd18578 135 ILQAIVTLVAGLIIAFVYGWKLALVGLATVPL-LLLAGYLRMR---LLSGFEEKnkkaYEESSKIASEAVSNIRTVASLT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 219 REPFEAARYRAANESLLQQGltVRRTVANAFplLFSVGN----LGVALVVWAGAVQVAHGRLTVGELvaFTSYLMLLlqp 294
Cdd:cd18578 211 LEDYFLEKYEEALEEPLKKG--LRRALISGL--GFGLSQsltfFAYALAFWYGGRLVANGEYTFEQF--FIVFMALI--- 281
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1309179971 295 lfvlgFGAQT----------IARAGASASRLFEVLDAETDV 325
Cdd:cd18578 282 -----FGAQSagqafsfapdIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
65-315 |
3.66e-34 |
|
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: 131.44 E-value: 3.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 65 ALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVG---GGLV 141
Cdd:cd18577 50 ALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGeklGLLI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 142 QAIAaaiMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREP 221
Cdd:cd18577 130 QSLS---TFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 222 FEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGRLTVGE-LVAFTSYLMLllqpLFVLGF 300
Cdd:cd18577 207 KEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDvLTVFFAVLIG----AFSLGQ 282
|
250
....*....|....*...
gi 1309179971 301 GA---QTIARAGASASRL 315
Cdd:cd18577 283 IApnlQAFAKARAAAAKI 300
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
341-566 |
2.62e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.10 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLAsLRGRIGV 420
Cdd:COG1131 1 IEVRGLTKRYGDKTA--LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENI-----AYGKPDATPDAIAaaaqaaqaDTFIEQ--LSDGYDTRVGergiKLSGGQRQRIAIARA 492
Cdd:COG1131 78 VPQEPALYPDlTVRENLrffarLYGLPRKEARERI--------DELLELfgLTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 493 LLIDPRVLIMDDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAE 566
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
339-565 |
3.74e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 136.02 E-value: 3.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 339 GRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRI 418
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSGTIAENIAYGKPDATPDAIAAAAQAAQADTfIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPR 498
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDV-IRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 499 VLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLA 565
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
39-315 |
4.54e-33 |
|
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: 128.69 E-value: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 39 LIAPQILRRIIDQGItaGRREVITSGALLLIGVAAAGGVAQFL---------QGFLSAKASHGAAYDMREAIFERLQTLS 109
Cdd:cd18554 16 LLLPLILKYIVDDVI--QGSSLTLDEKVYKLFTIIGIMFFIFLilrppveyyRQYFAQWIANKILYDIRKDLFDHLQKLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 110 FSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPM 189
Cdd:cd18554 94 LRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 190 FRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAV 269
Cdd:cd18554 174 TKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAY 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1309179971 270 QVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18554 254 LVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
341-558 |
5.89e-33 |
|
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: 125.71 E-value: 5.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLAslRGRIGV 420
Cdd:cd03259 1 LELKGLSKTYGSVRA--LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAYG-KPDATPDAIAAAAQAAQADTFIeqLSDGYDTRVGErgikLSGGQRQRIAIARALLIDPR 498
Cdd:cd03259 77 VFQDYALFPHlTVAENIAFGlKLRGVPKAEIRARVRELLELVG--LEGLLNRYPHE----LSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 499 VLIMDDSTSSVDAETESALRASLDRLI--GGRTTFIV------AQRLstvkrADEILVIEDGAVVARG 558
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQreLGITTIYVthdqeeALAL-----ADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
34-287 |
6.09e-33 |
|
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: 128.02 E-value: 6.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDqgITAGRREVITSG-------ALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERL- 105
Cdd:cd18573 8 SSAVTMSVPFAIGKLID--VASKESGDIEIFglslktfALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSIl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 106 -QTLSFsyHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLV---R 181
Cdd:cd18573 86 rQDAAF--FDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVfygR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 182 FVSKLGpmfRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVA 261
Cdd:cd18573 164 YVRKLS---KQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL 240
|
250 260
....*....|....*....|....*.
gi 1309179971 262 LVVWAGAVQVAHGRLTVGELVAFTSY 287
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMY 266
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
339-566 |
8.13e-33 |
|
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: 126.56 E-value: 8.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 339 GRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRI 418
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSGTIAENIaygKPD--ATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLID 496
Cdd:cd03288 98 SIILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 497 PRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAE 566
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
34-287 |
3.74e-32 |
|
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: 125.83 E-value: 3.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIID-------QGITAGRREVITSgALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQ 106
Cdd:cd18780 8 SSGTNLALPYFFGQVIDavtnhsgSGGEEALRALNQA-VLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 107 TLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKL 186
Cdd:cd18780 87 AQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 187 GPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWA 266
Cdd:cd18780 167 RKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWY 246
|
250 260
....*....|....*....|.
gi 1309179971 267 GAVQVAHGRLTVGELVAFTSY 287
Cdd:cd18780 247 GGRLVIDGELTTGLLTSFLLY 267
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
39-315 |
1.69e-31 |
|
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: 123.71 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 39 LIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQT 118
Cdd:cd18570 19 IAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 119 GQLITRLtSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLS 198
Cdd:cd18570 99 GEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 199 ALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGRLTV 278
Cdd:cd18570 178 ELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSL 257
|
250 260 270
....*....|....*....|....*....|....*...
gi 1309179971 279 GELVAFTSYLMLLLQPLFVLgFGAQ-TIARAGASASRL 315
Cdd:cd18570 258 GQLIAFNALLGYFLGPIENL-INLQpKIQEAKVAADRL 294
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
341-565 |
7.58e-31 |
|
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: 126.56 E-value: 7.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKT----SVVNLVPRFYDVtGGAVLLDDHDVRDLTLASLRG 416
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKStlalALMGLLPHGGRI-SGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 417 RIGVVMQD--SVLFSGTIAENIAYG--KPDATPDAIAAAAQAAQADTFIEQLSDGYDTRvgergikLSGGQRQRIAIARA 492
Cdd:COG1123 84 RIGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPHQ-------LSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 493 LLIDPRVLIMDDSTSSVDAETESALRASLDRLI--GGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
154-589 |
2.39e-30 |
|
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: 127.37 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 154 VVLLLAMNWQ------LALVALVA--IPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQenvaGIRVVKAFAREPfeaa 225
Cdd:TIGR00957 445 VILALYFLWLnlgpsvLAGVAVMVlmVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILN----GIKVLKLYAWEL---- 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 226 RYRAANESLLQQGLTVRRTVAnafpLLFSVGNLG-------VALVVWAGAVQVAHGRLTVGElVAFTSYLM--LLLQPLF 296
Cdd:TIGR00957 517 AFLDKVEGIRQEELKVLKKSA----YLHAVGTFTwvctpflVALITFAVYVTVDENNILDAE-KAFVSLALfnILRFPLN 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 297 VLGFGAQTIARAGASASRLFEVLDAETDVPERPGAIELTNARGR-VEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVG 375
Cdd:TIGR00957 592 ILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNsITVHNATFTWARDLPPTLNGITFSIPEGALVAVVG 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 376 STGSGKTSVVNLVPRFYDVTGGAVllddhdvrdltlaSLRGRIGVVMQDSVLFSGTIAENIAYGKPdATPDAIAAAAQAA 455
Cdd:TIGR00957 672 QVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFGKA-LNEKYYQQVLEAC 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 456 QADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALrasLDRLIG------GRT 529
Cdd:TIGR00957 738 ALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI---FEHVIGpegvlkNKT 814
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 530 TFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEIAASQLVGGEELDLPES 589
Cdd:TIGR00957 815 RILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDS 874
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
347-552 |
2.92e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.99 E-value: 2.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 347 HLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSV 426
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 427 LFSGTIAENIAYgkpdaTPDAIAAAAQAAQADTFIEQLsdGYDTRVGERGIK-LSGGQRQRIAIARALLIDPRVLIMDDS 505
Cdd:COG4619 85 LWGGTVRDNLPF-----PFQLRERKFDRERALELLERL--GLPPDILDKPVErLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 506 TSSVDAET----ESALRASLDRliGGRTTFIV------AQRLstvkrADEILVIEDG 552
Cdd:COG4619 158 TSALDPENtrrvEELLREYLAE--EGRAVLWVshdpeqIERV-----ADRVLTLEAG 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
341-565 |
3.20e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 124.63 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET---LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASL 414
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 415 RGRIGVVMQD--SVLFSG-TIAENIAYGkpdatPDAIAAAAQAAQADTfIEQLSD--GYDTRVGERGI-KLSGGQRQRIA 488
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRmTVGDIIAEP-----LRLHGLLSRAERRER-VAELLErvGLPPDLADRYPhELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 489 IARALLIDPRVLIMDDSTSSVDAETESALRASLDRL--IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
341-558 |
3.70e-30 |
|
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: 118.05 E-value: 3.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDV-----TGGAVLLDDHDVRDL--TLAS 413
Cdd:cd03260 1 IELRDLNVYYGDKHA--LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLdvDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 LRGRIGVVMQDSVLFSGTIAENIAYGKPDATpdaiaaAAQAAQADTFIEQL--SDGYDTRVGER--GIKLSGGQRQRIAI 489
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGLRLHG------IKLKEELDERVEEAlrKAALWDEVKDRlhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 490 ARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
341-565 |
1.49e-29 |
|
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: 117.00 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLRGR 417
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 418 IGVVMQDSVLFSG-TIAENIAY------GKPDATpdaiaaaaqaaqadtfIEQLSDGYDTRVGERGIK------LSGGQR 484
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFplrehtDLSEAE----------------IRELVLEKLELVGLPGAAdkmpseLSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 485 QRIAIARALLIDPRVLIMDDSTSSVDAETesalRASLDRLIG------GRTTFIVAQRLSTVKR-ADEILVIEDGAVVAR 557
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPIT----SAVIDELIRelrdelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAE 223
|
....*...
gi 1309179971 558 GTHEALLA 565
Cdd:COG1127 224 GTPEELLA 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
342-552 |
1.80e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 113.88 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVV 421
Cdd:cd00267 1 EIENLSFRYGGRTA--LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 422 MQdsvlfsgtiaeniaygkpdatpdaiaaaaqaaqadtfieqlsdgydtrvgergikLSGGQRQRIAIARALLIDPRVLI 501
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 502 MDDSTSSVDAETESALRASLDRLI-GGRTTFIVAQRLSTVKRA-DEILVIEDG 552
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
341-556 |
1.99e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 115.91 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNL-----VPrfydvTGGAVLLDDHDVRDLT--- 410
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggldRP-----TSGEVLIDGQDISSLSere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 411 LASLRGR-IGVVMQDSVLFSG-TIAENIAYGkpdATPDAIAAAAQAAQADTFIEQ--LSDGYDTRVGErgikLSGGQRQR 486
Cdd:COG1136 80 LARLRRRhIGFVFQFFNLLPElTALENVALP---LLLAGVSRKERRERARELLERvgLGDRLDHRPSQ----LSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 487 IAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLI--GGRTTFIVAQRLSTVKRADEILVIEDGAVVA 556
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNreLGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
341-558 |
3.92e-29 |
|
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: 115.30 E-value: 3.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLR 415
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 416 GRIGVVMQD---SVLFSGTIAENIA-----YGKPDATPDAIAAAAQAAQAdtfIEQLSDGYDTRVGErgikLSGGQRQRI 487
Cdd:cd03257 82 KEIQMVFQDpmsSLNPRMTIGEQIAeplriHGKLSKKEARKEAVLLLLVG---VGLPEEVLNRYPHE----LSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 488 AIARALLIDPRVLIMDDSTSSVDAETESALRASLDRL--IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
341-552 |
5.41e-29 |
|
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: 113.44 E-value: 5.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLAS--LRGRI 418
Cdd:cd03229 1 LELKNVSKRYGQKTV--LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSG-TIAENIAYGkpdatpdaiaaaaqaaqadtfieqlsdgydtrvgergikLSGGQRQRIAIARALLIDP 497
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 498 RVLIMDDSTSSVDAETESALRASLDRLI--GGRTTFIVAQRLSTVKR-ADEILVIEDG 552
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQaqLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
39-287 |
5.96e-29 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 116.79 E-value: 5.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 39 LIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQT 118
Cdd:cd18567 19 LASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 119 GQLITRLTSdVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAipLTILVLVRFVSkLGPMFRGFQQRLS 198
Cdd:cd18567 99 GDIVSRFGS-LDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAA--VALYALLRLAL-YPPLRRATEEQIV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 199 A---LNSILQENVAGIRVVKAFAREPFEAARY-----RAANESLLQQGLTVRRTVANAFplLFSVGNLgvaLVVWAGAVQ 270
Cdd:cd18567 175 AsakEQSHFLETIRGIQTIKLFGREAEREARWlnllvDAINADIRLQRLQILFSAANGL--LFGLENI---LVIYLGALL 249
|
250
....*....|....*..
gi 1309179971 271 VAHGRLTVGELVAFTSY 287
Cdd:cd18567 250 VLDGEFTVGMLFAFLAY 266
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
341-565 |
2.74e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 113.36 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRI 418
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQD---SVLFSGTIAENIA-----YGKPDAtpdaiaaaaqaaqADTFIEQLSD-GYDTRVGER-GIKLSGGQRQRIA 488
Cdd:COG1124 82 QMVFQDpyaSLHPRHTVDRILAeplriHGLPDR-------------EERIAELLEQvGLPPSFLDRyPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 489 IARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
34-284 |
3.56e-28 |
|
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: 114.61 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYH 113
Cdd:cd18782 14 VQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLtSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGF 193
Cdd:cd18782 94 DKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 QQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAH 273
Cdd:cd18782 173 AEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLR 252
|
250
....*....|.
gi 1309179971 274 GRLTVGELVAF 284
Cdd:cd18782 253 GELTLGQLIAF 263
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
341-565 |
8.48e-28 |
|
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: 112.01 E-value: 8.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSdAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAY-----GKPDATPDaIAAAAQAAQADTFIEQLSDGYDTrvgergiKLSGGQRQRIAIARALL 494
Cdd:cd03295 80 VIQQIGLFPHmTVEENIALvpkllKWPKEKIR-ERADELLALVGLDPAEFADRYPH-------ELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 495 IDPRVLIMDDSTSSVDAETESALR---ASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLA 565
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQeefKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
341-565 |
1.03e-27 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 111.52 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRG-- 416
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 417 -RIGVVMQDSVLFSG-TIAENIAY-----GKPDAtpdaiaaaAQAAQADTFIEQ--LSDGYDTRVGErgikLSGGQRQRI 487
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALpleiaGVPKA--------EIEERVLELLELvgLEDKADAYPAQ----LSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 488 AIARALLIDPRVLIMDDSTSSVDAE-TESALRASLD---RLigGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEA 562
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPEtTQSILALLRDinrEL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
...
gi 1309179971 563 LLA 565
Cdd:cd03258 228 VFA 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
341-559 |
2.03e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 113.65 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGrIGV 420
Cdd:COG3842 6 LELENVSKRYGDVTA--LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-PEKRN-VGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAYG-KPDATPDAIAAAAQAAQADTFieQLSDGYDTRVGErgikLSGGQRQRIAIARALLIDPR 498
Cdd:COG3842 82 VFQDYALFPHlTVAENVAFGlRMRGVPKAEIRARVAELLELV--GLEGLADRYPHQ----LSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 499 VLIMDDSTSSVDAETESALRASLDRLI---GgrTTFIV-------AQRLStvkraDEILVIEDGAVVARGT 559
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQrelG--ITFIYvthdqeeALALA-----DRIAVMNDGRIEQVGT 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
145-565 |
2.96e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 117.92 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 145 AAAIMLVGAVVLLLAmnwQL-------ALVALVAIPLTILVlvrfVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAF 217
Cdd:PLN03130 423 SAPFRIIIAMVLLYQ---QLgvasligSLMLVLMFPIQTFI----ISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCY 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 218 ARE-PFEAARYRAANESL-----LQQGLTVRRTVANAFPLLFSVGNLGVALVVwagavqvaHGRLTVGElvAFTSYLM-- 289
Cdd:PLN03130 496 AWEnSFQSKVQTVRDDELswfrkAQLLSAFNSFILNSIPVLVTVVSFGVFTLL--------GGDLTPAR--AFTSLSLfa 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 290 LLLQPLFVLGFGAQTIARAGASASRLFEVLDAETDV-----PERPG--AIELTNARGRVEfrdvhlryPGSDAETLNGVS 362
Cdd:PLN03130 566 VLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVllpnpPLEPGlpAISIKNGYFSWD--------SKAERPTLSNIN 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 363 FVVEPGATIALVGSTGSGKTSVVnlvprfydvtggAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKPd 442
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLI------------SAMLGELPPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSP- 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 443 ATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAET-----ESAL 517
Cdd:PLN03130 705 FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgrqvfDKCI 784
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1309179971 518 RASLdrliGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLA 565
Cdd:PLN03130 785 KDEL----RGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
341-554 |
3.59e-27 |
|
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: 109.50 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLR 415
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 416 GR-IGVVMQDSVLFSG-TIAENIAYGkpdATPDAIAAAAQAAQADTFIEQ--LSDGYDTRVGErgikLSGGQRQRIAIAR 491
Cdd:cd03255 81 RRhIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLERvgLGDRLNHYPSE----LSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 492 ALLIDPRVLIMDDSTSSVDAETESALRA---SLDRLIGgrTTFIVA---QRLstVKRADEILVIEDGAV 554
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMEllrELNKEAG--TTIVVVthdPEL--AEYADRIIELRDGKI 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
341-559 |
1.03e-26 |
|
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: 108.97 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLaslRGR-IG 419
Cdd:cd03296 3 IEVRNVSKRFGDFVA--LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERnVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 VVMQDSVLFSG-TIAENIAYG---KPDATPDAIAAAAQAAQADTFIEQLsDGYDTRVGErgiKLSGGQRQRIAIARALLI 495
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlrvKPRSERPPEAEIRAKVHELLKLVQL-DWLADRYPA---QLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 496 DPRVLIMDDSTSSVDAETESALRASLDRL---IGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGT 559
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLhdeLHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
341-552 |
1.35e-26 |
|
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: 106.33 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGRIGV 420
Cdd:cd03230 1 IEVRNLSKRYGKKTA--LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIaygkpdatpdaiaaaaqaaqadtfieqlsdgydtrvgergiKLSGGQRQRIAIARALLIDPRV 499
Cdd:cd03230 78 LPEEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 500 LIMDDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTV-KRADEILVIEDG 552
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAeRLCDRVAILNNG 171
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
341-513 |
1.54e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.83 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGsDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLRGR 417
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 418 IGVVMQDSVLFSG-TIAENIAY-----GKPDATpdaiaaaaqaaqadtfIEQ----------LSDGYDTRVGErgikLSG 481
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALplrvtGKSRKE----------------IRRrvrevldlvgLSDKAKALPHE----LSG 140
|
170 180 190
....*....|....*....|....*....|..
gi 1309179971 482 GQRQRIAIARALLIDPRVLIMDDSTSSVDAET 513
Cdd:COG2884 141 GEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
341-565 |
2.31e-26 |
|
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: 107.59 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLRGR 417
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 418 IGVVMQDSVLFSG-TIAENIAYGkpdatpdaiaAAAQAAQADTFIEQLSDGYDTRVGERGIK------LSGGQRQRIAIA 490
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFP----------LREHTRLSEEEIREIVLEKLEAVGLRGAEdlypaeLSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 491 RALLIDPRVLIMDDSTSSVDAETESAlrasLDRLI------GGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEAL 563
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGV----IDDLIrslkkeLGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 1309179971 564 LA 565
Cdd:cd03261 225 RA 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
335-548 |
2.64e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.25 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 335 TNARGRVEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLtla 412
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 413 slRGRIGVVMQDSVLFs-gTIAENIAYG-----KPDAtpdaiaaaAQAAQADTFIEQ--LSDGYDTRVGErgikLSGGQR 484
Cdd:COG1116 79 --GPDRGVVFQEPALLpwlTVLDNVALGlelrgVPKA--------ERRERARELLELvgLAGFEDAYPHQ----LSGGMR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 485 QRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLI--GGRTTFIV------AQRLstvkrADEILV 548
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVthdvdeAVFL-----ADRVVV 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
339-559 |
4.01e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 114.11 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 339 GRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRI 418
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSGTIAENIaygKP--DATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLI- 495
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKk 1463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 496 DPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGT 559
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
341-533 |
6.40e-26 |
|
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: 106.02 E-value: 6.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLtlaslRGRI 418
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFS-GTIAENIAYGkpdatpdaiaaAAQAAQADTFIEQLSDGYDTRVGERGIK------LSGGQRQRIAIAR 491
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG-----------LELQGVPKAEARERAEELLELVGLSGFEnayphqLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1309179971 492 ALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIV 533
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLV 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
100-573 |
1.64e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 112.38 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 100 AIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFvgGGLVQAIAAAIMLVGAVVLLLAMNWQLA-----LVALVAIPL 174
Cdd:PLN03232 379 AIFHKSLRLTHEARKNFASGKVTNMITTDANALQQI--AEQLHGLWSAPFRIIVSMVLLYQQLGVAslfgsLILFLLIPL 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 175 TILVLVRFVSKLGPMFRGFQQRLSALNSILqenvAGIRVVKAFARE-PFEAARYRAANESL-----LQQGLTVRRTVANA 248
Cdd:PLN03232 457 QTLIVRKMRKLTKEGLQWTDKRVGIINEIL----ASMDTVKCYAWEkSFESRIQGIRNEELswfrkAQLLSAFNSFILNS 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 249 FPLLFSVGNLGVALVVwagavqvaHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRLFEVLDAETDV--- 325
Cdd:PLN03232 533 IPVVVTLVSFGVFVLL--------GGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERIlaq 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 326 --PERPGAIELTNARGRVEFrDVHLRYPgsdaeTLNGVSFVVEPGATIALVGSTGSGKTSVVnlvprfydvtggAVLLDD 403
Cdd:PLN03232 605 npPLQPGAPAISIKNGYFSW-DSKTSKP-----TLSDINLEIPVGSLVAIVGGTGEGKTSLI------------SAMLGE 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 404 HDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIAYGKpDATPDAIAAAAQAAQADTFIEqLSDGYD-TRVGERGIKLSGG 482
Cdd:PLN03232 667 LSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTALQHDLD-LLPGRDlTEIGERGVNISGG 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 483 QRQRIAIARALLIDPRVLIMDDSTSSVDAE-TESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHE 561
Cdd:PLN03232 745 QKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFA 824
|
490
....*....|..
gi 1309179971 562 ALLAESCVYAEI 573
Cdd:PLN03232 825 ELSKSGSLFKKL 836
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
358-564 |
3.24e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 104.34 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlaSLRGRIGVVMQDSVLFSG-TIAENI 436
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP--PEKRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 437 AYGKPDATPDAIAAAAQAAQADTF--IEQLSDGYDTRvgergikLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETE 514
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEMlgIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 515 SALRASLDRLI-GGRTTFI-VAQRLSTVKR-ADEILVIEDGAVVARGTHEALL 564
Cdd:cd03299 166 EKLREELKKIRkEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
341-566 |
2.92e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.76 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQ--DSVLFSGTIAENIAYG------KPDATPDAIAAAAQAAQADTFIEQLSDgydtrvgergiKLSGGQRQRIAIARA 492
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 493 LLIDPRVLIMDDSTSSVDAETESALRASLDRL--IGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAE 566
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
341-559 |
8.60e-24 |
|
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: 100.00 E-value: 8.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLAslRGRIGV 420
Cdd:cd03300 1 IELENVSKFYGGFVA--LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAYG-KPDATPDAIAAAAQAAQADtfIEQLSDGYDTRVGErgikLSGGQRQRIAIARALLIDPR 498
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGlRLKKLPKAEIKERVAEALD--LVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 499 VLIMDDSTSSVDAETESALRASLDRL---IGgrTTFIV-------AQRLStvkraDEILVIEDGAVVARGT 559
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLqkeLG--ITFVFvthdqeeALTMS-----DRIAVMNKGKIQQIGT 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
342-566 |
9.82e-24 |
|
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: 99.82 E-value: 9.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGRIGV- 420
Cdd:cd03224 2 EVENLNAGYGKSQI--LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP-PHERARAGIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 -VMQDSVLFSG-TIAENI---AYGKPDATPDAIaaaaqaaqadtfIEQLsdgYD------TRVGERGIKLSGGQRQRIAI 489
Cdd:cd03224 79 yVPEGRRIFPElTVEENLllgAYARRRAKRKAR------------LERV---YElfprlkERRKQLAGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 490 ARALLIDPRVLIMDDSTS----SVDAETESALRASLDRligGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALL 564
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEglapKIVEEIFEAIRELRDE---GVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
..
gi 1309179971 565 AE 566
Cdd:cd03224 221 AD 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
344-559 |
1.08e-23 |
|
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: 99.82 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 344 RDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGRIGVVM- 422
Cdd:cd03219 4 RGLTKRFGGLVA--LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGRt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 423 -QDSVLFSG-TIAENIAYGKPDATPDAIAAAAQAAQADTFIEQ---------LSDGYDTRVGErgikLSGGQRQRIAIAR 491
Cdd:cd03219 81 fQIPRLFPElTVLENVMVAAQARTGSGLLLARARREEREARERaeellervgLADLADRPAGE----LSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 492 ALLIDPRVLIMDDSTSSVDAEtesaLRASLDRLI-----GGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGT 559
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPE----ETEELAELIrelreRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
341-555 |
4.07e-23 |
|
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: 97.71 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGrIGV 420
Cdd:cd03301 1 VELENVTKRFGNVTA--LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP-PKDRD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAYG-KPDATPDAIAAAAQAAQADTF-IEQLSDGYDTRvgergikLSGGQRQRIAIARALLIDP 497
Cdd:cd03301 77 VFQNYALYPHmTVYDNIAFGlKLRKVPKDEIDERVREVAELLqIEHLLDRKPKQ-------LSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 498 RVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQ-RLSTVKRADEILVIEDGAVV 555
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQ 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
341-559 |
6.46e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.15 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTS---VVNLVPRFydvTGGAVLLDDHDVRDLTLASLR 415
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLERP---TSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 416 G---RIGVVMQDSVLFSG-TIAENIAY-----GKPDATpdaiaaaaqaaqadtfIEQlsdgydtRVGER----GIK---- 478
Cdd:COG1135 79 AarrKIGMIFQHFNLLSSrTVAENVALpleiaGVPKAE----------------IRK-------RVAELlelvGLSdkad 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 479 -----LSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAE-TESALRasL-----DRLigGRTTFIVAQRLSTVKR-ADEI 546
Cdd:COG1135 136 aypsqLSGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILD--LlkdinREL--GLTIVLITHEMDVVRRiCDRV 211
|
250
....*....|...
gi 1309179971 547 LVIEDGAVVARGT 559
Cdd:COG1135 212 AVLENGRIVEQGP 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
357-558 |
9.01e-23 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 96.60 E-value: 9.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 357 TLNgVSFVVePGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRD----LTLASLRGRIGVVMQDSVLFSG-T 431
Cdd:cd03297 14 TLK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 432 IAENIAYGKPDATPDAIAAaaqaaqadtFIEQLSDGYD-TRVGERGI-KLSGGQRQRIAIARALLIDPRVLIMDDSTSSV 509
Cdd:cd03297 92 VRENLAFGLKRKRNREDRI---------SVDELLDLLGlDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 510 DAETESALRASLDRL--IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:cd03297 163 DRALRLQLLPELKQIkkNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
341-559 |
9.33e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.84 E-value: 9.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVrDLTLASLRGRIGV 420
Cdd:COG1118 3 IEVRNISKRFGSFTL--LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAYGKPDATPDAIAaaaqaaqadtfIEQLSDGYDTRVGERGIK------LSGGQRQRIAIARAL 493
Cdd:COG1118 80 VFQHYALFPHmTVAENIAFGLRVRPPSKAE-----------IRARVEELLELVQLEGLAdrypsqLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 494 LIDPRVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIV------AQRLstvkrADEILVIEDGAVVARGT 559
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVthdqeeALEL-----ADRVVVMNQGRIEQVGT 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
339-559 |
1.09e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.76 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 339 GRVEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGrI 418
Cdd:COG3839 2 ASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP-PKDRN-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLF-SGTIAENIAYG-----KPDATpdaiaaaaqaaqadtfIE----------QLSDGYDTRVGErgikLSGG 482
Cdd:COG3839 78 AMVFQSYALYpHMTVYENIAFPlklrkVPKAE----------------IDrrvreaaellGLEDLLDRKPKQ----LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 483 QRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIV------AQRLstvkrADEILVIEDGAV 554
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRrlGTTTIYVthdqveAMTL-----ADRIAVMNDGRI 212
|
....*
gi 1309179971 555 VARGT 559
Cdd:COG3839 213 QQVGT 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
341-565 |
1.10e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 96.99 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDV--RDLTLASLRGRI 418
Cdd:COG1126 2 IEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSG-TIAENIAYG--------KPDAtpdaiaaaaqaaqadtfiEQLSDGYDTRVG--ERG----IKLSGGQ 483
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLApikvkkmsKAEA------------------EERAMELLERVGlaDKAdaypAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 484 RQRIAIARALLIDPRVLIMDDSTSSVDAEtesalrasldrLIG------------GRTTFIV------AQRLstvkrADE 545
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDPE-----------LVGevldvmrdlakeGMTMVVVthemgfAREV-----ADR 205
|
250 260
....*....|....*....|
gi 1309179971 546 ILVIEDGAVVARGTHEALLA 565
Cdd:COG1126 206 VVFMDGGRIVEEGPPEEFFE 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
340-564 |
1.30e-22 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 97.42 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 340 RVEFRDVHLRYPGsdAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIG 419
Cdd:COG1120 1 MLEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 VVMQDSVL-FSGTIAENIAYG-----KPDATPDAIAAAAQAAQADTF-IEQLSDgydTRVGErgikLSGGQRQRIAIARA 492
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlGLFGRPSAEDREAVEEALERTgLEHLAD---RPVDE----LSGGERQRVLIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 493 LLIDPRVLIMDDSTSSVDAETESALRASLDRL--IGGRTTFIV------AQRLstvkrADEILVIEDGAVVARGTHEALL 564
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVlhdlnlAARY-----ADRLVLLKDGRIVAQGPPEEVL 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
341-511 |
2.63e-22 |
|
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: 97.82 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKT----SVVNLVPRFYdVTGGAVLLDDHDVRDLT---L 411
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKStlarAILGLLPPPG-ITSGEILFDGEDLLKLSekeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 412 ASLRGR-IGVVMQDS------VLfsgTIAENIA--------YGKPDATpdaiaaaaqaaqaDTFIEQLsdgydTRVG--- 473
Cdd:COG0444 81 RKIRGReIQMIFQDPmtslnpVM---TVGDQIAeplrihggLSKAEAR-------------ERAIELL-----ERVGlpd 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1309179971 474 -ERGIK-----LSGGQRQRIAIARALLIDPRVLIMDDSTSSVDA 511
Cdd:COG0444 140 pERRLDrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
114-573 |
3.09e-22 |
|
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: 101.91 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 114 DRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNwqlALVALVAIPLTILVLVrfvskLGPMFRGF 193
Cdd:TIGR01271 977 NTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQ---PYIFIAAIPVAVIFIM-----LRAYFLRT 1048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 194 QQRLSALN--------SILQENVAGIRVVKAFAREP-FEAARYRAANESLLQQGL---TVR---RTVANAFPLLFSVgnl 258
Cdd:TIGR01271 1049 SQQLKQLEsearspifSHLITSLKGLWTIRAFGRQSyFETLFHKALNLHTANWFLylsTLRwfqMRIDIIFVFFFIA--- 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 259 gvALVVWAGAVQVAHGRltVGELVAFTSYLMLLLQPLFVLGFGAQTIARagaSASRLFEVLDAETDVPERPGA------- 331
Cdd:TIGR01271 1126 --VTFIAIGTNQDGEGE--VGIILTLAMNILSTLQWAVNSSIDVDGLMR---SVSRVFKFIDLPQEEPRPSGGggkyqls 1198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 332 ----IELTNAR------GRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDvTGGAVLL 401
Cdd:TIGR01271 1199 tvlvIENPHAQkcwpsgGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQI 1277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 402 DDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIaygKPDA--TPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKL 479
Cdd:TIGR01271 1278 DGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVL 1354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 480 SGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGT 559
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
|
490
....*....|....
gi 1309179971 560 HEALLAESCVYAEI 573
Cdd:TIGR01271 1435 IQKLLNETSLFKQA 1448
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
341-587 |
3.36e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.74 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQ--DSVLFSGTIAENIAYG-KPDATP-DAIAAAAQAAQADTfieqlsDGYDTRVGERGiKLSGGQRQRIAIARALLID 496
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGlENHAVPyDEMHRRVSEALKQV------DMLERADYEPN-ALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 497 PRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVA--QRLSTVKRADEILVIEDGAVVARGTHEAllaescVYAEIA 574
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTE------IFDHAE 234
|
250
....*....|...
gi 1309179971 575 ASQLVGgeeLDLP 587
Cdd:PRK13648 235 ELTRIG---LDLP 244
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
342-563 |
3.75e-22 |
|
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: 95.71 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAeTLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLRGRI 418
Cdd:cd03256 2 EVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSG-TIAENIAYGKPDATPDAIAAAAQAAQADTFIE-------QLSDGYDTRVGErgikLSGGQRQRIAIA 490
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRAlaalervGLLDKAYQRADQ----LSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 491 RALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEAL 563
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
341-587 |
4.03e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 96.34 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:PRK13647 5 IEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQD--SVLFSGTIAENIAYGKPDA--TPDAIAAAAQAAQADTFIEQLSDgydtrvgERGIKLSGGQRQRIAIARALLID 496
Cdd:PRK13647 84 VFQDpdDQVFSSTVWDDVAFGPVNMglDKDEVERRVEEALKAVRMWDFRD-------KPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 497 PRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLS--TVKRADEILVIEDGAVVARGTHEALLAEscvyaeia 574
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVdlAAEWADQVIVLKEGRVLAEGDKSLLTDE-------- 228
|
250
....*....|...
gi 1309179971 575 asQLVGGEELDLP 587
Cdd:PRK13647 229 --DIVEQAGLRLP 239
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
341-587 |
5.46e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.41 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLvprfydvTGGAVLLDDHD-----VRDLTLAS-- 413
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKL-------INGLLLPDDNPnskitVDGITLTAkt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 ---LRGRIGVVMQ--DSVLFSGTIAENIAYGKPD-ATPDAIAAAAQAAQadtfieqLSD-GYDTRVGERGIKLSGGQRQR 486
Cdd:PRK13640 79 vwdIREKVGIVFQnpDNQFVGATVGDDVAFGLENrAVPRPEMIKIVRDV-------LADvGMLDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 487 IAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLI--GGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALL 564
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
250 260
....*....|....*....|...
gi 1309179971 565 AESCVYAEIAasqlvggeeLDLP 587
Cdd:PRK13640 232 SKVEMLKEIG---------LDIP 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
340-510 |
1.20e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.72 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 340 RVEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGA-----VLLDDHDV--RDLTLA 412
Cdd:COG1117 11 KIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 413 SLRGRIGVVMQDSVLFSGTIAENIAYG------KPDATPDAIaaaaqaaqadtfIEQ----------LSDgydtRVGERG 476
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEI------------VEEslrkaalwdeVKD----RLKKSA 152
|
170 180 190
....*....|....*....|....*....|....
gi 1309179971 477 IKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVD 510
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
341-534 |
1.25e-21 |
|
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: 93.63 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGsDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDL---TLASLRGR 417
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 418 IGVVMQDSVLFSG-TIAENIAY-----GKP-----DATPDAIAAAAQAAQADTFIEQLSdgydtrvgergiklsGGQRQR 486
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFalevtGVPpreirKRVPAALELVGLSHKHRALPAELS---------------GGEQQR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1309179971 487 IAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVA 534
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
341-566 |
1.35e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 94.00 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLtlaslRGRIGV 420
Cdd:COG1121 7 IELENLTVSYGGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDS------------VLFSGTIAENIAYGKPDATpdaiaaaaQAAQADTFIEQ--LSDGYDTRVGErgikLSGGQRQR 486
Cdd:COG1121 80 VPQRAevdwdfpitvrdVVLMGRYGRRGLFRRPSRA--------DREAVDEALERvgLEDLADRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 487 IAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIEDGaVVARGTHEALL 564
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGPPEEVL 226
|
..
gi 1309179971 565 AE 566
Cdd:COG1121 227 TP 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
361-567 |
1.53e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 96.33 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 361 VSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRD----LTLASLRGRIGVVMQDSVLFSG-TIAEN 435
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 436 IAYGKPDATPDAIAAAAqaaqaDTFIEQLsdGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETES 515
Cdd:TIGR02142 96 LRYGMKRARPSERRISF-----ERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 516 ALRASLDRLIG--GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAES 567
Cdd:TIGR02142 169 EILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
39-298 |
1.78e-21 |
|
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: 94.93 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 39 LIAPQILRRIIDQGITAGRRE---VITSGALLL-IGVAAAGGVAQFLQGFLSAKAShgaaYDMREAIFERLQTLSFSYHD 114
Cdd:cd18568 19 LALPLFTQIILDRVLVHKNISllnLILIGLLIVgIFQILLSAVRQYLLDYFANRID----LSLLSDFYKHLLSLPLSFFA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 115 RIQTGQLITRLtSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQ 194
Cdd:cd18568 95 SRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 195 QRLSALNSILQENVAGIRVVKAFAREPfeaaRYRAANESLLQQGLTVRRTVANAFPLLFSVGN----LGVALVVWAGAVQ 270
Cdd:cd18568 174 QANAEQQSFLVEALTGIATIKALAAER----PIRWRWENKFAKALNTRFRGQKLSIVLQLISSlinhLGTIAVLWYGAYL 249
|
250 260
....*....|....*....|....*...
gi 1309179971 271 VAHGRLTVGELVAFTSYLMLLLQPLFVL 298
Cdd:cd18568 250 VISGQLTIGQLVAFNMLFGSVINPLLAL 277
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
33-300 |
2.25e-21 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 94.49 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDQgITAGRREVITSGALLLIGVAAAGGVAQF---LQGFLSAKASHGAAYDMREAIFERLQTLS 109
Cdd:cd18582 7 LAKLLNVAVPFLLKYAVDA-LSAPASALLAVPLLLLLAYGLARILSSLfneLRDALFARVSQRAVRRLALRVFRHLHSLS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 110 FSYHDRIQTGQL---ITRLTSDVDLVrdfVGGGLVQAIAAAIMLVGAVVLLLAM-NWQLALVALVAIPLTILVLVRFVSK 185
Cdd:cd18582 86 LRFHLSRKTGALsraIERGTRGIEFL---LRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFTIKVTEW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 186 LgpmfRGFQQRLSAL----NSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVAnafplLFSVG----- 256
Cdd:cd18582 163 R----TKFRREMNEAdneaNAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLA-----LLNIGqalii 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1309179971 257 NLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGF 300
Cdd:cd18582 234 SLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGF 277
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
342-565 |
2.91e-21 |
|
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: 93.12 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGR-IGV 420
Cdd:COG0410 5 EVENLHAGYGGIHV--LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENI---AYGKPDATPDAiaaaaqaaqadtfiEQLSDGYDT--RVGER----GIKLSGGQRQRIAIA 490
Cdd:COG0410 83 VPEGRRIFPSlTVEENLllgAYARRDRAEVR--------------ADLERVYELfpRLKERrrqrAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 491 RALLIDPRVLIMDDSTS----SVDAETESALRASLDRligGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:COG0410 149 RALMSRPKLLLLDEPSLglapLIVEEIFEIIRRLNRE---GVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
341-513 |
5.59e-21 |
|
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: 91.44 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDV--RDLTLASLRGRI 418
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSG-TIAENIAYG--------KPDAtpdaiaaaaqaaqadtfiEQLSDGYDTRVG------ERGIKLSGGQ 483
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITLApikvkgmsKAEA------------------EERALELLEKVGladkadAYPAQLSGGQ 140
|
170 180 190
....*....|....*....|....*....|
gi 1309179971 484 RQRIAIARALLIDPRVLIMDDSTSSVDAET 513
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
342-558 |
7.89e-21 |
|
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: 90.19 E-value: 7.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVV 421
Cdd:cd03214 1 EVENLSVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 422 MQdsVLfsgtiaeniaygkpdatpdaiaaaaqaaqADTFIEQLSD-GYDTrvgergikLSGGQRQRIAIARALLIDPRVL 500
Cdd:cd03214 79 PQ--AL-----------------------------ELLGLAHLADrPFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 501 IMDDSTSSVDAETESALRASLDRLI--GGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLAreRGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
352-553 |
7.92e-21 |
|
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: 91.24 E-value: 7.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 352 GSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVL----LDDHDVRDLTLASLRGRIGVVMQDSVL 427
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 428 FSGTIAENIAYGKPdATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTS 507
Cdd:cd03290 91 LNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1309179971 508 SVDAE-TESALRASLDRLI--GGRTTFIVAQRLSTVKRADEILVIEDGA 553
Cdd:cd03290 170 ALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
339-566 |
8.33e-21 |
|
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: 92.61 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 339 GRVEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDvTGGAVLLDDHDVRDLTLASLRGRI 418
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSGTIAENI-AYGKpdATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDP 497
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLdPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 498 RVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAE 566
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
345-565 |
1.35e-20 |
|
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: 93.63 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 345 DVHLRYPGSdaeTLNgVSFVVEPGATIALVGSTGSGKTSVVNLV------PRFYDVTGGAVLLDDHdvRDLTLASLRGRI 418
Cdd:COG4148 6 DFRLRRGGF---TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIaglerpDSGRIRLGGEVLQDSA--RGIFLPPHRRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSG-TIAENIAYGKPDATPdaiaaAAQAAQADTFIEQLsdGYDTRVGERGIKLSGGQRQRIAIARALLIDP 497
Cdd:COG4148 80 GYVFQEARLFPHlSVRGNLLYGRKRAPR-----AERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 498 RVLIMDDSTSSVDAETESALRASLDRLiggRTTF---IV--------AQRLstvkrADEILVIEDGAVVARGTHEALLA 565
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERL---RDELdipILyvshsldeVARL-----ADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
340-558 |
1.46e-20 |
|
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: 89.92 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 340 RVEFRDVHLRYPGSDAET----LNGVSFVVEPGATIALVGSTGSGKTSVVNLVP--RFYDVTGGAVLLDDHDVRdltLAS 413
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 LRGRIGVVMQDSVLFSG-TIAENIAygkpdatpdaiaaaaqaaqadtFIEQLsdgydtrvgeRGIklSGGQRQRIAIARA 492
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLM----------------------FAAKL----------RGL--SGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 493 LLIDPRVLIMDDSTSSVDAETESALRASLDRLI-GGRTTFIVAQRLST--VKRADEILVIEDGAVVARG 558
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
341-587 |
1.90e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 91.62 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQ--DSVLFSGTIAENIAYG-KPDATPdaiaaaaqaaqADTFIEQLSDGYDtRVG------ERGIKLSGGQRQRIAIAR 491
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGlENIGVP-----------REEMVERVDQALR-QVGmedflnREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 492 ALLIDPRVLIMDDSTSSVDAETESALRASLDRLI--GGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCV 569
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
250
....*....|....*...
gi 1309179971 570 YAEIAasqlvggeeLDLP 587
Cdd:PRK13635 234 LQEIG---------LDVP 242
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
341-589 |
2.63e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.62 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRY-PGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDH----DVRDLTLAS 413
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 LRGRIGVVMQ--DSVLFSGTIAENIAYG-------KPDAtpdaiaaaaqAAQADTFIEQLsdGYDTRVGERG-IKLSGGQ 483
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGpmnfgvsEEDA----------KQKAREMIELV--GLPEELLARSpFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 484 RQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRL--IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTH 560
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
250 260
....*....|....*....|....*....
gi 1309179971 561 EALLAEScvyAEIAASQlvggeeLDLPES 589
Cdd:PRK13634 231 REIFADP---DELEAIG------LDLPET 250
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
39-315 |
3.18e-20 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 91.42 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 39 LIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQT 118
Cdd:cd18555 19 LLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 119 GQLITRLTSdVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIplTILVLVRFVSKlgPMFRGFQQR-- 196
Cdd:cd18555 99 GDLLFRANS-NVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLG--LLIVLLLLLTR--KKIKKLNQEei 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 197 --LSALNSILQENVAGIRVVKAFArepFEAARYRAANESLLQQ-GLTVRRTVANAF--PLLFSVGNLGVALVVWAGAVQV 271
Cdd:cd18555 174 vaQTKVQSYLTETLYGIETIKSLG---SEKNIYKKWENLFKKQlKAFKKKERLSNIlnSISSSIQFIAPLLILWIGAYLV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1309179971 272 AHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18555 251 INGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
373-566 |
3.71e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 91.79 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 373 LVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGrIGVVMQDSVLFSG-TIAENIAYG-KPDATPDAIAA 450
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-PHLRH-INMVFQSYALFPHmTVEENVAFGlKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 451 AAQAAQADTFieQLSDgydtRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRL---IGG 527
Cdd:TIGR01187 79 PRVLEALRLV--QLEE----FADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIqeqLGI 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1309179971 528 RTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAE 566
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
355-585 |
8.03e-20 |
|
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: 89.92 E-value: 8.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 355 AETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVlldDHDvrdltlaslrGRIGVVMQDSVLFSGTIAE 434
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHS----------GRISFSSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 435 NIAYGKP-DATPDAIAAAAQAAQADtfIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAET 513
Cdd:cd03291 117 NIIFGVSyDEYRYKSVVKACQLEED--ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 514 ESALRAS-LDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYaeiaASQLVGGEELD 585
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF----SSKLMGYDTFD 263
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
341-556 |
9.65e-20 |
|
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: 86.33 E-value: 9.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT-LASLRGRIG 419
Cdd:cd03216 1 LELRGITKRFGGVKA--LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 VVMQdsvlfsgtiaeniaygkpdatpdaiaaaaqaaqadtfieqlsdgydtrvgergikLSGGQRQRIAIARALLIDPRV 499
Cdd:cd03216 79 MVYQ-------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 500 LIMDDSTSSVDAETESALRASLDRLI-GGRTTFIVAQRLSTVKR-ADEILVIEDGAVVA 556
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVVG 162
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
303-552 |
9.75e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 9.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 303 QTIARAGASASRL---FEVLDAETDVPERPGAIELTNArGRVEFRDVHLRYPgSDAETLNGVSFVVEPGATIALVGSTGS 379
Cdd:COG4178 323 QSLAEWRATVDRLagfEEALEAADALPEAASRIETSED-GALALEDLTLRTP-DGRPLLEDLSLSLKPGERLLITGPSGS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 380 GKTSvvnlvprfydvtggavLLddhdvRdlTLASL----RGRIGVVMQDSVLF--------SGTIAENIAY-GKPDATPD 446
Cdd:COG4178 401 GKST----------------LL-----R--AIAGLwpygSGRIARPAGARVLFlpqrpylpLGTLREALLYpATAEAFSD 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 447 AIAAAAQAAQA-DTFIEQLSDGYD-TRVgergikLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASL-DR 523
Cdd:COG4178 458 AELREALEAVGlGHLAERLDEEADwDQV------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEE 531
|
250 260 270
....*....|....*....|....*....|
gi 1309179971 524 LIGgrTTFI-VAQRLSTVKRADEILVIEDG 552
Cdd:COG4178 532 LPG--TTVIsVGHRSTLAAFHDRVLELTGD 559
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
358-585 |
9.85e-20 |
|
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: 93.82 E-value: 9.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPrfydvtgGAVLLDDHDVRDltlaslRGRIGVVMQDSVLFSGTIAENIA 437
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM-------GELEPSEGKIKH------SGRISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 438 YGKP-DATPDAIAAAAQAAQADtfIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESA 516
Cdd:TIGR01271 509 FGLSyDEYRYTSVIKACQLEED--IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 517 LRAS-LDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYaeiaASQLVGGEELD 585
Cdd:TIGR01271 587 IFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDF----SSLLLGLEAFD 652
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
341-568 |
1.13e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 88.61 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRD--LTLASLRGRI 418
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSGTIA-ENIAYGkpdatPDAIAAAAQAAQADTFIEQLSD-GYDTRVGERGIKLSGGQRQRIAIARALLID 496
Cdd:PRK09493 80 GMVFQQFYLFPHLTAlENVMFG-----PLRVRGASKEEAEKQARELLAKvGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 497 PRVLIMDDSTSSVDAE-TESALRASLDRLIGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAESC 568
Cdd:PRK09493 155 PKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPP 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
342-558 |
1.73e-19 |
|
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: 87.20 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLtlaslRGRIGVV 421
Cdd:cd03235 1 EVEDLTVSYGGHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 422 MQDSVL---FSGTIAENIAYGK-PDATPDAIAAAAQAAQADTFIE--QLSDGYDTRVGErgikLSGGQRQRIAIARALLI 495
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLyGHKGLFRRLSKADKAKVDEALErvGLSELADRQIGE----LSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 496 DPRVLIMDDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIeDGAVVARG 558
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
33-308 |
1.73e-19 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 89.21 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDQgITAGRREVITSGALLLIGVAAAGGVAQF---LQGFLSAKASHGAAYDMREAIFERLQTLS 109
Cdd:cd18560 7 LGKACNVLAPLFLGRAVNA-LTLAKVKDLESAVTLILLYALLRFSSKLlkeLRSLLYRRVQQNAYRELSLKTFAHLHSLS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 110 FSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAM-NWQLALVALVAIPLTILVLVrfvsKLGP 188
Cdd:cd18560 86 LDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHfGAWLALIVFLSVLLYGVFTI----KVTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 189 MFRGFQQRlsalnSILQENVA-GIRV--------VKAFAREPFEAARYRAANESLLQQgltvRRTVANAFPLL----FSV 255
Cdd:cd18560 162 WRTKFRRA-----ANKKDNEAhDIAVdsllnfetVKYFTNEKYEVDRYGEAVKEYQKS----SVKVQASLSLLnvgqQLI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 256 GNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARA 308
Cdd:cd18560 233 IQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQS 285
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
341-510 |
1.77e-19 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 88.19 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGsDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDL---TLASLRGR 417
Cdd:COG3638 3 LELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 418 IGVVMQD-------SVLfsgtiaENIAYGKPDATPDAIAAAAQAAQAD-----TFIEQ--LSDGYDTRVGErgikLSGGQ 483
Cdd:COG3638 82 IGMIFQQfnlvprlSVL------TNVLAGRLGRTSTWRSLLGLFPPEDreralEALERvgLADKAYQRADQ----LSGGQ 151
|
170 180
....*....|....*....|....*..
gi 1309179971 484 RQRIAIARALLIDPRVLIMDDSTSSVD 510
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLD 178
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
101-315 |
2.76e-19 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 88.71 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 101 IFERLQTLSFSYHDRIQTGQLITRLtSDVDLVRDFVGGglvQAIAAAIMLVGAVVLLLAM---NWQLALVALVAIPLTIL 177
Cdd:cd18588 81 LFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFLTG---SALTLVLDLVFSVVFLAVMfyySPTLTLIVLASLPLYAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 178 VLVRfvskLGPMFRGF---QQRLSALN-SILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLF 253
Cdd:cd18588 157 LSLL----VTPILRRRleeKFQRGAENqSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQ 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 254 SVGNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18588 233 LIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
345-558 |
2.82e-19 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 86.48 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 345 DVHLRYPGSDAetLNGVSFVVEPGATiALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDlTLASLRGRIGVVMQD 424
Cdd:cd03264 5 NLTKRYGKKRA--LDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 425 SVLFSG-TIAENIAY-----GKPDATPDAIAAAAQAAQadtfieQLSDGYDTRVGergiKLSGGQRQRIAIARALLIDPR 498
Cdd:cd03264 81 FGVYPNfTVREFLDYiawlkGIPSKEVKARVDEVLELV------NLGDRAKKKIG----SLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 499 VLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
341-556 |
2.88e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT-LASLRGRIG 419
Cdd:COG1129 5 LEMRGISKSFGGVKA--LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 VVMQDSVLFSG-TIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLsdGYD----TRVGErgikLSGGQRQRIAIARALL 494
Cdd:COG1129 83 IIHQELNLVPNlSVAENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 495 IDPRVLIMDDSTSS-VDAETES------ALRASldrligGRTTFIVAQRLSTVKR-ADEILVIEDGAVVA 556
Cdd:COG1129 157 RDARVLILDEPTASlTEREVERlfriirRLKAQ------GVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
358-510 |
3.53e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.02 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLRGRIGVVMQDSvlFSG---- 430
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YASlnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 431 -TIAENIAygkpdaTPDAIAAAAQAAQADTFIEQLSDgydtRVG-----------ErgikLSGGQRQRIAIARALLIDPR 498
Cdd:COG4608 112 mTVGDIIA------EPLRIHGLASKAERRERVAELLE----LVGlrpehadryphE----FSGGQRQRIGIARALALNPK 177
|
170
....*....|..
gi 1309179971 499 VLIMDDSTSSVD 510
Cdd:COG4608 178 LIVCDEPVSALD 189
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
342-563 |
3.68e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 86.81 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSdaETLNGVSFVVEPGATIALVGSTGSGKTS----VVNLVPrfydVTGGAVLLDDHDVRDLTlASLRGR 417
Cdd:TIGR03410 2 EVSNLNVYYGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTllktLMGLLP----VKSGSIRLDGEDITKLP-PHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 418 --IGVVMQDSVLFSG-TIAENIAYGKpDATPDAIAAAaqaaqaDTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALL 494
Cdd:TIGR03410 75 agIAYVPQGREIFPRlTVEENLLTGL-AALPRRSRKI------PDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 495 IDPRVLIMDDSTS----SVDAETESALRASLDRliGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEAL 563
Cdd:TIGR03410 148 TRPKLLLLDEPTEgiqpSIIKDIGRVIRRLRAE--GGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
319-565 |
6.72e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 90.13 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 319 LDAETDVPERPGAielTNARGRVEFRDVHLRYPG---------SDAETLNGVSFVVEPGATIALVGSTGSGKTS----VV 385
Cdd:COG4172 257 LAAEPRGDPRPVP---PDAPPLLEARDLKVWFPIkrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 386 NLVPrfydvTGGAVLLDDHDVRDLT---LASLRGRIGVVMQDSvlFSG-----TIAENIAYG----KPDATPDAIAAAAq 453
Cdd:COG4172 334 RLIP-----SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARV- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 454 aaqadtfIEQLSD-GYDTRVGERGI-KLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLiggrttf 531
Cdd:COG4172 406 -------AEALEEvGLDPAARHRYPhEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL------- 471
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1309179971 532 ivaQR------------LSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:COG4172 472 ---QRehglaylfishdLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-519 |
6.97e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 338 RGRVEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDV-----TGGAVLLDDHDVRDLTLA 412
Cdd:PRK14247 1 MNKIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 413 SLRGRIGVVMQ-DSVLFSGTIAENIAYG-KPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIA 490
Cdd:PRK14247 79 ELRRRVQMVFQiPNPIPNLSIFENVALGlKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180
....*....|....*....|....*....
gi 1309179971 491 RALLIDPRVLIMDDSTSSVDAETESALRA 519
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIES 187
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
353-595 |
7.91e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.07 E-value: 7.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 353 SDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQ--DSVLFSG 430
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 431 TIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSdgYDTRVGERgikLSGGQRQRIAIARALLIDPRVLIMDDSTSSVD 510
Cdd:PRK13642 98 TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD--FKTREPAR---LSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 511 AETESALRASLDRLIGGR--TTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAESCVYAEIA-----ASQLVGG-- 581
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGldvpfSSNLMKDlr 252
|
250
....*....|....*
gi 1309179971 582 -EELDLPESCMLEGE 595
Cdd:PRK13642 253 kNGFDLPEKYLSEDE 267
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
358-566 |
9.76e-19 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 86.54 E-value: 9.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRG----RIGVVMQDSVLFSG-TI 432
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 433 AENIAYGKPDATPDAIAAAAQAaqadtfIEQLSdgydtRVGERGIK------LSGGQRQRIAIARALLIDPRVLIMDDST 506
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERA------AEALE-----LVGLEGWEhkypdeLSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 507 SSVDAETESALRASLDRLIG--GRTTFIVAQRLS-TVKRADEILVIEDGAVVARGTHEALLAE 566
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
347-559 |
1.73e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 86.25 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 347 HLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRD--LTLASLRGRIGVVM 422
Cdd:PRK13637 10 HIYMEGTPFEKkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 423 Q--DSVLFSGTIAENIAYGkpdatPDAIAAAAQAAQADTF--IEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPR 498
Cdd:PRK13637 90 QypEYQLFEETIEKDIAFG-----PINLGLSEEEIENRVKraMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 499 VLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQRLSTV-KRADEILVIEDGAVVARGT 559
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
344-542 |
2.11e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.21 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 344 RDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDV-----TGGAVLLDDHDV---RDLTLaSLR 415
Cdd:PRK14239 9 SDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIyspRTDTV-DLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 416 GRIGVVMQDSVLFSGTIAENIAYG------KPDATPDAIAaaaqaaqaDTFIEQLS--DGYDTRVGERGIKLSGGQRQRI 487
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAV--------EKSLKGASiwDEVKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 488 AIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKR 542
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASR 212
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
33-291 |
3.05e-18 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 33 GSSVADLIAPQILRRIIDqGITAGRREVITSGALLLIGVAAAGGvaqflqgflsakashGAAYDMREAIFE--------R 104
Cdd:cd18784 7 AAAVGEIFIPYYTGQVID-GIVIEKSQDKFSRAIIIMGLLAIAS---------------SVAAGIRGGLFTlamarlniR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 105 LQTLSF--------SYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLti 176
Cdd:cd18784 71 IRNLLFrsivsqeiGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPL-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 177 lvlVRFVSKL-GPMFRGF----QQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAAneslLQQGLTVRRTVANAFP- 250
Cdd:cd18784 149 ---IAIVSKVyGDYYKKLskavQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEK----LKDTYKLKIKEALAYGg 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1309179971 251 LLFSVGNLGVALVV---WAGAVQVAHGRLTVGELVAFTSYLMLL 291
Cdd:cd18784 222 YVWSNELTELALTVstlYYGGHLVITGQISGGNLISFILYQLEL 265
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
341-559 |
3.84e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.74 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLD----DHDVRDLTlaSLRG 416
Cdd:PRK13639 2 LETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepiKYDKKSLL--EVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 417 RIGVVMQ--DSVLFSGTIAENIAYGKPDatpdaiaaaaQAAQADTFIEQLSDGYDtRVGERGIK------LSGGQRQRIA 488
Cdd:PRK13639 79 TVGIVFQnpDDQLFAPTVEEDVAFGPLN----------LGLSKEEVEKRVKEALK-AVGMEGFEnkpphhLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 489 IARALLIDPRVLIMDDSTSSVDAETESALRASLDRL-IGGRTTFIVAQRLSTV-KRADEILVIEDGAVVARGT 559
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
39-315 |
4.19e-18 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 84.89 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 39 LIAPQILRRIIDQgITAGRREVITSGALLLIG--VAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRI 116
Cdd:cd18583 13 VLVPRQLGIIVDS-LSGGSGKSPWKEIGLYVLlrFLQSGGGLGLLRSWLWIPVEQYSYRALSTAAFNHVMNLSMDFHDSK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 117 QTGQLIT---RLTSDVDLVRDFvgggLVQAIAAAI-MLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRG 192
Cdd:cd18583 92 KSGEVLKaieQGSSINDLLEQI----LFQIVPMIIdLVIAIVYLYYLFDPYMGLIVAVVMVLYVWSTIKLTSWRTKLRRD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 193 FQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVR--RTVANAF-PLLFSVGNLGVALVVwagAV 269
Cdd:cd18583 168 MIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLfsLNLLNAVqSLILTLGLLAGCFLA---AY 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1309179971 270 QVAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18583 245 QVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
342-565 |
6.77e-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: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGsdaETLNgVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASlrgR-IGV 420
Cdd:COG3840 3 RLDDLTYRYGD---FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAYG-KPDATPDAIAAAAqaaqadtfIEQLSDgydtRVGERGIK------LSGGQRQRIAIARA 492
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlRPGLKLTAEQRAQ--------VEQALE----RVGLAGLLdrlpgqLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 493 LLIDPRVLIMDDSTSSVDAetesALRASLDRLIG------GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:COG3840 144 LVRKRPILLLDEPFSALDP----ALRQEMLDLVDelcrerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
351-513 |
9.03e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 82.70 E-value: 9.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 351 PGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVP---RFYDVTGGAVLLDDhdvRDLTLASLRGRIGVVMQDSVL 427
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 428 FSG-TIAENIAYGKPDATPDAIAAAAQAAQADTFIeqLSDGYDTRVGERGIK-LSGGQRQRIAIARALLIDPRVLIMDDS 505
Cdd:cd03234 93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVL--LRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
....*...
gi 1309179971 506 TSSVDAET 513
Cdd:cd03234 171 TSGLDSFT 178
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
347-563 |
9.66e-18 |
|
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: 82.42 E-value: 9.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 347 HLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGRIGVVMQDSV 426
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 427 LFSG-TIAENIA-----YGKPDAtpdaiaaaaqaaQADTFIEQLSDGYD-TRVGERGIK-LSGGQRQRIAIARALLIDPR 498
Cdd:cd03265 84 VDDElTGWENLYiharlYGVPGA------------ERRERIDELLDFVGlLEAADRLVKtYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 499 VLIMDDSTSSVDAETesalRASLDRLI------GGRTTFIVAQRLSTV-KRADEILVIEDGAVVARGTHEAL 563
Cdd:cd03265 152 VLFLDEPTIGLDPQT----RAHVWEYIeklkeeFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-565 |
1.11e-17 |
|
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: 86.28 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKT----SVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLR 415
Cdd:COG4172 8 SVEDLSVAFGQGGGTVeaVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 416 G----RIGVVMQDSV-----LFsgTIAENIA--------YGKPDATPDAiaaaaqaaqadtfIEQLsdgydTRVG----E 474
Cdd:COG4172 88 RirgnRIAMIFQEPMtslnpLH--TIGKQIAevlrlhrgLSGAAARARA-------------LELL-----ERVGipdpE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 475 RGIK-----LSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLiggrttfivaQR------------L 537
Cdd:COG4172 148 RRLDayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDL----------QRelgmalllithdL 217
|
250 260
....*....|....*....|....*....
gi 1309179971 538 STVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:COG4172 218 GVVRRfADRVAVMRQGEIVEQGPTAELFA 246
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
341-558 |
1.30e-17 |
|
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: 82.03 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRY--PGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRgRI 418
Cdd:cd03266 2 ITADALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSG-TIAENIAYG------KPDATPDAiaaaaqaaqadtfIEQLSDGYDTR--VGERGIKLSGGQRQRIAI 489
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFaglyglKGDELTAR-------------LEELADRLGMEelLDRRVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 490 ARALLIDPRVLIMDDSTSSVDAETESALRASLDRL-IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
65-316 |
1.52e-17 |
|
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: 83.36 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 65 ALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAI 144
Cdd:cd18574 45 ALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 145 AAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEA 224
Cdd:cd18574 125 RSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDREL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 225 ARYRAANE--SLLQQGLTVRRTVANAFPLLFsVGNLgVALVVWAGAVQVAHGRLTVGELVAFtsyLMlllqplfvlgfGA 302
Cdd:cd18574 205 ELYEEEVEkaAKLNEKLGLGIGIFQGLSNLA-LNGI-VLGVLYYGGSLVSRGELTAGDLMSF---LV-----------AT 268
|
250
....*....|....
gi 1309179971 303 QTIARAGASASRLF 316
Cdd:cd18574 269 QTIQRSLAQLSVLF 282
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
342-513 |
2.27e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.22 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRdlTLASLRGrig 419
Cdd:COG4525 5 TVRHVSVRYPGGGQPQpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGADRG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 VVMQDSVLFSG-TIAENIAY-----GKPDATpdaiaaaaqaaqadtfIEQLSDGYDTRVG-----ERGI-KLSGGQRQRI 487
Cdd:COG4525 80 VVFQKDALLPWlNVLDNVAFglrlrGVPKAE----------------RRARAEELLALVGladfaRRRIwQLSGGMRQRV 143
|
170 180
....*....|....*....|....*.
gi 1309179971 488 AIARALLIDPRVLIMDDSTSSVDAET 513
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALT 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
358-559 |
2.27e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.36 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVN-----LVPRFYDVTGGAVLLDDHDVRDLTLAS-----------LRGRIGVV 421
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 422 MQ--DSVLFSGTIAENIAYG-------KPDATPDAIAAAAQAAQADTFIEQLSDGydtrvgergikLSGGQRQRIAIARA 492
Cdd:PRK13631 122 FQfpEYQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFG-----------LSGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 493 LLIDPRVLIMDDSTSSVDAETESAL-RASLDRLIGGRTTFIVAQRLSTV-KRADEILVIEDGAVVARGT 559
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMmQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
341-565 |
2.87e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.47 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRY-PGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIG 419
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 VVMQ--DSVLFSGTIAENIAYGKPDATPDAiaaaaqaaqaDTFIEQLSDGYDTrVGERGIK------LSGGQRQRIAIAR 491
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGLENKGIPH----------EEMKERVNEALEL-VGMQDFKereparLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 492 ALLIDPRVLIMDDSTSSVDAETesalRASLDRLIG------GRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLA 565
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEG----RLELIKTIKgirddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
341-566 |
3.36e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.13 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRY-PGS--DAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDD----HDVRDLTLAS 413
Cdd:PRK13646 3 IRFDNVSYTYqKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 LRGRIGVVMQ--DSVLFSGTIAENIAYGkpdatPDAIAAAAQAAQADTFIEQLSDGYDTRVGERG-IKLSGGQRQRIAIA 490
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFG-----PKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 491 RALLIDPRVLIMDDSTSSVDAETESALRASLDRLI--GGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAE 566
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
356-595 |
4.02e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.21 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 356 ETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRgRIGVVMQDSVLFSG-TIAE 434
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-ARDR-KVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 435 NIAYG--------KPDAtpDAIAAAAQAAQADTFIEQLSDGYDTrvgergiKLSGGQRQRIAIARALLIDPRVLIMDDST 506
Cdd:PRK10851 94 NIAFGltvlprreRPNA--AAIKAKVTQLLEMVQLAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 507 SSVDAETESALRASLDRL---IGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAE-------------SCVY 570
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREpatrfvlefmgevNRLQ 244
|
250 260
....*....|....*....|....*.
gi 1309179971 571 AEIAASQL-VGGEELDLPESCMLEGE 595
Cdd:PRK10851 245 GTIRGGQFhVGAHRWPLGYTPAYQGP 270
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
341-513 |
4.57e-17 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 80.56 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLR 415
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaRARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 416 GR-IGVVMQDSVLFSG-TIAENIAY-----GKPDAtpdaiaaaaqaaqADTFIEQLSD-GYDTRVGERGIKLSGGQRQRI 487
Cdd:COG4181 89 ARhVGFVFQSFQLLPTlTALENVMLplelaGRRDA-------------RARARALLERvGLGHRLDHYPAQLSGGEQQRV 155
|
170 180
....*....|....*....|....*.
gi 1309179971 488 AIARALLIDPRVLIMDDSTSSVDAET 513
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAAT 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
358-565 |
5.03e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 82.32 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRD---LTLASLRGRIGVVMQDSvlfsgtiae 434
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNP--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 435 niaYG--KPDATpdaiaaaaqaaQADTFIEQLSDGYDTRVGER-----------GIK----------LSGGQRQRIAIAR 491
Cdd:PRK11308 102 ---YGslNPRKK-----------VGQILEEPLLINTSLSAAERrekalammakvGLRpehydryphmFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 492 ALLIDPRVLIMDDSTSSVDAETESA---LRASLDRLIGGRTTFIvAQRLSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQvlnLMMDLQQELGLSYVFI-SHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
358-559 |
7.91e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 7.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPrFYDVTG----GAVLLDDHDVrdlTLASLRGRIGVVMQDSVLF-SGTI 432
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPI---DAKEMRAISAYVQQDDLFIpTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 433 AENIAYGKPDATPDAIAAAAQAAQADTFIEQLS--DGYDTRVGERGIK--LSGGQRQRIAIARALLIDPRVLIMDDSTSS 508
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGlrKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 509 VDAETESALRASLDRLIGGRTTFIVA--QRLSTVKRA-DEILVIEDGAVVARGT 559
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTihQPSSELFELfDKIILMAEGRVAYLGS 250
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
45-314 |
8.01e-17 |
|
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: 81.17 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 45 LRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITR 124
Cdd:cd18561 19 LARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 125 LTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSIL 204
Cdd:cd18561 99 VVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 205 QENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGRLTVGELVaf 284
Cdd:cd18561 179 LDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLL-- 256
|
250 260 270
....*....|....*....|....*....|....*
gi 1309179971 285 tsyLMLLL-----QPLFVLGfGAQTIARAGASASR 314
Cdd:cd18561 257 ---LILFLsreffRPLRDLG-AYWHAGYQGISAAD 287
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
356-552 |
1.06e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.47 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 356 ETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTL---ASLRGR-IGVVMQ-DSVLFSG 430
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQfHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 431 TIAENIAygkpdaTPDAIAAAAQAAQADTFIEQLSD-GYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSV 509
Cdd:PRK11629 103 TALENVA------MPLLIGKKKPAEINSRALEMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1309179971 510 DAETESA---LRASLDRLIGgrTTF-IVAQRLSTVKRADEILVIEDG 552
Cdd:PRK11629 177 DARNADSifqLLGELNRLQG--TAFlVVTHDLQLAKRMSRQLEMRDG 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
341-561 |
1.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 80.62 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSdAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV 420
Cdd:PRK13652 4 IETRDLCYSYSGS-KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQ--DSVLFSGTIAENIAYGKPDATPDAIAAAAQAaqaDTFIEQLS-DGYDTRVGERgikLSGGQRQRIAIARALLIDP 497
Cdd:PRK13652 83 VFQnpDDQIFSPTVEQDIAFGPINLGLDEETVAHRV---SSALHMLGlEELRDRVPHH---LSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 498 RVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQRLSTV-KRADEILVIEDGAVVARGTHE 561
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVE 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
341-532 |
1.50e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRgRIGV 420
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENR-HVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAYG-KPDATPDAIAAAAQAAQADTFieQLSDgydtrVGERGIK-LSGGQRQRIAIARALLIDP 497
Cdd:PRK09452 91 VFQSYALFPHmTVFENVAFGlRMQKTPAAEITPRVMEALRMV--QLEE-----FAQRKPHqLSGGQQQRVAIARAVVNKP 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1309179971 498 RVLIMDDSTSSVDA----ETESALRAsLDRLIGgrTTFI 532
Cdd:PRK09452 164 KVLLLDESLSALDYklrkQMQNELKA-LQRKLG--ITFV 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
340-566 |
2.45e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 340 RVEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRdltLAS----LR 415
Cdd:COG3845 5 ALELRGITKRFGGVVA--NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---IRSprdaIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 416 GRIGVVMQDSVLFSG-TIAENIAYGkpdaTPDAIAAAAQAAQADTFIEQLSDGY------DTRVGErgikLSGGQRQRIA 488
Cdd:COG3845 80 LGIGMVHQHFMLVPNlTVAENIVLG----LEPTKGGRLDRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 489 IARALLIDPRVLIMDDSTsSV--DAETEsALRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIEDGAVVA----RGTH 560
Cdd:COG3845 152 ILKALYRGARILILDEPT-AVltPQEAD-ELFEILRRLAAeGKSIIFITHKLREVMAiADRVTVLRRGKVVGtvdtAETS 229
|
....*.
gi 1309179971 561 EALLAE 566
Cdd:COG3845 230 EEELAE 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
365-558 |
2.54e-16 |
|
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: 77.92 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 365 VEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLAslRGRIGVVMQDSVLFSG-TIAENIAYGKpda 443
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLGL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 444 TPDAIAAAAQAAQADTFIEQLS-DGYDTRVGErgiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDaeteSALRASLD 522
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGlAGLEKRLPG---ELSGGERQRVALARVLVRDKPVLLLDEPFAALD----PALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1309179971 523 RLIG------GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:cd03298 169 DLVLdlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
341-567 |
2.80e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.49 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRY-PGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT----LAS 413
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 LRGRIGVVMQ--DSVLFSGTIAENIAYGKPD--ATPDAIAAAAQaaqadTFIEQLsdGYDTRVGERG-IKLSGGQRQRIA 488
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKKV--GLSEDLISKSpFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 489 IARALLIDPRVLIMDDSTSSVDAET-ESALRASLDRLIGGRTTFIVAQRLSTV-KRADEILVIEDGAVVARGTHEALLAE 566
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSD 235
|
.
gi 1309179971 567 S 567
Cdd:PRK13641 236 K 236
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
65-295 |
3.30e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 79.55 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 65 ALLLIGVAAAGGVAQFLQGFLSAKASH-GAAYDMRE--AIFERLQTLSFSYHDRIQTGQLITRLTsDVDLVRDFVGGglv 141
Cdd:cd18566 42 QVLVIGVVIAILLESLLRLLRSYILAWiGARFDHRLsnAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTG--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 142 QAIAAAIMLVGAVVLLLAM---NWQLALVALVAIPLTILVLVRfvskLGPMFRgfqQRLSALN-------SILQENVAGI 211
Cdd:cd18566 118 QALLALLDLPFVLIFLGLIwylGGKLVLVPLVLLGLFVLVAIL----LGPILR---RALKERSraderrqNFLIETLTGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 212 RVVKAFAREPFEAARYR--AANESLLQQGLTVRRTVANAFPLLFSVgnLGVALVVWAGAVQVAHGRLTVGELVAFTSYLM 289
Cdd:cd18566 191 HTIKAMAMEPQMLRRYErlQANAAYAGFKVAKINAVAQTLGQLFSQ--VSMVAVVAFGALLVINGDLTVGALIACTMLSG 268
|
....*.
gi 1309179971 290 LLLQPL 295
Cdd:cd18566 269 RVLQPL 274
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
362-564 |
3.43e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.85 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 362 SFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLR----GRIGVVMQDSVLFSG-TIAENI 436
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 437 AYGKPDA--TPDAIAAAAQAAQADTFIEQLSDGYDTrvgergiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETE 514
Cdd:PRK10070 128 AFGMELAgiNAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 515 SALRASLDRLIGG--RTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALL 564
Cdd:PRK10070 201 TEMQDELVKLQAKhqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
354-580 |
4.67e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 354 DAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQD-SVLFSGTI 432
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDtSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 433 AENIAYGKpdaTPDAIAAAAQAAQADTFIEQLSDGYDT-RVGERGI-KLSGGQRQRIAIARALLIDPRVLIMDDSTSSVD 510
Cdd:PRK09536 95 RQVVEMGR---TPHRSRFDTWTETDRAAVERAMERTGVaQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 511 AETESALRASLDRLI-GGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAESCVYAEIAASQLVG 580
Cdd:PRK09536 172 INHQVRTLELVRRLVdDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAVG 243
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
39-315 |
5.85e-16 |
|
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: 78.74 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 39 LIAPQILRRIIDQGITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQT 118
Cdd:cd18779 19 LALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 119 GQLITRLTSDVdLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVrfvsklgpMFRGFQQRLS 198
Cdd:cd18779 99 GDLLMRLSSNA-TIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLL--------ATRRRVRELM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 199 A--------LNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQ 270
Cdd:cd18779 170 ArelaaqaeAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQ 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1309179971 271 VAHGRLTVGELVAFTSYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18779 250 VLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
358-569 |
5.92e-16 |
|
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: 77.58 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASlRGRIGVVM--QDSVLFSG-TIAE 434
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGYlpQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 435 NIA-----YGKPDAtpdaiaaaAQAAQADTFIEQLsdGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSV 509
Cdd:cd03218 95 NILavleiRGLSKK--------EREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 510 D----AETESALRASLDRLIGgrtTFI----VAQRLSTVKRAdeiLVIEDGAVVARGTHEALLAESCV 569
Cdd:cd03218 165 DpiavQDIQKIIKILKDRGIG---VLItdhnVRETLSITDRA---YIIYEGKVLAEGTPEEIAANELV 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
336-565 |
6.43e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.09 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 336 NARGRVEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHD---VRDL--- 409
Cdd:PRK10619 1 MSENKLNVIDLHKRY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlVRDKdgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 410 -------TLASLRGRIGVVMQDSVLFSG-TIAENIAygkpdATPDAIAAAAQAAQADTFIEQLSD-GYDTRV-GERGIKL 479
Cdd:PRK10619 79 lkvadknQLRLLRTRLTMVFQHFNLWSHmTVLENVM-----EAPIQVLGLSKQEARERAVKYLAKvGIDERAqGKYPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 480 SGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLI-GGRTTFIVAQRLSTVKR-ADEILVIEDGAVVAR 557
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
....*...
gi 1309179971 558 GTHEALLA 565
Cdd:PRK10619 234 GAPEQLFG 241
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-566 |
6.67e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.11 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYP-GSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT-LASLRGRI 418
Cdd:PRK13644 2 IRLENVSYSYPdGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQD-SVLFSG-TIAENIAYGKPDAT--PDAIAAAAQAAQADTFIEQlsdgYDTRVGErgiKLSGGQRQRIAIARALL 494
Cdd:PRK13644 80 GIVFQNpETQFVGrTVEEDLAFGPENLClpPIEIRKRVDRALAEIGLEK----YRHRSPK---TLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 495 IDPRVLIMDDSTSSVDAETESALRASLDRL-IGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAE 566
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
97-312 |
8.00e-16 |
|
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: 78.15 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 97 MREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVggglvqAIAAAIML------VGAVVLLLAMNWQLALVALV 170
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSV------ALNANVLLrslvktLGMLGFMLSLSWQLTLLTLI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 171 AIPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQgLTVRRTVANAFP 250
Cdd:cd18590 145 EMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNL-KDRRDTVRAVYL 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 251 LLFSVGNLGV-ALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPL--FVLGFGaQTIARAGASA 312
Cdd:cd18590 224 LVRRVLQLGVqVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVrtLVYIYG-DMLSNVGAAA 287
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
362-554 |
8.66e-16 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 76.44 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 362 SFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVrdLTLASLRGRIGVVMQDSVLFSG-TIAENIAYGk 440
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFAHlTVRQNIGLG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 441 pdATPDAIAAAAQAAQADTFIEQLS-DGYDTRVGErgiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDaeteSALRA 519
Cdd:TIGR01277 95 --LHPGLKLNAEQQEKVVDAAQQVGiADYLDRLPE---QLSGGQRQRVALARCLVRPNPILLLDEPFSALD----PLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1309179971 520 SLDRLIG------GRTTFIVAQRLSTVKR-ADEILVIEDGAV 554
Cdd:TIGR01277 166 EMLALVKqlcserQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
34-315 |
8.83e-16 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 77.91 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIdQGITAGRREVITSGALLLIGVAaaggVAQFLQGFLSAKASHGA---AYDMR----EAIFERLQ 106
Cdd:cd18579 9 EDLLSLAQPLLLGLLI-SYLSSYPDEPLSEGYLLALALF----LVSLLQSLLLHQYFFLSfrlGMRVRsalsSLIYRKAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 107 TLSFSYHDRIQTGQLITRLTSDVDLVRDFVgGGLVQAIAAAIMLVGAVVLLLamnWQLALVALVAIpLTILVLVRFVSKL 186
Cdd:cd18579 84 RLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLY---RLLGWAALAGL-GVLLLLIPLQAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 187 GPMFRGFQ--------QRLSALNSILQenvaGIRVVKAFARE-PFEA--ARYRAANESLLQQGLTVRrtVANAFpLLFSV 255
Cdd:cd18579 159 AKLISKLRkklmkatdERVKLTNEILS----GIKVIKLYAWEkPFLKriEELRKKELKALRKFGYLR--ALNSF-LFFST 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 256 GNLgVALVVWAGAVQVAHgRLTVGelVAFT--SYLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18579 232 PVL-VSLATFATYVLLGN-PLTAA--KVFTalSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
360-520 |
9.72e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.37 E-value: 9.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 360 GVSFVVEPGATIALVGSTGSGKTSVVN-----LVPRFydVTGGAVLLDDHDVRdlTLASLRGRIGVVMQDSVLFSG-TIA 433
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAaiagtLSPAF--SASGEVLLNGRRLT--ALPAEQRRIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 434 ENIAYGKPDATPdaiaaaaqAAQADTFIEQ------LSDGYDTRVGErgikLSGGQRQRIAIARALLIDPRVLIMDDSTS 507
Cdd:COG4136 95 ENLAFALPPTIG--------RAQRRARVEQaleeagLAGFADRDPAT----LSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170
....*....|...
gi 1309179971 508 SVDAetesALRAS 520
Cdd:COG4136 163 KLDA----ALRAQ 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
341-559 |
1.03e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 78.69 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDV-----RDLTLAs 413
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalseKELRKA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 lRGRIGVVMQD-SVLFSGTIAENIAY-----GKPDATPDAIAAAA-----QAAQADTFIEQLSDGYdtrvgergiklsgg 482
Cdd:PRK11153 81 -RRQIGMIFQHfNLLSSRTVFDNVALplelaGTPKAEIKARVTELlelvgLSDKADRYPAQLSGGQ-------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 483 qRQRIAIARALLIDPRVLIMDDSTSSVDAE-TES--ALRASLDRLIGGRTTFIVAQrLSTVKR-ADEILVIEDGAVVARG 558
Cdd:PRK11153 146 -KQRVAIARALASNPKVLLCDEATSALDPAtTRSilELLKDINRELGLTIVLITHE-MDVVKRiCDRVAVIDAGRLVEQG 223
|
.
gi 1309179971 559 T 559
Cdd:PRK11153 224 T 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
341-566 |
1.07e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.58 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDH--DVRDLTLASLRGRI 418
Cdd:PRK13636 6 LKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQ--DSVLFSGTIAENIAYGKPDAT--PDAIAAAAQAAQADTFIEQLSDgydtrvgERGIKLSGGQRQRIAIARALL 494
Cdd:PRK13636 85 GMVFQdpDNQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 495 IDPRVLIMDDSTSSVD----AETESALRASLDRLigGRTTFIVAQRLSTVK-RADEILVIEDGAVVARGTHEALLAE 566
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
347-561 |
1.16e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 75.64 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 347 HLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLV---PRfYDVTGGAVLLDDHDVRDLTlASLRGRIGVVM- 422
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPK-YEVTEGEILFKGEDITDLP-PEERARLGIFLa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 423 -QDSVLFSG-TIAEniaygkpdatpdaiaaaaqaaqadtFIEQLSDGydtrvgergikLSGGQRQRIAIARALLIDPRVL 500
Cdd:cd03217 83 fQYPPEIPGvKNAD-------------------------FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 501 IMDDSTSSVDAETESALRASLDRLIGGRTTFIVA---QRLSTVKRADEILVIEDGAVVARGTHE 561
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEGKSVLIIthyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
341-565 |
1.22e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.92 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASlRGRIGV 420
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQ-DSVLFSGTIAENIA-----YGKPDATpdaiaaaaQAAQADTFIE--QLSDGYDTRVGErgikLSGGQRQRIAIARA 492
Cdd:PRK13537 85 VPQfDNLDPDFTVRENLLvfgryFGLSAAA--------ARALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 493 LLIDPRVLIMDDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
341-563 |
1.66e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.22 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVrdlTLASLRGR-IG 419
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRdIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 VVMQDSVLFSG-TIAENIAYG-KPDATPDAIAAAAQAaqadtfiEQLS----DGYDTRVGErgiKLSGGQRQRIAIARAL 493
Cdd:PRK11432 82 MVFQSYALFPHmSLGENVGYGlKMLGVPKEERKQRVK-------EALElvdlAGFEDRYVD---QISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 494 LIDPRVLIMDDSTSSVDAETESALRASLDRL---IGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEAL 563
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELqqqFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
358-575 |
2.10e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.21 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDhdvrdltlaslrgRIGVVMQDSVLFSGTIAENIA 437
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-------------SIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 438 YGKPDATPDAIAAAAQAAQaDTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAET-ESA 516
Cdd:PTZ00243 743 FFDEEDAARLADAVRVSQL-EADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERV 821
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 517 LRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAEScVYAEIAA 575
Cdd:PTZ00243 822 VEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLAA 879
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
358-521 |
2.71e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 75.58 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLrgrigVVMQDSVLFSG-TIAENI 436
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 437 AYGKPDATPDAIAAAAQAAQADTF-IEQLSDGYDTRVGErgikLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETES 515
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIaLVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
....*.
gi 1309179971 516 ALRASL 521
Cdd:TIGR01184 152 NLQEEL 157
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
341-564 |
3.47e-15 |
|
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: 75.51 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRF-YDVTGGAVLLDDHDVRDLTLASLRGRIG 419
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 VV---MQDSVLFSGTIAENIAYGKPDAT-----PDAIAAAAQAAQADTF-IEQLSDgydTRVGErgikLSGGQRQRIAIA 490
Cdd:COG1119 82 LVspaLQLRFPRDETVLDVVLSGFFDSIglyrePTDEQRERARELLELLgLAHLAD---RPFGT----LSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 491 RALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVaqrLSTvKRADEI-------LVIEDGAVVARGTHEAL 563
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLV---LVT-HHVEEIppgithvLLLKDGRVVAAGPKEEV 230
|
.
gi 1309179971 564 L 564
Cdd:COG1119 231 L 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
358-566 |
6.21e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.79 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDV---RDLT-----LASLRGRIGVVMQDSVLFS 429
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 430 G-TIAENIAYG----KPDATpDAIAAAAQAAQADTFIEQLSDGYDTRvgergikLSGGQRQRIAIARALLIDPRVLIMDD 504
Cdd:PRK11264 99 HrTVLENIIEGpvivKGEPK-EEATARARELLAKVGLAGKETSYPRR-------LSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 505 STSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAE 566
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-510 |
7.11e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 350 YPGSDAET--LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVL 427
Cdd:COG1101 12 NPGTVNEKraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 428 ---FSGTIAEN--IAYGKpdATPDAIAAAAQAAQADTFIEQLS-------DGYDTRVGergiKLSGGQRQRIAIARALLI 495
Cdd:COG1101 92 gtaPSMTIEENlaLAYRR--GKRRGLRRGLTKKRRELFRELLAtlglgleNRLDTKVG----LLSGGQRQALSLLMATLT 165
|
170
....*....|....*
gi 1309179971 496 DPRVLIMDDSTSSVD 510
Cdd:COG1101 166 KPKLLLLDEHTAALD 180
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-574 |
7.36e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.13 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYD-VTG----GAVLLDDHDV---RDLTlaSLRGRIGVVMQDSVLFS 429
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkVSGyrysGDVLLGGRSIfnyRDVL--EFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 430 GTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSV 509
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 510 DAET----ESALRASLDRLiggrTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAeSCVYAEIA 574
Cdd:PRK14271 195 DPTTtekiEEFIRSLADRL----TVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS-SPKHAETA 259
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
356-559 |
9.85e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 9.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 356 ETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDV-----RDLTLASLRGRIGVVMQ--DSVLF 428
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKEVKRLRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 429 SGTIAENIAYGKPDATPDAIAAAAQAAQADTFIeQLSDGYDTRvgeRGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSS 508
Cdd:PRK13645 105 QETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDYVKR---SPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 509 VDAETESALRASLDRL---IGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGT 559
Cdd:PRK13645 181 LDPKGEEDFINLFERLnkeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
47-312 |
1.87e-14 |
|
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: 73.98 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 47 RIIDQGITAGR-REVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRL 125
Cdd:cd18584 21 RIIAGVFLEGAgLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 126 TSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTIL--VLVrfvsklGPMFRGFQQR----LSA 199
Cdd:cd18584 101 TEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLfmILI------GKAAQAASRRqwaaLSR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 200 LNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRtVA--NAFPL-LFSVgnLGVALVvwagAVQVAHgRL 276
Cdd:cd18584 175 LSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLR-VAflSSAVLeFFAT--LSIALV----AVYIGF-RL 246
|
250 260 270
....*....|....*....|....*....|....*....
gi 1309179971 277 TVGELVAFTSYLMLLLQPLFVL---GFGAQTIARAGASA 312
Cdd:cd18584 247 LGGSLTLFTALFVLLLAPEFYLplrQLGAAYHARADGLA 285
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-559 |
2.35e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.16 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 353 SDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDV------TGGAVLLDDHDVRDLTLASLRGRIGVVMQDSV 426
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 427 LFSG-TIAENIAYG-KPDATPDAIAAAAQAAQADTFIEQLSDGYDtRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDD 504
Cdd:PRK14246 101 PFPHlSIYDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 505 STSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGT 559
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
341-558 |
2.76e-14 |
|
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: 71.93 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlaslRGRIGV 420
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAY-------GKPDATPDaiaaaaqaaqADTFIEQ--LSDGYDTRVGErgikLSGGQRQRIAIA 490
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYlaqlkglKKEEARRR----------IDEWLERleLSEYANKRVEE----LSKGNQQKVQFI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 491 RALLIDPRVLIMDDSTSSVD-AETESALRASLDRLIGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDpVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
358-534 |
3.29e-14 |
|
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: 71.74 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGRIGVVMQDSVLFSG-TIAENI 436
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 437 A-----YGKPDATPDaiaaaaqaaqADTFIEQ--LSDGYDTRVGergiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSV 509
Cdd:COG4133 97 RfwaalYGLRADREA----------IDEALEAvgLAGLADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*
gi 1309179971 510 DAETESALRASLDRLIGGRTTFIVA 534
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLT 187
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
358-563 |
3.31e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.58 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVN-----LVPrfydvTGGAV---LLDDHD----------VRDLTLA------- 412
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnalLLP-----DTGTIewiFKDEKNkkktkekekvLEKLVIQktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 413 ----SLRGRIGVVMQ--DSVLFSGTIAENIAYG-------KPDAtpdaiaaaaqaaqadtfiEQLSDGYDTRVG------ 473
Cdd:PRK13651 98 kkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvsKEEA------------------KKRAAKYIELVGldesyl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 474 ERG-IKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRL-IGGRTTFIVAQRLSTV-KRADEILVIE 550
Cdd:PRK13651 160 QRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIFFK 239
|
250
....*....|....
gi 1309179971 551 DGAVVARG-THEAL 563
Cdd:PRK13651 240 DGKIIKDGdTYDIL 253
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
358-566 |
3.41e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGA-----VLLDDHDV--RDLTLASLRGRIGVVMQDSVLFSG 430
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFrvegkVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 431 TIAENIAYGkpdatpdaIAAAAQAAQADTFIEQ------LSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDD 504
Cdd:PRK14243 106 SIYDNIAYG--------ARINGYKGDMDELVERslrqaaLWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 505 STSSVDAETESALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHEALLAE 566
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVE 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
341-589 |
3.56e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.23 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRY-PGSD--AETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT----LAS 413
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 LRGRIGVVMQ--DSVLFSGTIAENIAYG-------KPDATPDAIAAAAQAAQADTFIEQlsdgydtrvgeRGIKLSGGQR 484
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqnfgipKEKAEKIAAEKLEMVGLADEFWEK-----------SPFELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 485 QRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRL-IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGThea 562
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT--- 227
|
250 260
....*....|....*....|....*..
gi 1309179971 563 llaESCVYAEIaasQLVGGEELDLPES 589
Cdd:PRK13643 228 ---PSDVFQEV---DFLKAHELGVPKA 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-542 |
5.41e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTG-----GAVLLDDHDV--RDLTLASLRGRIGVVMQDSVLFSG 430
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 431 TIAENIAYG------KPDATPDAIAAAAQAAQadtfieQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDD 504
Cdd:PRK14258 103 SVYDNVAYGvkivgwRPKLEIDDIVESALKDA------DLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1309179971 505 STSSVDA----ETESALRASldRLIGGRTTFIVAQRLSTVKR 542
Cdd:PRK14258 177 PCFGLDPiasmKVESLIQSL--RLRSELTMVIVSHNLHQVSR 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
341-592 |
6.04e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET----LNGVSFVVEPGATIALVGSTGSGKTSVVN-----LVPrfydvTGGAVLLDDHDVRDL-T 410
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnalLIP-----SEGKVYVDGLDTSDEeN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 411 LASLRGRIGVVMQ--DSVLFSGTIAENIAYG------KPDAtpdaiaaaaqaaqadtfIEQLSDGYDTRVGERGIK---- 478
Cdd:PRK13633 80 LWDIRNKAGMVFQnpDNQIVATIVEEDVAFGpenlgiPPEE-----------------IRERVDESLKKVGMYEYRrhap 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 479 --LSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQRLSTVKRADEILVIEDGAV 554
Cdd:PRK13633 143 hlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKV 222
|
250 260 270
....*....|....*....|....*....|....*...
gi 1309179971 555 VARGTHEAllaescVYAEIAASQLVGgeeLDLPESCML 592
Cdd:PRK13633 223 VMEGTPKE------IFKEVEMMKKIG---LDVPQVTEL 251
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
372-567 |
7.49e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.98 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 372 ALVGSTGSGKTSVVNLV-----P-RFYDVTGGAVLLDDHdvRDLTLASLRGRIGVVMQDSVLFSG-TIAENIAYGKPDAT 444
Cdd:PRK11144 28 AIFGRSGAGKTSLINAIsgltrPqKGRIVLNGRVLFDAE--KGICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 445 PDAIAAAAQAAQadtfIEQLSDGYDtrvgergIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRL 524
Cdd:PRK11144 106 VAQFDKIVALLG----IEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1309179971 525 IGGRTTFI--VAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAES 567
Cdd:PRK11144 175 AREINIPIlyVSHSLDEILRlADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
358-552 |
8.67e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTG--GAVLLDDhdvRDLTLASLRgRIGVVMQDSVLFSG-TIAE 434
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN---RKPTKQILK-RTGFVTQDDILYPHlTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 435 NIAYGKPDATPDAIAAAAQAAQADTFIEQL--SDGYDTRVGERGIK-LSGGQRQRIAIARALLIDPRVLIMDDSTSSVDA 511
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1309179971 512 ETESALRASLDRLIGGRTTFIVA--QRLSTVKRA-DEILVIEDG 552
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSmhQPSSRVYQMfDSVLVLSEG 283
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
334-510 |
1.26e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.51 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 334 LTNARGRVEFRDVHlrYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLAS 413
Cdd:PRK10247 1 MQENSPLLQLQNVG--YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 LRGRIGVVMQDSVLFSGTIAENIA--YGKPDATPDaiaaaaqaaqADTFIEQLSD-GYDTRVGERGI-KLSGGQRQRIAI 489
Cdd:PRK10247 79 YRQQVSYCAQTPTLFGDTVYDNLIfpWQIRNQQPD----------PAIFLDDLERfALPDTILTKNIaELSGGEKQRISL 148
|
170 180
....*....|....*....|.
gi 1309179971 490 ARALLIDPRVLIMDDSTSSVD 510
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALD 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
358-565 |
1.50e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDvTGGAVLLDDHDVRDLT---LASLRGRIGVVMQD---------S 425
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDpnsslnprlN 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 426 VLfsGTIAENIAYGKPDATPdaiaaaaqAAQADTFIEQLSD-GYDTRVGER-GIKLSGGQRQRIAIARALLIDPRVLIMD 503
Cdd:PRK15134 381 VL--QIIEEGLRVHQPTLSA--------AQREQQVIAVMEEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 504 DSTSSVDAETESALRASLDRLIGG-RTTFIVAQRLSTVKRA--DEILVIEDGAVVARGTHEALLA 565
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRAlcHQVIVLRQGEVVEQGDCERVFA 515
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
341-573 |
1.52e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.17 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASlRGRIGV 420
Cdd:PRK13536 42 IDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQ-DSVLFSGTIAEN-IAYGKPDATPDAIAAAAQAAQADtfIEQLSDGYDTRVGErgikLSGGQRQRIAIARALLIDPR 498
Cdd:PRK13536 119 VPQfDNLDLEFTVRENlLVFGRYFGMSTREIEAVIPSLLE--FARLESKADARVSD----LSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 499 VLIMDDSTSSVDAETE----SALRASLDRligGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAE--SCVYA 571
Cdd:PRK13536 193 LLILDEPTTGLDPHARhliwERLRSLLAR---GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEhiGCQVI 269
|
..
gi 1309179971 572 EI 573
Cdd:PRK13536 270 EI 271
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
60-295 |
1.76e-13 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 71.39 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 60 VITSGALLLIGVAAAGGvaqFLQGFLSAKAShgAAYDMR--EAIFERLQTLSFSYHDRIQTGQlITRLTSDVDLVRDFVG 137
Cdd:cd18783 43 VLTIGVVIALLFEGILG---YLRRYLLLVAT--TRIDARlaLRTFDRLLSLPIDFFERTPAGV-LTKHMQQIERIRQFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 138 GGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFvskLGPMFRGFQQRLSA---LNSILQENVAGIRVV 214
Cdd:cd18783 117 GQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAF---LPPFRRRLQALYRAegeRQAFLVETVHGIRTV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 215 KAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQP 294
Cdd:cd18783 194 KSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGP 273
|
.
gi 1309179971 295 L 295
Cdd:cd18783 274 L 274
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
358-567 |
1.95e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.43 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSG-TIAENI 436
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 437 AYGKpdaTP---------DAIAAAAQAAQADTFIEQLSdgyDTRVGErgikLSGGQRQRIAIARALLIDPRVLIMDDSTS 507
Cdd:PRK11231 98 AYGR---SPwlslwgrlsAEDNARVNQAMEQTRINHLA---DRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 508 SVDAETESALRASLDRL-IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAES 567
Cdd:PRK11231 168 YLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
356-569 |
2.16e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 356 ETLNGVSFVVEPGATIALVGSTGSGKTSVVNLV---PRfydVTGGAVLLDDHDVRDLTLAS-LRGRIGVVMQDSVLFSG- 430
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdPR---ATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRm 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 431 TIAENIAYGKPDATpdaiaaaaqaaqADTFIEQLSDGYD--TRVGERGIK----LSGGQRQRIAIARALLIDPRVLIMDD 504
Cdd:PRK11614 96 TVEENLAMGGFFAE------------RDQFQERIKWVYElfPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 505 STSSVDAETESALRASLDRLIG-GRTTFIVAQRLS-TVKRADEILVIEDGAVVARGTHEALLAESCV 569
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
346-524 |
2.88e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.11 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 346 VHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlaslrGRIGVVMQDS 425
Cdd:PRK11248 7 LYADYGGKPA--LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 426 VLFS-GTIAENIAYGKPDATPDAIAAAAQAAqadtfiEQLS----DGYDTRvgeRGIKLSGGQRQRIAIARALLIDPRVL 500
Cdd:PRK11248 80 GLLPwRNVQDNVAFGLQLAGVEKMQRLEIAH------QMLKkvglEGAEKR---YIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180
....*....|....*....|....
gi 1309179971 501 IMDDSTSSVDAETESALRASLDRL 524
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKL 174
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
358-559 |
3.01e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.54 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT----LASLRGRIGVVMQ--DSVLFSGT 431
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 432 IAENIAYG-------KPDATPDAIAAAAQAAQADTFIEQlsdgydtrvgeRGIKLSGGQRQRIAIARALLIDPRVLIMDD 504
Cdd:PRK13649 103 VLKDVAFGpqnfgvsQEEAEALAREKLALVGISESLFEK-----------NPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 505 STSSVDAETESALRASLDRL-IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGT 559
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
52-282 |
3.55e-13 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 70.77 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 52 GITAGRREVITSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDL 131
Cdd:cd18558 49 GPFEKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 132 VRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVSKLGPMFRGFQQRLSALNSILQENVAGI 211
Cdd:cd18558 129 INEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAF 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 212 RVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGRLTVGELV 282
Cdd:cd18558 209 RTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVL 279
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
351-563 |
4.78e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.51 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 351 PGSDAETLNGVSFVVEPGATIALVGSTGSGKTS----VVNLVPrfydVTGGAVLLDDHDVRDLTLASLRGR---IGVVMQ 423
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 424 D---SVLFSGTIAENIAygKPdatpdaiaaaaqaaqADTFIEQLSDG-YDTRVGERGIKL--------------SGGQRQ 485
Cdd:PRK15079 106 DplaSLNPRMTIGEIIA--EP---------------LRTYHPKLSRQeVKDRVKAMMLKVgllpnlinryphefSGGQCQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 486 RIAIARALLIDPRVLIMDDSTSSVDAETESA---LRASLDRLIGGRTTFIvAQRLSTVKR-ADEILVIEDGAVVARGTHE 561
Cdd:PRK15079 169 RIGIARALILEPKLIICDEPVSALDVSIQAQvvnLLQQLQREMGLSLIFI-AHDLAVVKHiSDRVLVMYLGHAVELGTYD 247
|
..
gi 1309179971 562 AL 563
Cdd:PRK15079 248 EV 249
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
324-510 |
6.92e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.63 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 324 DVPERPGAIELTNARGRVEFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDD 403
Cdd:PRK11607 3 DAIPRPQAKTRKALTPLLEIRNLTKSFDGQHA--VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 404 HDVRDLtlASLRGRIGVVMQDSVLFSG-TIAENIAYG-KPDATPdaiaaaaQAAQADTFIEQLSDGYDTRVGERGI-KLS 480
Cdd:PRK11607 81 VDLSHV--PPYQRPINMMFQSYALFPHmTVEQNIAFGlKQDKLP-------KAEIASRVNEMLGLVHMQEFAKRKPhQLS 151
|
170 180 190
....*....|....*....|....*....|
gi 1309179971 481 GGQRQRIAIARALLIDPRVLIMDDSTSSVD 510
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
356-565 |
8.51e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 68.71 E-value: 8.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 356 ETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDvrdLTLASLRGR---IGVVMQDSvlfSGTI 432
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHK---LEYGDYKYRckhIRMIFQDP---NTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 433 AENIAYGKPDATPDAIAAAAQAAQADTFIEQ-LsdgydTRVG------ERGIK-LSGGQRQRIAIARALLIDPRVLIMDD 504
Cdd:COG4167 101 NPRLNIGQILEEPLRLNTDLTAEEREERIFAtL-----RLVGllpehaNFYPHmLSSGQKQRVALARALILQPKIIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 505 STSSVDAETESA---LRASLDRLIGgrTTFI-VAQRLSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:COG4167 176 ALAALDMSVRSQiinLMLELQEKLG--ISYIyVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
342-581 |
8.97e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 71.29 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSD--AETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDL---TLASLRG 416
Cdd:PRK10535 6 ELKDIRRSYPSGEeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 417 R-IGVVMQDSVLFSG-TIAENIAygkpdaTPDAIAAAAQAAQADTFIEQLSD-GYDTRVGERGIKLSGGQRQRIAIARAL 493
Cdd:PRK10535 86 EhFGFIFQRYHLLSHlTAAQNVE------VPAVYAGLERKQRLLRAQELLQRlGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 494 LIDPRVLIMDDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKRADEILVIEDGAVV----ARGTHEALLAESC 568
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIVrnppAQEKVNVAGGTEP 239
|
250
....*....|....
gi 1309179971 569 VYAEIAA-SQLVGG 581
Cdd:PRK10535 240 VVNTASGwRQFVSG 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
356-563 |
1.24e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 67.73 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 356 ETLNGVSFVVEPGATIALVGSTGSGKTS---VVNL--VPRfydvtGGAVLLDDH------DVRDLTLASLRGRIGVVMQD 424
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSllrVLNLleTPD-----SGQLNIAGHqfdfsqKPSEKAIRLLRQKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 425 SVLFSG-TIAENIAygkpdATPDAIAAAAQAAQADTFIEQLSDGYDTRVGER-GIKLSGGQRQRIAIARALLIDPRVLIM 502
Cdd:COG4161 91 YNLWPHlTVMENLI-----EAPCKVLGLSKEQAREKAMKLLARLRLTDKADRfPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 503 DDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEAL 563
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDASHF 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
355-555 |
2.13e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 67.52 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 355 AETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRG---RIGVVMQDSVlfsGT 431
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQDSP---SA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 432 IAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTR---VGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSS 508
Cdd:TIGR02769 101 VNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRsedADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1309179971 509 VDAETESALRASLDRL--IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVV 555
Cdd:TIGR02769 181 LDMVLQAVILELLRKLqqAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
358-558 |
3.21e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT--LASLRGrIGVVMQD-SVLFSGTIAE 434
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhkLAAQLG-IGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 435 NIAYGKPDATP-------DAIAAAAQAAQAdTFIEQLSDGYDTRVGErgikLSGGQRQRIAIARALLIDPRVLIMDDSTS 507
Cdd:PRK09700 100 NLYIGRHLTKKvcgvniiDWREMRVRAAMM-LLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 508 SV-DAETESaLRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:PRK09700 175 SLtNKEVDY-LFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
362-580 |
5.73e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.76 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 362 SFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLAslRGRIGVVMQDSVLFSG-TIAENIAYGk 440
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLG- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 441 pdATPDAIAAAAQAAQADTFIEQ--LSDGYDTRVGErgikLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDaeteSALR 518
Cdd:PRK10771 96 --LNPGLKLNAAQREKLHAIARQmgIEDLLARLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALD----PALR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 519 AS----LDRLIGGR--TTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAescvyAEIAASQLVG 580
Cdd:PRK10771 166 QEmltlVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS-----GKASASALLG 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
342-563 |
5.88e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVR-DLTLASLRGRIGV 420
Cdd:PRK11288 6 SFDGIGKTFPGVKA--LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYD--TRVGErgikLSGGQRQRIAIARALLIDP 497
Cdd:PRK11288 84 IYQELHLVPEmTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 498 RVLIMDDSTSSVDA-ETE------SALRASldrligGRTTFIVAQRLSTVKR-ADEILVIEDGAVVArgTHEAL 563
Cdd:PRK11288 160 RVIAFDEPTSSLSArEIEqlfrviRELRAE------GRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDM 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
358-552 |
6.17e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLRGR-IGVVMQDSVLFSGTIA 433
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLRAKhVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 434 -ENIaygKPDATPDAIAAAAQAAQADTFIEQLsdGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAE 512
Cdd:PRK10584 106 lENV---ELPALLRGESSRQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1309179971 513 TE---SALRASLDRLIGgrTTFI-VAQRLSTVKRADEILVIEDG 552
Cdd:PRK10584 181 TGdkiADLLFSLNREHG--TTLIlVTHDLQLAARCDRRLRLVNG 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
341-554 |
6.66e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.36 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASlRGrIGV 420
Cdd:PRK11000 4 VTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-RG-VGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAYGKPDATPDAIAAaaqaaqaDTFIEQLSDGYD-TRVGERGIK-LSGGQRQRIAIARALLIDP 497
Cdd:PRK11000 80 VFQSYALYPHlSVAENMSFGLKLAGAKKEEI-------NQRVNQVAEVLQlAHLLDRKPKaLSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 498 RVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQ-RLSTVKRADEILVIEDGAV 554
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
343-513 |
7.72e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 343 FRDVHLRYPGsdAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDdhdvRDLtlaslrgRIGVVM 422
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGL-------RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 423 QDSVLFSG-TIAENIAYGKPD-------------ATPDAIAAAAQAAQADTFIEQLsDGY-------------------- 468
Cdd:COG0488 68 QEPPLDDDlTVLDTVLDGDAElraleaeleeleaKLAEPDEDLERLAELQEEFEAL-GGWeaearaeeilsglgfpeedl 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1309179971 469 DTRVGErgikLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAET 513
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
344-564 |
9.66e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.56 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 344 RDVHLRYPGsdAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQ 423
Cdd:PRK13548 6 RNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 424 DSVL-FSGTIAENIAYGkpdATPDAIAAAAQAAQADTFIEQLS-DGYDTRvgeRGIKLSGGQRQRIAIARALL------I 495
Cdd:PRK13548 84 HSSLsFPFTVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDlAHLAGR---DYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 496 DPRVLIMDDSTSSVD-AETESALRASLDRLIGGRTTFIV-------AQRLstvkrADEILVIEDGAVVARGTHEALL 564
Cdd:PRK13548 158 PPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAVIVvlhdlnlAARY-----ADRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
356-565 |
9.67e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.58 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 356 ETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSvlfSGTIAEN 435
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 436 IAYGKPDATPDAIAAAAQAAQADTFIEQLSdgydTRVGERGIK-------LSGGQRQRIAIARALLIDPRVLIMDDSTSS 508
Cdd:PRK15112 104 QRISQILDFPLRLNTDLEPEQREKQIIETL----RQVGLLPDHasyyphmLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 509 VDAetesALRASLDRLI------GGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:PRK15112 180 LDM----SMRSQLINLMlelqekQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
341-553 |
1.28e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 63.33 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAeTLNGVSFVVEPGATIALVGSTGSGKTSVVnlvprfydvtggavllddhdvRdlTLASL----RG 416
Cdd:cd03223 1 IELENLSLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLF---------------------R--ALAGLwpwgSG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 417 RIGVVMQDSVLF--------SGTIAENIAYgkpdatPdaiaaaaqaaqadtfieqlsdgydtrvgeRGIKLSGGQRQRIA 488
Cdd:cd03223 57 RIGMPEGEDLLFlpqrpylpLGTLREQLIY------P-----------------------------WDDVLSGGEQQRLA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 489 IARALLIDPRVLIMDDSTSSVDAETESALRASLDRLiggRTTFI-VAQRLSTVKRADEILVIEDGA 553
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVIsVGHRPSLWKFHDRVLDLDGEG 164
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
358-503 |
1.56e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.67 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKT----SVVNLVPrfydVTGGAVLLDDHDVRDLTLaSLRGR--IGVVMQDSVLFSG- 430
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTttfyMIVGLVK----PDSGRIFLDGEDITHLPM-HKRARlgIGYLPQEASIFRKl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 431 TIAENIA-----YGKPDATPDAIaaaaqaaqadtfIEQLSDGYD-TRVGE-RGIKLSGGQRQRIAIARALLIDPRVLIMD 503
Cdd:COG1137 94 TVEDNILavlelRKLSKKEREER------------LEELLEEFGiTHLRKsKAYSLSGGERRRVEIARALATNPKFILLD 161
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
341-524 |
1.58e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.02 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGsDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASlRGrIGV 420
Cdd:PRK11650 4 LKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RD-IAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 VMQDSVLFSG-TIAENIAYG-KPDATPDAIAAAAQAAQADTF-IEQLSDgydtrvgERGIKLSGGQRQRIAIARALLIDP 497
Cdd:PRK11650 81 VFQNYALYPHmSVRENMAYGlKIRGMPKAEIEERVAEAARILeLEPLLD-------RKPRELSGGQRQRVAMGRAIVREP 153
|
170 180
....*....|....*....|....*..
gi 1309179971 498 RVLIMDDSTSSVDAETESALRASLDRL 524
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRL 180
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
34-298 |
2.42e-11 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 64.80 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITSGALL--LIGVAAAggVAQFL-----QGFLSAKASHgaaydMREAIFERLQ 106
Cdd:cd18589 8 SSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVmsLLTIASA--VSEFVcdliyNITMSRIHSR-----LQGLVFAAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 107 TLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLtILVLVRFVSK- 185
Cdd:cd18589 81 RQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPL-LLLVPKFVGKf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 186 ---LGPMFrgfQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAAneslLQQGLTVRRTVANAFPL-LFSVGNLGVA 261
Cdd:cd18589 160 qqsLAVQV---QKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQR----LQKTYRLNKKEAAAYAVsMWTSSFSGLA 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1309179971 262 L---VVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVL 298
Cdd:cd18589 233 LkvgILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVL 272
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
341-518 |
2.68e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSdAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLRGR 417
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 418 IGVVMQDS-VLFSGTIAENIAygkpdatpdaIAAAAQAAQADTFIEQLSDGYDtRVG------ERGIKLSGGQRQRIAIA 490
Cdd:PRK10908 81 IGMIFQDHhLLMDRTVYDNVA----------IPLIIAGASGDDIRRRVSAALD-KVGlldkakNFPIQLSGGEQQRVGIA 149
|
170 180
....*....|....*....|....*....
gi 1309179971 491 RALLIDPRVLIMDDSTSSVD-AETESALR 518
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDdALSEGILR 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
342-563 |
5.08e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.47 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlASLRGRIGVV 421
Cdd:PRK11300 7 SVSGLMMRFGGLLA--VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 422 --MQDSVLF-SGTIAENIAYGKPD-----------ATPDaiaaaaqaaqadtFIEQLSDGYD------TRVGERGI---- 477
Cdd:PRK11300 84 rtFQHVRLFrEMTVIENLLVAQHQqlktglfsgllKTPA-------------FRRAESEALDraatwlERVGLLEHanrq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 478 --KLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQRLSTVKR-ADEILVIEDG 552
Cdd:PRK11300 151 agNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQG 230
|
250
....*....|.
gi 1309179971 553 AVVARGTHEAL 563
Cdd:PRK11300 231 TPLANGTPEEI 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
345-558 |
5.34e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 345 DVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVvnlvprFYDVTG------GAVLLDDH--DVRDLTLASLRG 416
Cdd:PRK13638 6 DLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTL------FMNLSGllrpqkGAVLWQGKplDYSKRGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 417 RIGVVMQD--SVLFSGTIAENIAY-----GKPDATpdaiaaaaqaaqadtfIEQLSDGYDTRVGERGIK------LSGGQ 483
Cdd:PRK13638 78 QVATVFQDpeQQIFYTDIDSDIAFslrnlGVPEAE----------------ITRRVDEALTLVDAQHFRhqpiqcLSHGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 484 RQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
344-554 |
7.38e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.77 E-value: 7.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 344 RDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLlddhdVRDLTLASLRGRIGVVMQ 423
Cdd:PRK11247 16 NAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 424 DSVLFS-GTIAENIAYG-----KPDAtpdaiaaaaqaaqadtfIEQLSD-GYDTRVGERGIKLSGGQRQRIAIARALLID 496
Cdd:PRK11247 89 DARLLPwKKVIDNVGLGlkgqwRDAA-----------------LQALAAvGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 497 PRVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQRLS-TVKRADEILVIEDGAV 554
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
356-562 |
7.45e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.72 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 356 ETLNGVSFVVEPGATIALVGSTGSGKTS---VVNL--VPRfydvTGGAVLLDDH-----DVRDLTLASLRGRIGVVMQDS 425
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLleMPR----SGTLNIAGNHfdfskTPSDKAIRELRRNVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 426 VLFSG-TIAENI--------AYGKPDATPDAIAAAAQAAqadtfIEQLSDGYDtrvgergIKLSGGQRQRIAIARALLID 496
Cdd:PRK11124 92 NLWPHlTVQQNLieapcrvlGLSKDQALARAEKLLERLR-----LKPYADRFP-------LHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 497 PRVLIMDDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEA 562
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDASC 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
361-569 |
8.09e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 361 VSFVVEPGATIALVGSTGSGKTS----VVNLVPRfydvTGGAVLLDDHDVRDLTL-ASLRGRIGVVMQDSVLFSG-TIAE 434
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 435 NIAYG---KPDATPDAIAAAAQAAQADTFIEQLSDGYdtrvgerGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDA 511
Cdd:PRK10895 98 NLMAVlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 512 ETESALRASLDRLI-GGRTTFI----VAQRLSTVKRAdeiLVIEDGAVVARGTHEALLAESCV 569
Cdd:PRK10895 171 ISVIDIKRIIEHLRdSGLGVLItdhnVRETLAVCERA---YIVSQGHLIAHGTPTEILQDEHV 230
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
42-308 |
9.00e-11 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350006 [Multi-domain] Cd Length: 289 Bit Score: 63.03 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 42 PQILRRIIDQgITAGRrevitsGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAI----FERLQTLSFSYHDRIQ 117
Cdd:cd18562 19 PVLFGRVVDA-LSSGG------DAFPLLALWAALGLFSILAGVLVALLADRLAHRRRLAVmasyFEHVITLPLSFHSQRG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 118 TGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLA--LVALVAIPLTILVLVrfVSKLGPMFRGFQQ 195
Cdd:cd18562 92 SGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLAllLVVLAAVYAALNRLV--MRRTKAGQAAVEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 196 RLSALNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFPLLFSVGNLGVALVVWAGAVQVAHGR 275
Cdd:cd18562 170 HHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRLLAAQYPVLNWWALASVLTRAASTLTMVAIFALGAWLVQRGE 249
|
250 260 270
....*....|....*....|....*....|....
gi 1309179971 276 LTVGELVAFTSYLMLLLQPL-FVLGFGAQTIARA 308
Cdd:cd18562 250 LTVGEIVSFVGFATLLIGRLdQLSGFINRLFMQA 283
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-510 |
1.20e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTG-----GAVLLDDHDV--RDLTLAS 413
Cdd:PRK14267 5 IETVNLRVYY--GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 LRGRIGVVMQDSVLFSG-TIAENIAYG-------KPDATPDAIAAAAQAAQAdtfieqLSDGYDTRVGERGIKLSGGQRQ 485
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNVAIGvklnglvKSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQ 156
|
170 180
....*....|....*....|....*
gi 1309179971 486 RIAIARALLIDPRVLIMDDSTSSVD 510
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANID 181
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
358-558 |
1.27e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 61.39 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLA-----SLRGRigvvmqDSVLFSGTI 432
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGggfnpELTGR------ENIYLNGRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 433 aeniaYGKPDATPDAIAAaaqaaqadtFIEQLS---DGYDTRVGErgikLSGGQRQRIAIARALLIDPRVLIMDDSTSSV 509
Cdd:cd03220 112 -----LGLSRKEIDEKID---------EIIEFSelgDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 510 DAET-ESALRASLDRLIGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:cd03220 174 DAAFqEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
342-556 |
2.10e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVT--GGAVLLDD-----HDVRDltlaSL 414
Cdd:PRK13549 7 EMKNITKTFGGVKA--LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGeelqaSNIRD----TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 415 RGRIGVVMQDSVLFSG-TIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYD--TRVGErgikLSGGQRQRIAIAR 491
Cdd:PRK13549 81 RAGIAIIHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGN----LGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 492 ALLIDPRVLIMDDSTSSV-DAETESALRASLDRLIGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVA 556
Cdd:PRK13549 157 ALNKQARLLILDEPTASLtESETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGRHIG 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
349-549 |
2.43e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.94 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 349 RYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDvrdltlaslrgRIGVVMQDSVL- 427
Cdd:NF040873 1 GYGGRPV--LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 428 --FSGTIAENIAYGK-PDATPDAIAAAAQAAQADTFIE--QLSDGYDTRVGErgikLSGGQRQRIAIARALLIDPRVLIM 502
Cdd:NF040873 68 dsLPLTVRDLVAMGRwARRGLWRRLTRDDRAAVDDALErvGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1309179971 503 DDSTSSVDAETESALRASLDRLIG-GRTTFIVAQRLSTVKRADEILVI 549
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
306-510 |
2.44e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 306 ARAGASASRLFEVLDAETDVPERPGAIELTNARGR--VEFRDVHLRYP---------GSDAETLNGVSFVVEPGATIALV 374
Cdd:PRK10261 277 AMKGLDYPRRFPLISLEHPAKQEPPIEQDTVVDGEpiLQVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 375 GSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLRGRIGVVMQDsvlfsgtiaeniaygkPDATPDAIAAA 451
Cdd:PRK10261 357 GESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQD----------------PYASLDPRQTV 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 452 AQAAQADTFIEQLSDGYDT---------RVGERGI-------KLSGGQRQRIAIARALLIDPRVLIMDDSTSSVD 510
Cdd:PRK10261 421 GDSIMEPLRVHGLLPGKAAaarvawlleRVGLLPEhawryphEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
119-315 |
3.80e-10 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 61.34 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 119 GQLITRLTSDvDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLvRFVSKlgpmfrgfqqRLS 198
Cdd:cd18569 99 GDIASRVQSN-DRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVL-RLVSR----------KRV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 199 ALNSILQEN--------VAGIRV---VKAFAREPFEAARYRA--ANESLLQQGLTVRRTVANAFPLLFSvgNLGVALVVW 265
Cdd:cd18569 167 DLNRRLLQDsgkltgttMSGLQMietLKASGAESDFFSRWAGyqAKVLNAQQELGRTNQLLGALPTLLS--ALTNAAILG 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 266 AGAVQVAHGRLTVGELVAFTSYLMLLLQPLFVL-GFGaQTIARAGASASRL 315
Cdd:cd18569 245 LGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLvGLG-GTLQEMRGDMERL 294
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
372-568 |
4.11e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.11 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 372 ALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVrDLTLASLRGRIGVVMQDSVLFSG-TIAENIAY-----GKpdaTP 445
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFyaqlkGR---SW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 446 DAIAAAAQAAQADTfieqlsdGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLI 525
Cdd:TIGR01257 1036 EEAQLEMEAMLEDT-------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR 1108
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1309179971 526 GGRTTFIVAQRLSTVK-RADEILVIEDGAVVARGTheALLAESC 568
Cdd:TIGR01257 1109 SGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT--PLFLKNC 1150
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
358-513 |
4.12e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVN-LVPRfydVTGGAVLLDDHDV----RDltlASLRGRIGVVMQDSV-LFSGT 431
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNvLAER---VTTGVITGGDRLVngrpLD---SSFQRSIGYVQQQDLhLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 432 IAENIAYGKPDATPDAIAAAAQAAQADTFIE--QLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLI-MDDSTSS 508
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSKSEKMEYVEEVIKllEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
....*
gi 1309179971 509 VDAET 513
Cdd:TIGR00956 933 LDSQT 937
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
326-566 |
5.63e-10 |
|
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: 62.13 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 326 PERPGAIELTNARGRVefRDVHLRYPGSD---AETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGA--VL 400
Cdd:TIGR03269 267 VEKECEVEVGEPIIKV--RNVSKRYISVDrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 401 LDDHDVrDLTL--ASLRGR----IGVVMQDSVLFS-----GTIAENIAYGKPD--ATPDAIAAAAQAAQADTFIEQLSDG 467
Cdd:TIGR03269 345 VGDEWV-DMTKpgPDGRGRakryIGILHQEYDLYPhrtvlDNLTEAIGLELPDelARMKAVITLKMVGFDEEKAEEILDK 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 468 YDTrvgergiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASL--DRLIGGRTTFIVAQRLSTVKR-AD 544
Cdd:TIGR03269 424 YPD-------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCD 496
|
250 260
....*....|....*....|..
gi 1309179971 545 EILVIEDGAVVARGTHEALLAE 566
Cdd:TIGR03269 497 RAALMRDGKIVKIGDPEEIVEE 518
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-559 |
6.02e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.51 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTlaslRGRIGV 420
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 V---------MqdsvlfsgTIAENIAY-------GKPDATPDaiaaaaqaaqADTFIE--QLSDGYDTRVGErgikLSGG 482
Cdd:COG4152 76 LpeerglypkM--------KVGEQLVYlarlkglSKAEAKRR----------ADEWLErlGLGDRANKKVEE----LSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 483 QRQRIAIARALLIDPRVLIMDDSTS---SVDAET-ESALRASLDRligGRTTFIVAQRLSTVKR-ADEILVIEDGAVVAR 557
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSgldPVNVELlKDVIRELAAK---GTTVIFSSHQMELVEElCDRIVIINKGRKVLS 210
|
..
gi 1309179971 558 GT 559
Cdd:COG4152 211 GS 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
358-532 |
6.77e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 59.37 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDdHDVRDLTLASL---------RGRIGVVMQ----- 423
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLAQAspreilalrRRTIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 424 ------DSV---LFSGTIAENIAYGKpdatpdaiaaaaqaaqADTFIEQLsdgydtRVGERGIKL-----SGGQRQRIAI 489
Cdd:COG4778 106 prvsalDVVaepLLERGVDREEARAR----------------ARELLARL------NLPERLWDLppatfSGGEQQRVNI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1309179971 490 ARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFI 532
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
358-554 |
8.24e-10 |
|
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: 58.21 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGR-IGVV----MQDSVLFSGTI 432
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 433 AENIAygkpdatpdaiaaaaqaaqadtfIEQLsdgydtrvgergikLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAE 512
Cdd:cd03215 96 AENIA-----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1309179971 513 TESALRASLDRLI-GGRTTFIVAQRLSTVKR-ADEILVIEDGAV 554
Cdd:cd03215 139 AKAEIYRLIRELAdAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
341-559 |
9.09e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.32 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDAET--------------------LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVl 400
Cdd:COG1134 5 IEVENVSKSYRLYHEPSrslkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 401 lddhdvrdltlaSLRGRI------GVVMQDSvlFSGtiAENI-----AYGKPDATPDAIAAaaqaaqadtFIE---QLSD 466
Cdd:COG1134 84 ------------EVNGRVsallelGAGFHPE--LTG--RENIylngrLLGLSRKEIDEKFD---------EIVefaELGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 467 GYDTRVGergiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAE-TESALRASLDRLIGGRTTFIVAQRLSTVKR-AD 544
Cdd:COG1134 139 FIDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCD 214
|
250
....*....|....*
gi 1309179971 545 EILVIEDGAVVARGT 559
Cdd:COG1134 215 RAIWLEKGRLVMDGD 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
346-565 |
1.14e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.87 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 346 VHLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKT----SVVNLVPRFYDV-TGGAVLLDDHDVRDLTLASLRG---- 416
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQTLRGvrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 417 RIGVVMQD---SVLFSGTIAENIAygkpdatpdAIAAAAQAAQADTFIEQLSDGYDtRVGERGIK---------LSGGQR 484
Cdd:PRK15134 93 KIAMIFQEpmvSLNPLHTLEKQLY---------EVLSLHRGMRREAARGEILNCLD-RVGIRQAAkrltdyphqLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 485 QRIAIARALLIDPRVLIMDDSTSSVDAETES---ALRASLDRLIGGRTTFIvAQRLSTVKR-ADEILVIEDGAVVARGTH 560
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAqilQLLRELQQELNMGLLFI-THNLSIVRKlADRVAVMQNGRCVEQNRA 241
|
....*
gi 1309179971 561 EALLA 565
Cdd:PRK15134 242 ATLFS 246
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
305-555 |
1.22e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 305 IARAGASASR---------LFEVLDAEtDVPERPGAIEL----TNARGR--VEFRDVHLRYPgsDAETLNGVSFVVEPGA 369
Cdd:COG0488 266 IRRFRAKARKakqaqsrikALEKLERE-EPPRRDKTVEIrfppPERLGKkvLELEGLSKSYG--DKTLLDDLSLRIDRGD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 370 TIALVGSTGSGKTSVVNLVprfydvtGGAVLLDDHDVRdltlaslRG---RIGVVMQDSVLFSG--TIAENIAYGKPDAT 444
Cdd:COG0488 343 RIGLIGPNGAGKSTLLKLL-------AGELEPDSGTVK-------LGetvKIGYFDQHQEELDPdkTVLDELRDGAPGGT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 445 pdaiaaaaqaaqaDTFIEQL-------SDGYDTRVGergiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAET---- 513
Cdd:COG0488 409 -------------EQEVRGYlgrflfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETleal 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1309179971 514 ESALRA--------SLDRliggrtTFIvaQRLstvkrADEILVIEDGAVV 555
Cdd:COG0488 472 EEALDDfpgtvllvSHDR------YFL--DRV-----ATRILEFEDGGVR 508
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
341-552 |
1.72e-09 |
|
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: 56.30 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGSDaeTLNGVSFVVEPGATIALVGSTGSGKTSVVNLVprfydvtggavllddhdvrdltlaslrgrigv 420
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 421 vMQDSVLFSGTI----AENIAYgkpdatpdaiaaaaqaaqadtfIEQLSdgydtrvgergiklsGGQRQRIAIARALLID 496
Cdd:cd03221 47 -AGELEPDEGIVtwgsTVKIGY----------------------FEQLS---------------GGEKMRLALAKLLLEN 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 497 PRVLIMDDSTSSVDAETESALRASLDRLIGgrtTFIVA----QRLSTVkrADEILVIEDG 552
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVshdrYFLDQV--ATKIIELEDG 143
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
341-558 |
2.68e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYPGsdAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT--LASLRGrI 418
Cdd:PRK15439 12 LCARSISKQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpaKAHQLG-I 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 419 GVVMQDSVLFSG-TIAENIAYGKPdATPDAIAAAAQaaqadtFIEQLSDGYDTRVgeRGIKLSGGQRQRIAIARALLIDP 497
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGLP-KRQASMQKMKQ------LLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 498 RVLIMDDSTSSVD-AETE---SALRASLDRLIGgrtTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:PRK15439 160 RILILDEPTASLTpAETErlfSRIRELLAQGVG---IVFISHKLPEIRQlADRISVMRDGTIALSG 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
350-515 |
4.55e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 350 YPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVR-DLTLASLRGRIGVVMQDSVLF 428
Cdd:PRK10762 14 FPGVKA--LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 429 SG-TIAENIAYGKPDATP-DAIAAAAQAAQADTFIEQLSDGY--DTRVGErgikLSGGQRQRIAIARALLIDPRVLIMDD 504
Cdd:PRK10762 92 PQlTIAENIFLGREFVNRfGRIDWKKMYAEADKLLARLNLRFssDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170
....*....|..
gi 1309179971 505 STSSV-DAETES 515
Cdd:PRK10762 168 PTDALtDTETES 179
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
360-565 |
5.38e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.40 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 360 GVSFVVEPGATIALVGSTGSGKT----SVVNLVPRFYDVTGGAVLLDDhdvRDLTLASLRGR-IGVVMQDS--------V 426
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG---KPVAPCALRGRkIATIMQNPrsafnplhT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 427 LFSGTIAENIAYGKPDAtpdaiaaaaqaaqADTFIEQLSD---GYDTRVGER-GIKLSGGQRQRIAIARALLIDPRVLIM 502
Cdd:PRK10418 98 MHTHARETCLALGKPAD-------------DATLTAALEAvglENAARVLKLyPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 503 DDSTSSVDAETESALRASLDRLIGGRT--TFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
360-517 |
5.56e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.42 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 360 GVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGvvMQDSVLFSGTIAENIA-- 437
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAENLEfw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 438 ---YGKPDATPDAIAAAAqaaqadtfieQLSDGYDTRVGErgikLSGGQRQRIAIARaLLIDPR-VLIMDDSTSSVDAET 513
Cdd:PRK13539 98 aafLGGEELDIAAALEAV----------GLAPLAHLPFGY----LSAGQKRRVALAR-LLVSNRpIWILDEPTAALDAAA 162
|
....
gi 1309179971 514 ESAL 517
Cdd:PRK13539 163 VALF 166
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
70-299 |
5.64e-09 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 57.64 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 70 GVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLIT---RLTSDVdlvrdfvgGGLVQAIAA 146
Cdd:cd18581 54 GGSGSVGLLSNLRSFLWIPVQQFTTREISVKLFAHLHSLSLRWHLSRKTGEVLRvmdRGTSSI--------NSLLSYVLF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 147 AI------MLVGAVVLLLAMNWQLALVALVA----IPLTILVlvrfvsklgPMFRG-FQQRLSALnsilqENVAGIR--- 212
Cdd:cd18581 126 NIgptiadIIIAIIYFAIAFNPWFGLIVFVTmalyLILTIII---------TEWRTkFRREMNKL-----DNEKRAKavd 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 213 ------VVKAFAREPFEAARYRAA------NESLLQQGLTVRRTVANafpLLFSVGNLGVALVVwagAVQVAHGRLTVGE 280
Cdd:cd18581 192 sllnfeTVKYYNAERFEVERYRRAiddyqvAEWKSNASLNLLNTAQN---LIITIGLLAGSLLC---AYFVVEGKLTVGD 265
|
250
....*....|....*....
gi 1309179971 281 LVAFTSYLMLLLQPLFVLG 299
Cdd:cd18581 266 FVLFLTYIIQLYAPLNFFG 284
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
358-555 |
6.25e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.39 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLA---SLRGRIGVVMQDSVlfsGTIAE 434
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDSI---SAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 435 NIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDTRVG---ERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDA 511
Cdd:PRK10419 105 RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSvldKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1309179971 512 ETESALRASLDRLI--GGRTTFIVAQRLSTVKR-ADEILVIEDGAVV 555
Cdd:PRK10419 185 VLQAGVIRLLKKLQqqFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
360-558 |
8.64e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.86 E-value: 8.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 360 GVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASL---------RGRIGVVMQD------ 424
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHprdglr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 425 -SVLFSGTIAENIA------YGKPDATpdaiaaaaqaaqADTFIEQLSDGYDtRVGERGIKLSGGQRQRIAIARALLIDP 497
Cdd:PRK11701 104 mQVSAGGNIGERLMavgarhYGDIRAT------------AGDWLERVEIDAA-RIDDLPTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 498 RVLIMDDSTSSVDAETESALrasLDRLIG-----GRTTFIVAQRLStVKR--ADEILVIEDGAVVARG 558
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQARL---LDLLRGlvrelGLAVVIVTHDLA-VARllAHRLLVMKQGRVVESG 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
356-513 |
1.97e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.79 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 356 ETLNGVSFVVEPGATIALVGSTGSGKTSVV----------NLVPRFYDVTGGAVLLDDHDVRDLTLAslRGRIGVVMQDS 425
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdKSAGSHIELLGRTVQREGRLARDIRKS--RANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 426 VLFSG-TIAENIAYGKPDATPDAIAAAAQAAQADtfiEQLSDGYDTRVG------ERGIKLSGGQRQRIAIARALLIDPR 498
Cdd:PRK09984 96 NLVNRlSVLENVLIGALGSTPFWRTCFSWFTREQ---KQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170
....*....|....*
gi 1309179971 499 VLIMDDSTSSVDAET 513
Cdd:PRK09984 173 VILADEPIASLDPES 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
328-558 |
1.98e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 55.42 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 328 RPGAIELTNARGRVEFRDVhlrypgsdaETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVR 407
Cdd:cd03267 16 EPGLIGSLKSLFKRKYREV---------EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 408 DLTLASLRgRIGVVM------------QDSVLFSGTIaeniaYGKPDAtpdaiaaaAQAAQADTFIE--QLSDGYDTRVg 473
Cdd:cd03267 87 KRRKKFLR-RIGVVFgqktqlwwdlpvIDSFYLLAAI-----YDLPPA--------RFKKRLDELSEllDLEELLDTPV- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 474 eRgiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIGGRTTFIVaqrLST------VKRADEIL 547
Cdd:cd03267 152 -R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVL---LTShymkdiEALARRVL 225
|
250
....*....|.
gi 1309179971 548 VIEDGAVVARG 558
Cdd:cd03267 226 VIDKGRLLYDG 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
354-582 |
2.09e-08 |
|
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: 56.76 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 354 DAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFY-------DVTGGAVLLDDHDVRDltlaSLRGRIGVVMQDSV 426
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgEIYWSGSPLKASNIRD----TERAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 427 LFSG-TIAENIAYGKPDATP-DAIAAAAQAAQADTFIEQLS--DGYDTR-VGERGiklsGGQRQRIAIARALLIDPRVLI 501
Cdd:TIGR02633 89 LVPElSVAENIFLGNEITLPgGRMAYNAMYLRAKNLLRELQldADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 502 MDDSTSSV-DAETESALRASLDRLIGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALLAESCVyaeiaaSQLV 579
Cdd:TIGR02633 165 LDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSEDDII------TMMV 238
|
...
gi 1309179971 580 GGE 582
Cdd:TIGR02633 239 GRE 241
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
101-283 |
4.58e-08 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 54.75 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 101 IFERLQTLSFSyHDRIQTGQLITRLtSDVDLVRDFVGGGlvqAIAAAIMLVGAVVLLLAM---NWQLALVALVAIPLTIL 177
Cdd:cd18587 81 LFERVLGLRLE-ARPASVGSFANNL-REFESVRDFFTSA---TLTALIDLPFVLLFLAVIaliGGPLALVPLVAIPLVLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 178 V-------LVRFVSKlgpMFRGFQQRlsalNSILQENVAGIRVVKAFAREPFEAARYRAANESLLQQGLTVRRTVANAFP 250
Cdd:cd18587 156 YglllqkpLRRLVEE---SMRESAQK----NALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATN 228
|
170 180 190
....*....|....*....|....*....|...
gi 1309179971 251 LLFSVGNLGVALVVWAGAVQVAHGRLTVGELVA 283
Cdd:cd18587 229 FAQFVQQLVTVAIVIVGVYLISDGELTMGGLIA 261
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
341-559 |
1.10e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 53.16 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDV-----RDL--TLAS 413
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsRELakRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 LRGRIGVVM----QDSVLF-----SGT---------IAENIAYGKpdatpdaiaaaaqaaqadtfIEQLSDGY-DTrvge 474
Cdd:COG4604 80 LRQENHINSrltvRELVAFgrfpySKGrltaedreiIDEAIAYLD--------------------LEDLADRYlDE---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 475 rgikLSGGQRQRIAIARALLIDPRVLIMDDSTSSVD----AETESALRASLDRLigGRTTFIV------AQRLstvkrAD 544
Cdd:COG4604 136 ----LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADEL--GKTVVIVlhdinfASCY-----AD 204
|
250
....*....|....*
gi 1309179971 545 EILVIEDGAVVARGT 559
Cdd:COG4604 205 HIVAMKDGRVVAQGT 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
315-541 |
1.48e-07 |
|
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: 54.37 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 315 LFEVLDA-------ETDVPERPGAIE------LTNARGRVEFRDVHLRYPGSDAETLNG------VSFVVEPGATIALVG 375
Cdd:TIGR00954 406 LLQVLDDvksgnfkRPRVEEIESGREggrnsnLVPGRGIVEYQDNGIKFENIPLVTPNGdvliesLSFEVPSGNNLLICG 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 376 STGSGKTSVVNLVPRFYDVTGGAvllddhdvrdLTLASlRGRIGVVMQDSVLFSGTIAENIAYgkpdatPDAIAAAAQAA 455
Cdd:TIGR00954 486 PNGCGKSSLFRILGELWPVYGGR----------LTKPA-KGKLFYVPQRPYMTLGTLRDQIIY------PDSSEDMKRRG 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 456 QADTFIEQLSDGYD-TRVGERGIK----------LSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRL 524
Cdd:TIGR00954 549 LSDKDLEQILDNVQlTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF 628
|
250
....*....|....*..
gi 1309179971 525 igGRTTFIVAQRLSTVK 541
Cdd:TIGR00954 629 --GITLFSVSHRKSLWK 643
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
353-510 |
1.69e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.87 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 353 SDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRdltLASLRGRI--GVVM------QD 424
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR---IRSPRDAIraGIAYvpedrkGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 425 SVLFSGTIAENIAYGKPDATPDAIA--AAAQAAQADTFIEQLS---DGYDTRVGErgikLSGGQRQRIAIARALLIDPRV 499
Cdd:COG1129 340 GLVLDLSIRENITLASLDRLSRGGLldRRRERALAEEYIKRLRiktPSPEQPVGN----LSGGNQQKVVLAKWLATDPKV 415
|
170
....*....|.
gi 1309179971 500 LIMDDSTSSVD 510
Cdd:COG1129 416 LILDEPTRGID 426
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
96-316 |
2.40e-07 |
|
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: 52.48 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 96 DMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLT 175
Cdd:cd18585 69 NLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 176 ILVLVRFVSKLGpmfRGFQQRL----SALNSILQENVAGIRVVKAFAREPFEAARYRAANESLL--QQGLTVRRTVANAF 249
Cdd:cd18585 149 GVVIPLLFYRLG---KKIGQQLvqlrAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIkeQRRLARLSGLSQAL 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179971 250 PLLFSvgNLGVALVVWAGAVQVAHGRLTvGELVAF------TSYLMLLLQPLFVLGFGaQTIaragASASRLF 316
Cdd:cd18585 226 MILLS--GLTVWLVLWLGAPLVQNGALD-GALLAMlvfavlASFEAVAPLPLAFQYLG-ETR----AAARRLF 290
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
341-563 |
2.43e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.46 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 341 VEFRDVHLRYpgSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLT---LASLRGR 417
Cdd:PRK11831 8 VDMRGVSFTR--GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 418 IGVVMQDSVLFSG-TIAENIAYGKPDATpdaiaAAAQAAQADTFIEQLSdgydtRVGERGI------KLSGGQRQRIAIA 490
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAYPLREHT-----QLPAPLLHSTVMMKLE-----AVGLRGAaklmpsELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179971 491 RALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG--GRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEAL 563
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
358-555 |
3.38e-07 |
|
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: 51.11 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTS----VVNLVPRFYDVTGgAVLLDDHDVrDLTLASLRGRIGVVMQDSVLFSG-TI 432
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVEG-DIHYNGIPY-KEFAEKYPGEIIYVSEEDVHFPTlTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 433 AENIAYgkpdatpdaiaaaAQAAQADTFIeqlsdgydtrvgeRGIklSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAE 512
Cdd:cd03233 101 RETLDF-------------ALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1309179971 513 TE----SALRASLDRLigGRTTFIVAQRLS--TVKRADEILVIEDGAVV 555
Cdd:cd03233 153 TAleilKCIRTMADVL--KTTTFVSLYQASdeIYDLFDKVLVLYEGRQI 199
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
340-504 |
4.93e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 340 RVEFRDVHLRYPGSDAEtLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIG 419
Cdd:PRK10522 322 TLELRNVTFAYQDNGFS-VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 VVMQDSVLFSGTIaeniaygKPDATPdaiaaaAQAAQADTFIEQLSDGYDTRVGE---RGIKLSGGQRQRIAIARALLID 496
Cdd:PRK10522 401 AVFTDFHLFDQLL-------GPEGKP------ANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEE 467
|
....*...
gi 1309179971 497 PRVLIMDD 504
Cdd:PRK10522 468 RDILLLDE 475
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
342-555 |
5.11e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 342 EFRDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDvTG---GAVLLDD-----HDVRDltlaS 413
Cdd:NF040905 3 EMRGITKTFPGVKA--LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGevcrfKDIRD----S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 LRGRIGVVMQDSVLFSG-TIAENIAYGKPDATPDAIAAAAQAAQADTFIEQ--LSDGYDTRVGERGIklsgGQRQRIAIA 490
Cdd:NF040905 76 EALGIVIIHQELALIPYlSIAENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGV----GKQQLVEIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 491 RALLIDPRVLIMDDSTSSVDaETESAlrASLDRLIG----GRTTFIVAQRLSTVKR-ADEILVIEDGAVV 555
Cdd:NF040905 152 KALSKDVKLLILDEPTAALN-EEDSA--ALLDLLLElkaqGITSIIISHKLNEIRRvADSITVLRDGRTI 218
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
118-315 |
6.66e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 51.34 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 118 TGQLITRLTSDVDLVRDFVGGgLVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTiLVLVRFVSKlgpMFRGFQQ-- 195
Cdd:cd18596 114 VGKINNLMSVDANRISEFAAF-LHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLL-LPLNGYLAK---RYSRAQKel 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 196 ------RLSALNSILQenvaGIRVVKAFAREPFEAARYRAANESLLQQgLTVRRTVANAFPLLFSVGNLGVALVVWAGAV 269
Cdd:cd18596 189 mkardaRVQLVTEVLQ----GIRMIKFFAWERKWEERILEAREEELKW-LRKRFLLDLLLSLLWFLIPILVTVVTFATYT 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1309179971 270 QVAHGRLTVGelVAFTS--YLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18596 264 LVMGQELTAS--VAFTSlaLFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
358-565 |
6.69e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVN-----LVPrfydvTGGAVLLDDHD-VRDLTlaSLRGRIGVVM--------- 422
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgiLVP-----TSGEVRVLGYVpFKRRK--EFARRIGVVFgqrsqlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 423 ---QDSVLFSGTIaeniaYGKPDAtpdaiaaaAQAAQADTFIE--QLSDGYDTRVgeRgiKLSGGQRQRIAIARALLIDP 497
Cdd:COG4586 111 lpaIDSFRLLKAI-----YRIPDA--------EYKKRLDELVEllDLGELLDTPV--R--QLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 498 RVLIMDDSTSSVDAETESALRASLDRLIGGR-TTFIvaqrLST-----VKR-ADEILVIEDGAVVARGTHEALLA 565
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTIL----LTShdmddIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
62-186 |
8.15e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. 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). 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: 350054 [Multi-domain] Cd Length: 290 Bit Score: 51.00 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 62 TSGALLLIGVAAAGGVAQFLQGFLSAKASHGAAYD----MREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVG 137
Cdd:cd18781 33 TASLLIVLGILAIAIIVRFICTRLASRASYRASADvkktLREKIYDKLLRLGPSYQEKVSTAEVVQLSVEGVEQLEIYFG 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 138 GGLVQ---AIAAAIMLvgaVVLLLAMNWQLALVALVA---IPLTILVLVRFVSKL 186
Cdd:cd18781 113 RYLPQffySMLAPLTL---FVVLAPINWKAALVLLICvplIPISIIAVQKIAKKL 164
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
361-552 |
9.42e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 361 VSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASlRGRIGVVM-----QDSVLF-SGTIAE 434
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVYlpedrQSSGLYlDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 435 NI---AYGKPdatpdaiaaaaqaaqadTFIEQlsDGYDTRVGER-----GIK----------LSGGQRQRIAIARALLID 496
Cdd:PRK15439 361 NVcalTHNRR-----------------GFWIK--PARENAVLERyrralNIKfnhaeqaartLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 497 PRVLIMDDSTSSVDAetesALRASLDRLI------GGRTTFIVAQRLSTVKRADEILVIEDG 552
Cdd:PRK15439 422 PQLLIVDEPTRGVDV----SARNDIYQLIrsiaaqNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
361-567 |
9.86e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.32 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 361 VSFVVEPGATIALVGSTGSGKTSvvnLVPRFYDVT--GGAVLLDDHDVRDLTLASL-RGRIGVVMQDSVLFSGTIAENIA 437
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLLpgSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 438 YGKPDATPDAIAAAAQAAQADTFieQLSDGYDTRVGErgikLSGGQRQRIAIARALL-IDP------RVLIMDDSTSSVD 510
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVAEAL--GLDDKLGRSVNQ----LSGGEWQRVRLAAVVLqVWPdinpagQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 511 AETESALRASLDRLIG-GRTTFIVAQRLS-TVKRADEILVIEDGAVVARGTHEALLAES 567
Cdd:PRK03695 166 VAQQAALDRLLSELCQqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
355-558 |
1.06e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.37 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 355 AETLNgVSfvVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSG-TIA 433
Cdd:PRK10253 23 AENLT-VE--IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 434 ENIAYGKPDATP------DAIAAAAQAAQADTFIEQLSD-GYDTrvgergikLSGGQRQRIAIARALLIDPRVLIMDDST 506
Cdd:PRK10253 100 ELVARGRYPHQPlftrwrKEDEEAVTKAMQATGITHLADqSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 507 SSVDAETESALRASLDRL--IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARG 558
Cdd:PRK10253 172 TWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
34-315 |
2.24e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 49.76 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIIDQGITAGRREVITS---GALLLIGVAAAggvaQFLQGFLSAKASHGAAY---DMR----EAIFE 103
Cdd:cd18597 9 ADVLQVLSPLLLKYLINFVEDAYLGGPPPSigyGIGYAIGLFLL----QLLSSLLLNHFFYRSMLtgaQVRaaltKAIYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 104 RLQTLSFSYHDRIQTGQLITRLTSDVDLVrDFVGGGLVQAIAAAIMLVGAVVLLLamnWQL---ALVALVAIPLTILVLV 180
Cdd:cd18597 85 KSLRLSGKSRHEFPNGKITNLMSTDLSRI-DFALGFFHFLWTAPIQIIIAIALLI---VNLgpsALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 181 RFVSKLGpMFRGFQ-----QRLSALNSILQenvaGIRVVKAFARE-PFEA--ARYRAANESLLQQGLTVRR---TVANAF 249
Cdd:cd18597 161 FLMKKLF-KLRKKAnkitdKRVKLTQEILQ----GIRVIKFYAWEdAFLEriTEIRKKELKYVRKLQILRSiltAVAFSL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 250 PLLFSVgnlgVALVVWAGavqvAHGRLTVGelVAFTS--YLMLLLQPLFVLGFGAQTIARAGASASRL 315
Cdd:cd18597 236 PVLASM----LSFITYYA----TGHTLDPA--NIFSSlaLFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-565 |
2.37e-06 |
|
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: 50.57 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 354 DAETLNGVSFVVEPGATIALVGSTGSGKTSVVNL----------------------------VPRFY----DVTGGAVLL 401
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVlrgmdqyeptsgriiyhvalcekcgyveRPSKVgepcPVCGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 402 DDHDVRDLT---LASLRGRIGVVMQDSVLFSG--TIAENIAYGKPDATPDAIAAAAQAAQadtFIEQLSDGYdtRVGERG 476
Cdd:TIGR03269 92 EEVDFWNLSdklRRRIRKRIAIMLQRTFALYGddTVLDNVLEALEEIGYEGKEAVGRAVD---LIEMVQLSH--RITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 477 IKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLI-GGRTTFIVAQRLSTV--KRADEILVIEDGA 553
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVieDLSDKAIWLENGE 246
|
250
....*....|..
gi 1309179971 554 VVARGTHEALLA 565
Cdd:TIGR03269 247 IKEEGTPDEVVA 258
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
322-534 |
2.42e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.80 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 322 ETDVPERPGAI-ELTNARGRVEFRDVhlrypgsdaetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPR---FYDVTGG 397
Cdd:COG2401 20 VLDLSERVAIVlEAFGVELRVVERYV-----------LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalkGTPVAGC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 398 AVLLDDHDVRDLTLAslrgrigvvmqDSVLFSGTIAENIAY----GkpdatpdaiaaaaqaaqadtfieqLSDG--YDTR 471
Cdd:COG2401 89 VDVPDNQFGREASLI-----------DAIGRKGDFKDAVELlnavG------------------------LSDAvlWLRR 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 472 VGErgikLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLI-GGRTTFIVA 534
Cdd:COG2401 134 FKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArRAGITLVVA 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
358-517 |
2.91e-06 |
|
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: 48.26 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIA 437
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 438 YGKPDATPDAiaaaaqaaqadtfIEQLSDgydtRVGERGIK------LSGGQRQRIAIARALLIDPRVLIMDDSTSSVDA 511
Cdd:cd03231 96 FWHADHSDEQ-------------VEEALA----RVGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
....*.
gi 1309179971 512 ETESAL 517
Cdd:cd03231 159 AGVARF 164
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
358-512 |
3.26e-06 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 48.12 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQDSVLFSGTIAENIA 437
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLH 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 438 YGKPDATPDAIAAAAQAAQADtfieqLSDGYDTRVGErgikLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAE 512
Cdd:TIGR01189 96 FWAAIHGGAQRTIEDALAAVG-----LTGFEDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-557 |
4.67e-06 |
|
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: 46.60 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 367 PGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDvrdltlaslrgrigvvmqdsvlfsgtiaeniaygkpdatpd 446
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 447 aiaaaaqaaqaDTFIEQLSDGYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLIG 526
Cdd:smart00382 40 -----------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180 190
....*....|....*....|....*....|....*..
gi 1309179971 527 ------GRTTFIVAQRLSTVKRADEILVIEDGAVVAR 557
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
317-556 |
5.57e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 317 EVLDAETDVPERPGAIeltnargRVEFRDVHLRyPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTG 396
Cdd:COG3845 241 EVLLRVEKAPAEPGEV-------VLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 397 GAVLLDDHDVRDLTLASLRGR-IGVVMQD-----SVLfSGTIAENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDGYDT 470
Cdd:COG3845 313 GSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrgLVP-DMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 471 RVGERGIK---LSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRaslDRLI----GGRTTFIVAQRLSTV-KR 542
Cdd:COG3845 392 RTPGPDTParsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIH---QRLLelrdAGAAVLLISEDLDEIlAL 468
|
250
....*....|....
gi 1309179971 543 ADEILVIEDGAVVA 556
Cdd:COG3845 469 SDRIAVMYEGRIVG 482
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
64-235 |
5.68e-06 |
|
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: 48.27 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 64 GALLLIGVAAAGGVAQFLQGFLSAKAShgaaydmrEAIFER-LQTL---SFSYHDRIQTGQLITRLTSDVDLVRDFVGGG 139
Cdd:cd18580 45 AALLVLASVLLVLLRWLLFVLAGLRAS--------RRLHDKlLRSVlraPMSFFDTTPSGRILNRFSKDIGLIDEELPLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 140 LVQAIAAAIMLVGAVVLLLAMNWQLALVALVAIPLTILVLVRFVS---KLgpmfrgfqQRL-----SALNSILQENVAGI 211
Cdd:cd18580 117 LLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRtsrQL--------RRLesesrSPLYSHFSETLSGL 188
|
170 180
....*....|....*....|....
gi 1309179971 212 RVVKAFAREpfeaARYRAANESLL 235
Cdd:cd18580 189 STIRAFGWQ----ERFIEENLRLL 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
358-571 |
5.91e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.05 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYD-VTGGAVLLDDHDVRDLTLA-SLRGRIGVVMQD----SVLFSGT 431
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAqAIRAGIAMVPEDrkrhGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 432 IAENIAYGKPDATpdaiaaaaqaaqadTFIEQLSDGYDTRVGERGIK---------------LSGGQRQRIAIARALLID 496
Cdd:TIGR02633 356 VGKNITLSVLKSF--------------CFKMRIDAAAELQIIGSAIQrlkvktaspflpigrLSGGNQQKAVLAKMLLTN 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 497 PRVLIMDDSTSSVDAetesALRASLDRLIG-----GRTTFIVAQRLSTV-KRADEILVIEDGAVVARGTHEALLAESCVY 570
Cdd:TIGR02633 422 PRVLILDEPTRGVDV----GAKYEIYKLINqlaqeGVAIIVVSSELAEVlGLSDRVLVIGEGKLKGDFVNHALTQEQVLA 497
|
.
gi 1309179971 571 A 571
Cdd:TIGR02633 498 A 498
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
358-555 |
7.50e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVN-LVPRfydVTGGAVlldDHDVR-------DLTLAslrgRIGVVMQDSVLFS 429
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDvLAGR---KTGGYI---EGDIRisgfpkkQETFA----RISGYCEQNDIHS 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 430 G--TIAENIAYGKPDATPDAIAAAAQAAQADTFIE--QLSDGYDTRVGERGIK-LSGGQRQRIAIARALLIDPRVLIMDD 504
Cdd:PLN03140 966 PqvTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMElvELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 505 STSSVDAETES-ALRASLDRLIGGRTTFIVAQRLS--TVKRADEILVIEDGAVV 555
Cdd:PLN03140 1046 PTSGLDARAAAiVMRTVRNTVDTGRTVVCTIHQPSidIFEAFDELLLMKRGGQV 1099
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
348-513 |
1.15e-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: 46.47 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 348 LRY----PGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVVN-LVPRFYD-VTGGAVLLDDHDVRDltlaSLRGRIGVV 421
Cdd:cd03232 9 LNYtvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAgVITGEILINGRPLDK----NFQRSTGYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 422 MQDSVLFSG-TIAENIaygkpdatpdaiaaaaqaaqadTFIEQLsdgydtrvgeRGikLSGGQRQRIAIARALLIDPRVL 500
Cdd:cd03232 85 EQQDVHSPNlTVREAL----------------------RFSALL----------RG--LSVEQRKRLTIGVELAAKPSIL 130
|
170
....*....|...
gi 1309179971 501 IMDDSTSSVDAET 513
Cdd:cd03232 131 FLDEPTSGLDSQA 143
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
464-534 |
1.24e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 1.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 464 LSDGYDTRVGE---RGIklSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETE----SALRASLDRLiggRTTFIVA 534
Cdd:TIGR00956 194 LSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAlefiRALKTSANIL---DTTPLVA 266
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
344-564 |
1.44e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.09 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 344 RDVHLRYPGSdaETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGVVMQ 423
Cdd:PRK10575 15 RNVSFRVPGR--TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 424 DSVLFSG-TIAENIAYGK----------PDATPDAIAAAAQAAQADTFIEQLSDgydtrvgergiKLSGGQRQRIAIARA 492
Cdd:PRK10575 93 QLPAAEGmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179971 493 LLIDPRVLIMDDSTSSVDAETESALRASLDRL--IGGRTTFIVAQRLSTVKR-ADEILVIEDGAVVARGTHEALL 564
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
358-561 |
1.46e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.18 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVRDLTLASLRGRIGV---------VMQDSVLF 428
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQseevdwsfpVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 429 SGTIAENIAYGKPDATpDAIAAAAQAAQADtfieqLSDGYDTRVGErgikLSGGQRQRIAIARALLIDPRVLIMDDSTSS 508
Cdd:PRK15056 103 MGRYGHMGWLRRAKKR-DRQIVTAALARVD-----MVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1309179971 509 VDAETESALRASLDRLIG-GRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHE 561
Cdd:PRK15056 173 VDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
358-524 |
2.37e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 358 LNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVllddhdVRDLTLaslrgRIGVVMQ----DSVLfsGTIA 433
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKL-----RIGYVPQklylDTTL--PLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 434 ENIAYGKPDATPDAIAAAAQAAQADTFIEQLSDgydtrvgergiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAET 513
Cdd:PRK09544 87 NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170
....*....|.
gi 1309179971 514 ESALRASLDRL 524
Cdd:PRK09544 156 QVALYDLIDQL 166
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
479-510 |
2.62e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 2.62e-05
10 20 30
....*....|....*....|....*....|..
gi 1309179971 479 LSGGQRQRIAIARALLIDPRVLIMDDSTSSVD 510
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
458-563 |
3.30e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 458 DTFIEQLSdgYDTRVGERGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLI-GGRTTFIVAQR 536
Cdd:NF000106 126 DELLERFS--LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQY 203
|
90 100
....*....|....*....|....*...
gi 1309179971 537 LSTVKR-ADEILVIEDGAVVARGTHEAL 563
Cdd:NF000106 204 MEEAEQlAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
65-292 |
8.40e-05 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 44.90 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 65 ALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGgglvqAI 144
Cdd:cd18559 41 LSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAP-----QV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 145 AAAIMLVGAVVLLLAMNWQLALVALVAIpLTILVLVRFVSKLGPMFRGFQQRL-----SALNSILQENVAGIRVVKAFAR 219
Cdd:cd18559 116 IKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNRVYAASSRQLKRLesvskDPRYKLFNETLLGISVIKAFEW 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 220 EpfeaARYRAANESLLQQGLTV-RRTVANAF--PLLFSVGNLGVALVVWAGAVQVAHGRLTVGELV----AFTSYLMLLL 292
Cdd:cd18559 195 E----EAFIRQVDAKRDNELAYlPSIVYLRAlaVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVfyslALTTYLNWPL 270
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
347-559 |
8.51e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 347 HLRYPGSDAETLNGVSFVVEPGATIALVGSTGSGKTSVV---------NLVPRFYDVTGGAVLLDD--HDVRDLTLASLR 415
Cdd:PRK13547 6 HLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLkalagdltgGGAPRGARVTGDVTLNGEplAAIDAPRLARLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 416 GRIGVVMQDSVLFSgtIAENIAYGK-PDATPDAIAAAAQAAQADTFIEQLsdGYDTRVGERGIKLSGGQRQRIAIARAL- 493
Cdd:PRK13547 86 AVLPQAAQPAFAFS--AREIVLLGRyPHARRAGALTHRDGEIAWQALALA--GATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179971 494 --------LIDPRVLIMDDSTSSVDAETESALRASLDRL-----IGGRTtfIVAQRLSTVKRADEILVIEDGAVVARGT 559
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLardwnLGVLA--IVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
350-513 |
9.24e-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: 45.31 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 350 YPGsDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRF-YDVTGGAVL--------------LDD-HDVRdltlas 413
Cdd:TIGR03719 14 VPP-KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFNGEARPqpgikvgylpqepqLDPtKTVR------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 414 lrgriGVVMQDSVLFSGTIAE----NIAYGKPDATPDAIAAAAQAAQ----------ADTFIEQLSDG-----YDTRVGe 474
Cdd:TIGR03719 87 -----ENVEEGVAEIKDALDRfneiSAKYAEPDADFDKLAAEQAELQeiidaadawdLDSQLEIAMDAlrcppWDADVT- 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1309179971 475 rgiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAET 513
Cdd:TIGR03719 161 ---KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
480-510 |
9.50e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.72 E-value: 9.50e-05
10 20 30
....*....|....*....|....*....|.
gi 1309179971 480 SGGQRQRIAIARALLIDPRVLIMDDSTSSVD 510
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
361-561 |
1.58e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 361 VSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDH----------DVRDLTLASLRGRIGVVMqdSVLFSG 430
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRGADM--AMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 431 ---------TIAENIA--------YGKPDATPDAIAAAAQAAQADTfieqlsdgyDTRVGERGIKLSGGQRQRIAIARAL 493
Cdd:PRK10261 113 pmtslnpvfTVGEQIAesirlhqgASREEAMVEAKRMLDQVRIPEA---------QTILSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179971 494 LIDPRVLIMDDSTSSVDAETES---ALRASLDRLIGGRTTFIVAQRLSTVKRADEILVIEDGAVVARGTHE 561
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAqilQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
65-295 |
1.69e-04 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 43.75 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 65 ALLLIGVAAAGGVAQFLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLItrltSDVDLVRDFVGGGLVQAI 144
Cdd:cd18586 45 TLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPLESRPSGYWQQLL----RDLDTLRNFLTGPSLFAF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 145 A-AAIMLVGAVVLLLAMNWqLALVALVAIPltILVLVRFVSklGPMFRGFQQRLSAL----NSILQENVAGIRVVKAFAR 219
Cdd:cd18586 121 FdLPWAPLFLAVIFLIHPP-LGWVALVGAP--VLVGLAWLN--HRATRKPLGEANEAqaarDALAAETLRNAETIKALGM 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 220 EPFEAARYRAANESLLQQGLTV--RRTVANAFPLLFSvgNLGVALVVWAGAVQVAHGRLTVGELVAFTSYLMLLLQPL 295
Cdd:cd18586 196 LGNLRRRWEARHAETLELQIRAsdLAGAISAIGKTLR--MALQSLILGVGAYLVIDGELTIGALIAASILSGRALAPI 271
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
34-299 |
2.11e-04 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 43.40 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 34 SSVADLIAPQILRRIID---QGITAGRREVITSGALLLIGVAA---AGGVAQFLQGFLSAKASHGAAYDMREAIFERLQT 107
Cdd:cd18556 14 SSILISISPVILAKITDlltSSSSDSYNYIVVLAALYVITISAtklLGFLSLYLQSSLRVELIISISSSYFRYLYEQPKT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 108 lSFSYHDRIQTGQLITRLTSDV-DLVRDFVGG---GLVQAIAAAimlvgaVVLLLAMNWQLALVALVAIPLTILVLVRFV 183
Cdd:cd18556 94 -FFVKENSGDITQRLNQASNDLyTLVRNLSTNilpPLLQLIIAI------VVILSSGDYFVAALFLLYAVLFVINNTIFT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 184 SKLGPMFRGFQQRLSALNSILQENVAGIRVVKAFAREPFEAARYRAA--NESLLQQG---LTVRRTVANAfplLFSVGNL 258
Cdd:cd18556 167 KKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATltNDRNSQKRywkLTFKMLILNS---LLNVILF 243
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1309179971 259 GVAlVVWAGAvQVAHGRLTVGELVAFTSYLMLLLQPLFVLG 299
Cdd:cd18556 244 GLS-FFYSLY-GVVNGQVSIGHFVLITSYILLLSTPIESLG 282
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
353-513 |
2.25e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 353 SDAETLNGVSFVVEPGATIALVGSTGSGKTSVVNlvprfydVTGGAVLLDDHDV---RDLTLASL-----RGRIGVVMqD 424
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK-------ILNGEVLLDDGRIiyeQDLIVARLqqdppRNVEGTVY-D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 425 SVlfSGTIAENIAYGKpdaTPDAIAAAAQAAQADTFIEQLS---------DGY--DTRVGERGIK-----------LSGG 482
Cdd:PRK11147 86 FV--AEGIEEQAEYLK---RYHDISHLVETDPSEKNLNELAklqeqldhhNLWqlENRINEVLAQlgldpdaalssLSGG 160
|
170 180 190
....*....|....*....|....*....|.
gi 1309179971 483 QRQRIAIARALLIDPRVLIMDDSTSSVDAET 513
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
65-220 |
2.88e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 43.23 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 65 ALLLIGVAAAGGVAQFLQGFLSAKASHgaaydmreAIFERLQ------TLSFsyHDRIQTGQLITRLTSDVDLVRDFVGG 138
Cdd:cd18604 50 ALISLLSVLLGTLRYLLFFFGSLRASR--------KLHERLLhsvlraPLRW--LDTTPVGRILNRFSKDIETIDSELAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 139 GLVQAIAAAIMLVGAVVLLLAMNWQLALVALVaipltILVLVRFVsklGPMFRGFQQRLSALNSI--------LQENVAG 210
Cdd:cd18604 120 SLSSLLESTLSLLVILIAIVVVSPAFLLPAVV-----LAALYVYI---GRLYLRASRELKRLESVarspilshFGETLAG 191
|
170
....*....|
gi 1309179971 211 IRVVKAFARE 220
Cdd:cd18604 192 LVTIRAFGAE 201
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
475-589 |
3.21e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 475 RGIKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLI-GGRTTFIVAQRLSTVKR-ADEILVIEDG 552
Cdd:PRK10938 132 RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADC 211
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1309179971 553 AVVARGTHEALLAESCVyaeiaaSQLVGGEELD---LPES 589
Cdd:PRK10938 212 TLAETGEREEILQQALV------AQLAHSEQLEgvqLPEP 245
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
477-550 |
4.03e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.40 E-value: 4.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 477 IKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRLI--GGRTTFIVAQRLSTVKR-ADEILVIE 550
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
344-556 |
4.50e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 344 RDVHLRYPGSDAetLNGVSFVVEPGATIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVR-DLTLASLRGRIGVVM 422
Cdd:PRK10982 2 SNISKSFPGVKA--LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 423 QD-SVLFSGTIAENIAYGK-PDATPDAIAAAAQAAQADTFiEQLSDGYDTRvgERGIKLSGGQRQRIAIARALLIDPRVL 500
Cdd:PRK10982 80 QElNLVLQRSVMDNMWLGRyPTKGMFVDQDKMYRDTKAIF-DELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179971 501 IMDDSTSSVDAETESALRASLDRLI--GGRTTFIVAQRLSTVKRADEILVIEDGAVVA 556
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKerGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
480-510 |
6.67e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 6.67e-04
10 20 30
....*....|....*....|....*....|.
gi 1309179971 480 SGGQRQRIAIARALLIDPRVLIMDDSTSSVD 510
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
469-513 |
6.99e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 6.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1309179971 469 DTRVGergiKLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAET 513
Cdd:PRK11819 158 DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
100-231 |
8.25e-04 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 41.85 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 100 AIFERLQTLSFSYHDRIQTGQLITRLTSDV---DLVRDFvgggLVQAIAAAIMLVGAVVLLlamnW-QLALVALVAIPLt 175
Cdd:cd18594 77 LIYKKTLKLSSSALSKITTGHIVNLLSNDVqkfDEVLVY----LHFLWIAPLQVIVLTGLL----WrEIGPSSLAGLGV- 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179971 176 ILVLVRFVSKLGPMFRGFQQRLSALNS----ILQENVAGIRVVKAFA-REPFE----------------AARYRAAN 231
Cdd:cd18594 148 LLLLLPLQAYLGKLFAKYRRKTAGLTDervkIMNEIISGMRVIKMYTwEESFAklienirkkelklirkAAYIRAFN 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
348-533 |
1.27e-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: 40.85 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 348 LRYPGSdAETLNGVSFVVEPGA-----TIALVGSTGSGKTSVVNLVPRFYDVTGGAVLLDDHDVR---DLTLASLRGRIg 419
Cdd:cd03237 1 YTYPTM-KKTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpQYIKADYEGTV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 420 vvmqDSVLFSGT-IAENIAYGKPD-ATPdaiaaaaqaaqadtfiEQLSDGYDTRVGErgikLSGGQRQRIAIARALLIDP 497
Cdd:cd03237 79 ----RDLLSSITkDFYTHPYFKTEiAKP----------------LQIEQILDREVPE----LSGGELQRVAIAACLSKDA 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 1309179971 498 RVLIMDDSTSSVDAETESALRASLDRLI--GGRTTFIV 533
Cdd:cd03237 135 DIYLLDEPSAYLDVEQRLMASKVIRRFAenNEKTAFVV 172
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
478-565 |
1.35e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 478 KLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRASLDRL--IGGRTTFIVAQRLSTV-KRADEILVIEDGAV 554
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 1309179971 555 VARGTHEALLA 565
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
69-263 |
2.11e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 40.54 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 69 IGVAAAGGVAQ----FLQGFLSAKASHGAAYDMREAIFERLQTLSFSYHDRIQTGQLITRLTSDVDLVRDFVGGGLVQAI 144
Cdd:cd18606 38 IGIYAGLGVLQaiflFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 145 AAAIMLVGAVVLLLAMnwqLALVALVAIPLTILVLV---------RFVSKLGPMFRgfqqrlSALNSILQENVAGIRVVK 215
Cdd:cd18606 118 YTLSSIIGTFILIIIY---LPWFAIALPPLLVLYYFianyyrassRELKRLESILR------SFVYANFSESLSGLSTIR 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179971 216 AFAREpfeaARYRAANESLL-------------QQGLTVR-RTVANAfpLLFSVGNLGVALV 263
Cdd:cd18606 189 AYGAQ----DRFIKKNEKLIdnmnrayfltianQRWLAIRlDLLGSL--LVLIVALLCVTRR 244
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
460-547 |
2.50e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.23 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 460 FIEQLSD------GYDTrVGERGIKLSGGQRQRIAIARALL--IDPRVLIMDDSTSSVDAETESALRASLDRLIG-GRTT 530
Cdd:cd03238 64 FIDQLQFlidvglGYLT-LGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLIDlGNTV 142
|
90
....*....|....*..
gi 1309179971 531 FIVAQRLSTVKRADEIL 547
Cdd:cd03238 143 ILIEHNLDVLSSADWII 159
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
462-522 |
9.22e-03 |
|
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: 38.76 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179971 462 EQLSDGYDT-RVGERGI---------------------KLSGGQRQRIAIARALLIDPRVLIMDDSTSSVDAETESALRA 519
Cdd:TIGR03719 405 EEISGGLDIiKLGKREIpsrayvgrfnfkgsdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEE 484
|
...
gi 1309179971 520 SLD 522
Cdd:TIGR03719 485 ALL 487
|
|
| |
