|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1-588 |
0e+00 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 1021.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 1 MSLLKIYWRAMQYLAVERTATITMCVASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVFVARGA 80
Cdd:PRK13657 1 MSLFRLYARVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGDIFPLLAAWAGFGLFNIIAGVLVARHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 81 DRLAHRRRLGVMIDSYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSL 160
Cdd:PRK13657 81 DRLAHRRRLAVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRLSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 161 VLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWA 240
Cdd:PRK13657 161 VLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 241 LASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLEEFFQMEDATADRQ 320
Cdd:PRK13657 241 LASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 321 EPENVADLNDVKGDIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTR 400
Cdd:PRK13657 321 DPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 401 TVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRL 480
Cdd:PRK13657 401 TVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 481 AIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERG 560
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARG 560
|
570 580
....*....|....*....|....*...
gi 552148158 561 GRFSDLLRAGGLKLEDKQPKQPVVEGSN 588
Cdd:PRK13657 561 GRFAALLRAQGMLQEDERRKQPAAEGAN 588
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
1-580 |
0e+00 |
|
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: 850.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 1 MSLLKIYWRAMQYLAVERTATITMCVASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVFVARGA 80
Cdd:TIGR01192 1 MSLFQVYVRALSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSDVLPTLALWAGFGVFNTIAYVLVAREA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 81 DRLAHRRRLGVMIDSYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSL 160
Cdd:TIGR01192 81 DRLAHGRRATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 161 VLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWA 240
Cdd:TIGR01192 161 VLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 241 LASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLEEFFQMEDATADRQ 320
Cdd:TIGR01192 241 LASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 321 EPENVADLNDVKGDIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTR 400
Cdd:TIGR01192 321 EPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 401 TVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRL 480
Cdd:TIGR01192 401 TVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 481 AIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERG 560
Cdd:TIGR01192 481 AIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKD 560
|
570 580
....*....|....*....|
gi 552148158 561 GRFSDLLRAGGLKLEDKQPK 580
Cdd:TIGR01192 561 GRFYKLLRRSGLLTNQPATK 580
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-569 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 530.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 2 SLLKIYWRAMQYLAVERTATITMCVASVLVALVALAEPVLFGRVIQSISDKGDiFSPLLMWAAL--------GGFNIMAA 73
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD-LSALLLLLLLllglallrALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 74 VFVARGADRLAHRRRLgvmiDSYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMT 153
Cdd:COG1132 83 YLLARLAQRVVADLRR----DLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 154 MDMRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQF 233
Cdd:COG1132 159 IDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 234 PVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLEEFFQME 313
Cdd:COG1132 239 RAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 314 DATADRQEPENVADLNDVKGDIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIM 393
Cdd:COG1132 319 DEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 394 IDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLS 473
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 474 GGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSF 553
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558
|
570
....*....|....*.
gi 552148158 554 NELAERGGRFSDLLRA 569
Cdd:COG1132 559 EELLARGGLYARLYRL 574
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
21-309 |
3.27e-162 |
|
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: 464.79 E-value: 3.27e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 21 TITMCVASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVFVARGADRLAHRRRLGVMIDSYERLI 100
Cdd:cd18562 1 ALGLALANVALAGVQFAEPVLFGRVVDALSSGGDAFPLLALWAALGLFSILAGVLVALLADRLAHRRRLAVMASYFEHVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 101 TMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLVMRKT 180
Cdd:cd18562 81 TLPLSFHSQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLALLLVVLAAVYAALNRLVMRRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 181 KDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVL 260
Cdd:cd18562 161 KAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRLLAAQYPVLNWWALASVLTRAASTLTMVAIFAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 552148158 261 GAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLEEF 309
Cdd:cd18562 241 GAWLVQRGELTVGEIVSFVGFATLLIGRLDQLSGFINRLFMQAPKLQEF 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-568 |
6.77e-128 |
|
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: 391.89 E-value: 6.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 8 WRAMQYLAVERTATITMCVASVLVALVALAEPVLFGRVIQSISDKGDIfsPLLMWAALGgfniMAAVFVARGADRLAHRR 87
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDL--STLWVLAIG----LLLALLFEGLLRLLRSY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 88 ---RLGVMIDS------YERLITMPLAWHQKRGTSnALHTLIRATDSLFTLwleFMRQHLTTVVALATLI---PVAMTMD 155
Cdd:COG2274 219 lllRLGQRIDLrlssrfFRHLLRLPLSFFESRSVG-DLASRFRDVESIREF---LTGSLLTALLDLLFVLiflIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 156 MRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNriaSETQALRDYAKNLE---NAQ 232
Cdd:COG2274 295 PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALG---AESRFRRRWENLLAkylNAR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 233 FPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLEEFFQM 312
Cdd:COG2274 372 FKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDI 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 313 EDATADRQEPENVADLNDVKGDIVFDNVTFEFPNSGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGR 391
Cdd:COG2274 452 LDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLdNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 392 IMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQ 471
Cdd:COG2274 532 ILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSN 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 472 LSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESG 551
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDG 691
|
570
....*....|....*..
gi 552148158 552 SFNELAERGGRFSDLLR 568
Cdd:COG2274 692 THEELLARKGLYAELVQ 708
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-566 |
9.02e-108 |
|
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: 336.41 E-value: 9.02e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 7 YWRAMQYLAVERTATITMCVASVLVALVALAEPVLFGRVIQSISDKGDIFS-PLLMWAALGGFNIMAAVFV-------AR 78
Cdd:COG5265 25 LLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVvPVGLLLAYGLLRLLSVLFGelrdalfAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 79 GADRLAhrRRLGVmiDSYERLITMPLAWHQKRGT----------SNALHTLIRATdsLFTLwlefmrqhlttvvaLATLI 148
Cdd:COG5265 105 VTQRAV--RRLAL--EVFRHLHALSLRFHLERQTgglsrdiergTKGIEFLLRFL--LFNI--------------LPTLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 149 PVAMTM-------DMRMSLVLIVLGVIYVMIGQLV------MRKT---KDGQAavekhHHKLFehvsDTISNVSVVQSYN 212
Cdd:COG5265 165 EIALVAgillvkyDWWFALITLVTVVLYIAFTVVVtewrtkFRREmneADSEA-----NTRAV----DSLLNYETVKYFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 213 RIASET----QALRDYaknlENAQfpVLNWWALaSGLNRMAS---TFSMVVVLVLGAYFVTKGQMRVGDVIAFIGF-VQL 284
Cdd:COG5265 236 NEAREArrydEALARY----ERAA--VKSQTSL-ALLNFGQAliiALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYlIQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 285 MI--GRLDQISAFINQtvtARAKLEEFFQMEDATADRQEPENVADLNDVKGDIVFDNVTFEFPNSGQGIYDVSFEVKPGQ 362
Cdd:COG5265 309 YIplNFLGFVYREIRQ---ALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 363 TVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVH 442
Cdd:COG5265 386 TVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 443 AAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRT 522
Cdd:COG5265 466 AAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRT 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 552148158 523 TFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDL 566
Cdd:COG5265 546 TLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
333-561 |
1.45e-101 |
|
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: 307.23 E-value: 1.45e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIA 412
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 413 TVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPI 492
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 493 LVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGG 561
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
335-566 |
1.52e-101 |
|
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: 307.62 E-value: 1.52e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIAT 413
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLrDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPIL 493
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 494 VLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDL 566
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
335-566 |
2.06e-100 |
|
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: 304.54 E-value: 2.06e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATV 414
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILV 494
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 495 LDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDL 566
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-561 |
3.06e-98 |
|
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: 310.54 E-value: 3.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 11 MQYLAVERTATITMCVASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALggfniMAAVFVAR-----GADRLAH 85
Cdd:COG4988 9 KRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGL-----LLAVLLLRallawLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 86 ----------RRRLgvmidsYERLITMPLAWHQKRGTSNALHTLIRATDSL---FTLWL-EFMrqhLTTVVALATLIPVA 151
Cdd:COG4988 84 raaarvkrrlRRRL------LEKLLALGPAWLRGKSTGELATLLTEGVEALdgyFARYLpQLF---LAALVPLLILVAVF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 152 mTMDMRMSLVLIVLG--VIYVMIgqLVMRKTKDgqaAVEKHH---HKLFEHVSDTISNVSVVQSYNRIASETQALRDYAK 226
Cdd:COG4988 155 -PLDWLSGLILLVTAplIPLFMI--LVGKGAAK---ASRRQWralARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 227 NLENAQFPVLnwwalasglnRMA--STFSM---------VVVLVLGAYFVTkgqmrvGDVIAFIGFVQLMIGR-----LD 290
Cdd:COG4988 229 DFRKRTMKVL----------RVAflSSAVLeffaslsiaLVAVYIGFRLLG------GSLTLFAALFVLLLAPefflpLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 291 QISAFINQTVTARAKLEEFFQMEDATADRQEPENVADLNDVKGDIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPT 370
Cdd:COG4988 293 DLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 371 GAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAA 450
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 451 HDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRL 530
Cdd:COG4988 453 DEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRL 532
|
570 580 590
....*....|....*....|....*....|.
gi 552148158 531 STVRSADLVLFMDKGHLVESGSFNELAERGG 561
Cdd:COG4988 533 ALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
59-568 |
7.86e-98 |
|
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: 309.39 E-value: 7.86e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 59 LLMWAALGG--FNIMAAV-----F-----VARGADRLA-HR---RRLGVM-IDSYERLITMPLAWHQKRGTSNALHTLIR 121
Cdd:COG4987 41 LIAAAALAPpiLNLFVPIvgvraFaigrtVFRYLERLVsHDatlRLLADLrVRLYRRLEPLAPAGLARLRSGDLLNRLVA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 122 ATDSLFTLWLefmRQHLTTVVALATLIpVAMTMDMRMSLVL-IVLGVIYVMIGQLV----MRKTKDGQAAVEKHHHKLFE 196
Cdd:COG4987 121 DVDALDNLYL---RVLLPLLVALLVIL-AAVAFLAFFSPALaLVLALGLLLAGLLLpllaARLGRRAGRRLAAARAALRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 197 HVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRvGDVI 276
Cdd:COG4987 197 RLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 277 AFIGFVQL----MIGRLDQISAFINQTVTARAKLeefFQMEDATADRQEPENVADLNDVkGDIVFDNVTFEFPNSGQGIY 352
Cdd:COG4987 276 ALLVLAALalfeALAPLPAAAQHLGRVRAAARRL---NELLDAPPAVTEPAEPAPAPGG-PSLELEDVSFRYPGAGRPVL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 -DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRV 431
Cdd:COG4987 352 dGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 GRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVK 511
Cdd:COG4987 432 ARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALL 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 512 QAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLR 568
Cdd:COG4987 512 ADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-566 |
1.81e-96 |
|
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: 306.26 E-value: 1.81e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 6 IYWRAMQYLAVERTATItmcVASVLVALVALAEPVLFGrVIQSISDKGDI--------FSPLLM-----WAALGGFniMA 72
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLV---LAGVAMILVAATESTLAA-LLKPLLDDGFGgrdrsvlwWVPLVViglavLRGICSF--VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 73 AVFVARGADRLAHRRRlgvmIDSYERLITMPLAWHQK--------RGTSNALHTLIRATDSLFTLwlefMRQHLTTVVAL 144
Cdd:TIGR02203 75 TYLLSWVSNKVVRDIR----VRMFEKLLGLPVSFFDRqptgtllsRITFDSEQVASAATDAFIVL----VRETLTVIGLF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 145 ATLipvaMTMDMRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQ----- 219
Cdd:TIGR02203 147 IVL----LYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRrfdav 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 220 --ALRDYAKNLENAQfpvlnwwALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFIN 297
Cdd:TIGR02203 223 snRNRRLAMKMTSAG-------SISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 298 QTVTARAKLEEFFQMEDATADRQEPENVadLNDVKGDIVFDNVTFEFPNSGQGIYD-VSFEVKPGQTVAIVGPTGAGKTT 376
Cdd:TIGR02203 296 PMQRGLAAAESLFTLLDSPPEKDTGTRA--IERARGDVEFRNVTFRYPGRDRPALDsISLVIEPGETVALVGRSGSGKST 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 377 LINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGR-ANATHEEVHAAAKAAAAHDFIL 455
Cdd:TIGR02203 374 LVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 456 AKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRS 535
Cdd:TIGR02203 454 KLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK 533
|
570 580 590
....*....|....*....|....*....|.
gi 552148158 536 ADLVLFMDKGHLVESGSFNELAERGGRFSDL 566
Cdd:TIGR02203 534 ADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
335-570 |
8.22e-96 |
|
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: 292.91 E-value: 8.22e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPN-SGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIA 412
Cdd:cd03249 1 IEFKNVSFRYPSrPDVPILkGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 413 TVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPI 492
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 493 LVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLRAG 570
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
26-568 |
3.71e-82 |
|
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: 272.00 E-value: 3.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFgrviQSISDKGDIFSPLLMWAALGGFNIMAAVF-VARGADR---LAH-RRRLGVMIDS--YER 98
Cdd:TIGR01846 146 LISLALQLFALVTPLLF----QVVIDKVLVHRGLSTLSVLALAMLAVAIFePALGGLRtylFAHlTSRIDVELGArlYRH 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 99 LITMPLAWHQKRGTSNalhTLIRATDslftlwLEFMRQHLT----TVVA--LATLIPVAMTMDMRMSLVLIVLG--VIYV 170
Cdd:TIGR01846 222 LLGLPLGYFESRRVGD---TVARVRE------LEQIRNFLTgsalTVVLdlLFVVVFLAVMFFYSPTLTGVVIGslVCYA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 171 MIGQLV---MRKTkdgqaaVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLE---NAQFPVLNWWALASG 244
Cdd:TIGR01846 293 LLSVFVgpiLRKR------VEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAayvAASFRVTNLGNIAGQ 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 245 LNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIG---RLDQISAFINQTVTARAKLEEFFQmedaTADRQE 321
Cdd:TIGR01846 367 AIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQpvlRLAQLWQDFQQTGIALERLGDILN----SPTEPR 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 322 PENVADLNDVKGDIVFDNVTFEF-PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTR 400
Cdd:TIGR01846 443 SAGLAALPELRGAITFENIRFRYaPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 401 TVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRL 480
Cdd:TIGR01846 523 IADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRI 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 481 AIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERG 560
Cdd:TIGR01846 603 AIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
....*...
gi 552148158 561 GRFSDLLR 568
Cdd:TIGR01846 683 GLYARLWQ 690
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-546 |
2.29e-78 |
|
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: 244.99 E-value: 2.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIAT 413
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLkDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQDAGLFNRSVEDNIrvgranatheevhaaakaaaahdfilaksegydtfvgergsqLSGGERQRLAIARAILKDSPIL 493
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 494 VLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGH 546
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
335-566 |
3.41e-77 |
|
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: 244.70 E-value: 3.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEF-PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIAT 413
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPIL 493
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 494 VLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDL 566
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
331-568 |
5.00e-73 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 244.54 E-value: 5.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 331 VKGDIVFDNVTFEFPNS-GQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRH 409
Cdd:PRK11176 338 AKGDIEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 410 AIATVFQDAGLFNRSVEDNIRVGRANA-THEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILK 488
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 489 DSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLR 568
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHK 577
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-542 |
9.85e-71 |
|
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: 237.18 E-value: 9.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 18 RTATITMCVASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALggfniMAAVFVARGA-----DRLAHRRRLGVM 92
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGA-----LALVLLLRALlgwlqERAAARAAAAVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 93 IDSYERLITMPLA----WHQKRGTSNALHTLIRATDSL---FTLWLEFMRqhLTTVVALATLIPVAmTMDMRMSLVLIV- 164
Cdd:TIGR02857 77 SQLRERLLEAVAAlgprWLQGRPSGELATLALEGVEALdgyFARYLPQLV--LAVIVPLAILAAVF-PQDWISGLILLLt 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 165 -LGVIYVMIgqLVMRKTkdgQAAVEKHHHKLFE---HVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWA 240
Cdd:TIGR02857 154 aPLIPIFMI--LIGWAA---QAAARKQWAALSRlsgHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 241 LASGLNRMASTFSMVVVLV-LGAYFVtkgqmrVGDVIAFIGFVQLMI-----GRLDQISAFINQTVTARAKLEEFFQMED 314
Cdd:TIGR02857 229 LSSAVLELFATLSVALVAVyIGFRLL------AGDLDLATGLFVLLLapefyLPLRQLGAQYHARADGVAAAEALFAVLD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 315 ATAdRQEPENVADLNDVKGDIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMI 394
Cdd:TIGR02857 303 AAP-RPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 395 DGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSG 474
Cdd:TIGR02857 382 NGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSG 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 475 GERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFM 542
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
330-547 |
2.23e-70 |
|
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: 226.58 E-value: 2.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 330 DVKGDIVFDNVTFEFPN--SGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSL 407
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 408 RHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAIL 487
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 488 KDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHL 547
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
152-567 |
7.10e-70 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 239.24 E-value: 7.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 152 MTMDMRMSLV-------LIVLGVIYVMIGQLVMRKTKDGQAavekhhhKLFEHVSDTISNVSVVQSYnriASETQALRDY 224
Cdd:TIGR00958 297 LWLSPRLTMVtlinlplVFLAEKVFGKRYQLLSEELQEAVA-------KANQVAEEALSGMRTVRSF---AAEEGEASRF 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 225 AKNLENAQfpVLNW-----WALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFvQLMIGR-LDQISAFINQ 298
Cdd:TIGR00958 367 KEALEETL--QLNKrkalaYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLY-QEQLGEaVRVLSYVYSG 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 299 TVTARAKLEEFFQMEDATADRQEPENVADLNdVKGDIVFDNVTFEFPN--SGQGIYDVSFEVKPGQTVAIVGPTGAGKTT 376
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPNIPLTGTLAPLN-LEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKST 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 377 LINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILA 456
Cdd:TIGR00958 523 VAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIME 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 457 KSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQavDELSHNRTTFIIAHRLSTVRSA 536
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERA 680
|
410 420 430
....*....|....*....|....*....|.
gi 552148158 537 DLVLFMDKGHLVESGSFNELAERGGRFSDLL 567
Cdd:TIGR00958 681 DQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-552 |
1.86e-62 |
|
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: 205.42 E-value: 1.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVFDNVTFEF-PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAI 411
Cdd:cd03244 1 GDIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLFNRSVednirvgRAN------ATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARA 485
Cdd:cd03244 81 SIIPQDPVLFSGTI-------RSNldpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 486 ILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGS 552
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-551 |
3.87e-62 |
|
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: 204.75 E-value: 3.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVFDNVTFEFPNSGQ-GIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAI 411
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSP 491
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESG 551
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
26-568 |
2.19e-60 |
|
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: 212.89 E-value: 2.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVF-VARGADRLahrrRLGVMIDS------YER 98
Cdd:TIGR03797 143 AMGLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFqLAQSLAVL----RLETRMDAslqaavWDR 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 99 LITMPLAWHQKRGT------------------SNALHTLIRATDSLFTLWLEFMRQHLTTVVALAtlipvamtmdmrmsL 160
Cdd:TIGR03797 219 LLRLPVSFFRQYSTgdlasramgisqirrilsGSTLTTLLSGIFALLNLGLMFYYSWKLALVAVA--------------L 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 161 VLIVLGVIYVmIGQLVMRKtkdgqaavekhHHKLFEhVSDTISNVsVVQSYN-----RIA-SETQALRDYAKNLENAQFP 234
Cdd:TIGR03797 285 ALVAIAVTLV-LGLLQVRK-----------ERRLLE-LSGKISGL-TVQLINgisklRVAgAENRAFARWAKLFSRQRKL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 235 VLNWWALASGL---NRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAF-IGFVQLMIGRLDQISAF--INQTVTARAKLEE 308
Cdd:TIGR03797 351 ELSAQRIENLLtvfNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFnTAFGSFSGAVTQLSNTLisILAVIPLWERAKP 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 309 FFQMEDATAdrqepENVADLNDVKGDIVFDNVTFEF-PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDP 387
Cdd:TIGR03797 431 ILEALPEVD-----EAKTDPGKLSGAIEVDRVTFRYrPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETP 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 388 AAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIrVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGE 467
Cdd:TIGR03797 506 ESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISE 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 468 RGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELshNRTTFIIAHRLSTVRSADLVLFMDKGHL 547
Cdd:TIGR03797 585 GGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRV 662
|
570 580
....*....|....*....|.
gi 552148158 548 VESGSFNELAERGGRFSDLLR 568
Cdd:TIGR03797 663 VQQGTYDELMAREGLFAQLAR 683
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
159-551 |
8.23e-57 |
|
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: 200.74 E-value: 8.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 159 SLVLIVLGVIyvmiGQLVMRKTkdgQAAVEKHHHKLFEHVSDTISNVSVVQS---YNRIASetQALRDYAKNLEnAQFPV 235
Cdd:COG4618 165 ALVLVALALL----NERLTRKP---LKEANEAAIRANAFAEAALRNAEVIEAmgmLPALRR--RWQRANARALA-LQARA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 236 LNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAfigfVQLMIGR----LDQISAFINQTVTARA---KLEE 308
Cdd:COG4618 235 SDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIA----ASILMGRalapIEQAIGGWKQFVSARQayrRLNE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 309 FFQMEDATADRqepenvADLNDVKGDIVFDNVTFEFPNSGQGI-YDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDP 387
Cdd:COG4618 311 LLAAVPAEPER------MPLPRPKGRLSVENLTVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 388 AAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNI-RVGRANAthEEVHAAAKAAAAHDFILAKSEGYDTFVG 466
Cdd:COG4618 385 TAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFGDADP--EKVVAAAKLAGVHEMILRLPDGYDTRIG 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 467 ERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDEL-SHNRTTFIIAHRLSTVRSADLVLFMDKG 545
Cdd:COG4618 463 EGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
....*.
gi 552148158 546 HLVESG 551
Cdd:COG4618 543 RVQAFG 548
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
261-568 |
2.08e-56 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 199.55 E-value: 2.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 261 GAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFIN---QTVTARAKLEEFFQMEDATADRQEPenvadLNDVKGDIVF 337
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNiveRGSAAYSRIRAMLAEAPVVKDGSEP-----VPEGRGELDV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 338 DNVTFEFP-NSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQ 416
Cdd:PRK10789 317 NIRQFTYPqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 417 DAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLD 496
Cdd:PRK10789 397 TPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 497 EATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLR 568
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
219-568 |
2.84e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 199.28 E-value: 2.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 219 QALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTkGQMRVGDVIAFIGFVQL-MIGRLDQIS-AF- 295
Cdd:PRK11160 224 QQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAAGGVG-GNAQPGALIALFVFAALaAFEALMPVAgAFq 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 296 -INQTVTARAKLEEffqMEDATADRQEPENvADLNDVKGDIVFDNVTFEFPNSGQG-IYDVSFEVKPGQTVAIVGPTGAG 373
Cdd:PRK11160 303 hLGQVIASARRINE---ITEQKPEVTFPTT-STAAADQVSLTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALLGRTGCG 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 374 KTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDf 453
Cdd:PRK11160 379 KSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEK- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 454 ILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTV 533
Cdd:PRK11160 458 LLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGL 537
|
330 340 350
....*....|....*....|....*....|....*
gi 552148158 534 RSADLVLFMDKGHLVESGSFNELAERGGRFSDLLR 568
Cdd:PRK11160 538 EQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
298-569 |
7.48e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 195.83 E-value: 7.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 298 QTVTARAKLEEFFQMEDATADRQEpenvADLNDVKG-DIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTT 376
Cdd:PRK11174 316 QAVGAAESLVTFLETPLAHPQQGE----KELASNDPvTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 377 LINLLQRvFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILA 456
Cdd:PRK11174 392 LLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 457 KSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSA 536
Cdd:PRK11174 471 LPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW 550
|
250 260 270
....*....|....*....|....*....|...
gi 552148158 537 DLVLFMDKGHLVESGSFNELAERGGRFSDLLRA 569
Cdd:PRK11174 551 DQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
255-569 |
3.89e-53 |
|
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: 193.03 E-value: 3.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 255 VVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARA---KLEEFFQMEDATADRQEPENVADLNdv 331
Cdd:TIGR01193 394 VVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVannRLNEVYLVDSEFINKKKRTELNNLN-- 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 332 kGDIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAI 411
Cdd:TIGR01193 472 -GDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLFNRSVEDNIRVG-RANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDS 490
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS 630
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 491 PILVLDEATSALDVETEEKVKQAVDELSHnRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLRA 569
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
60-530 |
6.43e-51 |
|
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: 183.72 E-value: 6.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 60 LMWAALG--GFNIMAAVFvaRGADRLA-HR---RRLGVM-IDSYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLE 132
Cdd:TIGR02868 52 LSVAAVAvrAFGIGRAVF--RYLERLVgHDaalRSLGALrVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 133 FMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLV-MRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSY 211
Cdd:TIGR02868 130 VIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVsLRAARAAEQALARLRGELAAQLTDALDGAAELVAS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 212 NRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMrVGDVIAFIGFVQL-MIGRLD 290
Cdd:TIGR02868 210 GALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRL-APVTLAVLVLLPLaAFEAFA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 291 QISAFINQTVTARAKLEEFFQMEDATADRQEPENVADLNDVKG--DIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVG 368
Cdd:TIGR02868 289 ALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGkpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 369 PTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAA 448
Cdd:TIGR02868 369 PSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERV 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 449 AAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAH 528
Cdd:TIGR02868 449 GLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
..
gi 552148158 529 RL 530
Cdd:TIGR02868 529 HL 530
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-547 |
9.85e-49 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 177.93 E-value: 9.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 14 LAVERTATITMCVASVLVALVALAEPV----LFGRVIQSISDKGDIFSPLLM---WAALGGFNIMAAVFVARGADRLAHR 86
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSFVINILMLAPPLymlqVYDRVLTSGSVPTLLMLTVLAlglYLFLGLLDALRSFVLVRIGEKLDGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 87 RRLGVMIDSYERLITmplawHQKRGTSNALHTLiratdslftlwlEFMRQHLTTVVALATL-IPVamtmdmrMSLVLIVL 165
Cdd:TIGR01842 81 LNQPIFAASFSATLR-----RGSGDGLQALRDL------------DQLRQFLTGPGLFAFFdAPW-------MPIYLLVC 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 166 GVIYVMIGQLVM------------------RKTKDGQAAVEKHHHklfeHVSDTISNVSVVQSYNRIASETqalrdyaKN 227
Cdd:TIGR01842 137 FLLHPWIGILALggavvlvglallnnratkKPLKEATEASIRANN----LADSALRNAEVIEAMGMMGNLT-------KR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 228 LENAQFPVLNWWALAS----GLNRMASTFSMVV---VLVLGAYFVTKGQMRVGDVIAfigfVQLMIGR----LDQISAFI 296
Cdd:TIGR01842 206 WGRFHSKYLSAQSAASdragMLSNLSKYFRIVLqslVLGLGAYLAIDGEITPGMMIA----GSILVGRalapIDGAIGGW 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 297 NQTVTARA---KLEEFFQMEDATADRQEpenvadLNDVKGDIVFDNVTFEFPNSGQGIY-DVSFEVKPGQTVAIVGPTGA 372
Cdd:TIGR01842 282 KQFSGARQaykRLNELLANYPSRDPAMP------LPEPEGHLSVENVTIVPPGGKKPTLrGISFSLQAGEALAIIGPSGS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 373 GKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHD 452
Cdd:TIGR01842 356 GKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 453 FILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDEL-SHNRTTFIIAHRLS 531
Cdd:TIGR01842 436 LILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPS 515
|
570
....*....|....*.
gi 552148158 532 TVRSADLVLFMDKGHL 547
Cdd:TIGR01842 516 LLGCVDKILVLQDGRI 531
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-552 |
2.18e-45 |
|
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: 159.50 E-value: 2.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVFDNVTFEF-PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAI 411
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLFNRSVEDNIRVgRANATHEEVHAAakaaaahdfiLAKSEGydtfvgerGSQLSGGERQRLAIARAILKDSP 491
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDP-FDEYSDEEIYGA----------LRVSEG--------GLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGS 552
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-551 |
3.37e-45 |
|
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: 157.86 E-value: 3.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYD-VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVsRRSLRHAIAT 413
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKnLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQDAGLFNRSVEDNIrvgranatheevhaaakaaaahdfilaksegydtfvgerGSQLSGGERQRLAIARAILKDSPIL 493
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 494 VLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESG 551
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
140-563 |
1.07e-44 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 167.59 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 140 TVVALATLIP---VAM-TMDMRMSLVLI-----VLGV--IYVMIGQLVMRKTKDGQAAVEKHHHklfehvsDTISNVSVV 208
Cdd:PRK10790 145 TVLRSAALIGamlVAMfSLDWRMALVAImifpaVLVVmvIYQRYSTPIVRRVRAYLADINDGFN-------EVINGMSVI 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 209 QSYNRIASETQALRDYAKNLENAQFPVLNwwaLASGLNR-MASTFSMVVV--LVLGAYFVTKGQMRVGDVIAFIGFvqlm 285
Cdd:PRK10790 218 QQFRQQARFGERMGEASRSHYMARMQTLR---LDGFLLRpLLSLFSALILcgLLMLFGFSASGTIEVGVLYAFISY---- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 286 IGRLDQ--ISAFINQTVTARAKL--EEFFQMEDATadrQEPENVADLNDVKGDIVFDNVTFEFPNSGQGIYDVSFEVKPG 361
Cdd:PRK10790 291 LGRLNEplIELTTQQSMLQQAVVagERVFELMDGP---RQQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSR 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 362 QTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRaNATHEEV 441
Cdd:PRK10790 368 GFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQV 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 442 HAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNR 521
Cdd:PRK10790 447 WQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT 526
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 552148158 522 TTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRF 563
Cdd:PRK10790 527 TLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-545 |
2.06e-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: 155.84 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIAT 413
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLrNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQDAGLFNRSVEDNIrvgranatheevhaaakaaaahdfilaksegydtfvgergsqLSGGERQRLAIARAILKDSPIL 493
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 494 VLDEATSALDVETEEKVKQAVDELS-HNRTTFIIAHRLSTVRSADLVLFMDKG 545
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
335-556 |
5.99e-43 |
|
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: 153.64 E-value: 5.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATV 414
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQ--DAGLFNRSVEDNIRVG-------------RANATHEEVHaaakaaaahdfiLAKSEGYDTFvgergsQLSGGERQR 479
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpenlglpreeireRVEEALELVG------------LEHLADRPPH------ELSGGQKQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 480 LAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTV-RSADLVLFMDKGHLVESGSFNEL 556
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
353-500 |
1.07e-42 |
|
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: 150.11 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNR-SVEDNIRV 431
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 432 GRANATHEEVHAAAKAaaahDFILAK---SEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:pfam00005 83 GLLLKGLSKREKDARA----EEALEKlglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
336-546 |
8.47e-42 |
|
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: 149.92 E-value: 8.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 336 VFDNVTFEFPNSGQ-GIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATV 414
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDA--GLFNRSVEDNIRVGRANATHEEVHaaakaaaahdfILAKSEGYDTFVGERG------SQLSGGERQRLAIARAI 486
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEE-----------IEERVEEALELVGLEGlrdrspFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 487 LKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTVRS-ADLVLFMDKGH 546
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
335-551 |
1.44e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 149.82 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRS---LRHAI 411
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGL-FNRSVEDNI----RVgrANATHEEVHAAAkaaaahDFILAKsegydtfVGERG------SQLSGGERQRL 480
Cdd:COG2884 82 GVVFQDFRLlPDRTVYENValplRV--TGKSRKEIRRRV------REVLDL-------VGLSDkakalpHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 481 AIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTVRSADL-VLFMDKGHLVESG 551
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
337-551 |
1.75e-41 |
|
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: 149.58 E-value: 1.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 337 FDNVTFEFPNSGQGIY---DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS---RRSLRHA 410
Cdd:cd03257 4 VKNLSVSFPTGGGSVKaldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IATVFQDAGL-FN--RSVEDNIRvgRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAIL 487
Cdd:cd03257 84 IQMVFQDPMSsLNprMTIGEQIA--EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 488 KDSPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESG 551
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
335-556 |
7.32e-41 |
|
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: 148.10 E-value: 7.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFD-----PAAGRIMIDGTD--TRTVSRRSL 407
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 408 RHAIATVFQDAGLFNRSVEDNIRVG-------RANATHEEVHAAAKAAAAHDFILAKSEGYDtfvgergsqLSGGERQRL 480
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 481 AIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNEL 556
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
335-556 |
1.74e-40 |
|
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: 146.96 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY---DVSFEVKPGQTVAIVGPTGAGKTTL---INLLQRvfdPAAGRIMIDGTDTRTVSRRSLR 408
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTalkDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER---PTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 409 HA---IATVFQDAGLFN-RSVEDNIrvgranATHEEVHAAAKaaaahDFILAKSEGYDTFVG--ERG----SQLSGGERQ 478
Cdd:cd03258 79 KArrrIGMIFQHFNLLSsRTVFENV------ALPLEIAGVPK-----AEIEERVLELLELVGleDKAdaypAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 479 RLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELshNR----TTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSF 553
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
...
gi 552148158 554 NEL 556
Cdd:cd03258 226 EEV 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-552 |
2.06e-40 |
|
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: 154.29 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY----DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRS---L 407
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVravdDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 408 RHAIATVFQD--AGLFNR-SVEDNI-------RVGRANATHEEVHAaakaaaahdfILAKSEGYDTFVGERGSQLSGGER 477
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRmTVGDIIaeplrlhGLLSRAERRERVAE----------LLERVGLPPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 478 QRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGS 552
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
335-562 |
2.81e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 146.93 E-value: 2.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRsLRHAIATV 414
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLFNR-SVEDNIR-VGRANATHEEVHAAAKAAAAHDFILakSEGYDTFVGErgsqLSGGERQRLAIARAILKDSPI 492
Cdd:COG4555 80 PDERGLYDRlTVRENIRyFAELYGLFDEELKKRIEELIELLGL--EEFLDRRVGE----LSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 493 LVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTV-RSADLVLFMDKGHLVESGSFNELAERGGR 562
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
335-559 |
1.27e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.82 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTvSRRSLRHAIATV 414
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLF-NRSVEDNIR-VGRANATHEEVHAAAKAAAAHDFilakseGYDTFVGERGSQLSGGERQRLAIARAILKDSPI 492
Cdd:COG1131 79 PQEPALYpDLTVRENLRfFARLYGLPRKEARERIDELLELF------GLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 493 LVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTV-RSADLVLFMDKGHLVESGSFNELAER 559
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
59-572 |
2.04e-39 |
|
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: 155.10 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 59 LLMWAALG---GFNIMAAVFVARGADRLAHRRrlgVMIDSYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMR 135
Cdd:TIGR00957 1008 LSVYGALGilqGFAVFGYSMAVSIGGIQASRV---LHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIK 1084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 136 QHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRia 215
Cdd:TIGR00957 1085 MFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEE-- 1162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 216 SETQALRDYAKNLEN--AQFP--VLNWWaLASGLNRMASTFSMVVVL--VLGAYFVTKGQmrVGDVIAFIGFVQLMIGRL 289
Cdd:TIGR00957 1163 QERFIHQSDLKVDENqkAYYPsiVANRW-LAVRLECVGNCIVLFAALfaVISRHSLSAGL--VGLSVSYSLQVTFYLNWL 1239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 290 DQISAFINQTVTARAKLEEFFQME-DATADRQE---PENVADlndvKGDIVFDNVTFEF-PNSGQGIYDVSFEVKPGQTV 364
Cdd:TIGR00957 1240 VRMSSEMETNIVAVERLKEYSETEkEAPWQIQEtapPSGWPP----RGRVEFRNYCLRYrEDLDLVLRHINVTIHGGEKV 1315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 365 AIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRvGRANATHEEVHAA 444
Cdd:TIGR00957 1316 GIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWA 1394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 445 AKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTF 524
Cdd:TIGR00957 1395 LELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVL 1474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 552148158 525 IIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLRAGGL 572
Cdd:TIGR00957 1475 TIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
335-558 |
3.94e-39 |
|
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: 143.48 E-value: 3.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSR---RSLRHAI 411
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLFNR-SVEDNIRVGRAnATHEEVHAAAKAAAAHDFILAKSE----GYDTFVGERGSQLSGGERQRLAIARAI 486
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRL-GRRSTWRSLFGLFPKEEKQRALAAlervGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 487 LKDSPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNELAE 558
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTD 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
335-552 |
8.00e-39 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 145.61 E-value: 8.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY---DVSFEVKPGQTVAIVGPTGAGKTTL---INLLQRvfdPAAGRIMIDGTDTRTVSRRSLR 408
Cdd:COG1135 2 IELENLSKTFPTKGGPVTaldDVSLTIEKGEIFGIIGYSGAGKSTLircINLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 409 HA---IATVFQDAGLFN-RSVEDNI----RVgrANATHEEvhaaakaaaahdfILAKSEGYDTFVG--ERG----SQLSG 474
Cdd:COG1135 79 AArrkIGMIFQHFNLLSsRTVAENValplEI--AGVPKAE-------------IRKRVAELLELVGlsDKAdaypSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 475 GERQRLAIARAILKDSPILVLDEATSALDVETEEKV----KQAVDELshNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVE 549
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSIldllKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 552148158 550 SGS 552
Cdd:COG1135 222 QGP 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
335-559 |
1.24e-38 |
|
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: 142.63 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY---DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAI 411
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPvlkDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLfnrSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSP 491
Cdd:COG1124 82 QMVFQDPYA---SLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNELAER 559
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLreERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
337-546 |
1.26e-38 |
|
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: 139.30 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 337 FDNVTFEFPNsGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQ 416
Cdd:cd00267 2 IENLSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 417 daglfnrsvednirvgranatheevhaaakaaaahdfilaksegydtfvgergsqLSGGERQRLAIARAILKDSPILVLD 496
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552148158 497 EATSALDVETEEKVKQAVDELS-HNRTTFIIAHRLSTV-RSADLVLFMDKGH 546
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-589 |
1.38e-38 |
|
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: 148.90 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSG-QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAA---GRIMIDGTDTRTVSRRSLRHA 410
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IATVFQDAG--LFNRSVEDNIRVGRAN--ATHEEVHAAAKAaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAI 486
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEALENlgLSRAEARARVLE-------LLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 487 LKDSPILVLDEATSALDVETEEKVKQAVDELS--HNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNELAERGGRF 563
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
250 260
....*....|....*....|....*....
gi 552148158 564 S---DLLRAGGLKLEDKQPKQPVVEGSNV 589
Cdd:COG1123 238 AavpRLGAARGRAAPAAAAAEPLLEVRNL 266
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
335-549 |
1.52e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.72 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY---DVSFEVKPGQTVAIVGPTGAGKTTLINL---LQRvfdPAAGRIMIDGTDTRTVSRRSL- 407
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTalrGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 408 ---RHAIATVFQDAGLFNR-SVEDNIRVGR--ANATHEEVHAAAKAaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLA 481
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPElTALENVALPLllAGVSRKERRERARE-------LLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 482 IARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNR-TTFIIA-HRLSTVRSADLVLFMDKGHLVE 549
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
335-551 |
1.04e-37 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 138.81 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD--TRTVSRRSlrhaIA 412
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtGVPPERRN----IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 413 TVFQDAGLF-NRSVEDNIRVG--RANATHEEVHAAAKAaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKD 489
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGlkLRGVPKAEIRARVRE-------LLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 490 SPILVLDEATSALDVETEEKVKQAVDELSHNR--TTFIIAHRLS-TVRSADLVLFMDKGHLVESG 551
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
22-307 |
1.18e-37 |
|
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: 141.15 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 22 ITMCVASVLVALVALAEPVLFGRVIQSISDKGD---IFSPLLMWAALGGFNIMAAVFVARGADRLAHRRRLGVMIDSYER 98
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDlslLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 99 LITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLVMR 178
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 179 KTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVL 258
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 552148158 259 VLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLE 307
Cdd:cd07346 242 LYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
335-547 |
3.89e-37 |
|
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: 137.24 E-value: 3.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY---DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSL---- 407
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 408 RHAIATVFQDAGLFNR-SVEDNIRV-----GRANATHEEVHAAakaaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLA 481
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEE----------LLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 482 IARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNR-TTFIIA-HRLSTVRSADLVLFMDKGHL 547
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
244-556 |
4.21e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 148.25 E-value: 4.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 244 GLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIgFVQLMIGRL-DQISAFINQTVTARAKLEEFFQMEDATADRQEP 322
Cdd:PTZ00265 1071 GFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSL-FTFLFTGSYaGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVR 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 323 EN----VADLNDVKGDIVFDNVTFEF---PNSGqgIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFD-------- 386
Cdd:PTZ00265 1150 DNggirIKNKNDIKGKIEIMDVNFRYisrPNVP--IYkDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhiv 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 387 ----------------------------------------------PAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGL 420
Cdd:PTZ00265 1228 fknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPML 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 421 FNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:PTZ00265 1308 FNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 501 ALDVETEEKVKQAVDELSH--NRTTFIIAHRLSTVRSAD-LVLFMD---KGHLVES-GSFNEL 556
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDkIVVFNNpdrTGSFVQAhGTHEEL 1450
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
335-547 |
4.42e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.87 E-value: 4.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATV 414
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLFNRSVEDNI----RVGRANATHEEVHAAAKAAAAHDFILAKSEgydtfvgergSQLSGGERQRLAIARAILKDS 490
Cdd:COG4619 80 PQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPV----------ERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 491 PILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAH--RLSTvRSADLVLFMDKGHL 547
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHdpEQIE-RVADRVLTLEAGRL 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
333-571 |
4.45e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 147.96 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVFDNVTFEF-PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAI 411
Cdd:PLN03130 1236 GSIKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLFNRSVEDNIRvgrANATHEEVHAAAKAAAAH--DFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKD 489
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLD---PFNEHNDADLWESLERAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRR 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 490 SPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNEL-AERGGRFSDLLR 568
Cdd:PLN03130 1393 SKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQ 1472
|
...
gi 552148158 569 AGG 571
Cdd:PLN03130 1473 STG 1475
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
335-547 |
7.43e-37 |
|
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: 135.22 E-value: 7.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNsGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTvSRRSLRHAIATV 414
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLFNR-SVEDNIRvgranatheevhaaakaaaahdfilaksegydtfvgergsqLSGGERQRLAIARAILKDSPIL 493
Cdd:cd03230 79 PEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 494 VLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTVRS-ADLVLFMDKGHL 547
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
323-542 |
8.61e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 147.10 E-value: 8.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 323 ENVAD---LNDVKgDIVFDNVTFEFPNSGQ-GIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMI-DG 396
Cdd:PTZ00265 369 ENNDDgkkLKDIK-KIQFKNVRFHYDTRKDvEIYkDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDS 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 397 TDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVG----------------RANATHE--------------------- 439
Cdd:PTZ00265 448 HNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsn 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 440 --------------------EVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEAT 499
Cdd:PTZ00265 528 ttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEAT 607
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 552148158 500 SALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRSADLVLFM 542
Cdd:PTZ00265 608 SSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
22-289 |
2.95e-36 |
|
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: 136.62 E-value: 2.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 22 ITMCVASVLVALVALAEPVLFGRVIQSISDKGD-----IFSPLLMWAALGGFNIMAAVFVARGADRLAHRRRLGVMIDSY 96
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDpetqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 97 ERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLV 176
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 177 MRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVV 256
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 552148158 257 VLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRL 289
Cdd:pfam00664 242 ALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
121-571 |
1.15e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 140.88 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 121 RATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMsLVLIVLGVIYVmigQLVMRKTKDGQAAVEKHHHKLFEHVSD 200
Cdd:PLN03232 1022 RNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPL-LILFYAAYLYY---QSTSREVRRLDSVTRSPIYAQFGEALN 1097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 201 TISNVSVVQSYNRIASETQALRDyaknlENAQFPVLN-----WWALasglnRMASTFSMVVVLVlgAYFVTKGQMRVGDV 275
Cdd:PLN03232 1098 GLSSIRAYKAYDRMAKINGKSMD-----NNIRFTLANtssnrWLTI-----RLETLGGVMIWLT--ATFAVLRNGNAENQ 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 276 IAFIGFVQLMIGRLDQISAFINQTVTARAKLEEFFQMEDATADRQE-PENVADLND---------VKGDIVFDNVTFEF- 344
Cdd:PLN03232 1166 AGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDlPSEATAIIEnnrpvsgwpSRGSIKFEDVHLRYr 1245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 345 PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRS 424
Cdd:PLN03232 1246 PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGT 1325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 425 VEDNIRvgrANATHEEVHAAAKAAAAH--DFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSAL 502
Cdd:PLN03232 1326 VRFNID---PFSEHNDADLWEALERAHikDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 503 DVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAER-GGRFSDLLRAGG 571
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRdTSAFFRMVHSTG 1472
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
353-552 |
1.62e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 130.88 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTL---INLLQRvfdPAAGRIMIDGTD--TRTVSRRSLRHAIATVFQDAGLF-NRSVE 426
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLFpHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 427 DNI--------RVGRANATHEEVHaaakaaaahdfILAKsegydtfVG--ERG----SQLSGGERQRLAIARAILKDSPI 492
Cdd:COG1126 96 ENVtlapikvkKMSKAEAEERAME-----------LLER-------VGlaDKAdaypAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 493 LVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTVRS-ADLVLFMDKGHLVESGS 552
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVtHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
335-546 |
2.44e-34 |
|
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: 128.46 E-value: 2.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS--RRSLRHAIA 412
Cdd:cd03229 1 LELKNVSKRYGQK-TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 413 TVFQDAGLFNR-SVEDNIRVGranatheevhaaakaaaahdfilaksegydtfvgergsqLSGGERQRLAIARAILKDSP 491
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTV-RSADLVLFMDKGH 546
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
335-545 |
2.83e-34 |
|
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: 129.13 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQ----GIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTdtrtvsrrslrha 410
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IATVFQDAGLFNRSVEDNI------------RVGRANATHEevhaaakaaaahDF-ILAKseGYDTFVGERGSQLSGGER 477
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgkpfdeeryeKVIKACALEP------------DLeILPD--GDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 478 QRLAIARAILKDSPILVLDEATSALDVETEEKV-KQAV-DELSHNRTTFIIAHRLSTVRSADLVLFMDKG 545
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
353-552 |
3.16e-34 |
|
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: 130.55 E-value: 3.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGL-FNRSVEDNIRV 431
Cdd:COG1120 19 DVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRELVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 GRA----------NATHEEVHAAAKAAAAHDFIlaksegyDTFVGErgsqLSGGERQRLAIARAILKDSPILVLDEATSA 501
Cdd:COG1120 99 GRYphlglfgrpsAEDREAVEEALERTGLEHLA-------DRPVDE----LSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 502 LD----VETEEKVKQAVDElsHNRTTFIIAHRLS-TVRSADLVLFMDKGHLVESGS 552
Cdd:COG1120 168 LDlahqLEVLELLRRLARE--RGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
335-556 |
5.59e-34 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 129.16 E-value: 5.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpnSGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHA--- 410
Cdd:cd03261 1 IELRGLTKSF--GGRTVLkGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IATVFQDAGLFNR-SVEDNIrvgrANATHEevHAAAKAAAAHDFILAKSEgydtFVGERG------SQLSGGERQRLAIA 483
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENV----AFPLRE--HTRLSEEEIREIVLEKLE----AVGLRGaedlypAELSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 484 RAILKDSPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNEL 556
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
335-558 |
1.08e-33 |
|
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: 128.56 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpnSGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS---RRSLRHA 410
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLdGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IATVFQDAGLF-NRSVEDNIRVG---RANATHEEVHaaakaaaahDFILAKSEgydtFVGERG------SQLSGGERQRL 480
Cdd:COG1127 84 IGMLFQGGALFdSLTVFENVAFPlreHTDLSEAEIR---------ELVLEKLE----LVGLPGaadkmpSELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 481 AIARAILKDSPILVLDEATSALDVETeekvKQAVDEL------SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSF 553
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPIT----SAVIDELirelrdELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
....*
gi 552148158 554 NELAE 558
Cdd:COG1127 227 EELLA 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
335-556 |
6.27e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.02 E-value: 6.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgqgIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRT-VSRRSlrhaIA 412
Cdd:COG3840 2 LRLDDLTYRYGDF---PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDlTALpPAERP----VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 413 TVFQDAGLFNR-SVEDNIRVG-----RANAT-HEEVHAaakaaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARA 485
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGlrpglKLTAEqRAQVEQ-----------ALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 486 ILKDSPILVLDEATSALD----VETEEKVKQAVDElsHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNEL 556
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
335-556 |
9.52e-33 |
|
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: 125.88 E-value: 9.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATV 414
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLF-NRSVEDNIR-VGRANATHEEVHAAAKAAAAHDFILAKSEgydtFVGERGSQLSGGERQRLAIARAILKDSPI 492
Cdd:cd03295 81 IQQIGLFpHMTVEENIAlVPKLLKWPKEKIRERADELLALVGLDPAE----FADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 493 LVLDEATSALDVETEEKVKQAVDELSH--NRTTFIIAHRL-STVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
351-559 |
1.01e-32 |
|
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: 125.53 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 351 IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRslRHAIATVFQDAGLF-NRSVEDNI 429
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 430 RVGRANAT------HEEVHAaakaaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALD 503
Cdd:cd03299 93 AYGLKKRKvdkkeiERKVLE-----------IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 504 VETEEKVKQAVDELSHN-RTTFI-IAHRLSTVRS-ADLVLFMDKGHLVESGSFNELAER 559
Cdd:cd03299 162 VRTKEKLREELKKIRKEfGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
353-551 |
1.28e-32 |
|
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: 123.70 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQdaglfnrSVEdnirvg 432
Cdd:cd03214 17 DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-------ALE------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 433 RANATHeevhaaakaaaahdfiLAksegydtfvgERG-SQLSGGERQRLAIARAILKDSPILVLDEATSALD----VETE 507
Cdd:cd03214 84 LLGLAH----------------LA----------DRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552148158 508 EKVKQAVDElsHNRTTFIIAHRLS-TVRSADLVLFMDKGHLVESG 551
Cdd:cd03214 138 ELLRRLARE--RGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
333-569 |
1.32e-32 |
|
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: 126.18 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVFDNVTFEFPNSGQGIYD-VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAI 411
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKhVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLFNRSVEDNIRVGRaNATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSP 491
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGS-FNELAERGGRFSDLLRA 569
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTpENLLAQEDGVFASLVRT 255
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-552 |
2.58e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.49 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNS-GQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIAT 413
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQ--DAGLFNRSVEDNIRVGRANA--THEEVhaaakaaaaHDFI--LAKSEGYDTFVGERGSQLSGGERQRLAIARAIL 487
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGLENKkvPPKKM---------KDIIddLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 488 KDSPILVLDEATSALDVETEEKVKQAVDELSHNRT-TFI-IAHRLSTVRSADLVLFMDKGHLVESGS 552
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-528 |
8.58e-32 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 122.58 E-value: 8.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQG---IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRslrhaI 411
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLFN-RSVEDNIRVG-----------RANATH--EEVHaaakaaaahdfiLAKSEGYdtfvgeRGSQLSGGER 477
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgvpkaeaRERAEEllELVG------------LSGFENA------YPHQLSGGMR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 478 QRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAH 528
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTH 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
335-528 |
1.09e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 123.66 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQG---IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRslrhaI 411
Cdd:COG1116 8 LELRGVSKRFPTGGGGvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLFN-RSVEDNIRVG-----------RANATH--EEVHaaakaaaahdfiLAKSEGYdtfvgeRGSQLSGGER 477
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlelrgvpkaerRERAREllELVG------------LAGFEDA------YPHQLSGGMR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 478 QRLAIARAILKDSPILVLDEATSALDVETEEKVkQavDEL-----SHNRTTFIIAH 528
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERL-Q--DELlrlwqETGKTVLFVTH 197
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
350-556 |
2.20e-31 |
|
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: 122.75 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 350 GIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSL----RHAIATVFQDAGLF-NRS 424
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 425 VEDNIRVGR--ANATHEEVHAAAKAAAAhdfiLAKSEGYDTFvgeRGSQLSGGERQRLAIARAILKDSPILVLDEATSAL 502
Cdd:cd03294 119 VLENVAFGLevQGVPRAEREERAAEALE----LVGLEGWEHK---YPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 503 D----VETEEKVKQAVDElsHNRTTFIIAHRLS-TVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:cd03294 192 DplirREMQDELLRLQAE--LQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
353-555 |
6.16e-31 |
|
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: 120.62 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTVSRRSLRHAIATVFQDAGLFNR-SVEDNIR 430
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDiTGLPPHEIARLGIGRTFQIPRLFPElTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 431 VGRANATHEEVHAAAKAAAAHDfILAKSEGYDTFVG------ERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDV 504
Cdd:cd03219 98 VAAQARTGSGLLLARARREERE-ARERAEELLERVGladladRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 505 ETEEKVKQAVDELSHNRTTF-IIAHRLSTVRS-ADLVLFMDKGHLVESGSFNE 555
Cdd:cd03219 177 EETEELAELIRELRERGITVlLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
337-551 |
7.23e-31 |
|
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: 119.95 E-value: 7.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 337 FDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRslrhaIATVFQ 416
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 417 DAGL---FNRSVEDNIRVGRANatHEEVHAAAKAAAAHDFILA-KSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPI 492
Cdd:cd03235 76 RRSIdrdFPISVRDVVLMGLYG--HKGLFRRLSKADKAKVDEAlERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 493 LVLDEATSALDVETEEKVKQAVDEL-SHNRTTFIIAHRLSTV-RSADLVLFMDKgHLVESG 551
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNR-TVVASG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
353-547 |
1.25e-30 |
|
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: 119.17 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTL---INLLQRvfdPAAGRIMIDGT--DTRTVSRRSLRHAIATVFQDAGLF-NRSVE 426
Cdd:cd03262 18 GIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLklTDDKKNINELRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 427 DNIRVG----------RANATHEEvhaaakaaaahdfILAKSeGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLD 496
Cdd:cd03262 95 ENITLApikvkgmskaEAEERALE-------------LLEKV-GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 497 EATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTVRS-ADLVLFMDKGHL 547
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVtHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
349-558 |
2.21e-30 |
|
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: 118.69 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 349 QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTVSRRSLRHAIATVFQDAGLFNR-SVE 426
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHERARAGIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 427 DNIRVGRANATHEEVHAAAkaaaahDFIlaksegYDTF--VGER----GSQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:cd03224 94 ENLLLGAYARRRAKRKARL------ERV------YELFprLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 501 ALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTVRS-ADLVLFMDKGHLVESGSFNELAE 558
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEGVTILLVeQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
335-527 |
7.83e-30 |
|
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: 116.74 E-value: 7.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRS---LRHAI 411
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLF-NRSVEDNI----RVgrANATHEEVHAAAKAAAAHDFILAKSEGYdtfvgerGSQLSGGERQRLAIARAI 486
Cdd:cd03292 81 GVVFQDFRLLpDRNVYENVafalEV--TGVPPREIRKRVPAALELVGLSHKHRAL-------PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552148158 487 LKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA 527
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
354-571 |
8.08e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 125.66 E-value: 8.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRvGR 433
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PF 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 434 ANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILK-DSPILVLDEATSALDVETEEKVKQ 512
Cdd:PTZ00243 1408 LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQA 1487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 513 AVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAE-RGGRFSDLLRAGG 571
Cdd:PTZ00243 1488 TVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMnRQSIFHSMVEALG 1547
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
352-551 |
8.81e-30 |
|
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: 116.82 E-value: 8.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 352 YDVSFEvkPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRT--VSRRSlrhaIATVFQDAGLFNR-SVEDN 428
Cdd:cd03298 17 FDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAapPADRP----VSMLFQENNLFAHlTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 429 IRVGRAnathEEVHAAAKAAAAHDFILAKSeGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEE 508
Cdd:cd03298 91 VGLGLS----PGLKLTAEDRQAIEVALARV-GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 552148158 509 KVKQAVDELSHNR--TTFIIAHRLSTVRS-ADLVLFMDKGHLVESG 551
Cdd:cd03298 166 EMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
355-556 |
5.07e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 115.06 E-value: 5.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 355 SFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTV-SRRSlrhaIATVFQDAGLFNR-SVEDNIRV 431
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPpSRRP----VSMLFQENNLFSHlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 G-----RANAT-HEEVHAaakaaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVE 505
Cdd:PRK10771 95 GlnpglKLNAAqREKLHA-----------IARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552148158 506 TEEKVKQAVDELSHNR--TTFIIAHRLS-TVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK10771 164 LRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
335-556 |
5.10e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 115.62 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTL---INLLQRvfdPAAGRI-----MIDGTdtRTVSR-- 404
Cdd:PRK11264 4 IEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQ---PEAGTIrvgdiTIDTA--RSLSQqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 405 ---RSLRHAIATVFQDAGLF-NRSVEDNIRVGRANATHEEVHAAAKAAAAhdfILAKsegydtfVGERGSQ------LSG 474
Cdd:PRK11264 78 gliRQLRQHVGFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARARE---LLAK-------VGLAGKEtsyprrLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 475 GERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSH-NRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGS 552
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGP 227
|
....
gi 552148158 553 FNEL 556
Cdd:PRK11264 228 AKAL 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
335-552 |
7.04e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.59 E-value: 7.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY---DVSFEVKPGQTVAIVGPTGAGKTTLI---NLLQRvfdPAAGRIMIDGTDTRTVSRRSLR 408
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIrciNLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 409 HA---IATVFQDaglFN----RSVEDNI----RVgrANATHEEVHAAAKAAAAHDFILAKSEGYDtfvgergSQLSGGER 477
Cdd:PRK11153 79 KArrqIGMIFQH---FNllssRTVFDNValplEL--AGTPKAEIKARVTELLELVGLSDKADRYP-------AQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 478 QRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELshNR----TTFIIAHRLSTVRS-ADLVLFMDKGHLVESGS 552
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-547 |
7.72e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.80 E-value: 7.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRslrhaIATV 414
Cdd:COG1121 7 IELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGlFNR----SVEDNIRVGRAN----------ATHEEVHAaakaaaahdfILAKSEGYDtFVGERGSQLSGGERQRL 480
Cdd:COG1121 81 PQRAE-VDWdfpiTVRDVVLMGRYGrrglfrrpsrADREAVDE----------ALERVGLED-LADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 481 AIARAILKDSPILVLDEATSALDVETEEKVKQAVDEL-SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHL 547
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
353-559 |
1.02e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 116.75 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSR---RSLRHAIATVFQD--AGLfN--RSV 425
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQDpyASL-NprMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 426 EDNI-------RVGRANATHEEVHAaakaaaahdfILAK----SEGYDTFVGErgsqLSGGERQRLAIARAILKDSPILV 494
Cdd:COG4608 115 GDIIaeplrihGLASKAERRERVAE----------LLELvglrPEHADRYPHE----FSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552148158 495 LDEATSALDVETEekvKQAV-------DELShnrTTFI-IAHRLSTVRS-ADLVLFMDKGHLVESGSFNELAER 559
Cdd:COG4608 181 CDEPVSALDVSIQ---AQVLnlledlqDELG---LTYLfISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-570 |
6.61e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.19 E-value: 6.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPN-SGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIAT 413
Cdd:PRK13635 6 IRVEHISFRYPDaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQ--DAGLFNRSVEDNIRVGRAN--ATHEE----VHAAAKAAAAHDFILaksegydtfvgERGSQLSGGERQRLAIArA 485
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLN-----------REPHRLSGGQKQRVAIA-G 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 486 ILKDSP-ILVLDEATSALDVETEEKVKQAVDELSHNR--TTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGgr 562
Cdd:PRK13635 154 VLALQPdIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG-- 231
|
....*...
gi 552148158 563 fSDLLRAG 570
Cdd:PRK13635 232 -HMLQEIG 238
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
335-551 |
7.15e-28 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 111.13 E-value: 7.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNsGQGIYDVSFEVKPGQTvAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTvSRRSLRHAIATV 414
Cdd:cd03264 1 LQLENLTKRYGK-KRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLFNR-SVED---------NIRVGRANATHEEVhaaakaaaahdfiLAKSEGYDtFVGERGSQLSGGERQRLAIAR 484
Cdd:cd03264 78 PQEFGVYPNfTVREfldyiawlkGIPSKEVKARVDEV-------------LELVNLGD-RAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 485 AILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESG 551
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-559 |
1.10e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 113.61 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 338 DNVTFEFPNSGQGIY---DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDP---AAGRIMIDGTDTRTVSRRSLRHA- 410
Cdd:COG0444 5 RNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 ---IATVFQDAGL-FN------RSVEDNIRVGRaNATHEEvhaaakaaaahdfilAKSEGYDTF--VG-----ERGS--- 470
Cdd:COG0444 85 greIQMIFQDPMTsLNpvmtvgDQIAEPLRIHG-GLSKAE---------------ARERAIELLerVGlpdpeRRLDryp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 471 -QLSGGERQRLAIARAILKDSPILVLDEATSALDVETEekvKQAVDEL-----SHNRTTFIIAHRLSTVRS-ADLVLFMD 543
Cdd:COG0444 149 hELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQ---AQILNLLkdlqrELGLAILFITHDLGVVAEiADRVAVMY 225
|
250
....*....|....*.
gi 552148158 544 KGHLVESGSFNELAER 559
Cdd:COG0444 226 AGRIVEEGPVEELFEN 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
335-559 |
2.18e-27 |
|
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: 110.40 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTV--SRRSlrhaIA 412
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLppHKRP----VN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 413 TVFQDAGLFNR-SVEDNIRVG------RANATHEEVHAAAKaaaahdfiLAKSEGYDtfvGERGSQLSGGERQRLAIARA 485
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALD--------LVQLEGYA---NRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 486 ILKDSPILVLDEATSALDVETEEKVKQAVDELSHN-RTTFI-IAHRLSTVRS-ADLVLFMDKGHLVESGSFNELAER 559
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVfVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
125-568 |
3.38e-27 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 117.74 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 125 SLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVlivlgviyvmigQLVMRKTKDGQAavekhhhKLfehVSDTISN 204
Cdd:TIGR00957 448 ALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTY------------QVAHMKSKDNRI-------KL---MNEILNG 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 205 VSVVQSYnriASETqALRDYAKNLENAQFPVLNWWALASGLnrmaSTFSMV-----VVLVLGAYFVTKGQMRVGDV---- 275
Cdd:TIGR00957 506 IKVLKLY---AWEL-AFLDKVEGIRQEELKVLKKSAYLHAV----GTFTWVctpflVALITFAVYVTVDENNILDAekaf 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 276 --IAFIGFVQLMIGRLDQISAFINQTVTARAKLEEFFQMEDATADRQEPENVADlnDVKGDIVFDNVTFEFPNS-GQGIY 352
Cdd:TIGR00957 578 vsLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKP--GEGNSITVHNATFTWARDlPPTLN 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTdtrtvsrrslrhaIATVFQDAGLFNRSVEDNIRVG 432
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFG 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 433 RANATHEEVHAAAKAAAAHDFILAKSeGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQ 512
Cdd:TIGR00957 723 KALNEKYYQQVLEACALLPDLEILPS-GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 513 AV---DELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLR 568
Cdd:TIGR00957 802 HVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLR 860
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-552 |
3.76e-27 |
|
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: 115.55 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTL----INLLqrvfdPAAGRIMIDGTDTRTVSR---RSLRHAIATVFQDA-GLFN-- 422
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRralRPLRRRMQVVFQDPfGSLSpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 423 RSVEDNI---------------RVGRANATHEEVhaaakaaaahdfilakseGYDTFVGER-GSQLSGGERQRLAIARA- 485
Cdd:COG4172 379 MTVGQIIaeglrvhgpglsaaeRRARVAEALEEV------------------GLDPAARHRyPHEFSGGQRQRIAIARAl 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552148158 486 ILKdsP-ILVLDEATSALDVETEekvKQAVDELS-----HNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGS 552
Cdd:COG4172 441 ILE--PkLLVLDEPTSALDVSVQ---AQILDLLRdlqreHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
334-559 |
4.16e-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: 112.88 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 334 DIVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTVSRRslRHaIA 412
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvTGLPPEK--RN-VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 413 TVFQDAGLF-NRSVEDNI-------RVGRAnATHEEVHAaakaaaahdfILA--KSEGYdtfvGERG-SQLSGGERQRLA 481
Cdd:COG3842 81 MVFQDYALFpHLTVAENVafglrmrGVPKA-EIRARVAE----------LLElvGLEGL----ADRYpHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 482 IARAILKDSPILVLDEATSALDVETEEKVKQAVDELsHNR--TTFIIA-HRLS---TVrsADLVLFMDKGHLVESGSFNE 555
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRL-QRElgITFIYVtHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222
|
....
gi 552148158 556 LAER 559
Cdd:COG3842 223 IYER 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
335-566 |
6.81e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.59 E-value: 6.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpNSGQGIY---DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAI 411
Cdd:PRK13650 5 IEVKNLTFKY-KEDQEKYtlnDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQ--DAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFIlakseGYDTFVGERGSQLSGGERQRLAIARAILKD 489
Cdd:PRK13650 84 GMVFQnpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELV-----GMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 490 SPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDL 566
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIrdDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQL 237
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
353-555 |
8.66e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 109.36 E-value: 8.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTVSRRSLRHAIATVFQDAGLFNR-SVEDNIR 430
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDiTGLPPHRIARLGIARTFQNPRLFPElTVLENVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 431 VGRANATHEEVHAAAK----AAAAHDFILAKSE------GYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:COG0411 102 VAAHARLGRGLLAALLrlprARREEREARERAEellervGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 501 AL-DVETEEkVKQAVDELS--HNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNE 555
Cdd:COG0411 182 GLnPEETEE-LAELIRRLRdeRGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
353-548 |
1.68e-26 |
|
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: 105.59 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS-RRSLRHAIATVFQdaglfnrsvednirv 431
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 granatheevhaaakaaaahdfilaksegydtfvgergsqLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVK 511
Cdd:cd03216 83 ----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190
....*....|....*....|....*....|....*....
gi 552148158 512 QAVDELSHNRTTFI-IAHRLSTVRS-ADLVLFMDKGHLV 548
Cdd:cd03216 123 KVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
353-527 |
2.14e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.79 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTvSRRSLRHAIATVFQDAGLFNR-SVEDNIRV 431
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 GRAnATHEEVHAAAKAAAAHDFILAKSEgyDTFVGergsQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVK 511
Cdd:COG4133 99 WAA-LYGLRADREAIDEALEAVGLAGLA--DLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA 171
|
170
....*....|....*.
gi 552148158 512 QAVDELSHNRTTFIIA 527
Cdd:COG4133 172 ELIAAHLARGGAVLLT 187
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
353-551 |
1.06e-25 |
|
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: 105.07 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVkPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGT---DTR-TVSRRSLRHAIATVFQDAGLF-NRSVED 427
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 NIRVGRanatheEVHAAAKAAAAHDFILAkSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETE 507
Cdd:cd03297 95 NLAFGL------KRKRNREDRISVDELLD-LLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552148158 508 EKVKQAVDELSH--NRTTFIIAHRLSTV-RSADLVLFMDKGHLVESG 551
Cdd:cd03297 168 LQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
159-578 |
2.11e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 111.99 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 159 SLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVS--DTISNVSVVQSYNriaSETQALRdyaknleNAQFPVL 236
Cdd:PLN03232 447 SLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILAsmDTVKCYAWEKSFE---SRIQGIR-------NEELSWF 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 237 NWWALASGLNR-MASTFSMVVVLV-LGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARA---KLEEFFQ 311
Cdd:PLN03232 517 RKAQLLSAFNSfILNSIPVVVTLVsFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVslqRIEELLL 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 312 MEDATADRQEPenvadLNDVKGDIVFDNVTFEFPN--SGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAa 389
Cdd:PLN03232 597 SEERILAQNPP-----LQPGAPAISIKNGYFSWDSktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA- 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 390 grimidgtDTRTVSrrsLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKseGYD-TFVGER 468
Cdd:PLN03232 671 --------ETSSVV---IRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLP--GRDlTEIGER 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 469 GSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKV-KQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHL 547
Cdd:PLN03232 738 GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
410 420 430
....*....|....*....|....*....|.
gi 552148158 548 VESGSFNELAERGGRFSDLLRAGGlKLEDKQ 578
Cdd:PLN03232 818 KEEGTFAELSKSGSLFKKLMENAG-KMDATQ 847
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-551 |
2.18e-25 |
|
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: 103.78 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNS-----GQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLL--QRVFDPAAGRIMIDGtdtRTVSRRSL 407
Cdd:cd03213 4 LSFRNLTVTVKSSpsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 408 RHAIATVFQDAGLF-NRSVEDNIRVGranatheevhaaakaaaahdfilAKSEGydtfvgergsqLSGGERQRLAIARAI 486
Cdd:cd03213 81 RKIIGYVPQDDILHpTLTVRETLMFA-----------------------AKLRG-----------LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 487 LKDSPILVLDEATSALDVETEEKVKQAVDELSH-NRTTFIIAHRLST--VRSADLVLFMDKGHLVESG 551
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
335-558 |
2.54e-25 |
|
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: 104.73 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDtrtVSRRSLR-HAIAT 413
Cdd:cd03296 3 IEVRNVSKRFGDF-VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED---ATDVPVQeRNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQDAGLFNR-SVEDNIRVG-RANATHEEVHAAAKAAAAHDfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSP 491
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHE--LLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDELSH--NRTTFIIAHRLS-TVRSADLVLFMDKGHLVESGSFNELAE 558
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
338-548 |
2.97e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 103.49 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 338 DNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDtrtVSRRSLRHAIATVFQD 417
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 418 AG--LFNRSVEDNIRVGrANATHEEVHAAAKaaaahdfILAKSEGYDtfVGERGSQ-LSGGERQRLAIARAILKDSPILV 494
Cdd:cd03226 80 VDyqLFTDSVREELLLG-LKELDAGNEQAET-------VLKDLDLYA--LKERHPLsLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 495 LDEATSALDVETEEKVKQAVDELS-HNRTTFIIAHRLSTV-RSADLVLFMDKGHLV 548
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
333-556 |
3.20e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.08 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD--TRTVSRRSlrha 410
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtDLPPKDRN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IATVFQDAGLF-NRSVEDNI----------------RVGRAnatheevhaaakaaaahdfilAKSEGYDTFVGERGSQLS 473
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIafplklrkvpkaeidrRVREA---------------------AELLGLEDLLDRKPKQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 474 GGERQRLAIARAILKDSPILVLDEATSALD----VETEEKVKQAVDELshnRTTFIIA-H------RLstvrsADLVLFM 542
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVtHdqveamTL-----ADRIAVM 207
|
250
....*....|....
gi 552148158 543 DKGHLVESGSFNEL 556
Cdd:COG3839 208 NDGRIQQVGTPEEL 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
349-551 |
3.57e-25 |
|
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: 103.60 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 349 QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTvSRRSLRHAIATVFQDAGLFNR-SVED 427
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 NIR-------VGRANATH--EEvhaaakaaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEA 498
Cdd:cd03266 98 NLEyfaglygLKGDELTArlEE--------------LADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 499 TSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTVRS-ADLVLFMDKGHLVESG 551
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
353-560 |
3.94e-25 |
|
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: 107.12 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVkPGQTV-AIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTdTRTVSRRSL-----RHAIATVFQDAGLF-NRSV 425
Cdd:TIGR02142 15 DADFTL-PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-TLFDSRKGIflppeKRRIGYVFQEARLFpHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 426 EDNIRVGRANATHEEVHAAAKAaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVE 505
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFER-------VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 506 TEEKVKQAVDELSH--NRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNELAERG 560
Cdd:TIGR02142 166 RKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
353-572 |
4.61e-25 |
|
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: 106.72 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINL---LQRvfdPAAGRIMIDGT---DTRtvSRRSL---RHAIATVFQDAGLF-N 422
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqDSA--RGIFLpphRRRIGYVFQEARLFpH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 423 RSVEDNIRVGRANATHEEVHAaakaaaahdfilakseGYDTFVG--------ERG-SQLSGGERQRLAIARAILKDSPIL 493
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRI----------------SFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 494 VLDEATSALDVETeekvKQAV--------DELShnrttfI----IAHRLSTV-RSADLVLFMDKGHLVESGSFNELAERg 560
Cdd:COG4148 156 LMDEPLAALDLAR----KAEIlpylerlrDELD------IpilyVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLSR- 224
|
250
....*....|..
gi 552148158 561 grfSDLLRAGGL 572
Cdd:COG4148 225 ---PDLLPLAGG 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
335-559 |
5.07e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 106.38 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD--TRTVSRRslRHaIA 412
Cdd:COG1118 3 IEVRNISKRFGSF-TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlfTNLPPRE--RR-VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 413 TVFQDAGLF-NRSVEDNIRVG-----------RANATH--EEVHAaakaaaahdfilaksegyDTFVGERGSQLSGGERQ 478
Cdd:COG1118 79 FVFQHYALFpHMTVAENIAFGlrvrppskaeiRARVEEllELVQL------------------EGLADRYPSQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 479 RLAIARAILKDSPILVLDEATSALDVeteeKVKQAV-DELSH-----NRTTFIIAH-RLSTVRSADLVLFMDKGHLVESG 551
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDA----KVRKELrRWLRRlhdelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVG 216
|
....*...
gi 552148158 552 SFNELAER 559
Cdd:COG1118 217 TPDEVYDR 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
349-551 |
1.11e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 103.58 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 349 QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFD--PAA---GRIMIDGTD--TRTVSRRSLRHAIATVFQDAGLF 421
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDiyDPDVDVVELRRRVGMVFQKPNPF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 422 NRSVEDNIRVG-RANATH-------------------EEVHaaakaaaahDfILAKSegydtfvgerGSQLSGGERQRLA 481
Cdd:COG1117 105 PKSIYDNVAYGlRLHGIKskseldeiveeslrkaalwDEVK---------D-RLKKS----------ALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 482 IARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLS-TVRSADLVLFMDKGHLVESG 551
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFG 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
353-552 |
1.34e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.05 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSR---RSLRHAIATVFQDA-GLFN--RSVE 426
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPyGSLNprKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 427 D--------NIRVGRANAThEEVHAaakaaaahdfILAK----SEGYDTFvgerGSQLSGGERQRLAIARAILKDSPILV 494
Cdd:PRK11308 113 QileeplliNTSLSAAERR-EKALA----------MMAKvglrPEHYDRY----PHMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 495 LDEATSALDVETEEKVKQAVDELSHN-RTTFI-IAHRLSTVRS-ADLVLFMDKGHLVESGS 552
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLNLMMDLQQElGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
353-556 |
1.40e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.41 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS-RRSLRHAIATVFQDAGLF-NRSVEDNIR 430
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVpNLSVAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 431 VGRA---------NATHEEVHAaakaaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSA 501
Cdd:COG1129 102 LGREprrgglidwRAMRRRARE-----------LLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 502 LDvETE-EKVKQAVDELSHNRTTFI-IAHRLSTVRS-ADLVLFMDKGHLVESGSFNEL 556
Cdd:COG1129 171 LT-EREvERLFRIIRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
353-551 |
1.83e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.08 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGL-FNRSVEDNIRV 431
Cdd:PRK09536 21 GVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 GRANATHEEVHAAAKAAAAHDFILAKSeGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALD----VETE 507
Cdd:PRK09536 101 GRTPHRSRFDTWTETDRAAVERAMERT-GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDinhqVRTL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552148158 508 EKVKQAVDElshNRTTFIIAHRLS-TVRSADLVLFMDKGHLVESG 551
Cdd:PRK09536 180 ELVRRLVDD---GKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
351-558 |
1.87e-24 |
|
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: 101.98 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 351 IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTVSRRSLRHAIATVFQDAGLFNR-SVEDN 428
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDiTGLPPHRIARLGIGYVPEGRRIFPSlTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 429 IRVG--------RANATHEEVhaaakaaaahdfilaksegYDTF--VGER----GSQLSGGERQRLAIARAILKDSPILV 494
Cdd:COG0410 99 LLLGayarrdraEVRADLERV-------------------YELFprLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 495 LDEATSALD---VeteEKVKQAVDELSHNRTTFIIA-HRLSTVRS-ADLVLFMDKGHLVESGSFNELAE 558
Cdd:COG0410 160 LDEPSLGLApliV---EEIFEIIRRLNREGVTILLVeQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
335-551 |
2.55e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFeFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD---TRTVSR---RSLR 408
Cdd:COG4161 3 IQLKNINC-FYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEkaiRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 409 HAIATVFQDAGLF-NRSVEDN-----IRVGRANATHeevhaaakAAAAHDFILAKSEgYDTFVGERGSQLSGGERQRLAI 482
Cdd:COG4161 82 QKVGMVFQQYNLWpHLTVMENlieapCKVLGLSKEQ--------AREKAMKLLARLR-LTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 483 ARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNR-TTFIIAHRLSTVRS-ADLVLFMDKGHLVESG 551
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQG 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
237-552 |
2.81e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.20 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 237 NWWALA------SGLNRMASTFSMVV--VLVLGAYFvtKGQMRVGDVI----AFiGFVQ----LMIGRLDQISAFinQTV 300
Cdd:COG4178 257 NWRRLIrrqrnlTFFTTGYGQLAVIFpiLVAAPRYF--AGEITLGGLMqaasAF-GQVQgalsWFVDNYQSLAEW--RAT 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 301 TARakLEEFFQ-MEDATADRQEPENVADLNDvkGDIVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLIN 379
Cdd:COG4178 332 VDR--LAGFEEaLEAADALPEAASRIETSED--GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLR 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 380 LLQRVFDPAAGRIMI-DGTDTRTVSRR------SLRHAI-----ATVFQDAGLfnRSVEDNIRVGR-ANATHEEVHaaak 446
Cdd:COG4178 408 AIAGLWPYGSGRIARpAGARVLFLPQRpylplgTLREALlypatAEAFSDAEL--REALEAVGLGHlAERLDEEAD---- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 447 aaaahdfilaksegydtfvgeRGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAV-DELSHnrTTFI 525
Cdd:COG4178 482 ---------------------WDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELPG--TTVI 538
|
330 340
....*....|....*....|....*...
gi 552148158 526 -IAHRLSTVRSADLVLfmdkgHLVESGS 552
Cdd:COG4178 539 sVGHRSTLAAFHDRVL-----ELTGDGS 561
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
335-555 |
3.22e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEF----PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD--TRTVSRRSLR 408
Cdd:PRK13637 3 IKIENLTHIYmegtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 409 HAIATVFQ--DAGLFNRSVEDNIRVGRAN--ATHEEVHAAAKAAAAhdfILAKSegYDTFVGERGSQLSGGERQRLAIAR 484
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINlgLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 485 AILKDSPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGS----FNE 555
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTprevFKE 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
335-551 |
4.36e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFeFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDG------TDTRTVSRRSLR 408
Cdd:PRK11124 3 IQLNGINC-FYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 409 HAIATVFQDAGLF-NRSVEDN-----IRVgrANATHEEVHAAAkaaaahDFILAKSEGYDtFVGERGSQLSGGERQRLAI 482
Cdd:PRK11124 82 RNVGMVFQQYNLWpHLTVQQNlieapCRV--LGLSKDQALARA------EKLLERLRLKP-YADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 483 ARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNR-TTFIIAHRLSTVRS-ADLVLFMDKGHLVESG 551
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
337-551 |
5.61e-24 |
|
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: 100.42 E-value: 5.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 337 FDNVTFEFPNSG---QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLL-QRVFDPAA--GRIMIDGtdtRTVSRRSLRHA 410
Cdd:cd03234 6 WWDVGLKAKNWNkyaRILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGTtsGQILFNG---QPRKPDQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IATVFQ-DAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILakSEGYDTFVG-ERGSQLSGGERQRLAIARAILK 488
Cdd:cd03234 83 VAYVRQdDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLL--RDLALTRIGgNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 489 DSPILVLDEATSALDVETEEKVKQAVDELSH-NRTTFIIAH--RLSTVRSADLVLFMDKGHLVESG 551
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
353-556 |
8.78e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 99.89 E-value: 8.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTvSRRSLRHAIATVFQDAGLF-NRSVEDNIRV 431
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFdELTVREHLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 ------GRANATHEEVHAAAKAAAAHDFIlaksegyDTFVGergsQLSGGERQRLAIARAILKDSPILVLDEATSALDVE 505
Cdd:cd03263 99 yarlkgLPKSEIKEEVELLLRVLGLTDKA-------NKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552148158 506 TEEKVKQAVDELSHNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNEL 556
Cdd:cd03263 168 SRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
353-552 |
9.98e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 9.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGL-FNRSVEDNIRV 431
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 GRANATHEEVHAAAKAaaahDFILAKSeGYDTFVGERGSQLSGGERQRLAIARAIL------KDSPILVLDEATSALDVE 505
Cdd:PRK13548 100 GRAPHGLSRAEDDALV----AAALAQV-DLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 552148158 506 TEEKVKQAVDELSHNRTTFIIA--HRLS-TVRSADLVLFMDKGHLVESGS 552
Cdd:PRK13548 175 HQHHVLRLARQLAHERGLAVIVvlHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
335-556 |
1.22e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.17 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTL---INLLQRVfdpAAGRIMIDGTDTR--TVSRRSLRH 409
Cdd:PRK09493 2 IEFKNVSKHFGPT-QVLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLEEI---TSGDLIVDGLKVNdpKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 410 AIATVFQDAGLFNR-SVEDNIRVGRAN---ATHEEVHAAAKAaaahdfILAKsegydtfVG--ERG----SQLSGGERQR 479
Cdd:PRK09493 78 EAGMVFQQFYLFPHlTALENVMFGPLRvrgASKEEAEKQARE------LLAK-------VGlaERAhhypSELSGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 480 LAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFII-AHRLSTVRS-ADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIvTHEIGFAEKvASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
335-556 |
1.67e-23 |
|
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: 98.98 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSrRSLRHAIATV 414
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLfnrsveDNIRVGRAN-ATHEEVHAAAKAAAAH--DFILAKSEGYDtFVGERGSQLSGGERQRLAIARAILKDSP 491
Cdd:cd03265 79 FQDLSV------DDELTGWENlYIHARLYGVPGAERREriDELLDFVGLLE-AADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNEL 556
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-555 |
2.20e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.39 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY---------------------DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIM 393
Cdd:COG1134 5 IEVENVSKSYRLYHEPSRslkelllrrrrtrreefwalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 394 IDGTdtrtvsrrslrhaIATVFQDAGLFNR--SVEDNIR-VGRA-NATHEEVHAAAkaaaahDFILAKSEgydtfVGERG 469
Cdd:COG1134 85 VNGR-------------VSALLELGAGFHPelTGRENIYlNGRLlGLSRKEIDEKF------DEIVEFAE-----LGDFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 470 SQ----LSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTVRS-ADLVLFMD 543
Cdd:COG1134 141 DQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLE 220
|
250
....*....|..
gi 552148158 544 KGHLVESGSFNE 555
Cdd:COG1134 221 KGRLVMDGDPEE 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
335-574 |
2.83e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDP---AAGRIMIDGTDTRTVSRRSLRHA 410
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALnDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IATVFQ--DAGLFNRSVEDNIRVGRANathEEVHAAAKAAAAHDfILAKSeGYDTFVGERGSQLSGGERQRLAIArAILK 488
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGLEN---RAVPRPEMIKIVRD-VLADV-GMLDYIDSEPANLSGGQKQRVAIA-GILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 489 DSP-ILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERggrfSD 565
Cdd:PRK13640 160 VEPkIIILDESTSMLDPAGKEQILKLIRKLkkKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK----VE 235
|
....*....
gi 552148158 566 LLRAGGLKL 574
Cdd:PRK13640 236 MLKEIGLDI 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
335-577 |
3.54e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEF----PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDG----TDTRTVSRRS 406
Cdd:PRK13641 3 IKFENVDYIYspgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 407 LRHAIATVFQ--DAGLFNRSVEDNIRVGRAN--ATHEEVHAAAKAAAahdfilaKSEGYDTFVGERGS-QLSGGERQRLA 481
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKALKWL-------KKVGLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 482 IARAILKDSPILVLDEATSALDVETEEKVKQA-VDELSHNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNE---- 555
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEifsd 235
|
250 260 270
....*....|....*....|....*....|.
gi 552148158 556 --------LAE-RGGRFSDLLRAGGLKLEDK 577
Cdd:PRK13641 236 kewlkkhyLDEpATSRFASKLEKGGFKFSEM 266
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
335-556 |
6.40e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 6.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDtrtVSRRSLRHA-IAT 413
Cdd:PRK11432 7 VVLKNITKRFGSN-TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQQRdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQDAGLF-NRSVEDNIRVG--RANATHEEVHAAAKAAAAhdfiLAKSEGY-DTFVgergSQLSGGERQRLAIARAILKD 489
Cdd:PRK11432 83 VFQSYALFpHMSLGENVGYGlkMLGVPKEERKQRVKEALE----LVDLAGFeDRYV----DQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 490 SPILVLDEATSALDVETEEKVKQAVDELSH--NRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-552 |
1.71e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.75 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSR-RSLRHAIAT 413
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQ--DAGLFNRSVEDNIRVGRANATHEEVHAAAKAaaahDFILAKSeGYDTFVGERGSQLSGGERQRLAIARAILKDSP 491
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKRV----DRALAEI-GLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDELSHNRTTFI-IAHRLSTVRSADLVLFMDKGHLVESGS 552
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-497 |
1.82e-22 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 101.41 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 1 MSLLKIYWRamQYLAVERTATITMCVASVL-VALVALaepvlfgrVIQSISDKGDIFSPLLMWAALggfnIMAAVFVARG 79
Cdd:COG4615 1 MNLLRLLLR--ESRWLLLLALLLGLLSGLAnAGLIAL--------INQALNATGAALARLLLLFAG----LLVLLLLSRL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 80 A-----DRLAH------RRRLgvmidsYERLITMPLAWHQKRGTSNALHTLIRATDSL--FTLWLEFMRQHLTTVVA--- 143
Cdd:COG4615 67 AsqlllTRLGQhavarlRLRL------SRRILAAPLERLERIGAARLLAALTEDVRTIsqAFVRLPELLQSVALVLGcla 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 144 -LATLIPVAMTMdmrmSLVLIVLGVIyvmIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTIS-------NvsvvqSYNRIA 215
Cdd:COG4615 141 yLAWLSPPLFLL----TLVLLGLGVA---GYRLLVRRARRHLRRAREAEDRLFKHFRALLEgfkelklN-----RRRRRA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 216 SETQALRDYAKNLENAQFPVLNWWALASGLNRMaSTFSMVVVLVLGAYFVTKGQMRVgdVIAFIGFVQLMIGRLDQISA- 294
Cdd:COG4615 209 FFDEDLQPTAERYRDLRIRADTIFALANNWGNL-LFFALIGLILFLLPALGWADPAV--LSGFVLVLLFLRGPLSQLVGa 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 295 --FINQTVTARAKLEEFFQMEDATADRQEPENVADLNDVKGDIVFDNVTFEFPNSGQG----IYDVSFEVKPGQTVAIVG 368
Cdd:COG4615 286 lpTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegftLGPIDLTIRRGELVFIVG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 369 PTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNR--SVEDNIRVGRANATHEEVHAAAK 446
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRllGLDGEADPARARELLERLELDHK 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 447 AaaahdfilaksegydTFVGERGS--QLSGGERQRLAIARAILKDSPILVLDE 497
Cdd:COG4615 446 V---------------SVEDGRFSttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
335-528 |
2.06e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.85 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQG---IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtdtRTVSRRSLRHAI 411
Cdd:COG4525 4 LTVRHVSVRYPGGGQPqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG---VPVTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 atVFQDAGLFN-RSVEDNI-------RVGRAnATHEEVHAaakaaaahdfILAKSeGYDTFVGERGSQLSGGERQRLAIA 483
Cdd:COG4525 81 --VFQKDALLPwLNVLDNVafglrlrGVPKA-ERRARAEE----------LLALV-GLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552148158 484 RAILKDSPILVLDEATSALDVETEEKVKQAVDELSH--NRTTFIIAH 528
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH 193
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-556 |
2.10e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.04 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGT------DTRTVSRRSLRHAIATVFQDAGLF-NRSV 425
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFpHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 426 EDNIRVG-RANATHEEVHAAAKAAAAHDFILAKSEGYDTfVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDV 504
Cdd:PRK14246 108 YDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKEVYDR-LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 505 ETEEKVKQAVDELSHNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK14246 187 VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
335-525 |
2.85e-22 |
|
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: 95.40 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDG---TDTRTVSRRslrhaI 411
Cdd:cd03301 1 VELENVTKRFGNV-TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvTDLPPKDRD-----I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLF-NRSVEDNI------RVGRANATHEEVHAAakaaaahdfilAKSEGYDTFVGERGSQLSGGERQRLAIAR 484
Cdd:cd03301 75 AMVFQNYALYpHMTVYDNIafglklRKVPKDEIDERVREV-----------AELLQIEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552148158 485 AILKDSPILVLDEATSALDVETEEKVKQAVDELSHN-RTTFI 525
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTI 185
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
353-599 |
4.11e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 101.74 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIdgtdtrtvsrrsLRHAIATVFQDAGLFNRSVEDNIRVG 432
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 433 RANATHEEVHAAAKAAAAHDfiLAKSEGYD-TFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKV- 510
Cdd:PLN03130 703 SPFDPERYERAIDVTALQHD--LDLLPGGDlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVf 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 511 -KQAVDELShNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLRAGGlKLEDKQPKQPVVEGSNV 589
Cdd:PLN03130 781 dKCIKDELR-GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAG-KMEEYVEENGEEEDDQT 858
|
250
....*....|
gi 552148158 590 MPFPVKGAVA 599
Cdd:PLN03130 859 SSKPVANGNA 868
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
339-574 |
6.82e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.91 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 339 NVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRtVSRRSL---RHAIATVF 415
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 416 Q--DAGLFNRSVEDNIRVGRANA--THEEVHAAAKAAAahdfilaKSEGYDTFVGERGSQLSGGERQRLAIArAILKDSP 491
Cdd:PRK13639 85 QnpDDQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAL-------KAVGMEGFENKPPHHLSGGQKKRVAIA-GILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 492 -ILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTV-RSADLVLFMDKGHLVESGSFNELaerggrFSD--L 566
Cdd:PRK13639 157 eIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEV------FSDieT 230
|
....*...
gi 552148158 567 LRAGGLKL 574
Cdd:PRK13639 231 IRKANLRL 238
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
349-560 |
7.31e-22 |
|
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: 94.51 E-value: 7.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 349 QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTVSRRSLRHAIATVFQDAGLFNR-SVE 426
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDiTKLPPHERARAGIAYVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 427 DNIRVGRANATHEEVHAAakaaaahDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVET 506
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIP-------DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 507 EEKVKQAVDELSHNRTTFII--AHRLSTVRS-ADLVLFMDKGHLVESGSFNELAERG 560
Cdd:TIGR03410 167 IKDIGRVIRRLRAEGGMAILlvEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
350-556 |
9.20e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.80 E-value: 9.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 350 GIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHA----IATVFQDAGLF-NRS 424
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMpHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 425 VEDNIRVGR--ANATHEEVHAAAKAAAAHDFILAKSEGYDtfvgergSQLSGGERQRLAIARAILKDSPILVLDEATSAL 502
Cdd:PRK10070 123 VLDNTAFGMelAGINAEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 503 D--VETEEKVKQAVDELSHNRTTFIIAHRL-STVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK10070 196 DplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
353-567 |
1.45e-21 |
|
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: 94.92 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRImidgtdtrtvsRRSLRhaIATVFQDAGLFNRSVEDNIRVG 432
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGR--ISFSSQFSWIMPGTIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 433 RANATHEEVHAAAKAAAAHDfILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKV-K 511
Cdd:cd03291 122 VSYDEYRYKSVVKACQLEED-ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 512 QAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLL 567
Cdd:cd03291 201 SCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
334-556 |
1.63e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.09 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 334 DIVFDNVTFEF----PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIdGTDTRTVSRR---- 405
Cdd:PRK13634 2 DITFQKVEHRYqyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKnkkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 406 -SLRHAIATVFQ--DAGLFNRSVEDNIRVGRAN--ATHEEVHAAAKAaaahdfiLAKSEGYDTFVGERGS-QLSGGERQR 479
Cdd:PRK13634 81 kPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKARE-------MIELVGLPEELLARSPfELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 480 LAIARAILKDSPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
353-551 |
2.27e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 92.67 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTrTVSRRSLRHaIATVFQDAGLF-NRSVEDNIRV 431
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRR-IGALIEAPGFYpNLTARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 -----GRANATHEEVHAAAkaaaahdfilakseGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVET 506
Cdd:cd03268 96 larllGIRKKRIDEVLDVV--------------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552148158 507 EEKVKQAVDELSHNRTTFIIA-HRLSTV-RSADLVLFMDKGHLVESG 551
Cdd:cd03268 162 IKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
335-548 |
2.32e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.02 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRS---LRHAI 411
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLF-NRSVEDNIRVGR--ANATHEEVHAAAKAAAAHDFILAKSEGYDTfvgergsQLSGGERQRLAIARAILK 488
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 489 DSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTV-RSADLVLFMDKGHLV 548
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMAtHDIGLIsRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
335-566 |
2.79e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.46 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEF----PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDG----TDTRTVSRRS 406
Cdd:PRK13646 3 IRFDNVSYTYqkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 407 LRHAIATVFQ--DAGLFNRSVEDNIRVGRAN--ATHEEVHAAAkaaaahdFILAKSEGYDTFVGERGS-QLSGGERQRLA 481
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVKNYA-------HRLLMDLGFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 482 IARAILKDSPILVLDEATSALDVETEEKVKQAVDELS--HNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNELAE 558
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
....*...
gi 552148158 559 RGGRFSDL 566
Cdd:PRK13646 236 DKKKLADW 243
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
349-551 |
3.15e-21 |
|
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: 92.34 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 349 QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTvsrrSLRHAIATVFQDAGLF-NRSVED 427
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLPEERGLYpKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 NIR-------VGRANATHEEvhaaakaaaahDFILAKSEGYDtFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:cd03269 90 QLVylaqlkgLKKEEARRRI-----------DEWLERLELSE-YANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 501 ALDVETEEKVKQAVDELSHNRTTFII-AHRLSTV-RSADLVLFMDKGHLVESG 551
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILsTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
162-567 |
5.08e-21 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 98.06 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 162 LIVLGVIYVMIGQLVMrKTKDGQAAVEKHHHKLfehVSDTISNVSVVQSYnriaSETQALRDYAKNLENAQFPVLNWWAL 241
Cdd:TIGR01271 231 LILLALFQACLGQKMM-PYRDKRAGKISERLAI---TSEIIENIQSVKAY----CWEEAMEKIIKNIRQDELKLTRKIAY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 242 ASGLNRMASTFS--MVVVLVLGAYFVTKGQM--RVGDVIAFIGFVQLMIGRldQISAFIN---QTVTARAKLEEFFQMED 314
Cdd:TIGR01271 303 LRYFYSSAFFFSgfFVVFLSVVPYALIKGIIlrRIFTTISYCIVLRMTVTR--QFPGAIQtwyDSLGAITKIQDFLCKEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 315 atadrqepENVADLNDVKGDIVFDNVT----------FE----------FPNSGQGIY-------------DVSFEVKPG 361
Cdd:TIGR01271 381 --------YKTLEYNLTTTEVEMVNVTaswdegigelFEkikqnnkarkQPNGDDGLFfsnfslyvtpvlkNISFKLEKG 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 362 QTVAIVGPTGAGKTTLINLLQRVFDPAAGRImidgtdtrtvsRRSLRhaIATVFQDAGLFNRSVEDNIRVGRANATHEEV 441
Cdd:TIGR01271 453 QLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGR--ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYT 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 442 HAAAKAAAAHDfILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKV-KQAVDELSHN 520
Cdd:TIGR01271 520 SVIKACQLEED-IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSN 598
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 552148158 521 RTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLL 567
Cdd:TIGR01271 599 KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
353-549 |
6.69e-21 |
|
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: 91.73 E-value: 6.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSL----RHAIATVFQDAGLF-NRSVED 427
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSFQLLpTLTALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 NI-----RVGRANAtheevhaaakaaaahdFILAKSE----GydtfVGERG----SQLSGGERQRLAIARAILKDSPILV 494
Cdd:COG4181 110 NVmlpleLAGRRDA----------------RARARALlervG----LGHRLdhypAQLSGGEQQRVALARAFATEPAILF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 495 LDEATSALDVETEEKVKQAVDELshNR---TTFIIA-HRLSTVRSADLVLFMDKGHLVE 549
Cdd:COG4181 170 ADEPTGNLDAATGEQIIDLLFEL--NRergTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
353-558 |
1.16e-20 |
|
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: 91.07 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD--TRTVSRRSlRHAIATVFQDAGLFNR-SVEDNI 429
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitKLPMHKRA-RLGIGYLPQEASIFRKlTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 430 R-------VGRANATHEEVHAAAKAAAAHdfiLAKSegydtfvgeRGSQLSGGERQRLAIARAILKDSPILVLDEATSAL 502
Cdd:cd03218 97 LavleirgLSKKEREEKLEELLEEFHITH---LRKS---------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 503 DVETEEKVKQAVDELS----------HN-RTTFIIAHRLSTVRSadlvlfmdkGHLVESGSFNELAE 558
Cdd:cd03218 165 DPIAVQDIQKIIKILKdrgigvlitdHNvRETLSITDRAYIIYE---------GKVLAEGTPEEIAA 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
353-519 |
1.20e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.93 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDN---- 428
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNlifp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 429 --IRvgraNATHEEVHAAAKaaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDvet 506
Cdd:PRK10247 105 wqIR----NQQPDPAIFLDD--------LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD--- 169
|
170
....*....|...
gi 552148158 507 eEKVKQAVDELSH 519
Cdd:PRK10247 170 -ESNKHNVNEIIH 181
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
353-549 |
1.36e-20 |
|
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: 91.79 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTV---SRRSLRHAIATVFQDA-GLFN--RSVE 426
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDSpSAVNprMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 427 DNIRVGRANATH-EEVHAAAKAAAAHDFILAKSEGYDtfvgERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVE 505
Cdd:TIGR02769 109 QIIGEPLRHLTSlDESEQKARIAELLDMVGLRSEDAD----KLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552148158 506 TEEKVKQAVDELSHNRTT--FIIAHRLSTVRS-ADLVLFMDKGHLVE 549
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
353-551 |
1.41e-20 |
|
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: 90.67 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTdtrtvsrrslrhaIATVFQDAGLFNR--SVEDNIR 430
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-------------VSSLLGLGGGFNPelTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 431 -VGRA-NATHEEVHAAAkaaaahDFILAKSEGYDtFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEE 508
Cdd:cd03220 107 lNGRLlGLSRKEIDEKI------DEIIEFSELGD-FIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552148158 509 KVKQAVDELSHNRTTFIIA-HRLSTVRS-ADLVLFMDKGHLVESG 551
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
329-552 |
1.54e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.99 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 329 NDVKGDIVF--DNVTFEF----PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMI-------- 394
Cdd:PRK13631 14 NPLSDDIILrvKNLYCVFdekqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 395 -------DGTDTRTVSR-RSLRHAIATVFQ--DAGLFNRSVEDNIRVGRAN--ATHEEVHAAAKaaaahdFILAKSEGYD 462
Cdd:PRK13631 94 knnheliTNPYSKKIKNfKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPVAlgVKKSEAKKLAK------FYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 463 TFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAV-DELSHNRTTFIIAHRLSTV-RSADLVL 540
Cdd:PRK13631 168 SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVlEVADEVI 247
|
250
....*....|..
gi 552148158 541 FMDKGHLVESGS 552
Cdd:PRK13631 248 VMDKGKILKTGT 259
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
335-544 |
1.55e-20 |
|
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: 88.75 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRI-MIDGTDTRTVSRR------SL 407
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFLPQRpylplgTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 408 RHAIATVFQDAglfnrsvednirvgranatheevhaaakaaaahdfilaksegydtfvgergsqLSGGERQRLAIARAIL 487
Cdd:cd03223 81 REQLIYPWDDV-----------------------------------------------------LSGGEQQRLAFARLLL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 488 KDSPILVLDEATSALDVETEEKVKQAVDELShnrTTFI-IAHRLSTVRSADLVLFMDK 544
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELG---ITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-530 |
2.81e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.92 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TR-TVSRRSLRhaIATVFQD--AGLF-NRSVED 427
Cdd:COG1101 24 GLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvTKlPEYKRAKY--IGRVFQDpmMGTApSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 N--------------IRVGRANATH--EEvhaaakaaaahdfiLAKS----EGY-DTFVGergsQLSGGERQRLAIARAI 486
Cdd:COG1101 102 NlalayrrgkrrglrRGLTKKRRELfrEL--------------LATLglglENRlDTKVG----LLSGGQRQALSLLMAT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 552148158 487 LKDSPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRL 530
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
335-595 |
4.34e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.58 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEF-PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIAT 413
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQ--DAGLFNRSVEDNIRVGRAN--ATHEEVHAAAKAaaahdfILAKSEGYDTFVGERGSqLSGGERQRLAIARAILKD 489
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGLENhaVPYDEMHRRVSE------ALKQVDMLERADYEPNA-LSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 490 SPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLl 567
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEELTRI- 239
|
250 260
....*....|....*....|....*...
gi 552148158 568 ragGLKLedkqpkqpvvegsnvmPFPVK 595
Cdd:PRK13648 240 ---GLDL----------------PFPIK 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-556 |
9.24e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 9.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFD--PAA---GRIMIDGTDTRTVSRRSLRHAIATVFQDAG-LFNRSVED 427
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpIPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 NIRVG----RANATHEEVHAAAKAAaahdfiLAKSEGYDTF---VGERGSQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:PRK14247 102 NVALGlklnRLVKSKKELQERVRWA------LEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 501 ALDVETEEKVKQAVDELSHNRTTFIIAH-RLSTVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
335-579 |
9.65e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 9.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEF-PNS---GQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSR----RS 406
Cdd:PRK13643 2 IKFEKVNYTYqPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 407 LRHAIATVFQ--DAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEgydtFVGERGSQLSGGERQRLAIAR 484
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADE----FWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 485 AILKDSPILVLDEATSALDVETEEKVKQAVDELSHN-RTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGS----FNEL-- 556
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTpsdvFQEVdf 237
|
250 260 270
....*....|....*....|....*....|
gi 552148158 557 -------AERGGRFSDLLRAGGLKLEDKQP 579
Cdd:PRK13643 238 lkahelgVPKATHFADQLQKTGAVTFEKLP 267
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
335-552 |
1.13e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEF----PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSR----RS 406
Cdd:PRK13649 3 INLQNVSYTYqagtPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 407 LRHAIATVFQ--DAGLFNRSVEDNIRVGRAN--ATHEEVHAaakaaaahdfiLAKSE----GYDTFVGERGS-QLSGGER 477
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEA-----------LAREKlalvGISESLFEKNPfELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 478 QRLAIArAILKDSP-ILVLDEATSALDVETEEKVKQAVDELSHNRTTFI-IAHRLSTVRS-ADLVLFMDKGHLVESGS 552
Cdd:PRK13649 152 RRVAIA-GILAMEPkILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
351-552 |
1.40e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.53 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 351 IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIA------------TVFQDA 418
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAllpqhhltpegiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 419 G--------LFNR-SVEDNIRVGRA-NATHeevhaaakaaaahdfilaksegYDTFVGERGSQLSGGERQRLAIARAILK 488
Cdd:PRK11231 98 AygrspwlsLWGRlSAEDNARVNQAmEQTR----------------------INHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 489 DSPILVLDEATSALDVETEEKVKQAVDELSHN-RTTFIIAHRLSTV-RSADLVLFMDKGHLVESGS 552
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGT 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
339-574 |
1.68e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.14 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 339 NVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDG--TDTRTVSRRSLRHAIATVFQ 416
Cdd:PRK13636 10 ELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 417 DAG--LFNRSVEDNIRVGRANAT--HEEVHAAAkaaaahDFILAKSeGYDTFVGERGSQLSGGERQRLAIARAILKDSPI 492
Cdd:PRK13636 90 DPDnqLFSASVYQDVSFGAVNLKlpEDEVRKRV------DNALKRT-GIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 493 LVLDEATSALD-VETEEKVKQAVDELSHNRTTFIIA-HRLSTVR-SADLVLFMDKGHLVESGSFNEL-AERggrfsDLLR 568
Cdd:PRK13636 163 LVLDEPTAGLDpMGVSEIMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEVfAEK-----EMLR 237
|
....*.
gi 552148158 569 AGGLKL 574
Cdd:PRK13636 238 KVNLRL 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
339-564 |
2.52e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 90.28 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 339 NVTFEFpnSGQ-GIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSrrSLRHAIATVFQD 417
Cdd:PRK11607 24 NLTKSF--DGQhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 418 AGLF-NRSVEDNIRVG-------------RANATHEEVHAAAkaaaahdfilaksegydtFVGERGSQLSGGERQRLAIA 483
Cdd:PRK11607 100 YALFpHMTVEQNIAFGlkqdklpkaeiasRVNEMLGLVHMQE------------------FAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 484 RAILKDSPILVLDEATSALDVETEEKVK-QAVDELSH-NRTTFIIAH-RLSTVRSADLVLFMDKGHLVESGSFNELAER- 559
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHp 241
|
....*
gi 552148158 560 GGRFS 564
Cdd:PRK11607 242 TTRYS 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
330-552 |
2.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.53 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 330 DVKGDIVFDNVTFEF----PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIM-----IDGTDTR 400
Cdd:PRK13645 2 DFSKDIILDNVSYTYakktPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdyaIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 401 TVSRRSLRHAIATVFQ--DAGLFNRSVEDNIRVGRAN--ATHEEVHAAAKAAAahDFILAKSEgydtFVGERGSQLSGGE 476
Cdd:PRK13645 82 IKEVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNlgENKQEAYKKVPELL--KLVQLPED----YVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 477 RQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFII--AHRLSTV-RSADLVLFMDKGHLVESGS 552
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
353-549 |
3.99e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.43 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSR---RSLRHAIATVFQDA-GLFN--RSVE 426
Cdd:PRK10419 30 NVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRaqrKAFRRDIQMVFQDSiSAVNprKTVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 427 DNIR-----------VGRANATHEevhaaakaaaahdfILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVL 495
Cdd:PRK10419 110 EIIReplrhllsldkAERLARASE--------------MLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 496 DEATSALDVETEEKVKQAVDELSHNRTT--FIIAHRLSTV-RSADLVLFMDKGHLVE 549
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
353-528 |
4.12e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.06 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtdtRTVSRRSLRHAIatVFQDAGLFN-RSVEDNIRV 431
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG---KPVEGPGAERGV--VFQNEGLLPwRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 GRANATHEEVHAAAKAAAahdfILAKSeGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVK 511
Cdd:PRK11248 94 GLQLAGVEKMQRLEIAHQ----MLKKV-GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170
....*....|....*....
gi 552148158 512 QAVDELSHN--RTTFIIAH 528
Cdd:PRK11248 169 TLLLKLWQEtgKQVLLITH 187
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
335-556 |
5.28e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.45 E-value: 5.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQG-----IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRR-SLR 408
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 409 HAIATVFQ--DAGLFNRSVEDNIRVGRAN--ATHEEVHAAAkaaaahDFILAKSEGYDtFVGERGSQLSGGERQRLAIAR 484
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGPENlgIPPEEIRERV------DESLKKVGMYE-YRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552148158 485 AILKDSPILVLDEATSALDVETEEKVKQAVDELS--HNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNkkYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
160-530 |
7.74e-19 |
|
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: 91.13 E-value: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 160 LVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRiASETQALRDYAKNLENAqfpvlNWW 239
Cdd:TIGR01271 1029 IAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGR-QSYFETLFHKALNLHTA-----NWF 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 240 ALASGLNRMASTFSMVVVLV-LGAYFVTKGQMRVGDviAFIGF-VQLMIGRLDQISAFINQTVTARA---KLEEFFQMED 314
Cdd:TIGR01271 1103 LYLSTLRWFQMRIDIIFVFFfIAVTFIAIGTNQDGE--GEVGIiLTLAMNILSTLQWAVNSSIDVDGlmrSVSRVFKFID 1180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 315 ATADRQEPENVADLNDVKGDIVFDN--VTFEFPNSGQG----------------IYDVSFEVKPGQTVAIVGPTGAGKTT 376
Cdd:TIGR01271 1181 LPQEEPRPSGGGGKYQLSTVLVIENphAQKCWPSGGQMdvqgltakyteagravLQDLSFSVEGGQRVGLLGRTGSGKST 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 377 LINLLQRVFDpAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRvGRANATHEEVHAAAKAAAAHDFILA 456
Cdd:TIGR01271 1261 LLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQ 1338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552148158 457 KSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRL 530
Cdd:TIGR01271 1339 FPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
338-556 |
8.94e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.69 E-value: 8.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 338 DNVTFEFPNSG--QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVF 415
Cdd:PRK13642 8 ENLVFKYEKESdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 416 Q--DAGLFNRSVEDNIRVGRANathEEVHAAAKAAAAHDFILAKSegYDTFVGERGSQLSGGERQRLAIARAILKDSPIL 493
Cdd:PRK13642 88 QnpDNQFVGATVEDDVAFGMEN---QGIPREEMIKRVDEALLAVN--MLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 494 VLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
353-551 |
1.01e-18 |
|
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: 85.46 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTvSRRSLRHAIATVF-QDAGL-FNRSVEDNIR 430
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVFgQKTQLwWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 431 VGRANATHEEVHAAAKAAAAHDfILAKSEGYDTFVgergSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKV 510
Cdd:cd03267 118 LLAAIYDLPPARFKKRLDELSE-LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 552148158 511 KQAVDELSHNRTTFII--AHRLSTVRS-ADLVLFMDKGHLVESG 551
Cdd:cd03267 193 RNFLKEYNRERGTTVLltSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
22-304 |
1.14e-18 |
|
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: 86.72 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 22 ITMCVASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAAL----GGFNIMAAVFVARGADRLAHRRRLGVmidsYE 97
Cdd:cd18551 2 ILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALfllqAVLSALSSYLLGRTGERVVLDLRRRL----WR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 98 RLITMPLAWHQKRGTSNalhTLIRAT-DSlfTLWLEFMRQHLTTVVA-----LATLIpVAMTMDMRMSLVLI----VLGV 167
Cdd:cd18551 78 RLLRLPVSFFDRRRSGD---LVSRVTnDT--TLLRELITSGLPQLVTgvltvVGAVV-LMFLLDWVLTLVTLavvpLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 168 IYVMIGQLVMRKTKDGQAAVEKhhhkLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNR 247
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGE----LSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMG 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 248 MASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARA 304
Cdd:cd18551 228 LAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALG 284
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
353-556 |
1.21e-18 |
|
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: 85.52 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAG-RIMIDGTDTRTVSRRSLRHAIATVfqDAGLFNR-----SVE 426
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLV--SPALQLRfprdeTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 427 DNIR------VGR-ANATHEEVHAAAKaaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEAT 499
Cdd:COG1119 99 DVVLsgffdsIGLyREPTDEQRERARE--------LLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 500 SALDVETEEKVKQAVDELSHNRTTFII--AHRLStvrsaDL------VLFMDKGHLVESGSFNEL 556
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGAPTLVlvTHHVE-----EIppgithVLLLKDGRVVAAGPKEEV 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
351-567 |
1.42e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.99 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 351 IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFD-----PAAGRIMIDGTD--TRTVSRRSLRHAIATVFQDAGLFNR 423
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 424 SVEDNIRVG-RANATH----EEVHAAAKAAAAHDFILAKsegydtfVGERGSQLSGGERQRLAIARAILKDSPILVLDEA 498
Cdd:PRK14243 106 SIYDNIAYGaRINGYKgdmdELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 499 TSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTV-RSADLVLFmdkghlvesgsFN-ELAERGGRFSDLL 567
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAF-----------FNvELTEGGGRYGYLV 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
346-556 |
1.43e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.60 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 346 NSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFD-----PAAGRIMIDGTD-----TRTVSrrsLRHAIATVF 415
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiysprTDTVD---LRKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 416 QDAGLFNRSVEDNIRVG-RANATH------EEVHAAAKAAAAHDFIlaKSEGYDTFVGergsqLSGGERQRLAIARaILK 488
Cdd:PRK14239 93 QQPNPFPMSIYENVVYGlRLKGIKdkqvldEAVEKSLKGASIWDEV--KDRLHDSALG-----LSGGQQQRVCIAR-VLA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 489 DSP-ILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK14239 165 TSPkIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
320-558 |
1.50e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.97 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 320 QEPENVADLNDV---KGD-IVFDNVTFEFPNsgqgiydvsfevkpGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMID 395
Cdd:PRK11831 2 QSVANLVDMRGVsftRGNrCIFDNISLTVPR--------------GKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 396 GTDTRTVSRRSL---RHAIATVFQDAGLF-NRSVEDNIrvgrANATHEevHAAAKAAAAHDFILAKSEGydtfVGERG-- 469
Cdd:PRK11831 68 GENIPAMSRSRLytvRKRMSMLFQSGALFtDMNVFDNV----AYPLRE--HTQLPAPLLHSTVMMKLEA----VGLRGaa 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 470 ----SQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSH--NRTTFIIAHRLSTVRS-ADLVLFM 542
Cdd:PRK11831 138 klmpSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIV 217
|
250
....*....|....*.
gi 552148158 543 DKGHLVESGSFNELAE 558
Cdd:PRK11831 218 ADKKIVAHGSAQALQA 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
353-545 |
1.59e-18 |
|
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: 84.79 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMID----GTDTRTVSRRSL----RHAIATVFQdaglFNRS 424
Cdd:COG4778 29 GVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREIlalrRRTIGYVSQ----FLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 425 VEdniRVG---------RANATHEEVhaaakaaaahdfilAKSEGYDTF----VGERGSQL-----SGGERQRLAIARAI 486
Cdd:COG4778 105 IP---RVSaldvvaeplLERGVDREE--------------ARARARELLarlnLPERLWDLppatfSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 487 LKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFI-IAHRLSTV-RSADLVLFMDKG 545
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVReAVADRVVDVTPF 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
353-558 |
1.59e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.93 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtdtRTVSRRSLRHAIAT----VFQDAGLFNR-SVED 427
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRDAIALgigmVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 NI----------RVGRANATHEevhaaakaaaahdfILAKSEGY------DTFVGergsQLSGGERQRLAIARAILKDSP 491
Cdd:COG3845 100 NIvlgleptkggRLDRKAARAR--------------IRELSERYgldvdpDAKVE----DLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 492 ILVLDEATSAL-DVETEEkVKQAVDELSHNRTTFI-IAHRLSTVRS-ADLVLFMDKGHLVESG-----SFNELAE 558
Cdd:COG3845 162 ILILDEPTAVLtPQEADE-LFEILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVVGTVdtaetSEEELAE 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
339-574 |
2.02e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 339 NVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQ-- 416
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 417 DAGLFNRSVEDNIRVGRAN-ATHEEVHAAAKAAAAHDFilakseGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVL 495
Cdd:PRK13652 88 DDQIFSPTVEQDIAFGPINlGLDEETVAHRVSSALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 496 DEATSALDVETEEKVKQAVDELS--HNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNELAERggrfSDLLRAGGL 572
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPetYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ----PDLLARVHL 237
|
..
gi 552148158 573 KL 574
Cdd:PRK13652 238 DL 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
353-547 |
2.84e-18 |
|
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: 82.87 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTVSRRSLRHAIATVFQD---AGLF-NRSVED 427
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvTRRSPRDAIRAGIAYVPEDrkrEGLVlDLSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 NIRVGRanatheevhaaakaaaahdfilaksegydtfvgergsQLSGGERQRLAIARAILKDSPILVLDEATSALDVETE 507
Cdd:cd03215 98 NIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552148158 508 EKVKQAVDELSHNRTTFIIahrLST-----VRSADLVLFMDKGHL 547
Cdd:cd03215 141 AEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-552 |
3.52e-18 |
|
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: 87.82 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKT----TLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRH----AIATVFQDAG----- 419
Cdd:COG4172 28 GVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMtslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 420 LFnrSVEDNI--------RVGRANATHEEVHaaakaaaahdfILAKsegydtfVG----ER--GS---QLSGGERQRLAI 482
Cdd:COG4172 108 LH--TIGKQIaevlrlhrGLSGAAARARALE-----------LLER-------VGipdpERrlDAyphQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 483 ARAILKDSPILVLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGS 552
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqrELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
335-574 |
3.96e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.79 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATV 414
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAG--LFNRSVEDNIRVGRANA--THEEVHAAAKAAAahdfilaKSEGYDTFVGERGSQLSGGERQRLAIARAILKDS 490
Cdd:PRK13647 85 FQDPDdqVFSSTVWDDVAFGPVNMglDKDEVERRVEEAL-------KAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 491 PILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTVRS-ADLVLFMDKGHLVESGSFNELAERggrfsDLLR 568
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE-----DIVE 232
|
....*.
gi 552148158 569 AGGLKL 574
Cdd:PRK13647 233 QAGLRL 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
353-555 |
4.26e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.08 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVK---PGQTV-AIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGT---DTRtvSRRSL----RHaIATVFQDAGLF 421
Cdd:PRK11144 12 DLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAE--KGICLppekRR-IGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 422 -NRSVEDNIRVGRANATHEEvhaaakaaaahdfilaksegYDTFVGERG---------SQLSGGERQRLAIARAILKDSP 491
Cdd:PRK11144 89 pHYKVRGNLRYGMAKSMVAQ--------------------FDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDELSHNRTTFII--AHRLSTV-RSADLVLFMDKGHLVESGSFNE 555
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERLAREINIPILyvSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
26-302 |
4.40e-18 |
|
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: 84.92 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDI--FSPLLMWaaLGGFNIMAAVFVA-----------RGADRLahRRRLgvm 92
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTIIKGGDLdvLNELALI--LLAIYLLQSVFTFvryylfniageRIVARL--RRDL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 93 idsYERLITMPLAWHQKRGTSNALHTLIRATDSL---FTLWL-EFMRQHLTTVVALATLIpvamTMDMRMSLVLIVLGVI 168
Cdd:cd18557 76 ---FSSLLRQEIAFFDKHKTGELTSRLSSDTSVLqsaVTDNLsQLLRNILQVIGGLIILF----ILSWKLTLVLLLVIPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 169 YVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRiasETQALRDYAKNLENA-----QFPVLNwwALAS 243
Cdd:cd18557 149 LLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSA---EEKEIRRYSEALDRSyrlarKKALAN--ALFQ 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 244 GLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTA 302
Cdd:cd18557 224 GITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKA 282
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
351-566 |
5.07e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 351 IYDVSFEVKPGQTVAIVGPTGAGKTTLINLL-QRvfDPA----AGRIMIDGtdtRTVSRRSLRHAIATVFQDaGLFNRS- 424
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFR--SPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQD-DLFIPTl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 425 -VEDNI------RVGRANATHEEVHAAAKAAAahDFILAKSEgyDTFVGERGSQ--LSGGERQRLAIARAILKDSPILVL 495
Cdd:TIGR00955 115 tVREHLmfqahlRMPRRVTKKEKRERVDEVLQ--ALGLRKCA--NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552148158 496 DEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLST--VRSADLVLFMDKGHLVESGSFNELAErggRFSDL 566
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP---FFSDL 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
353-552 |
6.76e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFdPAAGRIMIDGTDTRTVSRRSL---RHAIATVFQDAglfNRSVEDNI 429
Cdd:PRK15134 304 NISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---NSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 430 RVGRANATHEEVHAAAKAAAAHD--FILAKSE-GYDTFVGER-GSQLSGGERQRLAIARAILKDSPILVLDEATSALDVE 505
Cdd:PRK15134 380 NVLQIIEEGLRVHQPTLSAAQREqqVIAVMEEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 552148158 506 TEEKVKQAVDEL--SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGS 552
Cdd:PRK15134 460 VQAQILALLKSLqqKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGD 509
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
353-540 |
7.37e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.90 E-value: 7.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDT------RTVSRRSL----RHAIAT-VFQDAGLF 421
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpqRSEVPDSLpltvRDLVAMgRWARRGLW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 422 NR-SVEDNIRVGRAnatHEEVhaaakaaaahdfilakseGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:NF040873 90 RRlTRDDRAAVDDA---LERV------------------GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552148158 501 ALDVETEEKVKQAVDELSH-NRTTFIIAHRLSTVRSADLVL 540
Cdd:NF040873 149 GLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCV 189
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
353-545 |
8.83e-18 |
|
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: 82.38 E-value: 8.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRI----MIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDN 428
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 429 IRVGRANATHEEVHAAAKAAAAHDFILAkSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEE 508
Cdd:cd03290 99 ITFGSPFNKQRYKAVTDACSLQPDIDLL-PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552148158 509 KVKQA-VDELSHN--RTTFIIAHRLSTVRSADLVLFMDKG 545
Cdd:cd03290 178 HLMQEgILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-562 |
1.07e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.00 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDtrtvSRRSLRHAIATVFQDAGLF-NRSVEDNIR- 430
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP----LDPEDRRRIGYLPEERGLYpKMKVGEQLVy 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 431 ------VGRANATHEEvhaaakaaaahDFILAKSEgydtfVGERG----SQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:COG4152 95 larlkgLSKAEAKRRA-----------DEWLERLG-----LGDRAnkkvEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 501 ALDVETEEKVKQAVDELSHNRTTfII--AHRLSTV-RSADLVLFMDKGHLVESGSFNELAERGGR 562
Cdd:COG4152 159 GLDPVNVELLKDVIRELAAKGTT-VIfsSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
353-547 |
1.35e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.17 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS---RRSLR-HAIATVFQDAGL---FNrSV 425
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRnQKLGFIYQFHHLlpdFT-AL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 426 ED--------NIRVGRANATHEEvhaaakaaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAiLKDSPILVL-D 496
Cdd:PRK11629 106 ENvamplligKKKPAEINSRALE--------------MLAAVGLEHRANHRPSELSGGERQRVAIARA-LVNNPRLVLaD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 497 EATSALDVETEEKVKQAVDELSHNRTT--FIIAHRLSTVRSADLVLFMDKGHL 547
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-558 |
1.52e-17 |
|
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: 86.01 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRI-------MIDGTDTRTVSRRSLRHAIATVFQDAGLF-NRSV 425
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 426 EDNI----------RVGRANATHeevhaaakaaaahdfiLAKSEGYD-----TFVGERGSQLSGGERQRLAIARAILKDS 490
Cdd:TIGR03269 383 LDNLteaiglelpdELARMKAVI----------------TLKMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 491 PILVLDEATSALDVETEEKVKQAV----DELshNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNELAE 558
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSIlkarEEM--EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
335-552 |
1.97e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.98 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDtrtVSRRSLR-HAIAT 413
Cdd:PRK10851 3 IEIANIKKSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTD---VSRLHARdRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQDAGLFNR-SVEDNIRVG--------RANAtheevhaaakaaaahDFILAKSEGYDTFV-----GER-GSQLSGGERQ 478
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGltvlprreRPNA---------------AAIKAKVTQLLEMVqlahlADRyPAQLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 479 RLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELsHNR---TTFIIAH-RLSTVRSADLVLFMDKGHLVESGS 552
Cdd:PRK10851 144 RVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQL-HEElkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
354-552 |
2.33e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLinlLQRV--FDPAAGRIMIDGTDTRTVSRRSLRH------------AIATVFQDAG 419
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTL---LARMagLLPGQGEILLNGRPLSDWSAAELARhraylsqqqsppFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 420 LFnrsvednirvGRANATHEEVHAAAKAaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSP-------I 492
Cdd:COG4138 92 LH----------QPAGASSEAVEQLLAQ-------LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPtinpegqL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 493 LVLDEATSALDVETEEKVKQAVDELSH-NRTTFIIAHRLS-TVRSADLVLFMDKGHLVESGS 552
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
26-302 |
2.76e-17 |
|
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: 82.47 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDIFspLLMWAAL---------GGFNIMAAVFVARGADRLAH--RRRLgvmid 94
Cdd:cd18552 6 LGMILVAATTAALAWLLKPLLDDIFVEKDLE--ALLLVPLaiiglfllrGLASYLQTYLMAYVGQRVVRdlRNDL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 95 sYERLITMPLAWHQKRGTSNALHTLI----RATDSLFTLWLEFMRQHLTTVVALATLIpvamTMDMRMSLVLIVLG--VI 168
Cdd:cd18552 79 -FDKLLRLPLSFFDRNSSGDLISRITndvnQVQNALTSALTVLVRDPLTVIGLLGVLF----YLDWKLTLIALVVLplAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 169 YVM--IGQLVMRKTKDGQAAVEKhhhkLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLN 246
Cdd:cd18552 154 LPIrrIGKRLRKISRRSQESMGD----LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLM 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 247 RMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIG---RLDQISAFINQTVTA 302
Cdd:cd18552 230 ELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQpikRLSNVNANLQRGLAA 288
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
351-559 |
2.92e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.84 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 351 IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSlRHaIATVFQDAGLF-NRSVEDNI 429
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH-VNTVFQSYALFpHMTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 430 RVG-RANAT-HEEVHAAAKAAAAhdfiLAKSEGydtFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETE 507
Cdd:PRK09452 108 AFGlRMQKTpAAEITPRVMEALR----MVQLEE---FAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 508 ekvKQAVDELSH-NRT---TFI-IAH----RLSTvrsADLVLFMDKGHLVESGSFNELAER 559
Cdd:PRK09452 181 ---KQMQNELKAlQRKlgiTFVfVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
354-545 |
3.34e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTVSRRSLRHAIATVFQDAGLFNR-SVEDNIRV 431
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiEGLPGHQIARMGVVRTFQHVRLFREmTVIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 grANATHEEVHAAAKAAAAHDFILAKSEGYD------------TFVGERGSQLSGGERQRLAIARAILKDSPILVLDEAT 499
Cdd:PRK11300 104 --AQHQQLKTGLFSGLLKTPAFRRAESEALDraatwlervgllEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 552148158 500 SALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRS-ADLVLFMDKG 545
Cdd:PRK11300 182 AGLNPKETKELDELIAELrnEHNVTVLLIEHDMKLVMGiSDRIYVVNQG 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
353-497 |
3.50e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.23 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTT----LINLLQrvfdPAAGRIMIDGTD-TR-TVSRRSlRHAIATVFQDAGLFNR-SV 425
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDiTHlPMHKRA-RLGIGYLPQEASIFRKlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 426 EDNI-------------RVGRANATHEEVHaaakaaAAHdfiLAKSegydtfvgeRGSQLSGGERQRLAIARAILKDSPI 492
Cdd:COG1137 96 EDNIlavlelrklskkeREERLEELLEEFG------ITH---LRKS---------KAYSLSGGERRRVEIARALATNPKF 157
|
....*
gi 552148158 493 LVLDE 497
Cdd:COG1137 158 ILLDE 162
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
26-286 |
3.80e-17 |
|
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: 82.07 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAAL--------GGFNIMAAVFVARGADRLAH--RRRLgvmids 95
Cdd:cd18541 6 LFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLilllalliGIFRFLWRYLIFGASRRIEYdlRNDL------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 96 YERLITMPLAWHQKRGTSNalhtLI-RAT-DslftlwLEFMRQ-------HLTTVVALATLIPVAM-TMDMRMSLV---- 161
Cdd:cd18541 80 FAHLLTLSPSFYQKNRTGD----LMaRATnD------LNAVRMalgpgilYLVDALFLGVLVLVMMfTISPKLTLIallp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 162 LIVLGVIYVMIGQLVMRKTKDGQAAVEKhhhkLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWAL 241
Cdd:cd18541 150 LPLLALLVYRLGKKIHKRFRKVQEAFSD----LSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDAL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 552148158 242 ASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMI 286
Cdd:cd18541 226 FFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLI 270
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
335-551 |
5.01e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.06 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEF----PNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRI------------------ 392
Cdd:PRK13651 3 IKVKNIVKIFnkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 393 -MIDGTDTRTVSRR-----SLRHAIATVFQDA--GLFNRSVEDNIRVGRAN--ATHEEVhaaakaaaahdfiLAKSEGYD 462
Cdd:PRK13651 83 vLEKLVIQKTRFKKikkikEIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmgVSKEEA-------------KKRAAKYI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 463 TFVG------ERGS-QLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA-HRLSTV- 533
Cdd:PRK13651 150 ELVGldesylQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVtHDLDNVl 229
|
250
....*....|....*...
gi 552148158 534 RSADLVLFMDKGHLVESG 551
Cdd:PRK13651 230 EWTKRTIFFKDGKIIKDG 247
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-561 |
6.08e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.06 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtdtRTVSRRSLRHA--IATVFqdaGlfNRS------ 424
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKRRKEFArrIGVVF---G--QRSqlwwdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 425 -VEDNIRVGRA-----NATHEE-VHAAAKAAAAHDFIlaksegyDTFVgeRgsQLSGGERQRLAIARAILKDSPILVLDE 497
Cdd:COG4586 112 pAIDSFRLLKAiyripDAEYKKrLDELVELLDLGELL-------DTPV--R--QLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 498 ATSALDVETEEKVKQAVDELSHNR-TTFIIA-HRLSTV-RSADLVLFMDKGHLVESGSFNELAERGG 561
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIeALCDRVIVIDHGRIIYDGSLEELKERFG 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
335-525 |
7.28e-17 |
|
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: 77.49 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNsGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTrtvsrrslrhaIATV 414
Cdd:cd03221 1 IELENLSKTYGG-KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-----------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 fqdaglfnrsvednirvgranatheevhaaakaaaahdfilaksegydtfvgergSQLSGGERQRLAIARAILKDSPILV 494
Cdd:cd03221 69 -------------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 552148158 495 LDEATSALDVETEEKVKQAVDEL-------SHNRtTFI 525
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYpgtvilvSHDR-YFL 130
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
333-521 |
8.39e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVF--DNVTFEFPnsGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIdGTDTRtvsrrslrh 409
Cdd:COG0488 312 GKKVLelEGLSKSYG--DKTLLdDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 410 aIATVFQDAGLF--NRSVEDNIRVGRANATHEEVHAaakaaaahdfILA----KSEGYDTFVGErgsqLSGGERQRLAIA 483
Cdd:COG0488 380 -IGYFDQHQEELdpDKTVLDELRDGAPGGTEQEVRG----------YLGrflfSGDDAFKPVGV----LSGGEKARLALA 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 552148158 484 RAILKDSPILVLDEATSALDVETEEKVKQAVDE-------LSHNR 521
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtvllVSHDR 489
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
353-514 |
9.13e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.45 E-value: 9.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINL----LQRVFDpAAGRIMIDGTDTRTVSRRsLRHaIATVFQDAGLF-NRSVED 427
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAiagtLSPAFS-ASGEVLLNGRRLTALPAE-QRR-IGILFQDDLLFpHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 NI------RVGRAN--ATHEEVhaaakaaaahdfiLAKSeGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEAT 499
Cdd:COG4136 96 NLafalppTIGRAQrrARVEQA-------------LEEA-GLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170
....*....|....*
gi 552148158 500 SALDVETEEKVKQAV 514
Cdd:COG4136 162 SKLDAALRAQFREFV 176
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
337-558 |
1.31e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 337 FDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTR-TVSRRSLRHAIATVF 415
Cdd:PRK11288 7 FDGIGKTFPGV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 416 QDAGLF-NRSVEDNIRVGRANATHEEVHAAAKAAAAHDFIlaKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILV 494
Cdd:PRK11288 86 QELHLVpEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQL--EHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 495 LDEATSALDVETEEKVKQAVDEL-SHNRTTFIIAHRLSTV-RSADLVLFMDKGHLVEsgSFNELAE 558
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDMAQ 227
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
20-307 |
1.58e-16 |
|
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: 80.27 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 20 ATITMCVAsVLVALVALAEPVLFGRVIQSISDKGDIFSPLLmWAALggfnIMAAVFVAR-----GADRLAHRRRLGVMID 94
Cdd:cd18778 1 LILTLLCA-LLSTLLGLVPPWLIRELVDLVTIGSKSLGLLL-GLAL----LLLGAYLLRallnfLRIYLNHVAEQKVVAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 95 S----YERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVV----------------ALATLIPVamtm 154
Cdd:cd18778 75 LrsdlYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLtlvgvaiilfsinpklALLTLIPI---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 155 dmrmsLVLIVLGVIYVMIGQLVMRKTKDGQAAvekhhhkLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFP 234
Cdd:cd18778 151 -----PFLALGAWLYSKKVRPRYRKVREALGE-------LNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLR 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 235 VLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLE 307
Cdd:cd18778 219 AMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAE 291
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-556 |
1.66e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.70 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 342 FEFPNSGQGIYD-VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFD-----PAAGRIMIDGTDT--RTVSRRSLRHAIAT 413
Cdd:PRK14258 13 LSFYYDTQKILEgVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLNRLRRQVSM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQDAGLFNRSVEDNIRVG-RANATHEEVHAAAKAAAAhdfiLAKSEGYDTF---VGERGSQLSGGERQRLAIARAILKD 489
Cdd:PRK14258 93 VHPKPNLFPMSVYDNVAYGvKIVGWRPKLEIDDIVESA----LKDADLWDEIkhkIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 490 SPILVLDEATSALDVETEEKVKQAVD--ELSHNRTTFIIAHRLSTV-RSADLVLFMDK-----GHLVESGSFNEL 556
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
354-514 |
3.74e-16 |
|
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: 77.15 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVsRRSLRHAIATVFQDAGLFNR-SVEDNIRVG 432
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-RDSIARGLLYLGHAPGIKTTlSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 433 RANATHEEVHaaakaaaahdfilaksEGYDTfVGERG------SQLSGGERQRLAIARAILKDSPILVLDEATSALDVET 506
Cdd:cd03231 98 HADHSDEQVE----------------EALAR-VGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
....*...
gi 552148158 507 EEKVKQAV 514
Cdd:cd03231 161 VARFAEAM 168
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
348-551 |
3.88e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.43 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 348 GQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS---------RRSLRHAIATVFQDA 418
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseaerRRLLRTEWGFVHQHP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 419 --GL-FNRSVEDNI-----RVG-------RANATHeevhaaakaaaahdfILAKSEGYDTFVGERGSQLSGGERQRLAIA 483
Cdd:PRK11701 99 rdGLrMQVSAGGNIgerlmAVGarhygdiRATAGD---------------WLERVEIDAARIDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552148158 484 RAiLKDSPILVL-DEATSALDVETEEK----VKQAVDELshNRTTFIIAHRLSTVR-SADLVLFMDKGHLVESG 551
Cdd:PRK11701 164 RN-LVTHPRLVFmDEPTGGLDVSVQARlldlLRGLVREL--GLAVVIVTHDLAVARlLAHRLLVMKQGRVVESG 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
333-556 |
5.66e-16 |
|
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: 78.36 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVFDNVTFEFPNSGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDpAAGRIMIDGTDTRTVSRRSLRHAI 411
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLeNISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 ATVFQDAGLFNRSVEDNIRvGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSP 491
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
346-569 |
5.82e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.13 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 346 NSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVF--DPAAG-RIMIDGtdtRTVSR--------RSLRHAIATV 414
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGsHIELLG---RTVQRegrlardiRKSRANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLFNR-SVEDNIRVGRANAT---HEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDS 490
Cdd:PRK09984 92 FQQFNLVNRlSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 491 PILVLDEATSALDVETEEKVKQAVDELSHNR--TTFIIAHRLS-TVRSADLVLFMDKGHLVESGSFNELAERggRFSDLL 567
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNE--RFDHLY 249
|
..
gi 552148158 568 RA 569
Cdd:PRK09984 250 RS 251
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
325-556 |
6.04e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 79.37 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 325 VADLNdVKGDIVFDNVTF-EFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS 403
Cdd:PRK15079 11 VADLK-VHFDIKDGKQWFwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 404 ---RRSLRHAIATVFQD--AGLFNR-SVEDNI----RVGRANATHEEVHAAAKAaaahdfILAKSEGYDTFVGERGSQLS 473
Cdd:PRK15079 90 ddeWRAVRSDIQMIFQDplASLNPRmTIGEIIaeplRTYHPKLSRQEVKDRVKA------MMLKVGLLPNLINRYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 474 GGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNR--TTFIIAHRLSTVRS-ADLVLFMDKGHLVES 550
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVEL 243
|
....*.
gi 552148158 551 GSFNEL 556
Cdd:PRK15079 244 GTYDEV 249
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
353-508 |
6.72e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.84 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATvfQDAGLFNRSVEDNIRVG 432
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGH--RNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 433 RA--NATHEEVHAAAKAAAAHDfILAKSEGYdtfvgergsqLSGGERQRLAIARAILKDSPILVLDEATSALDVETEE 508
Cdd:PRK13539 98 AAflGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
337-506 |
7.90e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.49 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 337 FDNVTFEFPnsGQGIY-DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtDTRtvsrrslrhaIATVF 415
Cdd:COG0488 1 LENLSKSFG--GRPLLdDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 416 QDAGLF-NRSVEDNIR--VGRANATHEEVHAAAKAAAAHDFILAK----------SEGYDT------------FVGERG- 469
Cdd:COG0488 68 QEPPLDdDLTVLDTVLdgDAELRALEAELEELEAKLAEPDEDLERlaelqeefeaLGGWEAearaeeilsglgFPEEDLd 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 552148158 470 ---SQLSGGERQRLAIARAILKDSPILVLDEATSALDVET 506
Cdd:COG0488 148 rpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-556 |
8.93e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.83 E-value: 8.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 326 ADLNDVKGDIVFDNVTFEFpnSGQGIYD-VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAG-----------RIM 393
Cdd:PRK14271 13 ADVDAAAPAMAAVNLTLGF--AGKTVLDqVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggRSI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 394 IDGTDTRTVSRRslrhaIATVFQDAGLFNRSVEDNIRVG-RAnatHEEVHAAAKAAAAHDFIlaKSEGYDTFVGERGS-- 470
Cdd:PRK14271 91 FNYRDVLEFRRR-----VGMLFQRPNPFPMSIMDNVLAGvRA---HKLVPRKEFRGVAQARL--TEVGLWDAVKDRLSds 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 471 --QLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLS-TVRSADLVLFMDKGHL 547
Cdd:PRK14271 161 pfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRL 240
|
....*....
gi 552148158 548 VESGSFNEL 556
Cdd:PRK14271 241 VEEGPTEQL 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
335-551 |
1.13e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLrhaIATV 414
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGL---FNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDtFVGERGSQLSGGERQRLAIARAILKDSP 491
Cdd:PRK15056 84 PQSEEVdwsFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVE-FRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDEL-SHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESG 551
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
353-556 |
1.26e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.86 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS-RRSLRHAIATVFQDAGLFNR-SVEDNI- 429
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSVYDNLm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 430 -------------RVGRANATHEEVHAAAKAAAAhdfilaksegydtfvgerGSQLSGGERQRLAIARAILKDSPILVLD 496
Cdd:PRK10895 101 avlqirddlsaeqREDRANELMEEFHIEHLRDSM------------------GQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 497 EATSALDVETEEKVKQAVDEL-SHNRTTFIIAHRL-STVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLrDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
335-556 |
3.80e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATV 414
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLFNR-SVEDNIRVGR--------ANATHEEVHAAAKAAAAHDFilaksegYDTFVGErgsqLSGGERQRLAIARA 485
Cdd:COG4604 81 RQENHINSRlTVRELVAFGRfpyskgrlTAEDREIIDEAIAYLDLEDL-------ADRYLDE----LSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 486 ILKDSPILVLDEATSALD----VETEEKVKQAVDELshNRTTFIIAHRLS-TVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADEL--GKTVVIVLHDINfASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
335-543 |
3.81e-15 |
|
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: 78.64 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDgTDTRT--------VSRRS 406
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP-AKGKLfyvpqrpyMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 407 LRHAIatVFQDaglfnrSVEDNIRVGRANATHEEVhaaaKAAAAHDFILAKSEGYDTfVGERGSQLSGGERQRLAIARAI 486
Cdd:TIGR00954 531 LRDQI--IYPD------SSEDMKRRGLSDKDLEQI----LDNVQLTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLF 597
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 487 LKDSPILVLDEATSALDVETEEKVKQAVDELshNRTTFIIAHRLSTVRSADLVLFMD 543
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
354-556 |
4.46e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.39 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTV-------------SRRSLRHAIATVFQDAGL 420
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 421 FNR-SVEDNIR--------VGRANATHEEVhaaakaaaahdFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSP 491
Cdd:PRK10619 104 WSHmTVLENVMeapiqvlgLSKQEARERAV-----------KYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDELSHN-RTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
354-516 |
6.27e-15 |
|
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: 73.55 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVsRRSLRHAIATVFQDAGLFNR-SVEDNIRVG 432
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLGHLPGLKPElSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 433 RANATHEEvhaaakaAAAHDfILAKsegydtfVGERG------SQLSGGERQRLAIARAILKDSPILVLDEATSALDVET 506
Cdd:TIGR01189 98 AAIHGGAQ-------RTIED-ALAA-------VGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170
....*....|
gi 552148158 507 EEKVKQAVDE 516
Cdd:TIGR01189 163 VALLAGLLRA 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-558 |
7.17e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 351 IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFD--PAA---GRIMIDGTD--TRTVSRRSLRHAIATVFQDAGLF-N 422
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPFpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 423 RSVEDNIRVG-RANATheeVHAAAKAAAAHDFILAKSEGYDTF---VGERGSQLSGGERQRLAIARAILKDSPILVLDEA 498
Cdd:PRK14267 100 LTIYDNVAIGvKLNGL---VKSKKELDERVEWALKKAALWDEVkdrLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 499 TSALDVETEEKVKQAVDELSHNRTTFIIAHR-LSTVRSADLVLFMDKGHLVESGSFNELAE 558
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
353-559 |
7.39e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.61 E-value: 7.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSlRHAIATVFQDAGLF-NRSVEDNIRV 431
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVPQFDNLDpDFTVRENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 -GR-----ANATHEEVHAAAKaaaahdfiLAKSEG-YDTFVGErgsqLSGGERQRLAIARAILKDSPILVLDEATSALDV 504
Cdd:PRK13537 104 fGRyfglsAAAARALVPPLLE--------FAKLENkADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 505 ETE----EKVKQAvdeLSHNRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNELAER 559
Cdd:PRK13537 172 QARhlmwERLRSL---LARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
353-559 |
9.10e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 73.33 E-value: 9.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQ-----RVFDpaaGRIMIDGTDTR--TVSRRSLrhaiatvfqdAGL---FN 422
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpkyEVTE---GEILFKGEDITdlPPEERAR----------LGIflaFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 423 RSVE-DNIRVGranatheevhaaakaaaahDFILAKSEGydtfvgergsqLSGGERQRLAIARAILKDSPILVLDEATSA 501
Cdd:cd03217 85 YPPEiPGVKNA-------------------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 502 LDVETEEKVKQAVDEL-SHNRTTFIIAH--RLSTVRSADLVLFMDKGHLVESGSFnELAER 559
Cdd:cd03217 135 LDIDALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDK-ELALE 194
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
338-556 |
1.20e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.67 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 338 DNVTFEFPNSGQG---IYDVSFEVKPGQTVAIVGPTGAGKT-TLINLLQRVFDPAA----GRIMIDGTDTRTVSRRSLRH 409
Cdd:PRK15134 9 ENLSVAFRQQQTVrtvVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 410 A----IATVFQDAGL-FN--RSVEDNI-------RVGRANATHEEvhaaakaaaahdfILAKSEGydtfVGERGS----- 470
Cdd:PRK15134 89 VrgnkIAMIFQEPMVsLNplHTLEKQLyevlslhRGMRREAARGE-------------ILNCLDR----VGIRQAakrlt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 471 ----QLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSH--NRTTFIIAHRLSTVRS-ADLVLFMD 543
Cdd:PRK15134 152 dyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQ 231
|
250
....*....|...
gi 552148158 544 KGHLVESGSFNEL 556
Cdd:PRK15134 232 NGRCVEQNRAATL 244
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
353-547 |
1.34e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMidgtdTRTVSRRSLRHAIATVFQDAGLFN-RSVEDNIRV 431
Cdd:PRK11247 30 QLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLLPwKKVIDNVGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 G-----RANATH--EEVhaaakaaaahdfilakseGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDV 504
Cdd:PRK11247 105 GlkgqwRDAALQalAAV------------------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 552148158 505 ETEEKVKQAVDEL--SHNRTTFIIAHRLS-TVRSADLVLFMDKGHL 547
Cdd:PRK11247 167 LTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
349-548 |
1.47e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 349 QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTVSRRSLRHAIATVFQDAGLFNR-SVE 426
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAVAIVPEGRRVFSRmTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 427 DNIRVGRANATHEEVHAAAKAAaahdfilaksegYDTF--VGERGSQ----LSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:PRK11614 99 ENLAMGGFFAERDQFQERIKWV------------YELFprLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 552148158 501 ALDVETEEKVKQAVDEL-SHNRTTFIIAHRLS-TVRSADLVLFMDKGHLV 548
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLrEQGMTIFLVEQNANqALKLADRGYVLENGHVV 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
333-521 |
1.94e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.53 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVFD--NVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIdGTDTRTVSRRSLRHA 410
Cdd:PRK11147 316 GKIVFEmeNVNYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IatvfqDAglfNRSVEDNIRVGRanathEEVhaAAKAAAAH------DFIlaksegydtFVGERGSQ----LSGGERQRL 480
Cdd:PRK11147 394 L-----DP---EKTVMDNLAEGK-----QEV--MVNGRPRHvlgylqDFL---------FHPKRAMTpvkaLSGGERNRL 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 552148158 481 AIARAILKDSPILVLDEATSALDVETEEKVKQAVDE-------LSHNR 521
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSyqgtvllVSHDR 497
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
353-545 |
2.07e-14 |
|
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: 72.88 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtdtRTVSRRSLRHAIatVFQDAGLFN-RSVEDNI-- 429
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQITEPGPDRMV--VFQNYSLLPwLTVRENIal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 430 RVGRANATHEEVHAAAKAAAAHDFIlakseGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEK 509
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIVEEHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 552148158 510 VKQAVDEL--SHNRTTFIIAHRL-STVRSADLVLFMDKG 545
Cdd:TIGR01184 153 LQEELMQIweEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
353-548 |
2.66e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.92 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSL----RHAIATVFQDAGLFNR-SVED 427
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 NIRVGRANATHEEVHAAAKAAAahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETE 507
Cdd:PRK10535 106 NVEVPAVYAGLERKQRLLRAQE-----LLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552148158 508 EKVKQAVDEL-SHNRTTFIIAHRLSTVRSADLVLFMDKGHLV 548
Cdd:PRK10535 181 EEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
335-551 |
3.16e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTD-TRTVSRRSLRHAIAT 413
Cdd:PRK09700 6 ISMAGIGKSFGPV-HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINyNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 414 VFQDAGLFNR-SVEDNIRVGRanatHEEVHAAAKAAAAHDFILAKSE----------GYDTFVGErgsqLSGGERQRLAI 482
Cdd:PRK09700 85 IYQELSVIDElTVLENLYIGR----HLTKKVCGVNIIDWREMRVRAAmmllrvglkvDLDEKVAN----LSISHKQMLEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 483 ARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFI-IAHRLSTVRS-ADLVLFMDKGHLVESG 551
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
353-552 |
3.44e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.90 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDG--TDTRTVSRRSLRhaIATVFQDAG----------- 419
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQR--IRMIFQDPStslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 420 ------LFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKsegydtfvgergsqlsgGERQRLAIARAILKDSPIL 493
Cdd:PRK15112 109 ildfplRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAP-----------------GQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 494 VLDEATSALDVETEEKVKQAVDEL--SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGS 552
Cdd:PRK15112 172 IADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
353-558 |
5.24e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.59 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMidgtdtrtvSRRSlrhaIATVFQDAGLFNRSVEDNIRV- 431
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---------AERS----IAYVPQQAWIMNATVRGNILFf 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 --GRANATHEEVHAAAKAAAahdfiLAK-SEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEE 508
Cdd:PTZ00243 745 deEDAARLADAVRVSQLEAD-----LAQlGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 552148158 509 KVkqaVDELS----HNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAE 558
Cdd:PTZ00243 820 RV---VEECFlgalAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
354-556 |
5.87e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtdtRTVSRRSLRHA----IATVFQDAGLF-NRSVEDN 428
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG---NPCARLTPAKAhqlgIYLVPQEPLLFpNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 429 IRVG--RANATHEEVHAAAKAAAAHdFILAKSEGydtfvgergsQLSGGERQRLAIARAILKDSPILVLDEATSALD-VE 505
Cdd:PRK15439 107 ILFGlpKRQASMQKMKQLLAALGCQ-LDLDSSAG----------SLEVADRQIVEILRGLMRDSRILILDEPTASLTpAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 552148158 506 TEEKVKQAVDELSHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK15439 176 TERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
353-556 |
6.39e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGL-FNRSVEDniRV 431
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQE--LV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 GRANATHEEVHAAAKAAAAHDFILA-KSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKV 510
Cdd:PRK10253 103 ARGRYPHQPLFTRWRKEDEEAVTKAmQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 552148158 511 KQAVDELSHNR--TTFIIAHRLS-TVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK10253 183 LELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEI 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
337-578 |
7.97e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 74.16 E-value: 7.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 337 FDNVTFEFPNSGQGIY-----DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTvsrrslrhAI 411
Cdd:PRK13545 21 FDKLKDLFFRSKDGEYhyalnNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI--------AI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 412 AtvfqdAGLFNR-SVEDNIRVG--RANATHEEVHAAAKAAAAHDFIlaksegyDTFVGERGSQLSGGERQRLAIARAILK 488
Cdd:PRK13545 93 S-----SGLNGQlTGIENIELKglMMGLTKEKIKEIIPEIIEFADI-------GKFIYQPVKTYSSGMKSRLGFAISVHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 489 DSPILVLDEATSALDVETEEKVKQAVDELSHN-RTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNELAERGGRFsdL 566
Cdd:PRK13545 161 NPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEF--L 238
|
250
....*....|..
gi 552148158 567 LRAGGLKLEDKQ 578
Cdd:PRK13545 239 KKYNQMSVEERK 250
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
353-559 |
9.67e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 71.25 E-value: 9.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLL--QRVFDPAAGRIMIDGTD--TRTVSRRSlRHAIATVFQD----AGLfnrS 424
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDilELSPDERA-RAGIFLAFQYpveiPGV---S 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 425 VEDNIRVGrANATHEEvhaAAKAAAAHDFILAKSE--GYDTFVGERG--SQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:COG0396 94 VSNFLRTA-LNARRGE---ELSAREFLKLLKEKMKelGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 501 ALDVETEEKVKQAVDEL-SHNRTTFIIAH--RLSTVRSADLVLFMDKGHLVESGSFnELAER 559
Cdd:COG0396 170 GLDIDALRIVAEGVNKLrSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-ELALE 230
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
26-297 |
1.33e-13 |
|
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: 71.69 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDifSPLLMWAALG--GFNIMAAVFV-------ARGADRLAHRRRLgvmiDSY 96
Cdd:cd18542 6 LALLLATALNLLIPLLIRRIIDSVIGGGL--RELLWLLALLilGVALLRGVFRylqgylaEKASQKVAYDLRN----DLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 97 ERLITMPLAWHQKRGTSNalhtLI-RATDSLFTLW-------LEFMRQHLTTVVALATLipvaMTMDMRMSLVLIVLGVI 168
Cdd:cd18542 80 DHLQRLSFSFHDKARTGD----LMsRCTSDVDTIRrflafglVELVRAVLLFIGALIIM----FSINWKLTLISLAIIPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 169 YVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRM 248
Cdd:cd18542 152 IALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDF 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 552148158 249 ASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFIN 297
Cdd:cd18542 232 LSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLIN 280
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
354-552 |
1.35e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFdPAAGRIMIDGTDTRTVSRRSL-RHAIATVFQDAGLFNRSVEDNIRVG 432
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 433 RANATHEEVHAAAKAAaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSP-------ILVLDEATSALDVE 505
Cdd:PRK03695 94 QPDKTRTEAVASALNE------VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDVA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 552148158 506 TEEKVKQAVDELSHNRTTFIIA-HRLS-TVRSADLVLFMDKGHLVESGS 552
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASGR 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
351-556 |
1.43e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.88 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 351 IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPA----AGRIMIDGTdtrTVSRRSLR-HAIATVFQDAglfnRSV 425
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK---PVAPCALRgRKIATIMQNP----RSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 426 EDNIRVGRANATheEVHAAAKAAAAHDFILAKSEGY-----DTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:PRK10418 92 FNPLHTMHTHAR--ETCLALGKPADDATLTAALEAVglenaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 501 ALDVETEEKVKQAVDELSHNRT--TFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-559 |
1.84e-13 |
|
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: 72.91 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRV--FDPAAGRIM------------------- 393
Cdd:TIGR03269 1 IEVKNLTKKFDGK-EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 394 --------------IDGTDTRTVSRRSLRHAIATVFQDA-GLF-NRSVEDNI-------------RVGRANATHEEVHAA 444
Cdd:TIGR03269 80 epcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTfALYgDDTVLDNVlealeeigyegkeAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 445 AKAAaaHdfiLAKsegydtfvgergsQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDEL-SHNRTT 523
Cdd:TIGR03269 160 HRIT--H---IAR-------------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGIS 221
|
250 260 270
....*....|....*....|....*....|....*...
gi 552148158 524 FIIAHRLSTVRS--ADLVLFMDKGHLVESGSFNELAER 559
Cdd:TIGR03269 222 MVLTSHWPEVIEdlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
333-527 |
3.22e-13 |
|
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: 72.28 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIV--FDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDgtdtRTV-------S 403
Cdd:TIGR03719 319 GDKVieAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETVklayvdqS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 404 RRSLrHAIATVFQD--AGLfnrsveDNIRVGRAnatheEVhaaakaaaahdfilaKSEGYDTFVGERGS-------QLSG 474
Cdd:TIGR03719 394 RDAL-DPNKTVWEEisGGL------DIIKLGKR-----EI---------------PSRAYVGRFNFKGSdqqkkvgQLSG 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 475 GERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDE-------LSHNR------TTFIIA 527
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNfagcavvISHDRwfldriATHILA 512
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
22-304 |
3.44e-13 |
|
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: 70.51 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 22 ITMCVASVLVALVALAEPVLFGRVIQSISDKGDI-----FSPLLMWAA-LGGFNIMAAVF-------VARGADRLAHRRR 88
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGgggvdFSGLLRILLlLLGLYLLSALFsylqnrlMARVSQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 89 lgvmIDSYERLITMPLAW--HQKRGtsnalHTLIRAT---DSLFtlwlEFMRQHLTTVV-ALATLIPVAMTM---DMRMS 159
Cdd:cd18547 82 ----KDLFEKLQRLPLSYfdTHSHG-----DIMSRVTndvDNIS----QALSQSLTQLIsSILTIVGTLIMMlyiSPLLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 160 LVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRiasETQALRDYAK-NLE------NAQ 232
Cdd:cd18547 149 LIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNR---EEEAIEEFDEiNEElykasfKAQ 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 233 FpvlnwwalASGL----NRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARA 304
Cdd:cd18547 226 F--------YSGLlmpiMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALA 293
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
338-556 |
3.68e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.82 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 338 DNVTFEFPNSGQgIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQD 417
Cdd:PRK10575 15 RNVSFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 418 ----AGLfnrSVEDNIRVGR----------ANATHEEVHAAAKAAaahdfilakseGYDTFVGERGSQLSGGERQRLAIA 483
Cdd:PRK10575 94 lpaaEGM---TVRELVAIGRypwhgalgrfGAADREKVEEAISLV-----------GLKPLAHRLVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 484 RAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIA--HRLS-TVRSADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
335-503 |
4.23e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.03 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINL---LQRVfdpAAGRIMIDGtdtRTVSRRSLR-HA 410
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGG---RVVNELEPAdRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IATVFQDAGLF-NRSVEDNI-------RVGRA--NATHEEVhaaakaaaahdfilAKSEGYDTFVGERGSQLSGGERQRL 480
Cdd:PRK11650 78 IAMVFQNYALYpHMSVRENMayglkirGMPKAeiEERVAEA--------------ARILELEPLLDRKPRELSGGQRQRV 143
|
170 180
....*....|....*....|...
gi 552148158 481 AIARAILKDSPILVLDEATSALD 503
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
324-556 |
4.45e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 324 NVADLNDVkgdIVFDNVTFEFPNSGQ---GIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTR 400
Cdd:PRK10261 5 DELDARDV---LAVENLNIAFMQEQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 401 TVSR-------------RSLRHA-IATVFQDAGL-------FNRSVEDNIRVGRaNATHEEVHAAAKAAAAHDFIlAKSE 459
Cdd:PRK10261 82 RRSRqvielseqsaaqmRHVRGAdMAMIFQEPMTslnpvftVGEQIAESIRLHQ-GASREEAMVEAKRMLDQVRI-PEAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 460 gydTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRT--TFIIAHRLSTVRS-A 536
Cdd:PRK10261 160 ---TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiA 236
|
250 260
....*....|....*....|
gi 552148158 537 DLVLFMDKGHLVESGSFNEL 556
Cdd:PRK10261 237 DRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
26-303 |
5.01e-13 |
|
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: 69.82 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDIFSplLMWAALggfnIMAAVFVARGADRLAHRRRLGVM---------IDSY 96
Cdd:cd18576 3 ILLLLSSAIGLVFPLLAGQLIDAALGGGDTAS--LNQIAL----LLLGLFLLQAVFSFFRIYLFARVgervvadlrKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 97 ERLITMPLAWHQKRGT-------SNALhTLIRATdslFTLWL-EFMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVI 168
Cdd:cd18576 77 RHLQRLPLSFFHERRVgeltsrlSNDV-TQIQDT---LTTTLaEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 169 YVMIGQLVMRKTKDGQAAVEKhhhkLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRM 248
Cdd:cd18576 153 AVLFGRRIRKLSKKVQDELAE----ANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 249 ASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTAR 303
Cdd:cd18576 229 LLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKAL 283
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
26-302 |
7.16e-13 |
|
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: 69.46 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVI--QSISDKGDIFSPLLMW--AALGGFNIMAAVF-VARG------ADRLAH--RRRLgvm 92
Cdd:cd18563 6 LLMLLGTALGLVPPYLTKILIddVLIQLGPGGNTSLLLLlvLGLAGAYVLSALLgILRGrllarlGERITAdlRRDL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 93 idsYERLITMPLAWHQKRGTSNALHTLIRATDSL---FTLWLEFMRQHLTTVVALATLIpvaMTMDMRMSLvLIVLGVIY 169
Cdd:cd18563 83 ---YEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLqdfLSDGLPDFLTNILMIIGIGVVL---FSLNWKLAL-LVLIPVPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 170 VMIGQLVMRKtkdgqaAVEKHHHKLFE-------HVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALA 242
Cdd:cd18563 156 VVWGSYFFWK------KIRRLFHRQWRrwsrlnsVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 243 SGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLD---QISAFINQTVTA 302
Cdd:cd18563 230 FPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQwlsRLNNWITRALTS 292
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
335-559 |
9.51e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 9.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATV 414
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLFNRSVE------DNIRVGRANATHEEVHAAakaaaahdfilaksegydTFVGERGS--QLSGGERQRLAIARAI 486
Cdd:PRK10522 403 FTDFHLFDQLLGpegkpaNPALVEKWLERLKMAHKL------------------ELEDGRISnlKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 487 LKDSPILVLDEatsaldveteekvkQAVDELSHNR----------------TTFIIAHRLSTVRSADLVLFMDKGHLVE- 549
Cdd:PRK10522 465 AEERDILLLDE--------------WAADQDPHFRrefyqvllpllqemgkTIFAISHDDHYFIHADRLLEMRNGQLSEl 530
|
250
....*....|
gi 552148158 550 SGSFNELAER 559
Cdd:PRK10522 531 TGEERDAASR 540
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
339-533 |
1.33e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 339 NVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFdPAA---GRIMIDGTDTRTVS-RRSLRHAIATV 414
Cdd:PRK13549 10 NITKTFGGV-KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNiRDTERAGIAII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLF-NRSVEDNIRVGRANATHEEVHAAAKAAAAHDfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPIL 493
Cdd:PRK13549 88 HQELALVkELSVLENIFLGNEITPGGIMDYDAMYLRAQK--LLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 552148158 494 VLDEATSALdveTEEKVKQAVDEL----SHNRTTFIIAHRLSTV 533
Cdd:PRK13549 166 ILDEPTASL---TESETAVLLDIIrdlkAHGIACIYISHKLNEV 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
354-526 |
1.53e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTV---SRRSLR-HAIATVFQD-------AGLFN 422
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRaKHVGFVFQSfmliptlNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 423 RSVEDNIRVGRANATHEEVHAaakaaaahdfiLAKSEGydtfVGER----GSQLSGGERQRLAIARAILKDSPILVLDEA 498
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKA-----------LLEQLG----LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180
....*....|....*....|....*...
gi 552148158 499 TSALDVETEEKVKQAVDELSHNRTTFII 526
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHGTTLI 201
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
353-549 |
1.99e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIAtvfqDAGLFNRSVEDNIRVG 432
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIG----RKGDFKDAVELLNAVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 433 RANATheevhaaakaaaahdFILAKSegydtfvgergSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQ 512
Cdd:COG2401 124 LSDAV---------------LWLRRF-----------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552148158 513 AVDELSH-NRTTFIIAHRLSTVRSA---DLVLFMDKGHLVE 549
Cdd:COG2401 178 NLQKLARrAGITLVVATHHYDVIDDlqpDLLIFVGYGGVPE 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
354-569 |
2.59e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.23 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTT-------LINLLQRVfdpAAGRIMIDGTDTRTVS---RRSLRHA-IATVFQDAGL-F 421
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGRV---MAEKLEFNGQDLQRISekeRRNLVGAeVAMIFQDPMTsL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 422 NRSVEDNIRVGRANATHEEVHAAAKAAAAHDFIlaksegydTFVG--ERGS-------QLSGGERQRLAIARAILKDSPI 492
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLL--------NQVGipDPASrldvyphQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 493 LVLDEATSALDVETEEKVKQAVDELSH--NRTTFIIAHRLSTV-RSADLVLFMDKGHLVESGSFNEL--AERGGRFSDLL 567
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIfrAPRHPYTQALL 254
|
..
gi 552148158 568 RA 569
Cdd:PRK11022 255 RA 256
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
17-314 |
2.92e-12 |
|
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: 67.86 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 17 ERTATITMCVASVLVALVALAEPVLFGRVIQSIS--------DKGDIFSplLMWAALGG----FNIMAAVFVARGADRLA 84
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSlpdddelrSEANFWA--LMFLVLAIvagiAYFLQGYLFGIAGERLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 85 HRRRLgvmiDSYERLITMPLAWH-QKRGTSNAL-HTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVL 162
Cdd:cd18578 85 RRLRK----LAFRAILRQDIAWFdDPENSTGALtSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 163 IVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRiasETQALRDYAKNLENAQ---FPVLNWW 239
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTL---EDYFLEKYEEALEEPLkkgLRRALIS 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 240 ALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDV-IAFIGFVQ--LMIGrldQISAFINQTVTARAKLEEFFQMED 314
Cdd:cd18578 238 GLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFfIVFMALIFgaQSAG---QAFSFAPDIAKAKAAAARIFRLLD 312
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
22-307 |
3.01e-12 |
|
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: 67.51 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 22 ITMCVASVLV-ALVALAEPVLFGRVIQSISDKGDifSPLLMWAALGGFNIMAAVFVARGAD-----RLAHRRRLGVMIDS 95
Cdd:cd18546 1 LALALLLVVVdTAASLAGPLLVRYGIDSGVRAGD--LGVLLLAAAAYLAVVLAGWVAQRAQtrltgRTGERLLYDLRLRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 96 YERLITMPLAWHQkRGTSNALHTliRAT---DSLftlwLEFMRQHLTT-VVALATLIPVAMTM---DMRMSLVLIVLGVI 168
Cdd:cd18546 79 FAHLQRLSLDFHE-RETSGRIMT--RMTsdiDAL----SELLQTGLVQlVVSLLTLVGIAVVLlvlDPRLALVALAALPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 169 YVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRM 248
Cdd:cd18546 152 LALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVEL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 249 ASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLE 307
Cdd:cd18546 232 LGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALE 290
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
347-554 |
4.14e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 347 SGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS-RRSLRHAIATVFQDA---GL-F 421
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdGLvL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 422 NRSVEDNI----------RVGRANATHEEvhaaakaAAAHDFILA---KSEGYDTFVGErgsqLSGGERQRLAIARAILK 488
Cdd:PRK10762 344 GMSVKENMsltalryfsrAGGSLKHADEQ-------QAVSDFIRLfniKTPSMEQAIGL----LSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552148158 489 DSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIahrlstVRS--------ADLVLFMDKGHLveSGSFN 554
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL------VSSempevlgmSDRILVMHEGRI--SGEFT 478
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
344-528 |
4.33e-12 |
|
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: 66.28 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 344 FPNSGQGIYDVSFEVKPG-----QTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDT----------RTVSRRSLR 408
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyikadYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 409 HAIATVFQDAGLFNRSVEDNIRVgranathEEVhaaakaaaahdfilaksegYDTFVGErgsqLSGGERQRLAIARAILK 488
Cdd:cd03237 83 SSITKDFYTHPYFKTEIAKPLQI-------EQI-------------------LDREVPE----LSGGELQRVAIAACLSK 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552148158 489 DSPILVLDEATSALDVETEEKVKQAVDE--LSHNRTTFIIAH 528
Cdd:cd03237 133 DADIYLLDEPSAYLDVEQRLMASKVIRRfaENNEKTAFVVEH 174
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
353-517 |
5.35e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVsRRSLRHAIATVFQDAGLFNR-SVEDNIRV 431
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQDLLYLGHQPGIKTElTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 grANATHEEVHAAAKAAaahdfILAKsegydtfVGERG------SQLSGGERQRLAIARAILKDSPILVLDEATSALDve 505
Cdd:PRK13538 98 --YQRLHGPGDDEALWE-----ALAQ-------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID-- 161
|
170
....*....|..
gi 552148158 506 teekvKQAVDEL 517
Cdd:PRK13538 162 -----KQGVARL 168
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
317-551 |
5.43e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 317 ADRQEPENVADlNDVKGDIVFD--NVTFEFP-NSG---------QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRV 384
Cdd:PRK10261 295 PAKQEPPIEQD-TVVDGEPILQvrNLVTRFPlRSGllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 385 FDPAAGRIMIDGTDTRTVSRR---SLRHAIATVFQD--AGLFNR-----SVEDNIRV---GRANATHEEVhaaakaaaah 451
Cdd:PRK10261 374 VESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDpyASLDPRqtvgdSIMEPLRVhglLPGKAAAARV---------- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 452 DFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNR--TTFIIAHR 529
Cdd:PRK10261 444 AWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHD 523
|
250 260
....*....|....*....|...
gi 552148158 530 LSTV-RSADLVLFMDKGHLVESG 551
Cdd:PRK10261 524 MAVVeRISHRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
26-298 |
7.92e-12 |
|
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: 66.32 E-value: 7.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDIfSPLLMWAAlggfnIMAAVFVARGA-----DRLAHRrrLGVMI------D 94
Cdd:cd18549 9 FCAVLIAALDLVFPLIVRYIIDDLLPSKNL-RLILIIGA-----ILLALYILRTLlnyfvTYWGHV--MGARIetdmrrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 95 SYERLITMPLAWHQKRGTSnalHTLIRATDSLFtlWLEFMRQHL--TTVVALATLIP-VAMTMDMRMSLVLIVLGVIYVM 171
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTG---QLMSRITNDLF--DISELAHHGpeDLFISIITIIGsFIILLTINVPLTLIVFALLPLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 172 I--GQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMA 249
Cdd:cd18549 156 IifTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFF 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 552148158 250 STFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQ 298
Cdd:cd18549 236 TNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQ 284
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
346-504 |
9.62e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 346 NSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS-RRSLRHAIATVFQD---AGLF 421
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPEDrkgEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 422 -NRSVEDNI------RVGRANAtheeVHAAAKAAAAHDFI--LA-KSEGYDTFVGergsQLSGGERQRLAIARAILKDSP 491
Cdd:COG1129 343 lDLSIRENItlasldRLSRGGL----LDRRRERALAEEYIkrLRiKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPK 414
|
170
....*....|...
gi 552148158 492 ILVLDEATSALDV 504
Cdd:COG1129 415 VLILDEPTRGIDV 427
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
358-530 |
1.04e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 358 VKPGQTVAIVGPTGAGKTTLINLLqrvfdpaAGRIMID-GTDTRTVSR-RSLRHAIATVFQDagLFNRSVEDNIRV---- 431
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELIPNlGDYEEEPSWdEVLKRFRGTELQN--YFKKLYNGEIKVvhkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 -----------GRANATHEEVHAAAKAAAahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:PRK13409 167 qyvdlipkvfkGKVRELLKKVDERGKLDE-----VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|
gi 552148158 501 ALDVETEEKVKQAVDELSHNRTTFIIAHRL 530
Cdd:PRK13409 242 YLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
358-530 |
1.42e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 358 VKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHA-IATVFQDAGLF-NRSVEDNIRVGRAN 435
Cdd:PRK10762 27 VYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIpQLTIAENIFLGREF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 436 ATH------EEVHAAAkaaaahDFILAK---SEGYDTFVGErgsqLSGGERQRLAIARAILKDSPILVLDEATSAL-DVE 505
Cdd:PRK10762 107 VNRfgridwKKMYAEA------DKLLARlnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
|
170 180
....*....|....*....|....*.
gi 552148158 506 TEEKVKqAVDEL-SHNRTTFIIAHRL 530
Cdd:PRK10762 177 TESLFR-VIRELkSQGRGIVYISHRL 201
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
327-556 |
1.62e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 327 DLNDVKgDIvfdNVTFEFPNSG-QGIYDVSFEVKPGQTVAIVGPTGAGKT----TLINLLQrvfdpAAGRI----MIDGT 397
Cdd:PRK09473 11 ALLDVK-DL---RVTFSTPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA-----ANGRIggsaTFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 398 DTRTVSRRSLR----HAIATVFQDAglfNRSVEDNIRVGRANATHEEVHAAakaaaahdfiLAKSEGYDTFV-------- 465
Cdd:PRK09473 82 EILNLPEKELNklraEQISMIFQDP---MTSLNPYMRVGEQLMEVLMLHKG----------MSKAEAFEESVrmldavkm 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 466 -------GERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFI--IAHRLSTVR-S 535
Cdd:PRK09473 149 pearkrmKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIimITHDLGVVAgI 228
|
250 260
....*....|....*....|.
gi 552148158 536 ADLVLFMDKGHLVESGSFNEL 556
Cdd:PRK09473 229 CDKVLVMYAGRTMEYGNARDV 249
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
360-544 |
1.99e-11 |
|
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: 62.39 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 360 PGQTVAIVGPTGAGKTTLINLLQRVFDPAAGR-IMIDGTDTRTVSRRSLRHAIatvfqdaglfnrsvednirvgranath 438
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 439 eevhaaakaaaahdfilaksegydtfVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVD--- 515
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|...
gi 552148158 516 ----ELSHNRTTFIIAHRLSTVRSADLVLFMDK 544
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
357-528 |
2.21e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 357 EVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDgtdtRTVSRRS--LRHAI-ATVfqdaGLFNRSVEDNIRvgr 433
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISYKPqyIKPDYdGTV----EDLLRSITDDLG--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 434 anatheevhaaaKAAAAHDFI--LAKSEGYDTFVGErgsqLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVK 511
Cdd:PRK13409 430 ------------SSYYKSEIIkpLQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
|
170
....*....|....*....
gi 552148158 512 QAVDELSHNR--TTFIIAH 528
Cdd:PRK13409 494 KAIRRIAEEReaTALVVDH 512
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
22-301 |
2.39e-11 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 64.86 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 22 ITMCVASVLVALValaePVLFGRVIQSIS--DKGDIFSPLLMWAALGGFNIMAAVFVARGA-----DRLAhRRRLGVMid 94
Cdd:cd18583 3 LCLLAERVLNVLV----PRQLGIIVDSLSggSGKSPWKEIGLYVLLRFLQSGGGLGLLRSWlwipvEQYS-YRALSTA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 95 SYERLITMPLAWHQKRGTSNALHTLIRATD-SLFTLWLEFmrQHLTTVVAL-ATLIPVAMTMDMRMSLVLIVLGVIYVMI 172
Cdd:cd18583 76 AFNHVMNLSMDFHDSKKSGEVLKAIEQGSSiNDLLEQILF--QIVPMIIDLvIAIVYLYYLFDPYMGLIVAVVMVLYVWS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 173 GQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASET----QALRDYAKnlenAQFPVLNWWALASGLNRM 248
Cdd:cd18583 154 TIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKeryrEAVKNYQK----AERKYLFSLNLLNAVQSL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 249 ASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVT 301
Cdd:cd18583 230 ILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQS 282
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
22-307 |
2.44e-11 |
|
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: 64.80 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 22 ITMCVASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVF-------VARGADRLAH--RRRLgvm 92
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVAsrlriylMAKVGQRILYdlRQDL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 93 idsYERLITMPLAWHQKRGTSNALHTLIRATDSLftlwLEFMRQHLTTVVA-LATL--IPVAM-TMDMRMSLV-LIVLGV 167
Cdd:cd18545 80 ---FSHLQKLSFSFFDSRPVGKILSRVINDVNSL----SDLLSNGLINLIPdLLTLvgIVIIMfSLNVRLALVtLAVLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 168 IYVMIGQLvmrktkdgqaavEKHHHKLFEHVSDTISNVS-----------VVQSYNRiASETQALRDyAKNLENaqfpvL 236
Cdd:cd18545 153 LVLVVFLL------------RRRARKAWQRVRKKISNLNaylhesisgirVIQSFAR-EDENEEIFD-ELNREN-----R 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 237 NWWALASGLN-------RMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLE 307
Cdd:cd18545 214 KANMRAVRLNalfwplvELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAE 291
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
353-503 |
3.19e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.85 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSrRSLRHAIATVFQdaglFNR-----SVED 427
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQ----FDNldlefTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 428 NIRV-GRANATH----EEVhaaakAAAAHDFILAKSEGyDTfvgeRGSQLSGGERQRLAIARAILKDSPILVLDEATSAL 502
Cdd:PRK13536 134 NLLVfGRYFGMStreiEAV-----IPSLLEFARLESKA-DA----RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
.
gi 552148158 503 D 503
Cdd:PRK13536 204 D 204
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
21-307 |
3.29e-11 |
|
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: 64.43 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 21 TITMCVASVLVALVALAEPVLFGRVIQSISDKGDiFSPLLMWA-ALGGFNIMAAVF-------VARGADRLAHRRRLGVm 92
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGD-RSALWPLVlLLLALGVAEAVLsflrrylAGRLSLGVEHDLRTDL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 93 idsYERLITMPLAWHQK--------RGTSNAlhTLIRAtdslftlWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVLIV 164
Cdd:cd18543 79 ---FAHLQRLDGAFHDRwqsgqllsRATSDL--SLVQR-------FLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 165 LGVIYVMIGQL-------VMRKTKDGQAAVEkhhhklfEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVL- 236
Cdd:cd18543 147 SLPPLVLVARRfrrryfpASRRAQDQAGDLA-------TVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAAr 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552148158 237 ---NWWALASGLnrmaSTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLE 307
Cdd:cd18543 220 lraRFWPLLEAL----PELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAE 289
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
335-552 |
3.78e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAG---------------RIMIDGTDT 399
Cdd:PRK09544 5 VSLENVSVSFGQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGvikrngklrigyvpqKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 400 RTVSR-RSLRHAIatvfqdaglfnRSVEDNIRVGRANATHeevhaaakaaaAHDFILAKsegydtfvgergsqLSGGERQ 478
Cdd:PRK09544 84 LTVNRfLRLRPGT-----------KKEDILPALKRVQAGH-----------LIDAPMQK--------------LSGGETQ 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 479 RLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSH--NRTTFIIAHRLSTVRS-ADLVLFMDkGHLVESGS 552
Cdd:PRK09544 128 RVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMAkTDEVLCLN-HHICCSGT 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-532 |
5.91e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 359 KPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMiDGTDTRTVsrrsLRHAIATVFQDagLFNRSVEDNIRV------- 431
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD-EEPSWDEV----LKRFRGTELQD--YFKKLANGEIKVahkpqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 --------GRANAtheevhaaakaaaahdfILAKsegydtfVGERG-------------------SQLSGGERQRLAIAR 484
Cdd:COG1245 170 dlipkvfkGTVRE-----------------LLEK-------VDERGkldelaeklglenildrdiSELSGGELQRVAIAA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 552148158 485 AILKDSPILVLDEATSALDVETEEKVKQAVDELS-HNRTTFIIAHRLST 532
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAeEGKYVLVVEHDLAI 274
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
353-559 |
6.97e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 62.66 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLqrVFDPA----AGRIMIDGTDTRTVS--RRSlRHAIATVFQD----AGLfn 422
Cdd:TIGR01978 18 GVNLTVKKGEIHAIMGPNGSGKSTLSKTI--AGHPSyevtSGTILFKGQDLLELEpdERA-RAGLFLAFQYpeeiPGV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 423 rSVEDNIRVGrANA-THEEVHAAAKAAAAHDFILAKSE--GYDTFVGERGSQ--LSGGERQRLAIARAILKDSPILVLDE 497
Cdd:TIGR01978 93 -SNLEFLRSA-LNArRSARGEEPLDLLDFEKLLKEKLAllDMDEEFLNRSVNegFSGGEKKRNEILQMALLEPKLAILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 498 ATSALDVETEEKVKQAVDEL-SHNRTTFIIAH--RLSTVRSADLVLFMDKGHLVESGSFnELAER 559
Cdd:TIGR01978 171 IDSGLDIDALKIVAEGINRLrEPDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSGDV-ELAKE 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
333-521 |
6.98e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIV--FDNVTFEFpnsgqG----IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIdGTdtrTV---- 402
Cdd:PRK11819 321 GDKVieAENLSKSF-----GdrllIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE---TVklay 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 403 ---SRRSLrHAIATVFQD--AGLfnrsveDNIRVGRAnatheEVhaaakaaaahdfilaKSEGYDTFVGERGS------- 470
Cdd:PRK11819 392 vdqSRDAL-DPNKTVWEEisGGL------DIIKVGNR-----EI---------------PSRAYVGRFNFKGGdqqkkvg 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 471 QLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDE-------LSHNR 521
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEfpgcavvISHDR 502
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
25-298 |
7.39e-11 |
|
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: 63.56 E-value: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 25 CVASVLVALVALAEPVLFGRVI-QSISDKGDIFSPLLMWAAL-GGFNIMAAVF-------VARGADRLAHRRRlgvmIDS 95
Cdd:cd18544 5 LLLLLLATALELLGPLLIKRAIdDYIVPGQGDLQGLLLLALLyLGLLLLSFLLqylqtylLQKLGQRIIYDLR----RDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 96 YERLITMPLAWHQKrgtsNALHTLI-RAT---DSLFTLWLEFMRQHLTTVVALATLIpVAM-TMDMRMSLV-LIVLGVIY 169
Cdd:cd18544 81 FSHIQRLPLSFFDR----TPVGRLVtRVTndtEALNELFTSGLVTLIGDLLLLIGIL-IAMfLLNWRLALIsLLVLPLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 170 VMIgQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMA 249
Cdd:cd18544 156 LAT-YLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 552148158 250 STFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQ 298
Cdd:cd18544 235 SSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNI 283
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-531 |
7.63e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.77 E-value: 7.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 358 VKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMiDGTDTRTVsrrsLRHAIATVFQDagLFNRSVEDNIRV------ 431
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEI----LDEFRGSELQN--YFTKLLEGDVKVivkpqy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 ---------GRANATHEEVHAAAKAAaahdfILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSAL 502
Cdd:cd03236 96 vdlipkavkGKVGELLKKKDERGKLD-----ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|
gi 552148158 503 DVETEEKVKQAVDELS-HNRTTFIIAHRLS 531
Cdd:cd03236 171 DIKQRLNAARLIRELAeDDNYVLVVEHDLA 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
347-547 |
1.14e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 347 SGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtdtRTVSRRSLRHAIAT--VF-----QDAG 419
Cdd:PRK15439 275 TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG---KEINALSTAQRLARglVYlpedrQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 420 LF-NRSVEDN------------IRVGRANATHEEVHAAakaaaahdfILAKSEGYDTFVGergsQLSGGERQRLAIARAI 486
Cdd:PRK15439 352 LYlDAPLAWNvcalthnrrgfwIKPARENAVLERYRRA---------LNIKFNHAEQAAR----TLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 487 LKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFI-IAHRLSTVRS-ADLVLFMDKGHL 547
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
356-505 |
1.54e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 356 FEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRslRHaIATVFQDAGL-FNRSVEDNIRVgrA 434
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--RF-MAYLGHLPGLkADLSTLENLHF--L 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 435 NATHEEVHAAAKAAAAHDFILAKSEgyDTFVgergSQLSGGERQRLAIARAILKDSPILVLDEATSALDVE 505
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAIVGLAGYE--DTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
339-510 |
3.64e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 339 NVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTR-TVSRRSLRHAIATVFQD 417
Cdd:PRK10982 3 NISKSFPGV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 418 AGLF-NRSVEDNIRVGRanatheevHAAAKAAAAHDFILAKSE------GYDTFVGERGSQLSGGERQRLAIARAILKDS 490
Cdd:PRK10982 82 LNLVlQRSVMDNMWLGR--------YPTKGMFVDQDKMYRDTKaifdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180
....*....|....*....|
gi 552148158 491 PILVLDEATSALdveTEEKV 510
Cdd:PRK10982 154 KIVIMDEPTSSL---TEKEV 170
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
26-304 |
3.85e-10 |
|
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: 61.43 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDIFSPL----------------------LMWAALGGFNIMAAVFVARGADRL 83
Cdd:cd18565 6 LASILNRLFDLAPPLLIGVAIDAVFNGEASFLPLvpaslgpadprgqlwllggltvAAFLLESLFQYLSGVLWRRFAQRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 84 AHRRRLgvmiDSYERLITMPLAWHQKRGTSNALHTL---IRATDSLFTLWLEFMRQHLTTVV-------------ALATL 147
Cdd:cd18565 86 QHDLRT----DTYDHVQRLDMAFFEDRQTGDLMSVLnndVNQLERFLDDGANSIIRVVVTVLgigailfylnwqlALVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 148 IPVamtmdmrmslVLIVLGVIYVMigQLVMRKTKDGQAAVEKhhhkLFEHVSDTISNVSVVQSYNRIASETQALRDYAKN 227
Cdd:cd18565 162 LPV----------PLIIAGTYWFQ--RRIEPRYRAVREAVGD----LNARLENNLSGIAVIKAFTAEDFERERVADASEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 228 LENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKG------QMRVGDVIAFIGFVQLMIGRLDQISAFINQTVT 301
Cdd:cd18565 226 YRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQR 305
|
...
gi 552148158 302 ARA 304
Cdd:cd18565 306 AMA 308
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
308-545 |
3.86e-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: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 308 EFFQMEDATADRQEPENVADLNDVKGDIVFD--NVTFEFPNSG---QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLL- 381
Cdd:TIGR00956 731 EVLGSTDLTDESDDVNDEKDMEKESGEDIFHwrNLTYEVKIKKekrVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLa 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 382 QRVfdpaAGRIMIDGtdTRTVSRRSLRHAIATVF-----QDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFI-L 455
Cdd:TIGR00956 811 ERV----TTGVITGG--DRLVNGRPLDSSFQRSIgyvqqQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIkL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 456 AKSEGY-DTFVGERGSQLSGGERQRLAIA-RAILKDSPILVLDEATSALDVETEEKVKQAVDELS-HNRTTFIIAHRLST 532
Cdd:TIGR00956 885 LEMESYaDAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLAdHGQAILCTIHQPSA 964
|
250
....*....|....*
gi 552148158 533 VRSA--DLVLFMDKG 545
Cdd:TIGR00956 965 ILFEefDRLLLLQKG 979
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
360-547 |
4.85e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 360 PGQTVAIVGPTGAGKTTLINLLqrvfdpaAGRIMIDG------TDTRTVSRRSLRHaIATVFQDAGLF-NRSVEDNI--- 429
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNftgtilANNRKPTKQILKR-TGFVTQDDILYpHLTVRETLvfc 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 430 ---RVGRANATHEEVhaAAKAAAAHDFILAKSEgyDTFVGE---RGsqLSGGERQRLAIARAILKDSPILVLDEATSALD 503
Cdd:PLN03211 165 sllRLPKSLTKQEKI--LVAESVISELGLTKCE--NTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 504 VETEEKVKQAVDELSHNRTTFIIA-HRLST----------VRSADLVLFMDKGHL 547
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSmHQPSSrvyqmfdsvlVLSEGRCLFFGKGSD 293
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
357-528 |
5.35e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.11 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 357 EVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMID----------GTDT-RTVsRRSLRHAIATVFQDAGLFNRSV 425
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyiSPDYdGTV-EEFLRSANTDDFGSSYYKTEII 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 426 E----DNIrvgranatheevhaaakaaaahdfilaksegYDTFVGErgsqLSGGERQRLAIARAILKDSPILVLDEATSA 501
Cdd:COG1245 441 KplglEKL-------------------------------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180
....*....|....*....|....*....
gi 552148158 502 LDVETEEKVKQAVDEL--SHNRTTFIIAH 528
Cdd:COG1245 486 LDVEQRLAVAKAIRRFaeNRGKTAMVVDH 514
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
349-535 |
5.55e-10 |
|
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: 61.76 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 349 QGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAA--GRIMIDGTDTRTVS-RRSLRHAIATVFQDAGLF-NRS 424
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVpELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 425 VEDNIRVGRaNATHE--EVHAAAKAAAAHDfILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSAL 502
Cdd:TIGR02633 95 VAENIFLGN-EITLPggRMAYNAMYLRAKN-LLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190
....*....|....*....|....*....|....
gi 552148158 503 -DVETEEKVKQAVDELSHNRTTFIIAHRLSTVRS 535
Cdd:TIGR02633 173 tEKETEILLDIIRDLKAHGVACVYISHKLNEVKA 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
311-552 |
6.32e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 311 QMEDATADRQEPENVADLND----------VKGdIVFDNVTFEFPNSGQGIYD-VSFEVKPGQTVAIVGPTGAGKTTLIN 379
Cdd:TIGR01257 896 KTEPLTEEMEDPEHPEGINDsfferelpglVPG-VCVKNLVKIFEPSGRPAVDrLNITFYENQITAFLGHNGAGKTTTLS 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 380 LLQRVFDPAAGRIMIDGTDTRTvSRRSLRHAIATVFQDAGLFNR-SVEDNIRV-----GRanaTHEEVHAAAKAaaahdf 453
Cdd:TIGR01257 975 ILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFyaqlkGR---SWEEAQLEMEA------ 1044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 454 iLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTV 533
Cdd:TIGR01257 1045 -MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEA 1123
|
250 260
....*....|....*....|
gi 552148158 534 RS-ADLVLFMDKGHLVESGS 552
Cdd:TIGR01257 1124 DLlGDRIAIISQGRLYCSGT 1143
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
339-550 |
6.35e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 339 NVTFEFPNSgQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFdPAA---GRIMIDGTDTRTVS-RRSLRHAIATV 414
Cdd:NF040905 6 GITKTFPGV-KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCRFKDiRDSEALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 415 FQDAGLF-NRSVEDNIRVGRANATH-----EEVHAAAKAaaahdfILAK---SEGYDTFVGERGSqlsgGERQRLAIARA 485
Cdd:NF040905 84 HQELALIpYLSIAENIFLGNERAKRgvidwNETNRRARE------LLAKvglDESPDTLVTDIGV----GKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 486 ILKDSPILVLDEATSALDVETEEKVKQAVDEL-SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVES 550
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELkAQGITSIIISHKLNEIRRvADSITVLRDGRTIET 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
353-503 |
6.36e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.20 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTV--SRRSlrhaIATVFQDAGLF-NRSVEDNI 429
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVppAERG----VGMVFQSYALYpHLSVAENM 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 430 RVGR--ANATHEEVHAAAKAAAAhdfILAKSEGYDtfvgERGSQLSGGERQRLAIARAILKDSPILVLDEATSALD 503
Cdd:PRK11000 97 SFGLklAGAKKEEINQRVNQVAE---VLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
353-547 |
1.72e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPA-AGRIMIDG--TDTRTVSrRSLRHAIATVFQD---AGLFNR-SV 425
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPA-QAIRAGIAMVPEDrkrHGIVPIlGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 426 EDNI---------RVGRANATHEEVHAAAKAAAAHdfilAKSEGYDTFVGergsQLSGGERQRLAIARAILKDSPILVLD 496
Cdd:TIGR02633 357 GKNItlsvlksfcFKMRIDAAAELQIIGSAIQRLK----VKTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 497 EATSALDVETEEKVKQAVDELSHNRTTFI-IAHRLSTVRS-ADLVLFMDKGHL 547
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIIvVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
24-286 |
4.34e-09 |
|
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: 57.79 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 24 MCVASVLVALVALAE---PVLFGRVIQSISDKGDI-----FSPLLMWAALGG--FNIMAAVFVARGADRLAH--RRRLgv 91
Cdd:cd18548 1 AILAPLFKLLEVLLElllPTLMADIIDEGIANGDLsyilrTGLLMLLLALLGliAGILAGYFAAKASQGFGRdlRKDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 92 midsYERLITMPLAWHQKRGTSnalhTLI-RAT---DSLFTLWLEFMRQHLTT-VVALATLIpVAMTMDMRMSLVLIV-- 164
Cdd:cd18548 79 ----FEKIQSFSFAEIDKFGTS----SLItRLTndvTQVQNFVMMLLRMLVRApIMLIGAII-MAFRINPKLALILLVai 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 165 --LGVIYVMIGQLVMRKTKDGQAAVEKhhhkLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALA 242
Cdd:cd18548 150 piLALVVFLIMKKAIPLFKKVQKKLDR----LNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 552148158 243 SGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMI 286
Cdd:cd18548 226 NPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQIL 269
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
339-551 |
6.96e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 56.12 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 339 NVTFEFPNSGQGIY---DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAA---GRIMIDGTDTRTVSRRSLRHAIA 412
Cdd:cd03233 8 NISFTTGKGRSKIPilkDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 413 TVFQDAGLFNRSVEDNIR-VGRANAtheevhaaakaaaaHDFIlaksegydtfvgeRGsqLSGGERQRLAIARAILKDSP 491
Cdd:cd03233 88 VSEEDVHFPTLTVRETLDfALRCKG--------------NEFV-------------RG--ISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDELSH--NRTTFIIAHRLS--TVRSADLVLFMDKGHLVESG 551
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
20-304 |
8.33e-09 |
|
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: 57.10 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 20 ATITMCVASVLVALVAlaepVLFGRVIQSISDKG------DIFSPLLMWAALggfnIMAAVFVARG-------------A 80
Cdd:cd18577 4 GLLAAIAAGAALPLMT----IVFGDLFDAFTDFGsgesspDEFLDDVNKYAL----YFVYLGIGSFvlsyiqtacwtitG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 81 DRLAH--RRRLgvmidsYERLITMPLAWHQKRGTSNALHTLIRATDSL---------FTLwlefmrQHLTTVVALatLIp 149
Cdd:cd18577 76 ERQARriRKRY------LKALLRQDIAWFDKNGAGELTSRLTSDTNLIqdgigeklgLLI------QSLSTFIAG--FI- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 150 VAMTMDMRMSLVLI----VLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEhvsdTISNVSVVQSYNRiasETQALRDYA 225
Cdd:cd18577 141 IAFIYSWKLTLVLLatlpLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEE----ALSSIRTVKAFGG---EEKEIKRYS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 226 KNLENAQFPVL---NWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIA-----FIGFVQLMigrldQISAFIN 297
Cdd:cd18577 214 KALEKARKAGIkkgLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTvffavLIGAFSLG-----QIAPNLQ 288
|
....*..
gi 552148158 298 QTVTARA 304
Cdd:cd18577 289 AFAKARA 295
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
335-545 |
1.06e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 55.33 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 335 IVFDNVTFEFPNSGQG---IYDVSFEVKPGQTVAIVGPTGAGKTTLINLL-QRVFDPA-AGRIMIDGtdtrtvsrrslrh 409
Cdd:cd03232 4 LTWKNLNYTVPVKGGKrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILING------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 410 aiatvfqdaglfnRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGydtfvgergsqLSGGERQRLAIARAILKD 489
Cdd:cd03232 71 -------------RPLDKNFQRSTGYVEQQDVHSPNLTVREALRFSALLRG-----------LSVEQRKRLTIGVELAAK 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 490 SPILVLDEATSALDVETEEKVKQAVDEL-SHNRTTFIIAHRLSTV--RSADLVLFMDKG 545
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
22-304 |
1.45e-08 |
|
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: 56.30 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 22 ITMCVASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVF-VARG--ADRLAHRRRLGVMIDSYER 98
Cdd:cd18570 5 ILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLsYIRSylLLKLSQKLDIRLILGYFKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 99 LITMPLAWHQKR--G--TS--NALHTLIRA-TDSLFTLWLEFmrqhLTTVVALATLIpvamTMDMRMSLVLIVLGVIYVM 171
Cdd:cd18570 85 LLKLPLSFFETRktGeiISrfNDANKIREAiSSTTISLFLDL----LMVIISGIILF----FYNWKLFLITLLIIPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 172 IGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMAST 251
Cdd:cd18570 157 IILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 252 FSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARA 304
Cdd:cd18570 237 IGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKV 289
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
20-286 |
3.01e-08 |
|
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: 55.58 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 20 ATITMCVASVLVALValaePVLFGRVIQSISDKGD--IFSPLLMWAALGGFNIMAAVFV-ARGA--DRLAHR--RRLGVm 92
Cdd:cd18582 1 ALLLLVLAKLLNVAV----PFLLKYAVDALSAPASalLAVPLLLLLAYGLARILSSLFNeLRDAlfARVSQRavRRLAL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 93 iDSYERLITMPLAWHQKRGTSnALHTLI-RATDSLFTLwLEFMRQHLttvvaLATLIPVAMTM-------DMRMSLVLIV 164
Cdd:cd18582 76 -RVFRHLHSLSLRFHLSRKTG-ALSRAIeRGTRGIEFL-LRFLLFNI-----LPTILELLLVCgilwylyGWSYALITLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 165 LGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQfpVLNWWALAsg 244
Cdd:cd18582 148 TVALYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAA--VKSQTSLA-- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 552148158 245 LNRMASTF----SMVVVLVLGAYFVTKGQMRVGDVIAFIGFV-QLMI 286
Cdd:cd18582 224 LLNIGQALiislGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLlQLYQ 270
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
354-572 |
6.35e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.24 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtDTRTVSRR---SLRHAIATVFQDAG--LFNRSVEDN 428
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRgllALRQQVATVFQDPEqqIFYTDIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 429 IRVGRANATHEEVHAAAKAAAAHDFILAKSegydtFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEE 508
Cdd:PRK13638 99 IAFSLRNLGVPEAEITRRVDEALTLVDAQH-----FRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552148158 509 KVKQAVDEL-SHNRTTFIIAHRLSTVRS-ADLVLFMDKGHLVESGSFNELAERGgrfsDLLRAGGL 572
Cdd:PRK13638 174 QMIAIIRRIvAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACT----EAMEQAGL 235
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
353-552 |
7.06e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAA--------GRIMIDGTDTRTVSRRSLRHAIATVFQDAG-LFNR 423
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 424 SVEDNIRVGR---ANATHEEVHAAAKAAaahDFILAKSeGYDTFVGERGSQLSGGERQRLAIARAILKDSP--------- 491
Cdd:PRK13547 99 SAREIVLLGRyphARRAGALTHRDGEIA---WQALALA-GATALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqppr 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552148158 492 ILVLDEATSALDVETEEKVKQAVDELSH--NRTTFIIAHRLS-TVRSADLVLFMDKGHLVESGS 552
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
333-504 |
1.64e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVF--DNVTFEFP-NSG-QGIYDVSFEVKPGQTVAIVGPTGAGKTTLInllQRVFDPAAGR----IMIDG--TDTRTv 402
Cdd:PRK13549 256 GEVILevRNLTAWDPvNPHiKRVDDVSFSLRRGEILGIAGLVGAGRTELV---QCLFGAYPGRwegeIFIDGkpVKIRN- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 403 SRRSLRHAIATVFQDA---GLF-NRSVEDNI---------RVGRANATHEEVHAAAKAAAAHdfilAKSEGYDTFVGerg 469
Cdd:PRK13549 332 PQQAIAQGIAMVPEDRkrdGIVpVMGVGKNItlaaldrftGGSRIDDAAELKTILESIQRLK----VKTASPELAIA--- 404
|
170 180 190
....*....|....*....|....*....|....*
gi 552148158 470 sQLSGGERQRLAIARAILKDSPILVLDEATSALDV 504
Cdd:PRK13549 405 -RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
460-551 |
1.85e-07 |
|
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: 51.17 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 460 GYDTfVGERGSQLSGGERQRLAIARAILKDSP--ILVLDEATSALDVETEEKVKQAVDEL-SHNRTTFIIAHRLSTVRSA 536
Cdd:cd03238 77 GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNLDVLSSA 155
|
90 100
....*....|....*....|.
gi 552148158 537 DLVLFMDK------GHLVESG 551
Cdd:cd03238 156 DWIIDFGPgsgksgGKVVFSG 176
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
354-560 |
1.92e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLL--QRVFDPAAGRIMIDGTDTRTVS-RRSLRHAIATVFQ--------DAGLFN 422
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQypveipgvSNQFFL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 423 RSVEDNIRVGRANATHEEVHAAakaaaahDFILAKSE----GYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEA 498
Cdd:PRK09580 100 QTALNAVRSYRGQEPLDRFDFQ-------DLMEEKIAllkmPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 499 TSALDVETEEKVKQAVDELSHNRTTFIIA---HRLSTVRSADLVLFMDKGHLVESGSFN---ELAERG 560
Cdd:PRK09580 173 DSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFTlvkQLEEQG 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
333-517 |
2.14e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 333 GDIVF--DNVTFEFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLL--QRVfdPAAGRIMIDGTDTRTVSRRSLR 408
Cdd:COG3845 254 GEVVLevENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLRP--PASGSIRLDGEDITGLSPRERR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 409 HA-IATVFQD---AGLF-NRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYD---TFVGERGSQLSGGERQRL 480
Cdd:COG3845 332 RLgVAYIPEDrlgRGLVpDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDvrtPGPDTPARSLSGGNQQKV 411
|
170 180 190
....*....|....*....|....*....|....*..
gi 552148158 481 AIARAILKDSPILVLDEATSALDVETEEKVKQAVDEL 517
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL 448
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
26-285 |
3.04e-07 |
|
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: 52.51 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEP---------VLFGRVIQSISDKGDIFSP----LLMWAAL---------GGFNIMAAVFVARGADRL 83
Cdd:cd18564 6 LALLLETALRLLEPwplkvviddVLGDKPLPGLLGLAPLLGPdplaLLLLAAAalvgiallrGLASYAGTYLTALVGQRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 84 AH--RRRLgvmidsYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLwleFMRQHLTTVVALATLI---PVAMTMDMRM 158
Cdd:cd18564 86 VLdlRRDL------FAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDL---LVSGVLPLLTNLLTLVgmlGVMFWLDWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 159 SLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDyaknlENAQfpvlnw 238
Cdd:cd18564 157 ALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR-----ENRK------ 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 239 wALASGL--NRMASTFSMVV----------VLVLGAYFVTKGQMRVGDVIAFIGFVQLM 285
Cdd:cd18564 226 -SLRAGLraARLQALLSPVVdvlvavgtalVLWFGAWLVLAGRLTPGDLLVFLAYLKNL 283
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
123-302 |
3.05e-07 |
|
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: 52.42 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 123 TDSLFTLWLEfmrqhlttVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTI 202
Cdd:cd18554 121 TTGLMNIWLD--------MITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 203 SNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFV 282
Cdd:cd18554 193 QGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYM 272
|
170 180
....*....|....*....|...
gi 552148158 283 QLMIG---RLDQISAFINQTVTA 302
Cdd:cd18554 273 ERMYSplrRLVNSFTTLTQSFAS 295
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
357-530 |
3.75e-07 |
|
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: 50.65 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 357 EVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDtrtvsrrslrhaiatvfqdaglfnrsvednirvgrana 436
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT-------------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 437 theevhaaakaaaahdfILAKSEGYDtfvgergsqLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDE 516
Cdd:cd03222 63 -----------------PVYKPQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170
....*....|....*.
gi 552148158 517 LSHN--RTTFIIAHRL 530
Cdd:cd03222 117 LSEEgkKTALVVEHDL 132
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
26-278 |
4.17e-07 |
|
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: 51.82 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGD------IFSPLLMWAAL-GGFNIMAAVFVARGADRLAhrRRLGVMIdsYER 98
Cdd:cd18782 9 ALSFVVQLLGLANPLLFQVIIDKVLVQQDlatlyvIGVVMLVAALLeAVLTALRTYLFTDTANRID--LELGGTI--IDH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 99 LITMPLAWHQKR---GTSNALHTL--IR--ATDSLFTLWLEFmrqhLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVM 171
Cdd:cd18782 85 LLRLPLGFFDKRpvgELSTRISELdtIRgfLTGTALTTLLDV----LFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 172 IGQLVMRKTKDGQAAVEKHHHKLFEHvsdtISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMAST 251
Cdd:cd18782 161 FGPILRRQIRRRAEASAKTQSYLVES----LTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNK 236
|
250 260
....*....|....*....|....*..
gi 552148158 252 FSMVVVLVLGAYFVTKGQMRVGDVIAF 278
Cdd:cd18782 237 LSSLLVLWVGAYLVLRGELTLGQLIAF 263
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
276-503 |
6.30e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 276 IAFIGFVQLMIGRLDQISAFINQTVTARAKLEEFFQMEDATADRQEPENVADLNDVkgdIVFDNVTFEFPNSGQGIYD-V 354
Cdd:TIGR01257 1882 MAVEGVVYFLLTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAEERQRIISGGNKTDI---LRLNELTKVYSGTSSPAVDrL 1958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 355 SFEVKPGQTVAIVGPTGAGKTTLINLLqrvfdpaAGRIMIDGTDTrTVSRRSLRHAIATVFQDAGLFNR-SVEDNIRVGR 433
Cdd:TIGR01257 1959 CVGVRPGECFGLLGVNGAGKTTTFKML-------TGDTTVTSGDA-TVAGKSILTNISDVHQNMGYCPQfDAIDDLLTGR 2030
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552148158 434 AN---------ATHEEVHAAAKAAAahdfilaKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALD 503
Cdd:TIGR01257 2031 EHlylyarlrgVPAEEIEKVANWSI-------QSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
351-526 |
7.80e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 351 IYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtdtRTVSRRSLRHAIATVF-------QDAGLF-N 422
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINNHNANEAINHGFalvteerRSTGIYaY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 423 RSVEDNIRVGRANATHEEVHAAAKAAAAHDF------ILAKSEGYDTFVGergsQLSGGERQRLAIARAILKDSPILVLD 496
Cdd:PRK10982 341 LDIGFNSLISNIRNYKNKVGLLDNSRMKSDTqwvidsMRVKTPGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190
....*....|....*....|....*....|
gi 552148158 497 EATSALDVETEEKVKQAVDELSHNRTTFII 526
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
20-279 |
8.12e-07 |
|
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: 50.98 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 20 ATITMCVASvlvaLVALAEPVLFGRVIQSISDKGDIFSPLLM------WAALGGFNIMAAVFVARG------ADRLAHRR 87
Cdd:cd18573 1 ALALLLVSS----AVTMSVPFAIGKLIDVASKESGDIEIFGLslktfaLALLGVFVVGAAANFGRVyllriaGERIVARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 88 RLGVmidsYERLITMPLAWHQKRGTSNALHTLirATDSL-----FTLWL-EFMRQHLTTVVALATLIPVAMTMDMRMSLV 161
Cdd:cd18573 77 RKRL----FKSILRQDAAFFDKNKTGELVSRL--SSDTSvvgksLTQNLsDGLRSLVSGVGGIGMMLYISPKLTLVMLLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 162 LIVLGVIYVMIGQLVMRKTKDGQAAVEKhhhkLFEHVSDTISNVSVVQSYnriASETQALRDYAKNLENaqfpVLN---- 237
Cdd:cd18573 151 VPPIAVGAVFYGRYVRKLSKQVQDALAD----ATKVAEERLSNIRTVRAF---AAERKEVERYAKKVDE----VFDlakk 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 552148158 238 ---WWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFI 279
Cdd:cd18573 220 ealASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFL 264
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
364-528 |
1.01e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 49.62 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 364 VAIVGPTGAGKTTLINLLQRVFDPAAGR--------IMIDGTDTR------------TVSRR-------------SLRHA 410
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYALYGKARSrsklrsdlINVGSEEASvelefehggkryRIERRqgefaefleakpsERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 411 IATVFQDAGLfnRSVEDNIRVGRANAThEEVHAAAKAAAAHDFILAKSEGYDTFvgergSQLSGGERQRLAIARAILkds 490
Cdd:COG0419 106 LKRLLGLEIY--EELKERLKELEEALE-SALEELAELQKLKQEILAQLSGLDPI-----ETLSGGERLRLALADLLS--- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 552148158 491 piLVLDeaTSALDVETEEKVKQAVDELShnrttfIIAH 528
Cdd:COG0419 175 --LILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
95-289 |
1.45e-06 |
|
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: 50.30 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 95 SYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLwLEFMRQHL--TTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMI 172
Cdd:cd18560 77 TFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTL-LSYLVFYLvpTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 173 GQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTF 252
Cdd:cd18560 156 TIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQL 235
|
170 180 190
....*....|....*....|....*....|....*..
gi 552148158 253 SMVVVLVLGAYFVTKGQMRVGDVIAfigfVQLMIGRL 289
Cdd:cd18560 236 GLTLGLLLAGYRVVDGGLSVGDFVA----VNTYIFQL 268
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
25-305 |
2.19e-06 |
|
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: 49.85 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 25 CVASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVFVA-RGADRLAHRRRL--GVMIDSYERLIT 101
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGlRGGCFSYAGTRLvrRLRRDLFRSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 102 MPLAWHQKRGTSNALHTLIRATDSL---FTLWLEFMrqhLTTVVALATLIPVAMTMDMRMSLV-LIVLGVIYVMI---GQ 174
Cdd:cd18572 82 QDIAFFDATKTGELTSRLTSDCQKVsdpLSTNLNVF---LRNLVQLVGGLAFMFSLSWRLTLLaFITVPVIALITkvyGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 175 LVMRKTKDGQAAVEKHHhklfEHVSDTISNVSVVQSYnriASETQALRDYAKNLENAqfpvLNWW---ALASGLNRMAST 251
Cdd:cd18572 159 YYRKLSKEIQDALAEAN----QVAEEALSNIRTVRSF---ATEEREARRYERALDKA----LKLSvrqALAYAGYVAVNT 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 252 FSM----VVVLVLGAYFVTKGQMRVGDVIAFIgFVQLMIGR-----LDQISAFInQTVTARAK 305
Cdd:cd18572 228 LLQngtqVLVLFYGGHLVLSGRMSAGQLVTFM-LYQQQLGEafqslGDVFSSLM-QAVGAAEK 288
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
471-546 |
2.42e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 471 QLSGGERQRLAIARAI----LKDSPILVLDEATSALDVETEEKVKQAVDELS-HNRTTFIIAHRLSTVRSADLVLFMDKG 545
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIKKV 156
|
.
gi 552148158 546 H 546
Cdd:cd03227 157 I 157
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
96-298 |
2.50e-06 |
|
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: 49.38 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 96 YERLITMPLAWHQKRGTS------NALHTLIRA-TDSLFTLWLEfmrqhltTVVALATLipVAMTM-DMRMSLVLIVLGV 167
Cdd:cd18567 82 FRHLLRLPLSYFEKRHLGdivsrfGSLDEIQQTlTTGFVEALLD-------GLMAILTL--VMMFLySPKLALIVLAAVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 168 IYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNR 247
Cdd:cd18567 153 LYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANG 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 552148158 248 MASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRldqISAFINQ 298
Cdd:cd18567 233 LLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSR---ASSLIDK 280
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
26-293 |
2.77e-06 |
|
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: 49.48 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEP----VLFGRVIqSISDKGDIFSPLLMWAALGGFNIMAAVFVARGADRLAHRRRLGVMIDSYERLIT 101
Cdd:cd18568 9 LASLLLQLLGLALPlftqIILDRVL-VHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 102 MPLAWHQKRGTSNALHTL-----IRA--TDSLFTLWLEFmrqhLTTVVALATLipvaMTMDMRMSLVLIVLGVIYVMIGQ 174
Cdd:cd18568 88 LPLSFFASRKVGDIITRFqenqkIRRflTRSALTTILDL----LMVFIYLGLM----FYYNLQLTLIVLAFIPLYVLLTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 175 LVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSY---NRIASETQALrdYAKNLeNAQFPVLNWWALASGLNRMAST 251
Cdd:cd18568 160 LSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALaaeRPIRWRWENK--FAKAL-NTRFRGQKLSIVLQLISSLINH 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 552148158 252 FSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQIS 293
Cdd:cd18568 237 LGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALV 278
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-307 |
3.89e-06 |
|
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: 49.02 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 22 ITMCVASVLVALVALAEPVLFGRVIQSISDKGDIfsPLLMWAALGgfniMAAVFVARGADRLAHRR---RLG--VMID-- 94
Cdd:cd18550 2 ALVLLLILLSALLGLLPPLLLREIIDDALPQGDL--GLLVLLALG----MVAVAVASALLGVVQTYlsaRIGqgVMYDlr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 95 --SYERLITMPLAWHQKRGTS---NALHTLIRATDSLFTLWLEFMRQHLTTVVALAtlipVAM-TMDMRMSLVLIVLGVI 168
Cdd:cd18550 76 vqLYAHLQRMSLAFFTRTRTGeiqSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATL----VAMlALDWRLALLSLVLLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 169 YVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDT--ISNVSVVQSYNRIASETQALRDYAKNLENAQ--FPVLNWWALASg 244
Cdd:cd18550 152 FVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGvrQALAGRWFFAA- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 245 lnrMASTFSMVVVLV--LGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLE 307
Cdd:cd18550 231 ---LGLFTAIGPALVywVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFE 292
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
301-560 |
4.54e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 301 TARAKLEEFFQMEDATAD-RQEPEnvadlndvkgdIVFD-------------NVTFEFPNsGQGIYDVSFEVKPGQTVAI 366
Cdd:PRK15064 283 TSRAKQIDKIKLEEVKPSsRQNPF-----------IRFEqdkklhrnaleveNLTKGFDN-GPLFKNLNLLLEAGERLAI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 367 VGPTGAGKTTLINLLQRVFDPAAGriMIDGTDTRTVSRRSLRHAiATVFQDAGLFN-----RSVEDNIRVGRAnatheev 441
Cdd:PRK15064 351 IGENGVGKTTLLRTLVGELEPDSG--TVKWSENANIGYYAQDHA-YDFENDLTLFDwmsqwRQEGDDEQAVRG------- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 442 haaakaaaahdfILakseGYDTF----VGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDE- 516
Cdd:PRK15064 421 ------------TL----GRLLFsqddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKy 484
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 517 ------LSHNRtTFI--IAHRLSTVRSADLVLFmdkghlveSGSFNE-LAERG 560
Cdd:PRK15064 485 egtlifVSHDR-EFVssLATRIIEITPDGVVDF--------SGTYEEyLRSQG 528
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
466-552 |
6.10e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 466 GERGSQLSGGERQRLAIARAILKDSP---ILVLDEATSALDVETEEKVKQAVDELSHN-RTTFIIAHRLSTVRSADLVLF 541
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNLDVIKCADWIID 243
|
90
....*....|....*..
gi 552148158 542 M-----DK-GHLVESGS 552
Cdd:cd03271 244 LgpeggDGgGQVVASGT 260
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
22-307 |
8.46e-06 |
|
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: 47.89 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 22 ITMCVASVLVALVALAEPVLFGRVIQSISDKGDI-FSPLLMWAAL------GGFNIMAAVFVARgadrlahrrrLGVMID 94
Cdd:cd18555 5 ISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLnLLNVLGIGILilfllyGLFSFLRGYIIIK----------LQTKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 95 S------YERLITMPLAWHQKRgTSNALhtLIRAtDSLFTLWLEFMRQHLTTVVALATLIPVAMTM---DMRMSLVLIVL 165
Cdd:cd18555 75 KslmsdfFEHLLKLPYSFFENR-SSGDL--LFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMlyySPLLTLIVLLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 166 GVIYVMIGQLVMRKTKDG-------QAAVEKHhhklfehVSDTISNVSVVQSynrIASETQAL---RDYAKNLENAQFPV 235
Cdd:cd18555 151 GLLIVLLLLLTRKKIKKLnqeeivaQTKVQSY-------LTETLYGIETIKS---LGSEKNIYkkwENLFKKQLKAFKKK 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 236 LNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLE 307
Cdd:cd18555 221 ERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLE 292
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
473-560 |
9.25e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 473 SGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSH-NRTTFIIAH--RLSTVRSADLVLFMDKGHLVE 549
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
90
....*....|....
gi 552148158 550 SGSF---NELAERG 560
Cdd:CHL00131 233 TGDAelaKELEKKG 246
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
322-518 |
9.49e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 322 PENVADLNDVKGDIVFD--NVTfefPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDT 399
Cdd:PRK09700 251 NAMKENVSNLAHETVFEvrNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 400 RTVSR-RSLRHAIATVFQ---DAGLF-NRSVEDNIRVGR---------ANATHEEVHAAAKAAAAHDFILAKSEGYDTFV 465
Cdd:PRK09700 328 SPRSPlDAVKKGMAYITEsrrDNGFFpNFSIAQNMAISRslkdggykgAMGLFHEVDEQRTAENQRELLALKCHSVNQNI 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 552148158 466 GErgsqLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELS 518
Cdd:PRK09700 408 TE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA 456
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
354-562 |
1.02e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLInLLQRVFDPAAGRIMIDgTDTRTVSRRSLRHAIATvfqdaglfNRSVEDNIR--- 430
Cdd:NF000106 32 VDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWR-F*TWCANRRALRRTIG*--------HRPVR*GRResf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 431 --------VGRANATHEEVHAAAKAAAAHDFILAKSegydtfVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSAL 502
Cdd:NF000106 102 sgrenlymIGR*LDLSRKDARARADELLERFSLTEA------AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 503 DVETEEKVKQAVDELSHNRTTFIIAHRL--STVRSADLVLFMDKGHLVESGSFNELAER-GGR 562
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVIDRGRVIADGKVDELKTKvGGR 238
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
470-537 |
1.04e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 46.69 E-value: 1.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 470 SQLSGGERQRLAIAR--AIL--KDSPILVLDEATSALDVETEEKVKQAVDELSHNrTTFI-IAHRLSTVRSAD 537
Cdd:cd03278 112 SLLSGGEKALTALALlfAIFrvRPSPFCVLDEVDAALDDANVERFARLLKEFSKE-TQFIvITHRKGTMEAAD 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
354-504 |
1.22e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 354 VSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGtdtRTVSRRSLRHAIAtvfqdAGLF------------ 421
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIR-----AGIMlcpedrkaegii 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 422 -NRSVEDNIRVG-----------------RANATHeevhaaakaaaahdFILA---KSEGYDTFVGergsQLSGGERQRL 480
Cdd:PRK11288 344 pVHSVADNINISarrhhlragclinnrweAENADR--------------FIRSlniKTPSREQLIM----NLSGGNQQKA 405
|
170 180
....*....|....*....|....
gi 552148158 481 AIARAILKDSPILVLDEATSALDV 504
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDV 429
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
470-548 |
1.26e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 470 SQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQ-------AVDELSHNRtTFIiaHRLSTvRSADLvlfm 542
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGflktfqgSIIFISHDR-SFI--RNMAT-RIVDL---- 226
|
....*.
gi 552148158 543 DKGHLV 548
Cdd:PRK11147 227 DRGKLV 232
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
472-557 |
1.51e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 472 LSGGERQRLAIARAILKDS---PILVLDEATSALDVETEEKVKQAVDELSHN-RTTFIIAHRLSTVRSADLVLFM----- 542
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNLDVIKTADYIIDLgpegg 909
|
90
....*....|....*.
gi 552148158 543 DK-GHLVESGSFNELA 557
Cdd:TIGR00630 910 DGgGTVVASGTPEEVA 925
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
29-279 |
1.69e-05 |
|
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: 47.09 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 29 VLVALVALAEPVL-FGRVIQSISDKGDIF-SPLLMWAALGGFNIMAAV----------FVARGADRLAHRRRlgvmIDSY 96
Cdd:cd18575 1 ALIALLIAAAATLaLGQGLRLLIDQGFAAgNTALLNRAFLLLLAVALVlalasalrfyLVSWLGERVVADLR----KAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 97 ERLITMPLAWHQKRGTSNALH------TLIRAT-DSLFTLWLefmRQHLTTVVALATLIpvaMTMDMRMSLVLIVLGVIY 169
Cdd:cd18575 77 AHLLRLSPSFFETTRTGEVLSrlttdtTLIQTVvGSSLSIAL---RNLLLLIGGLVMLF---ITSPKLTLLVLLVIPLVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 170 VMI---GQLVMRKTKDGQAAVEKhhhkLFEHVSDTISNVSVVQSYNRiasETQALRDYAKNLENAqFPVlnwwALASGLN 246
Cdd:cd18575 151 LPIilfGRRVRRLSRASQDRLAD----LSAFAEETLSAIKTVQAFTR---EDAERQRFATAVEAA-FAA----ALRRIRA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 552148158 247 R-------MASTF-SMVVVLVLGAYFVTKGQMRVGDVIAFI 279
Cdd:cd18575 219 RalltalvIFLVFgAIVFVLWLGAHDVLAGRMSAGELSQFV 259
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
254-533 |
1.71e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 254 MVVVLVLGayfvtkgqmRVGDVIAFIGFVQLM-------IGRLDQISAfinQTVTARAKLEEffQMEDAT-ADRQEPENV 325
Cdd:PRK10938 186 ITLVLVLN---------RFDEIPDFVQFAGVLadctlaeTGEREEILQ---QALVAQLAHSE--QLEGVQlPEPDEPSAR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 326 ADLNDVKGDIVFDNVTFEFpNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLL-----------------QRvfdpA 388
Cdd:PRK10938 252 HALPANEPRIVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndltlfgrRR----G 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 389 AGRIMID------------GTDTRtVSrRSLRHAIATVFQDA-GLFnRSVEDNIRVgRANATHEEVHAaakaaaahDFIL 455
Cdd:PRK10938 327 SGETIWDikkhigyvssslHLDYR-VS-TSVRNVILSGFFDSiGIY-QAVSDRQQK-LAQQWLDILGI--------DKRT 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 456 AKSEGYDtfvgergsqLSGGErQRLA-IARAILKDSPILVLDEATSALDVETEEKVKQAVDEL-SHNRTTFI-------- 525
Cdd:PRK10938 395 ADAPFHS---------LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEGETQLLfvshhaed 464
|
330
....*....|..
gi 552148158 526 ----IAHRLSTV 533
Cdd:PRK10938 465 apacITHRLEFV 476
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
353-544 |
1.98e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.68 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVaIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATV-FQDAGlfnrsvEDNIRV 431
Cdd:cd03240 15 RSEIEFFSPLTL-IVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIREGEVRAQVKLaFENAN------GKKYTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 GRANATHEEVhaaakaaaahdfILAKSEGYDTFVGERGSQLSGGERQ------RLAIARAILKDSPILVLDEATSALDVE 505
Cdd:cd03240 88 TRSLAILENV------------IFCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552148158 506 T-EEKVKQAVDELSH--NRTTFIIAHRLSTVRSADLVLFMDK 544
Cdd:cd03240 156 NiEESLAEIIEERKSqkNFQLIVITHDEELVDAADHIYRVEK 197
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
470-537 |
2.24e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 2.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 470 SQLSGGERQRLAIAR--AIL--KDSPILVLDEATSALDVETEEKVKQAVDELSHNrTTFI-IAHRLSTVRSAD 537
Cdd:TIGR02168 1088 SLLSGGEKALTALALlfAIFkvKPAPFCILDEVDAPLDDANVERFANLLKEFSKN-TQFIvITHNKGTMEVAD 1159
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
470-537 |
3.56e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.89 E-value: 3.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552148158 470 SQLSGGERQRLAIA--RAIL--KDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFIIAHRLSTVRSAD 537
Cdd:pfam02463 1076 DLLSGGEKTLVALAliFAIQkyKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKAD 1147
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
470-556 |
3.87e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 470 SQLSGGERQRLAIARAILKDSP---ILVLDEATSAL---DVETEEKVKQAVDELSHnrTTFIIAHRLSTVRSADLVLFMD 543
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLhthDIKALIYVLQSLTHQGH--TVVIIEHNMHVVKVADYVLELG 885
|
90
....*....|....*....
gi 552148158 544 K------GHLVESGSFNEL 556
Cdd:PRK00635 886 PeggnlgGYLLASCSPEEL 904
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
160-278 |
4.59e-05 |
|
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: 45.65 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 160 LVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSynrIASETQALRDYAKNLEN---AQFPVL 236
Cdd:cd18566 145 LVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKA---MAMEPQMLRRYERLQANaayAGFKVA 221
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 552148158 237 NWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAF 278
Cdd:cd18566 222 KINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIAC 263
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
96-291 |
5.18e-05 |
|
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: 45.57 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 96 YERLITMPLAWHQKRGTSN------ALHTlIRA--TDSLFTLWLEFmrqhLTTVVALATLIPVAMTMDMRMSLVLIVLGV 167
Cdd:cd18588 82 FRHLLRLPLSYFESRQVGDtvarvrELES-IRQflTGSALTLVLDL----VFSVVFLAVMFYYSPTLTLIVLASLPLYAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 168 IYVMIGQLVMRKTKDGQAAVEKHHHKLFEhvsdTISNVSVVQSynrIASETQALRDYAKNLEN---AQFPVLNWWALASG 244
Cdd:cd18588 157 LSLLVTPILRRRLEEKFQRGAENQSFLVE----TVTGIETVKS---LAVEPQFQRRWEELLARyvkASFKTANLSNLASQ 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552148158 245 LNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFigfvQLMIGRLDQ 291
Cdd:cd18588 230 IVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAF----NMLAGQVSQ 272
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
26-295 |
5.79e-05 |
|
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: 45.35 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDIFSplLMWAALGgfniMAAVFVARG---------ADRLAHRRRLGVMIDSY 96
Cdd:cd18561 3 LLGLLITALYIAQAWLLARALARIFAGGPWED--IMPPLAG----IAGVIVLRAallwlrervAHRAAQRVKQHLRRRLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 97 ERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLV 176
Cdd:cd18561 77 AKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 177 MRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVV 256
Cdd:cd18561 157 DRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTAL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 552148158 257 VLVLGAYFVTKGQMRvgdviAFIGFVQLMIGR-----LDQISAF 295
Cdd:cd18561 237 ALGVGALRVLGGQLT-----LSSLLLILFLSReffrpLRDLGAY 275
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
353-503 |
6.06e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVS-RRSLRHAIATVFQdaGL-----FNRSVE 426
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhRRAVCPRIAYMPQ--GLgknlyPTLSVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 427 DNI----------------RVGRanatheevhaaakaaaahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDS 490
Cdd:NF033858 97 ENLdffgrlfgqdaaerrrRIDE---------------------LLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170
....*....|...
gi 552148158 491 PILVLDEATSALD 503
Cdd:NF033858 156 DLLILDEPTTGVD 168
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
353-558 |
6.79e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTdtrtvsrrslrhaIATVFQDAGLFNR-SVEDNIRV 431
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAISAGLSGQlTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 432 GR--ANATHEEVHAAAKAaaahdfILAKSEGYDtFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEK 509
Cdd:PRK13546 109 KMlcMGFKRKEIKAMTPK------IIEFSELGE-FIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 552148158 510 VKQAVDEL-SHNRTTFIIAHRLSTVRSadlvlFMDKGHLVESGSFNELAE 558
Cdd:PRK13546 182 CLDKIYEFkEQNKTIFFVSHNLGQVRQ-----FCTKIAWIEGGKLKDYGE 226
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
357-544 |
7.66e-05 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 43.84 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 357 EVKPG--QTVAIVGPTGAGKTTLINLLQRVFDpaagrimidGTDTRTVSRRSLrhaiatvfQDAGLFNRSvednirvgRA 434
Cdd:cd03239 16 TVVGGsnSFNAIVGPNGSGKSNIVDAICFVLG---------GKAAKLRRGSLL--------FLAGGGVKA--------GI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 435 NATHEEVHAAAkaaaaHDFILaksegydtFVGERGSQLSGGERQRLAIAR--AI--LKDSPILVLDEATSALDVETEEKV 510
Cdd:cd03239 71 NSASVEITFDK-----SYFLV--------LQGKVEQILSGGEKSLSALALifALqeIKPSPFYVLDEIDAALDPTNRRRV 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 552148158 511 KQAVDELSHNRTTFI-IAHRLSTVRSADL---VLFMDK 544
Cdd:cd03239 138 SDMIKEMAKHTSQFIvITLKKEMFENADKligVLFVHG 175
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
351-504 |
8.28e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 351 IYDVSFEVKPGQTVAIVGPTGAGKTtliNLLQRVFDPA-----AGRIMIDGT--DTRTVSRrSLRHAIATVFQD---AGL 420
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRT---ELAMSVFGRSygrniSGTVFKDGKevDVSTVSD-AIDAGLAYVTEDrkgYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 421 fnrSVEDNIRVGRANATHEEVHAAAKAAAAHDFILA---------KSEGYDTFVGergsQLSGGERQRLAIARAILKDSP 491
Cdd:NF040905 352 ---NLIDDIKRNITLANLGKVSRRGVIDENEEIKVAeeyrkkmniKTPSVFQKVG----NLSGGNQQKVVLSKWLFTDPD 424
|
170
....*....|...
gi 552148158 492 ILVLDEATSALDV 504
Cdd:NF040905 425 VLILDEPTRGIDV 437
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
353-506 |
8.99e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFD----PAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDN 428
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 429 ----IRVGRANATHEEVHAAAKAAAAHDFILAK---SEGYDTFVGE---RGsqLSGGERQRLAIARAILKDSPILVLDEA 498
Cdd:TIGR00956 159 ldfaARCKTPQNRPDGVSREEYAKHIADVYMATyglSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNA 236
|
....*...
gi 552148158 499 TSALDVET 506
Cdd:TIGR00956 237 TRGLDSAT 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
470-506 |
1.01e-04 |
|
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: 1.01e-04
10 20 30
....*....|....*....|....*....|....*..
gi 552148158 470 SQLSGGERQRLAIARAILKDSPILVLDEATSALDVET 506
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
340-501 |
1.83e-04 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 43.74 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 340 VTFEFPN----SGQGIydvsfevKPGQTVaIVGPTGAGKTTLINLLQR-VFDPAAGrimiDG-----TDTRTVSRRSlrh 409
Cdd:pfam09818 62 VEIELPNggtvSGMGI-------PKGITL-IVGGGFHGKSTLLEALERgVYNHIPG----DGrefvvTDPDAVKIRA--- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 410 aiatvfqdaglfnrsvEDNIRVGRANATheevhaaakaaaahDFILAKSEGYDT--FVGERGsqlSGGERQRLAIARAIL 487
Cdd:pfam09818 127 ----------------EDGRSVHGVDIS--------------PFINNLPPGKDTtdFSTEDA---SGSTSQAANIMEALE 173
|
170
....*....|....
gi 552148158 488 KDSPILVLDEATSA 501
Cdd:pfam09818 174 AGASLLLIDEDTSA 187
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
26-228 |
2.16e-04 |
|
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: 43.55 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALggfniMAAVFVARGA-----DRLAH----------RRRLg 90
Cdd:cd18584 3 LLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLL-----LLAALLLRALlawaqERLAAraaarvkaelRRRL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 91 vmidsYERLITMPLAWHQKRGTSNALHTLIRATDSL---FTLWLEFMRqhLTTVVALATLIPVAmTMDMRMSLVLIVLG- 166
Cdd:cd18584 77 -----LARLLALGPALLRRQSSGELATLLTEGVDALdgyFARYLPQLV--LAAIVPLLILVAVF-PLDWVSALILLVTAp 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 167 ---VIYVMIGqlvmRKTkdgQAAVEKHHHKLFE---HVSDTISNVSVVQSYNRIASETQALRDYAKNL 228
Cdd:cd18584 149 lipLFMILIG----KAA---QAASRRQWAALSRlsgHFLDRLRGLPTLKLFGRARAQAARIARASEDY 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
470-506 |
2.73e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 2.73e-04
10 20 30
....*....|....*....|....*....|....*..
gi 552148158 470 SQLSGGERQRLAIARAILKDSPILVLDEATSALDVET 506
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
365-434 |
2.88e-04 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 41.85 E-value: 2.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552148158 365 AIVGPTGAGKTTLINLL--QRVFDPAAgrimIDGTdTRTVSRRSLRHAIAT--VFQD-AGLFNRSVEDNIRVGRA 434
Cdd:cd00880 1 AIFGRPNVGKSSLLNALlgQNVGIVSP----IPGT-TRDPVRKEWELLPLGpvVLIDtPGLDEEGGLGRERVEEA 70
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
26-307 |
3.22e-04 |
|
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: 42.92 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIM-AAVFVARGADRLAHRRRL--GVMIDSYERLITM 102
Cdd:cd18779 9 LASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTqLLAGLLRSHLLLRLRTRLdtQLTLGFLEHLLRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 103 PLAWHQKRGTSNAL-----HTLIRatdslftlwlEFMRQHLTTVV---ALATLIPVAMT-MDMRMSLVLIVLGVIYVMIG 173
Cdd:cd18779 89 PYRFFQQRSTGDLLmrlssNATIR----------ELLTSQTLSALldgTLVLGYLALLFaQSPLLGLVVLGLAALQVALL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 174 QLVMRKTkdgQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAknleNAQFPVLNWW-------ALASGLN 246
Cdd:cd18779 159 LATRRRV---RELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWS----NLFVDQLNASlrrgrldALVDALL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552148158 247 RMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARAKLE 307
Cdd:cd18779 232 ATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLE 292
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
348-381 |
3.45e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 43.00 E-value: 3.45e-04
10 20 30
....*....|....*....|....*....|....
gi 552148158 348 GQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLL 381
Cdd:PRK01889 182 GEGLDVLAAWLSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
132-281 |
3.60e-04 |
|
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: 43.01 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 132 EFMRQHLTTVVALATLipvaMTMDMRMSLVLI----VLGVIYVMIGQLVMRKTKDGQAAVEKHHhklfEHVSDTISNVSV 207
Cdd:cd18780 122 MLLRYLVQIIGGLVFM----FTTSWKLTLVMLsvvpPLSIGAVIYGKYVRKLSKKFQDALAAAS----TVAEESISNIRT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 208 VQSYnriASETQALRDYAKNLENAqfpvLNW---WALASGL----NRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIG 280
Cdd:cd18780 194 VRSF---AKETKEVSRYSEKINES----YLLgkkLARASGGfngfMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLL 266
|
.
gi 552148158 281 F 281
Cdd:cd18780 267 Y 267
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
361-382 |
5.05e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.61 E-value: 5.05e-04
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
471-556 |
5.57e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 471 QLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVKQAVDELSHNRTTFI--IAHRLSTVRS-ADLVLFMDKGHL 547
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQwADKINVLYCGQT 237
|
....*....
gi 552148158 548 VESGSFNEL 556
Cdd:PRK15093 238 VETAPSKEL 246
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
139-283 |
6.24e-04 |
|
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: 42.08 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 139 TTVVALATLIPVAMTM---DMRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFehvSDTISNVSVVQSYNRIA 215
Cdd:cd18569 121 TTVLNLVMAVFYALLMlqyDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLT---GTTMSGLQMIETLKASG 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 216 SETQALRD----YAKNLENAQ-FPVLNwwALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFVQ 283
Cdd:cd18569 198 AESDFFSRwagyQAKVLNAQQeLGRTN--QLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMA 268
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
364-420 |
8.72e-04 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 40.17 E-value: 8.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 364 VAIVGPTGAGKTTLINLLQRVFDPAA-------GRIMIDgtdtrT----VSRRSLRHAIATVFQDAGL 420
Cdd:COG4917 4 IMLIGRSGAGKTTLTQALNGEELEYRktqaveyYDNIID-----TpgeyIENPRFYKALIATAQDADV 66
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
353-389 |
9.09e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 9.09e-04
10 20 30
....*....|....*....|....*....|....*..
gi 552148158 353 DVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAA 389
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
343-505 |
1.56e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 343 EFPNSGQGIYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHaiatVFQDAGL-F 421
Cdd:PRK13541 8 QFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTY----IGHNLGLkL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 422 NRSVEDNIRV-GRANATHEEVHAAAKAAAAHDFIlaksegydtfvGERGSQLSGGERQRLAIARAILKDSPILVLDEATS 500
Cdd:PRK13541 84 EMTVFENLKFwSEIYNSAETLYAAIHYFKLHDLL-----------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
....*
gi 552148158 501 ALDVE 505
Cdd:PRK13541 153 NLSKE 157
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
346-382 |
1.87e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.45 E-value: 1.87e-03
10 20 30
....*....|....*....|....*....|....*..
gi 552148158 346 NSGQGIYDVSFEVKpGQTVAIVGPTGAGKTTLINLLQ 382
Cdd:pfam03193 92 KTGEGIEALKELLK-GKTTVLAGQSGVGKSTLLNALL 127
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
350-391 |
1.91e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.76 E-value: 1.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 552148158 350 GIYDVSFEVKPGQTVaIVGPTGAGKTTLINLLQRVFDPAAGR 391
Cdd:COG3593 13 SIKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
355-551 |
2.31e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 355 SFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQD--AGLFNRSVEDnirVG 432
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRnnTDMLSPGEDD---TG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 433 R--ANATHEEVHAAAKAAAahdfiLAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKV 510
Cdd:PRK10938 100 RttAEIIQDEVKDPARCEQ-----LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 552148158 511 KQAVDELSHNRTTFI-IAHRLSTVRS-ADLVLFMDKGHLVESG 551
Cdd:PRK10938 175 AELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETG 217
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
26-304 |
2.53e-03 |
|
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: 40.22 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 26 VASVLVALVALAEPVLFGRVIQSISDK---------GDIFSP----LLMWAALGGFNIMAAVFVARGADRLAHRRRlgvm 92
Cdd:cd18574 3 LSALAAALVNIQIPLLLGDLVNVISRSlketngdfiEDLKKPalklLGLYLLQSLLTFAYISLLSVVGERVAARLR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 93 IDSYERLITMPLAWHQKRGT---SNALHTLIRATDSLF----TLWLEFMRQHLTTVVALATLIPvAMTMdmrmsLVLIVL 165
Cdd:cd18574 79 NDLFSSLLRQDIAFFDTHRTgelVNRLTADVQEFKSSFkqcvSQGLRSVTQTVGCVVSLYLISP-KLTL-----LLLVIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 166 GVIYV---MIGQLVMRKTKDGQAAVEKhhhklFEHVSD-TISNVSVVQSYnriASETQALRDYAKNLENAQfpvlnwwAL 241
Cdd:cd18574 153 PVVVLvgtLYGSFLRKLSRRAQAQVAK-----ATGVADeALGNIRTVRAF---AMEDRELELYEEEVEKAA-------KL 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552148158 242 AS------GLNRMASTF---SMV-VVLVLGAYFVTKGQMRVGDVIAFIGFVQLMIGRLDQISAFINQTVTARA 304
Cdd:cd18574 218 NEklglgiGIFQGLSNLalnGIVlGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKS 290
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
141-284 |
3.88e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 39.77 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 141 VVALATLIPVA---MTMDMRMSLVLIVLGVIYVMIGQLVMRKTkdGQAAVEKHHhKLFEHVSDTISNVSVVQSYNRIASE 217
Cdd:cd18585 121 LVILATILFLAffsPALALILLAGLLLAGVVIPLLFYRLGKKI--GQQLVQLRA-ELRTELVDGLQGMAELLIFGALERQ 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552148158 218 TQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRvGDVIAFIGFVQL 284
Cdd:cd18585 198 RQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALD-GALLAMLVFAVL 263
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
472-544 |
4.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552148158 472 LSGGERQ------RLAIARAILKDSPILVLDEATSALDVETEEKVKQAVD----ELSHNRTTFIIAHRLSTVRSADLVLF 541
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEyslkDSSDIPQVIMISHHRELLSVADVAYE 881
|
...
gi 552148158 542 MDK 544
Cdd:PRK01156 882 VKK 884
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
337-379 |
6.41e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 6.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 552148158 337 FDNVTFEFpnsGQGIydvsfevkpgqtVAIVGPTGAGKTTLIN 379
Cdd:pfam13476 9 FRDQTIDF---SKGL------------TLITGPNGSGKTTILD 36
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
363-381 |
8.40e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.44 E-value: 8.40e-03
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
471-544 |
8.67e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 8.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552148158 471 QLSGGERQRLAIAR--AILK--DSPILVLDEATSALDVETEEKVKQAVDELSHNrTTFIIAhrlsTVRSaDLVLFMDK 544
Cdd:cd03272 158 QLSGGQKSLVALALifAIQKcdPAPFYLFDEIDAALDAQYRTAVANMIKELSDG-AQFITT----TFRP-ELLEVADK 229
|
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| |
