|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-542 |
0e+00 |
|
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: 667.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 13 YKGYLVKIALTSFISGGAIIAQAYLIAYIINGAFLAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIR 92
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 93 NVLLEKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVF 172
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 173 MMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATI 252
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 253 STAMVAVEVGLRLLYGKMEFLQAFFVLLLAPELYLPLRNLGSSFHAGRTAIAFSQKLWTIIEEKEsRVFLNKRSITWDSP 332
Cdd:TIGR02857 241 SVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAP-RPLAGKAPVTAAPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVG 412
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKI 492
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 499664576 493 VILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILI 542
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-560 |
0e+00 |
|
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: 662.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 2 IEKRLNQEALKYKGYLVKIALTSFISGGAIIAQAYLIAYIINGAFLAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGA 81
Cdd:COG4988 4 LDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 82 NLASKVTGEIRNVLLEKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGII 161
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 162 MLLTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFL 241
Cdd:COG4988 164 LLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 242 SALALEVLATISTAMVAVEVGLRLLYGKMEFLQAFFVLLLAPELYLPLRNLGSSFHAGRTAIAFSQKLWTIIEEKESRVF 321
Cdd:COG4988 244 SSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 322 LNKRSITWDSPPEIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWE 401
Cdd:COG4988 324 AGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 402 LKEKDWYDQVGYLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIA 481
Cdd:COG4988 404 LDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLA 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 482 LARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAEN 560
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-573 |
3.30e-147 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 436.52 E-value: 3.30e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 4 KRLNQEALKYKGYLVKIALTSFISGGAIIAQAYLIAYIINGAFlAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANL 83
Cdd:COG1132 10 RRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 84 ASKVTGEIRNVLLEKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIML 163
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 164 LTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSA 243
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 244 LALEVLATISTAMVAVEVGLRLLYGKMEFLQAFFVLLLAPELYLPLRNLGSSFHAGRTAIAFSQKLWTIIEEKESRVFLN 323
Cdd:COG1132 249 PLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 324 KRSITWDSPPEIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELK 403
Cdd:COG1132 329 GAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 404 EKDWYDQVGYLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVgeggrglsggerQRIALA 483
Cdd:COG1132 409 LESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVgergvnlsggqrQRIAIA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 484 RVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELY 563
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLY 568
|
570
....*....|
gi 499664576 564 RQLITAYRGE 573
Cdd:COG1132 569 ARLYRLQFGE 578
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-574 |
4.42e-146 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 433.89 E-value: 4.42e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 25 FISGGAIIAQAYLIAYIINGAFLAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIAALGT 104
Cdd:PRK11174 32 FLSGLLLIAQAWLLATILQALIIENIPREALLPPFILLILLFVLRALLAWLRERVGFKAGQHIRQQIRQQVLDKLQQLGP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 105 KVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAEKLA 184
Cdd:PRK11174 112 AWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTAPLIPLFMALVGMGAADAN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 185 QKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVAVEVGLR 264
Cdd:PRK11174 192 RRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASISIALVAVYFGFS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 265 LLyGKMEF--------LQA-FFVLLLAPELYLPLRNLGSSFHAGRTAIAFSQKLWTIIEEKESRVFLNKRSITWDSPPEI 335
Cdd:PRK11174 272 YL-GELNFghygtgvtLFAgFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDPVTI 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 336 I---LKQVSHSyipGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMrPAEGEILINGVPLWELKEKDWYDQVG 412
Cdd:PRK11174 351 EaedLEILSPD---GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLS 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKI 492
Cdd:PRK11174 427 WVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQL 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 493 VILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLITAYRG 572
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
..
gi 499664576 573 EV 574
Cdd:PRK11174 587 EI 588
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
21-309 |
4.42e-123 |
|
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: 364.04 E-value: 4.42e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 21 ALTSFISGGAIIAQAYLIAYIINGAFLAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIA 100
Cdd:cd18584 2 VLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 101 ALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFA 180
Cdd:cd18584 82 ALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 181 EKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVAVE 260
Cdd:cd18584 162 QAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAVY 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499664576 261 VGLRLLYGKMEFLQAFFVLLLAPELYLPLRNLGSSFHAGRTAIAFSQKL 309
Cdd:cd18584 242 IGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-567 |
1.01e-97 |
|
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: 312.54 E-value: 1.01e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 4 KRLNQEALKYKGYLVKIALTSFISGGAIIAQAYLIAYIINGAfLAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANL 83
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRV-LPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 84 ASKVTGEIRNVLLEKIAALGTKVLLPEKTGELLTLILEgVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIML 163
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 164 LTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSA 243
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 244 LALEVLATISTAMVAVEVGLRLLYGKM---EFL--QAFFVLLLAPelylpLRNLGSSFHAGRTAIAFSQKLWTIIEEKES 318
Cdd:COG2274 383 TLSGLLQQLATVALLWLGAYLVIDGQLtlgQLIafNILSGRFLAP-----VAQLIGLLQRFQDAKIALERLDDILDLPPE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 319 RVFLNKRSITWDSPPEIILKQVSHSYIP-GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGV 397
Cdd:COG2274 458 REEGRSKLSLPRLKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 398 PLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGER 477
Cdd:COG2274 538 DLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQR 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 478 QRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLL 557
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
570
....*....|
gi 499664576 558 AENELYRQLI 567
Cdd:COG2274 698 ARKGLYAELV 707
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-566 |
2.06e-94 |
|
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: 299.76 E-value: 2.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 12 KYKGYLVKIALTSFISGGAIIAQAYLIAYIINGAFLAkkglgelwPFFPALFL-IVTLR-FSLG-----YfGEK-VGANL 83
Cdd:COG4987 12 PHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALA--------PPILNLFVpIVGVRaFAIGrtvfrY-LERlVSHDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 84 ASKVTGEIRNVLLEKIAALGTKVLLPEKTGELLTLILEGVESLEVYYAR-YLPQLISAGIIPLMILVV---VLALDLISG 159
Cdd:COG4987 83 TLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRvLLPLLVALLVILAAVAFLaffSPALALVLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 160 IIMLLTAPLIPVFMMLIGSfaeKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVA 239
Cdd:COG4987 163 LGLLLAGLLLPLLAARLGR---RAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 240 FLSALALEVLATISTAMVAVEVGLRLLYGKME--FLQAFFVLLLA-PELYLPLRNLGSsfHAGRTAIAfSQKLWTIIEEK 316
Cdd:COG4987 240 ALAQALLQLAAGLAVVAVLWLAAPLVAAGALSgpLLALLVLAALAlFEALAPLPAAAQ--HLGRVRAA-ARRLNELLDAP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 317 ESRVFlNKRSITWDSPPEIILKQVSHSYIPGKE-VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILIN 395
Cdd:COG4987 317 PAVTE-PAEPAPAPGGPSLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 396 GVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGG 475
Cdd:COG4987 396 GVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 476 ERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQ 555
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE 555
|
570
....*....|.
gi 499664576 556 LLAENELYRQL 566
Cdd:COG4987 556 LLAQNGRYRQL 566
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
334-560 |
1.16e-81 |
|
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: 255.23 E-value: 1.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGY 413
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIV 493
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAEN 560
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
335-569 |
1.18e-80 |
|
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: 252.85 E-value: 1.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYI--PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVG 412
Cdd:cd03249 1 IEFKNVSFRYPsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKI 492
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 493 VILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLITA 569
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
335-566 |
1.27e-77 |
|
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: 244.83 E-value: 1.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIP-GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGY 413
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIV 493
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQL 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 |
1.30e-74 |
|
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: 237.13 E-value: 1.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYL 414
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVI 494
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499664576 495 LDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQL 566
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-566 |
1.07e-71 |
|
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: 240.39 E-value: 1.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 4 KRLNQEALKYKGYLVKIALTSFISGGAIIAQAYLIAYIINGAFlAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANL 83
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGF-GGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 84 ASKVTGEIRNVLLEKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIML 163
Cdd:TIGR02203 82 SNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 164 LTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSA 243
Cdd:TIGR02203 162 VMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 244 LALEVLATISTAMVAVEVGLRLLYGKMEF--LQAFFVLLLApeLYLPLRNLGSSFHAGRTAIAFSQKLWTIIeekesrvf 321
Cdd:TIGR02203 242 PITQLIASLALAVVLFIALFQAQAGSLTAgdFTAFITAMIA--LIRPLKSLTNVNAPMQRGLAAAESLFTLL-------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 322 lnkrsitwDSPPE--------------IILKQVSHSYIP-GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMR 386
Cdd:TIGR02203 312 --------DSPPEkdtgtraierargdVEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 387 PAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGK-KGAKGEEIKRAASLAGAHQFIAELPQGYDTKV 465
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 466 GEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRG 545
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543
|
570 580
....*....|....*....|.
gi 499664576 546 EIRGMGRHEQLLAENELYRQL 566
Cdd:TIGR02203 544 RIVERGTHNELLARNGLYAQL 564
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-546 |
2.58e-69 |
|
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: 221.10 E-value: 2.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPG-KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGY 413
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFIFPGSIAENIalgkkgakgeeikraasLAGAHQfiaelpqgydtkvgeggrglsggerQRIALARVFLKDAKIV 493
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------LSGGQR-------------------------QRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGE 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 |
3.96e-66 |
|
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: 215.04 E-value: 3.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIP-GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLwELKEKDWYD-QVG 412
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL-ALADPAWLRrQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKI 492
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 493 VILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQL 566
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
285-566 |
1.03e-64 |
|
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: 222.39 E-value: 1.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 285 LYLPLRNLGSSFHAGRTAIAFSQKLWTIIEEKesrvflnkRSITwDSP---------PEIILKQVSHSYIPGKEVLKNIN 355
Cdd:COG5265 308 LYIPLNFLGFVYREIRQALADMERMFDLLDQP--------PEVA-DAPdapplvvggGEVRFENVSFGYDPERPILKGVS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 356 LTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGKKG 435
Cdd:COG5265 379 FEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 436 AKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFD 515
Cdd:COG5265 459 ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499664576 516 ELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQL 566
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
21-309 |
1.37e-61 |
|
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: 205.21 E-value: 1.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 21 ALTSFISGGAIIAQAYLIAYIINGAFlAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIA 100
Cdd:cd18561 2 VLLGLLITALYIAQAWLLARALARIF-AGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 101 ALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFA 180
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 181 EKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVAVE 260
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499664576 261 VGLRLLYGKMEFLQAFFVLLLAPELYLPLRNLGSSFHAGRTAIAFSQKL 309
Cdd:cd18561 241 GALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
334-547 |
4.16e-60 |
|
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: 198.58 E-value: 4.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYiPGKE--VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQV 411
Cdd:cd03245 2 RIEFRNVSFSY-PNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAK 491
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 492 IVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEI 547
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
335-566 |
3.37e-58 |
|
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: 206.52 E-value: 3.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGK-EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGY 413
Cdd:TIGR01846 456 ITFENIRFRYAPDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIV 493
Cdd:TIGR01846 536 VLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRIL 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQL 566
Cdd:TIGR01846 616 IFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
85-567 |
5.30e-58 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 206.11 E-value: 5.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 85 SKVTGEIRNVLLEKIAALGTKVLLPEKTGELLTLILEGVESLevyyARYLPQLISAGIIPLMILVVVLALdLISG----- 159
Cdd:TIGR00958 230 ARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTM----SRSLSLNVNVLLRNLVMLLGLLGF-MLWLsprlt 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 160 IIMLLTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKeqvNELKKsglmFRDATMEVLRVA 239
Cdd:TIGR00958 305 MVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEE---GEASR----FKEALEETLQLN 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 240 FLSALALEVLATISTAM-----VAV-EVGLRL-LYGKMEFLQAFFVLLLAPELYLPLRNLGSSFHAGRTAIAFSQKLWTI 312
Cdd:TIGR00958 378 KRKALAYAGYLWTTSVLgmliqVLVlYYGGQLvLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 313 IEEKESrvflnkrsitwdSPPEIIL-----------KQVSHSYI--PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVK 379
Cdd:TIGR00958 458 LDRKPN------------IPLTGTLaplnlegliefQDVSFSYPnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 380 LLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQ 459
Cdd:TIGR00958 526 LLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPN 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 460 GYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKafDELFQNRTVIIIAHRLSSLYRADKI 539
Cdd:TIGR00958 606 GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQI 683
|
490 500
....*....|....*....|....*...
gi 499664576 540 ILIDRGEIRGMGRHEQLLAENELYRQLI 567
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
140-566 |
5.99e-58 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 203.71 E-value: 5.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 140 AGIIPLMILVVVLALDLisGIIMLLTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVN 219
Cdd:PRK11176 151 ASIIGLFIMMFYYSWQL--SLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 220 ELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVavevglrlLYGK-----MEFLQA-----FFVLLLApeLYLPL 289
Cdd:PRK11176 229 RFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFV--------LYAAsfpsvMDTLTAgtitvVFSSMIA--LMRPL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 290 R---NLGSSFHAGrtaIAFSQKLWTIIE---EKESRVFLNKRSitwdsPPEIILKQVSHSYiPGKEV--LKNINLTIKPL 361
Cdd:PRK11176 299 KsltNVNAQFQRG---MAACQTLFAILDleqEKDEGKRVIERA-----KGDIEFRNVTFTY-PGKEVpaLRNINFKIPAG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 362 EKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGKKGAKG-EE 440
Cdd:PRK11176 370 KTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSrEQ 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 441 IKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN 520
Cdd:PRK11176 450 IEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN 529
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 499664576 521 RTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQL 566
Cdd:PRK11176 530 RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
74-530 |
1.34e-56 |
|
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: 198.74 E-value: 1.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 74 YFGEKVGANLASKVTGEIRNVLLEKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLA 153
Cdd:TIGR02868 71 YLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 154 LDLISGIIMLLTAPLIPVFMMLIGSFAEKLA-QKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGlmfRDAT 232
Cdd:TIGR02868 151 LSVPAALILAAGLLLAGFVAPLVSLRAARAAeQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEAD---RELT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 233 MEVLRVAFLSAL--ALEVLATISTAMVAVEVGLRLLYGKMEFLQAFFVLLLAP----ELYLPLRNLGSSFHAGRTAIAfs 306
Cdd:TIGR02868 228 RAERRAAAATALgaALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPlaafEAFAALPAAAQQLTRVRAAAE-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 307 qklwTIIEEKESRVFLNKRSITWDSP-----PEIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLL 381
Cdd:TIGR02868 306 ----RIVEVLDAAGPVAEGSAPAAGAvglgkPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 382 LGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGY 461
Cdd:TIGR02868 382 AGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGL 461
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 462 DTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEK-LLEKAFDELfQNRTVIIIAHRL 530
Cdd:TIGR02868 462 DTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADeLLEDLLAAL-SGRTVVLITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
338-547 |
8.45e-55 |
|
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: 184.98 E-value: 8.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 338 KQVSHSYI--PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLH 415
Cdd:cd03248 15 QNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 416 QTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVIL 495
Cdd:cd03248 95 QEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499664576 496 DEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEI 547
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
146-569 |
1.62e-54 |
|
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: 196.50 E-value: 1.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 146 MILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFA---EKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQ----- 217
Cdd:TIGR01193 282 ILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKrtfNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERyskid 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 218 ---VNELKKSglmFRDATMEVLRVAFLSALALEVLATISTAMVAVEVGLRLLYGKMEFLQAFFVLLLAPelYLPLRNLGS 294
Cdd:TIGR01193 362 sefGDYLNKS---FKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTP--LENIINLQP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 295 SFHAGRTAIAFSQKLWTIIEEkesrvFLNKRSITWDSPP--EIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGA 372
Cdd:TIGR01193 437 KLQAARVANNRLNEVYLVDSE-----FINKKKRTELNNLngDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGS 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 373 GKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALG-KKGAKGEEIKRAASLAGAH 451
Cdd:TIGR01193 512 GKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIK 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 452 QFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKlleKAFDEL--FQNRTVIIIAHR 529
Cdd:TIGR01193 592 DDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEK---KIVNNLlnLQDKTIIFVAHR 668
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 499664576 530 LSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLITA 569
Cdd:TIGR01193 669 LSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
97-567 |
2.97e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 190.42 E-value: 2.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 97 EKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAgiiPLMILVVVLALDLIS-------GIIMLLTAPLI 169
Cdd:PRK11160 101 SKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAA---LVVILVLTIGLSFFDltlaltlGGILLLLLLLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 170 P-VFMMLIGSFAEKLAQKQwsslSRLSGKFFELLQGIADLKAFG---RSKEQVNELKKSgLMFRDATMevlrvAFLSAL- 244
Cdd:PRK11160 178 PlLFYRLGKKPGQDLTHLR----AQYRVQLTEWLQGQAELTLFGaedRYRQQLEQTEQQ-WLAAQRRQ-----ANLTGLs 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 245 -ALEVLA-----TISTAMVAVEVGLRLLYGKMEFLQAFFVL----LLAPelylplrnLGSSF-HAGRTaIAFSQKLWTII 313
Cdd:PRK11160 248 qALMILAngltvVLMLWLAAGGVGGNAQPGALIALFVFAALaafeALMP--------VAGAFqHLGQV-IASARRINEIT 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 314 EEKESRVFLNKRSITWDSPpEIILKQVSHSYIPGKE-VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEI 392
Cdd:PRK11160 319 EQKPEVTFPTTSTAAADQV-SLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 393 LINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIaELPQGYDTKVGEGGRGL 472
Cdd:PRK11160 398 LLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 473 SGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGR 552
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
490
....*....|....*
gi 499664576 553 HEQLLAENELYRQLI 567
Cdd:PRK11160 557 HQELLAQQGRYYQLK 571
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
350-559 |
1.22e-52 |
|
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: 188.80 E-value: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENI 429
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 430 A-LGKkgAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEK 508
Cdd:COG4618 427 ArFGD--ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEA 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499664576 509 LLEKAFDEL-FQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAE 559
Cdd:COG4618 505 ALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
348-571 |
6.45e-52 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 186.84 E-value: 6.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAE 427
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 428 NIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTE 507
Cdd:PRK10789 408 NIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 508 KLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLitaYR 571
Cdd:PRK10789 488 HQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM---YR 548
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
334-569 |
2.30e-51 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 185.55 E-value: 2.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGY 413
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIV 493
Cdd:PRK13657 414 VFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLITA 569
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-551 |
6.98e-51 |
|
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: 174.22 E-value: 6.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYIPG-KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQV 411
Cdd:cd03244 1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPGSIAENIA-LGKKGAkgEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDA 490
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGEYSD--EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499664576 491 KIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMG 551
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
136-567 |
1.37e-48 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 179.75 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 136 QLISAGIIPLMI---LVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKA-- 210
Cdd:TIGR03796 270 QLATTALDAVMLvfyALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKAsg 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 211 -----FGR-SKEQ---VNELKKSGLmfrdatmevlRVAFLSALAlEVLATISTAMVAVEVGLRLLYGKMEF--LQAFFVL 279
Cdd:TIGR03796 350 lesdfFSRwAGYQaklLNAQQELGV----------LTQILGVLP-TLLTSLNSALILVVGGLRVMEGQLTIgmLVAFQSL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 280 LLApeLYLPLRNLGSSFHAGRTAIAFSQKLWTIIEEKESRVFLNKRSITWDSPP------EIILKQVSHSYIP-GKEVLK 352
Cdd:TIGR03796 419 MSS--FLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPVDPLLEEPEGSAATSEPprrlsgYVELRNITFGYSPlEPPLIE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 353 NINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALG 432
Cdd:TIGR03796 497 NFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLW 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 433 KKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLek 512
Cdd:TIGR03796 577 DPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII-- 654
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 513 afDELFQNR--TVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLI 567
Cdd:TIGR03796 655 --DDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
20-309 |
1.48e-48 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 170.41 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 20 IALTSFISGGAIIAQAYLIAYIINGAFLAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKI 99
Cdd:cd18781 1 TVLLQWISLLANIAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 100 AALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSF 179
Cdd:cd18781 81 LRLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 180 AEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVAV 259
Cdd:cd18781 161 AKKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVAYGGAALGII 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499664576 260 EVGLRLLYGKMEFLQAFFVLLLAPELYLPLRNLGSSFHAGRTAIAFSQKL 309
Cdd:cd18781 241 LALLQFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASDKI 290
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
335-562 |
7.26e-48 |
|
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: 166.74 E-value: 7.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYL 414
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPF--IFPGSIAENIALGKK--GAKGEEIKR----AASLAG----AHQFIAELPQGydtkvgeggrglsggERQRIAL 482
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFGPEnlGLPREEIRErveeALELVGlehlADRPPHELSGG---------------QKQRVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 483 ARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ-NRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAEN 560
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
..
gi 499664576 561 EL 562
Cdd:COG1122 226 EL 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
345-559 |
3.30e-47 |
|
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: 173.30 E-value: 3.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 345 IPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGS 424
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 425 IAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDA 504
Cdd:TIGR01842 408 VAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 505 HTEKLLEKAFDEL-FQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAE 559
Cdd:TIGR01842 488 EGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-547 |
1.07e-44 |
|
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: 156.32 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIP-GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELkEKDWYDQVGY 413
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFIFPGSIAENiaLGKKGAKGEEikraaslagahqfiaelpqgydtkvgeggrglsggerQRIALARVFLKDAKIV 493
Cdd:cd03247 80 LNQRPYLFDTTLRNN--LGRRFSGGER-------------------------------------QRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 494 ILDEPTAGLDAHTE-KLLEKAFDELfQNRTVIIIAHRLSSLYRADKIILIDRGEI 547
Cdd:cd03247 121 LLDEPTVGLDPITErQLLSLIFEVL-KDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-547 |
2.80e-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: 155.07 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKE--VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVG 412
Cdd:cd03246 1 LEVENVSFRY-PGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPGSIAENIalgkkgakgeeikraasLAGahqfiaelpqGYdtkvgeggrglsggeRQRIALARVFLKDAKI 492
Cdd:cd03246 80 YLPQDDELFSGSIAENI-----------------LSG----------GQ---------------RQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 493 VILDEPTAGLDAHTEKLLEKAFDEL-FQNRTVIIIAHRLSSLYRADKIILIDRGEI 547
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
334-569 |
3.82e-43 |
|
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: 162.75 E-value: 3.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGY 413
Cdd:TIGR01192 334 AVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIAT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIV 493
Cdd:TIGR01192 414 VFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLITA 569
Cdd:TIGR01192 494 VLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
137-566 |
9.84e-42 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 158.73 E-value: 9.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 137 LISAGIIPLMiLVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAF---GR 213
Cdd:PRK10790 147 LRSAALIGAM-LVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFrqqAR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 214 SKEQVNELKKSGLMFRdatMEVLRvafLSALALEVLATISTAMVAVevGLRLLYG-------KMEFLQAFFVLLlaPELY 286
Cdd:PRK10790 226 FGERMGEASRSHYMAR---MQTLR---LDGFLLRPLLSLFSALILC--GLLMLFGfsasgtiEVGVLYAFISYL--GRLN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 287 LPLRNLGSSFHAGRTAIAFSQKLWTIIEEKESRVFLNKRSITWDSppeIILKQVSHSYIPGKEVLKNINLTIKPLEKVAI 366
Cdd:PRK10790 296 EPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQSGR---IDIDNVSFAYRDDNLVLQNINLSVPSRGFVAL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 367 VGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGKKGAKgEEIKRAAS 446
Cdd:PRK10790 373 VGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISE-EQVWQALE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 447 LAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIII 526
Cdd:PRK10790 452 TVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI 531
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 499664576 527 AHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQL 566
Cdd:PRK10790 532 AHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
330-574 |
6.27e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 6.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 330 DSPPEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKdwyd 409
Cdd:COG1121 2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 qVGYLHQTPFI---FPGSIAENIALGKKGAKG----------EEIKRAASLAG----AHQFIAELPQGydtkvgeggrgl 472
Cdd:COG1121 77 -IGYVPQRAEVdwdFPITVRDVVLMGRYGRRGlfrrpsradrEAVDEALERVGledlADRPIGELSGG------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 473 sggERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDEL-FQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRgM 550
Cdd:COG1121 144 ---QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLVA-H 219
|
250 260
....*....|....*....|....
gi 499664576 551 GRHEQLLAENELYRqlitAYRGEV 574
Cdd:COG1121 220 GPPEEVLTPENLSR----AYGGPV 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
335-567 |
3.26e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 143.28 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKdWYDQVGYL 414
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPG-SIAENIA-------LGKKGAKG--EEIKRAASLAG-AHQFIAELPQGYdtkvgeggrglsggeRQRIALA 483
Cdd:COG1131 79 PQEPALYPDlTVRENLRffarlygLPRKEAREriDELLELFGLTDaADRKVGTLSGGM---------------KQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 484 RVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAE-- 559
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARll 223
|
....*...
gi 499664576 560 NELYRQLI 567
Cdd:COG1131 224 EDVFLELT 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-546 |
4.41e-39 |
|
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: 142.22 E-value: 4.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYIPGKE-VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLH 415
Cdd:cd03225 2 LKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 416 QTP---FIFPgSIAENIALGKK--GAKGEEIKRAASLAG--------AHQFIAELPQGydtkvgeggrglsggERQRIAL 482
Cdd:cd03225 82 QNPddqFFGP-TVEEEVAFGLEnlGLPEEEIEERVEEALelvgleglRDRSPFTLSGG---------------QKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 483 ARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAHRLSSLYR-ADKIILIDRGE 546
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
337-547 |
9.02e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.11 E-value: 9.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYIpGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQ 416
Cdd:COG4619 3 LEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TPFIFPGSIAENIALGKKgAKGEEIKRAASLAGAHQFiaELPQGY-DTKVgeggrglsggER------QRIALARVFLKD 489
Cdd:COG4619 82 EPALWGGTVRDNLPFPFQ-LRERKFDRERALELLERL--GLPPDIlDKPV----------ERlsggerQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 490 AKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAH------RLsslyrADKIILIDRGEI 547
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
332-547 |
1.31e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.33 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 332 PPEIILKQVSHSYIPGKE---VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDW- 407
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 408 ---YDQVGYLHQTPFIFPG-SIAENIALG---KKGAKGEEIKRAASLAG-------AHQFIAELPQGydtkvgeggrgls 473
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPElTALENVALPlllAGVSRKERRERARELLErvglgdrLDHRPSQLSGG------------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 474 ggERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYRADKIILIDRGEI 547
Cdd:COG1136 149 --QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
330-567 |
4.32e-38 |
|
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: 140.50 E-value: 4.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 330 DSPPEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD 409
Cdd:COG1127 1 MSEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 ---QVGYLHQTPFIFPG-SIAENIALG---KKGAKGEEIKRAAS-------LAGA-HQFIAELPQGYdtkvgeggrglsg 474
Cdd:COG1127 80 lrrRIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLeklelvgLPGAaDKMPSELSGGM------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 475 geRQRIALARVFLKDAKIVILDEPTAGLDAHTekllEKAFDELFQNR------TVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:COG1127 147 --RKRVALARALALDPEILLYDEPTAGLDPIT----SAVIDELIRELrdelglTSVVVTHDLDSAFAiADRVAVLADGKI 220
|
250 260
....*....|....*....|.
gi 499664576 548 RGMGRHEQLLA-ENELYRQLI 567
Cdd:COG1127 221 IAEGTPEELLAsDDPWVRQFL 241
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
337-545 |
8.09e-38 |
|
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: 138.82 E-value: 8.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLwelkEKDWyDQVGYLHQ 416
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKER-KRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TPFI---FPGSIAENIALGKKGAKG----------EEIKRAASLAG----AHQFIAELPQGydtkvgeggrglsggERQR 479
Cdd:cd03235 76 RRSIdrdFPISVRDVVLMGLYGHKGlfrrlskadkAKVDEALERVGlselADRQIGELSGG---------------QQQR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 480 IALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ-NRTVIIIAHRLSS-LYRADKIILIDRG 545
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLvLEYFDRVLLLNRT 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
335-547 |
2.33e-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: 135.99 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWElKEKDWYDQVGYL 414
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPG-SIAENIALgKKGAKgeeikraaslagahqfiaelpqgydtkvgeggrglsggerQRIALARVFLKDAKIV 493
Cdd:cd03230 79 PEEPSLYENlTVRENLKL-SGGMK----------------------------------------QRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDEL-FQNRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
337-546 |
6.63e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 134.29 E-value: 6.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQ 416
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 tpfifpgsiaenialgkkgakgeeikraasLAGAHQfiaelpqgydtkvgeggrglsggerQRIALARVFLKDAKIVILD 496
Cdd:cd00267 81 ------------------------------LSGGQR-------------------------QRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499664576 497 EPTAGLDAHTEKLLEKAFDELFQ-NRTVIIIAHRLSSLYRA-DKIILIDRGE 546
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
326-546 |
7.06e-37 |
|
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: 136.06 E-value: 7.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 326 SITWDSPPEiilkqvshsyiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGvplwelkek 405
Cdd:cd03250 7 SFTWDSGEQ-----------ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 406 dwydQVGYLHQTPFIFPGSIAENIALGKK--GAKGEEIKRAASLagaHQFIAELPQGYDT-------------Kvgeggr 470
Cdd:cd03250 67 ----SIAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKACAL---EPDLEILPDGDLTeigekginlsggqK------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 471 glsggerQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLekaFDELFQ-----NRTVIIIAHRLSSLYRADKIILIDRG 545
Cdd:cd03250 134 -------QRISLARAVYSDADIYLLDDPLSAVDAHVGRHI---FENCILglllnNKTRILVTHQLQLLPHADQIVVLDNG 203
|
.
gi 499664576 546 E 546
Cdd:cd03250 204 R 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
335-547 |
9.20e-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: 136.08 E-value: 9.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKE---VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDW---- 407
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 408 YDQVGYLHQTPFIFPG-SIAENIALG--KKGAKGEEIK-RAASLAG-------AHQFIAELPQGydtkvgeggrglsggE 476
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPllLAGVPKKERReRAEELLErvglgdrLNHYPSELSGG---------------Q 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 477 RQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDEL--FQNRTVIIIAHRLSSLYRADKIILIDRGEI 547
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
335-564 |
1.20e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 136.71 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYL 414
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFI-FPGSIAENIALGKKGAKG----------EEIKRAASLAG----AHQFIAELPQGydtkvgeggrglsggERQR 479
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRYPHLGlfgrpsaedrEAVEEALERTGlehlADRPVDELSGG---------------ERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 480 IALARVFLKDAKIVILDEPTAGLD-AHTEKLLEkAFDEL--FQNRTVIIIAH--RLSSLYrADKIILIDRGEIRGMGRHE 554
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDlAHQLEVLE-LLRRLarERGRTVVMVLHdlNLAARY-ADRLVLLKDGRIVAQGPPE 223
|
250
....*....|...
gi 499664576 555 QLL-AEN--ELYR 564
Cdd:COG1120 224 EVLtPELleEVYG 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
351-500 |
1.92e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.77 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPG-SIAENI 429
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 430 ALgkkGAKGEEIKRAASLAGAHQFIAELPQGY--DTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTA 500
Cdd:pfam00005 81 RL---GLLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
335-559 |
3.18e-35 |
|
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: 132.67 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWElKEKDWYDQVGYL 414
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPG-SIAENIALGKK--GAKGEEIK-RAASLAG-------AHQFIAELPQGYDTKVgeggrglsggerqriALA 483
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFAElyGLFDEELKkRIEELIEllgleefLDRRVGELSTGMKKKV---------------ALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 484 RVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAE 559
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
330-569 |
3.66e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 138.88 E-value: 3.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 330 DSPPEIILKQVSHSY----IPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEK 405
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 406 DWYD---QVGYLHQTPF--IFP-----GSIAENIALGKKGAKGEEIKRAASLAG--------AHQFIAELPQGydtkvge 467
Cdd:COG1123 336 SLRElrrRVQMVFQDPYssLNPrmtvgDIIAEPLRLHGLLSRAERRERVAELLErvglppdlADRYPHELSGG------- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 468 ggrglsggERQRIALARVFLKDAKIVILDEPTAGLDAHTE----KLLEKAFDELfqNRTVIIIAHRLSSLYR-ADKIILI 542
Cdd:COG1123 409 --------QRQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLLRDLQREL--GLTYLFISHDLAVVRYiADRVAVM 478
|
250 260
....*....|....*....|....*....
gi 499664576 543 DRGEIRGMGRHEQLLA-ENELY-RQLITA 569
Cdd:COG1123 479 YDGRIVEDGPTEEVFAnPQHPYtRALLAA 507
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-542 |
9.64e-35 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 130.67 E-value: 9.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPG---KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKekdwyDQV 411
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFP-GSIAENIALGKK--GAKGEEIKRAAS-------LAG-AHQFIAELPQGydtkvgeggrglsggERQRI 480
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERAEellelvgLSGfENAYPHQLSGG---------------MRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAHTEKLLEkafDELFQ-----NRTVIIIAHRLS-SLYRADKIILI 542
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQ---EELLDiwretGKTVLLVTHDIDeAVFLADRVVVL 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
334-567 |
1.59e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 139.78 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYI--PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLL----------------------------- 382
Cdd:PTZ00265 1165 KIEIMDVNFRYIsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 383 ------GLMRPAE-------------------GEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGKKGAK 437
Cdd:PTZ00265 1245 deeqnvGMKNVNEfsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 438 GEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDEL 517
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 518 FQ--NRTVIIIAHRLSSLYRADKIILIDRGE-----IRGMGRHEQLL-AENELYRQLI 567
Cdd:PTZ00265 1405 KDkaDKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGVYKKYV 1462
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
337-547 |
3.10e-34 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 127.94 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQ 416
Cdd:cd03214 2 VENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 tpfifpgsiaeniALGKKGakgeeikrAASLagAHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIVILD 496
Cdd:cd03214 81 -------------ALELLG--------LAHL--ADRPFNELSGG---------------ERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499664576 497 EPTAGLD-AHTEKLLEKAFDE-LFQNRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:cd03214 123 EPTSHLDiAHQIELLELLRRLaRERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
335-565 |
3.86e-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: 129.54 E-value: 3.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD---QV 411
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPG-SIAENIA--LGKKGAKGEEIKR--------AASLAGA-HQFIAELPQGydtkvgeggrglsggERQR 479
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAfpLREHTRLSEEEIReivlekleAVGLRGAeDLYPAELSGG---------------MKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 480 IALARVFLKDAKIVILDEPTAGLDAHTekllEKAFDELFQ------NRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGR 552
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIA----SGVIDDLIRslkkelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGT 220
|
250
....*....|....
gi 499664576 553 HEQLLA-ENELYRQ 565
Cdd:cd03261 221 PEELRAsDDPLVRQ 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
335-547 |
4.88e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.94 E-value: 4.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKD---WYDQV 411
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPG-SIAENIALGKK--GAKGEEIKRAAS-------LAG-AHQFIAELPQGydtkvgeggrglsggERQRI 480
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALPLRvtGKSRKEIRRRVRevldlvgLSDkAKALPHELSGG---------------EQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAHT-EKLLEkAFDELFQNRTVIIIA---HRLSSLYRAdKIILIDRGEI 547
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETsWEIME-LLEEINRRGTTVLIAthdLELVDRMPK-RVLELEDGRL 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
335-572 |
5.73e-33 |
|
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: 126.46 E-value: 5.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSY---IPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQV 411
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFifpGS----------IAENIALGKKGAKGEEIKRAASLAG-----AHQFIAELPQGydtkvgeggrglsggE 476
Cdd:COG1124 82 QMVFQDPY---ASlhprhtvdriLAEPLRIHGLPDREERIAELLEQVGlppsfLDRYPHQLSGG---------------Q 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 477 RQRIALARVFLKDAKIVILDEPTAGLDAHTEK----LLEKAFDElfQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMG 551
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAeilnLLKDLREE--RGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
250 260
....*....|....*....|...
gi 499664576 552 RHEQLL--AENELYRQLITAYRG 572
Cdd:COG1124 222 TVADLLagPKHPYTRELLAASLA 244
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
329-552 |
6.00e-33 |
|
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: 125.22 E-value: 6.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 329 WDSPPEIILKQVSHSYIPG-KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDW 407
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 408 YDQVGYLHQTPFIFPGSIAENIALGKKGAKgEEIKRAASLAGAHQfiaELPQGydtkvgeggrglsggERQRIALARVFL 487
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSD-EEIYGALRVSEGGL---NLSQG---------------QRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 488 KDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGR 552
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
328-563 |
1.10e-32 |
|
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: 134.30 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 328 TWDSPPEIILKQVSHSYIPGKE-VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKD 406
Cdd:TIGR00957 1278 GWPPRGRVEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 407 WYDQVGYLHQTPFIFPGSIAENIALGKKGAKgEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVF 486
Cdd:TIGR00957 1358 LRFKITIIPQDPVLFSGSLRMNLDPFSQYSD-EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 487 LKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELY 563
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
335-546 |
1.54e-32 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 123.07 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKE--KDWYDQVG 412
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPG-SIAENIALGkkgakgeeikraasLAGAHQfiaelpqgydtkvgeggrglsggerQRIALARVFLKDAK 491
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG--------------LSGGQQ-------------------------QRVALARALAMDPD 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 492 IVILDEPTAGLDAHT----EKLLEKAFDELfqNRTVIIIAHRLSSLYR-ADKIILIDRGE 546
Cdd:cd03229 121 VLLLDEPTSALDPITrrevRALLKSLQAQL--GITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
331-574 |
3.41e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.82 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 331 SPPEIILKQVSHSYIPGK---EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKekdw 407
Cdd:COG1116 4 AAPALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 408 yDQVGYLHQTPFIFP-GSIAENIALG--KKGAKGEEIKRAAS-------LAG-AHQFIAELPQGydtkvgeggrglsggE 476
Cdd:COG1116 80 -PDRGVVFQEPALLPwLTVLDNVALGleLRGVPKAERRERARellelvgLAGfEDAYPHQLSGG---------------M 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 477 RQRIALARVFLKDAKIVILDEPTAGLDAHT----EKLLEKAFDElfQNRTVIIIAHRLS-SLYRADKIILIDR--GEIRG 549
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTrerlQDELLRLWQE--TGKTVLFVTHDVDeAVFLADRVVVLSArpGRIVE 221
|
250 260 270
....*....|....*....|....*....|....*
gi 499664576 550 M-------GRHEQLLAE---NELYRQLITAYRGEV 574
Cdd:COG1116 222 EidvdlprPRDRELRTSpefAALRAEILDLLREEA 256
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
335-551 |
6.84e-32 |
|
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: 122.24 E-value: 6.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPL--WELKEKDwydqVG 412
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVtgVPPERRN----IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPG-SIAENIALG---KKGAKGEEIKRAASLA-------GAHQFIAELPQGydtkvgeggrglsggERQRIA 481
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlklRGVPKAEIRARVRELLelvglegLLNRYPHELSGG---------------QQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 482 LARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRLSSLYR-ADKIILIDRGEIRGMG 551
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-558 |
2.47e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 127.71 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYIPG-KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPA---EGEILINGVPLWELKEKDWY 408
Cdd:COG1123 3 PLLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 409 DQVGYLHQTPF--IFPGSIAENIA--LGKKGAKGEEIKRAASLA--------GAHQFIAELPQGydtkvgeggrglsggE 476
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQIAeaLENLGLSRAEARARVLELleavglerRLDRYPHQLSGG---------------Q 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 477 RQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRLSS-LYRADKIILIDRGEIRGMGRH 553
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPP 227
|
....*
gi 499664576 554 EQLLA 558
Cdd:COG1123 228 EEILA 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
337-556 |
4.10e-31 |
|
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: 120.75 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGL-----MRPAEGEILINGVPLWELKEKDWY--D 409
Cdd:cd03260 3 LRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLElrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 QVGYLHQTPFIFPGSIAENIALG--------------------KKGAKGEEIKR---AASLAGAHQfiaelpqgydtkvg 466
Cdd:cd03260 82 RVGMVFQKPNPFPGSIYDNVAYGlrlhgiklkeelderveealRKAALWDEVKDrlhALGLSGGQQ-------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 467 eggrglsggerQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRG 545
Cdd:cd03260 148 -----------QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNG 216
|
250
....*....|.
gi 499664576 546 EIRGMGRHEQL 556
Cdd:cd03260 217 RLVEFGPTEQI 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
347-544 |
1.09e-30 |
|
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: 118.74 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkDWYDQVGYLHQTPFIFPG-SI 425
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLGHADGLKPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 AENI----ALGKKGAKGEEIKRAASLAG----AHQFIAELPQGydTKvgeggrglsggerQRIALARVFLKDAKIVILDE 497
Cdd:COG4133 93 RENLrfwaALYGLRADREAIDEALEAVGlaglADLPVRQLSAG--QK-------------RRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499664576 498 PTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDR 544
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
337-547 |
2.99e-30 |
|
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: 117.74 E-value: 2.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPlweLKEKDWYDQVGYLHQ 416
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TP--FIFPGSIAENIALGKK--GAKGEEIKRAASLAGAHQFIAELPQgydtkvgeggrGLSGGERQRIALARVFLKDAKI 492
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKelDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 493 VILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
337-547 |
8.47e-30 |
|
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: 117.22 E-value: 8.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYIPGK---EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKE---KDWYDQ 410
Cdd:cd03257 4 VKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 VGYLHQTPF--------IFpGSIAENIALGKKGAKGEEIKRAASLAG---------AHQFIAELPQGydtkvgeggrgls 473
Cdd:cd03257 84 IQMVFQDPMsslnprmtIG-EQIAEPLRIHGKLSKKEARKEAVLLLLvgvglpeevLNRYPHELSGG------------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 474 ggERQRIALARVFLKDAKIVILDEPTAGLDAHTE----KLLEKAFDELfqNRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:cd03257 150 --QRQRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLKKLQEEL--GLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
334-568 |
1.53e-29 |
|
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: 117.65 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYIP-GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRpAEGEILINGVPLWELKEKDWYDQVG 412
Cdd:cd03289 2 QMTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPGSIAENIALGKKgAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKI 492
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGK-WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 493 VILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLIT 568
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
335-547 |
1.10e-28 |
|
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: 114.20 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKD---WYDQV 411
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQT-PFIFPGSIAENIALGKKGAKG-----------EEIKRAAS------LAG-AHQFIAELPQGydtkvgeggrgl 472
Cdd:cd03256 81 GMIFQQfNLIERLSVLENVLSGRLGRRStwrslfglfpkEEKQRALAalervgLLDkAYQRADQLSGG------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 473 sggERQRIALARVFLKDAKIVILDEPTAGLDAHTEK----LLEKAFDElfQNRTVIIIAHRLsSLYR--ADKIILIDRGE 546
Cdd:cd03256 149 ---QQQRVAIARALMQQPKLILADEPVASLDPASSRqvmdLLKRINRE--EGITVIVSLHQV-DLAReyADRIVGLKDGR 222
|
.
gi 499664576 547 I 547
Cdd:cd03256 223 I 223
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
348-571 |
2.05e-28 |
|
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: 114.24 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAE 427
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 428 NIALGKKgAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTE 507
Cdd:cd03288 114 NLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 508 KLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLA-ENELYRQLITAYR 571
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGVFASLVRTDK 257
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
329-561 |
2.86e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 120.61 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 329 WDSPPEIILKQVSHSYIPG-KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDW 407
Cdd:PLN03130 1232 WPSSGSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 408 YDQVGYLHQTPFIFPGSIAENIAlgkkgaKGEEIKRA---ASLAGAH--QFIAELPQGYDTKVGEGGRGLSGGERQRIAL 482
Cdd:PLN03130 1312 RKVLGIIPQAPVLFSGTVRFNLD------PFNEHNDAdlwESLERAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSL 1385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 483 ARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAeNE 561
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS-NE 1463
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
335-561 |
1.32e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.45 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPG----KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWE--LKEKDWY 408
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 409 DQVGYLHQTP--FIFPGSIAENIALGKK--GAKGEEI----KRAASLAGAHqfiaelpqgYDTKVGEGGRGLSGGERQRI 480
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPInlGLSEEEIenrvKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAhteklleKAFDELFQ---------NRTVIIIAHRLSSLYR-ADKIILIDRGEIRGM 550
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDP-------KGRDEILNkikelhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQ 226
|
250
....*....|.
gi 499664576 551 GRHEQLLAENE 561
Cdd:PRK13637 227 GTPREVFKEVE 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
146-569 |
2.94e-27 |
|
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: 117.32 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 146 MILVVVLALDLISGI---IMLLTAPLIPVFMMLIGSFAEKLAQ-KQWSSLSRlSGKFFEL---LQGIADLKAFGRSKEQV 218
Cdd:TIGR01271 1009 LTLIVLGAIFVVSVLqpyIFIAAIPVAVIFIMLRAYFLRTSQQlKQLESEAR-SPIFSHLitsLKGLWTIRAFGRQSYFE 1087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 219 NELKK-------------SGLMFRDATMEVLRVAFLSALALEVLATISTAMVAVEVGLRLLYGKMEFLQ-AFFVLLLAPE 284
Cdd:TIGR01271 1088 TLFHKalnlhtanwflylSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQwAVNSSIDVDG 1167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 285 L---------YLPLRNLGSSFHAGRTAIAFSQKLwtIIEEKESRVflnkrsiTWDSPPEIILKQVSHSYIP-GKEVLKNI 354
Cdd:TIGR01271 1168 LmrsvsrvfkFIDLPQEEPRPSGGGGKYQLSTVL--VIENPHAQK-------CWPSGGQMDVQGLTAKYTEaGRAVLQDL 1238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 355 NLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRpAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPGSIAENIALGKK 434
Cdd:TIGR01271 1239 SFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQ 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 435 GAKgEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAF 514
Cdd:TIGR01271 1318 WSD-EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTL 1396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 515 DELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLITA 569
Cdd:TIGR01271 1397 KQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSA 1451
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
337-547 |
9.27e-27 |
|
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: 106.36 E-value: 9.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPlwelkekdwydqvgylhq 416
Cdd:cd03216 3 LRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 tpfIFPGSIAENIALGkkgakgeeIKRAASLAGAHQfiaelpqgydtkvgeggrglsggerQRIALARVFLKDAKIVILD 496
Cdd:cd03216 64 ---VSFASPRDARRAG--------IAMVYQLSVGER-------------------------QMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 497 EPTAGLDAH-TEKLLE-----KAfdelfQNRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:cd03216 108 EPTAALTPAeVERLFKvirrlRA-----QGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
347-557 |
9.91e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.05 E-value: 9.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPL-----WELKEkdwydQVGYLHQ-TPFI 420
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawspWELAR-----RRAVLPQhSSLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 421 FPGSIAENIALG------KKGAKGEEIKRAASLAG----AHQFIAELPQGydtkvgeggrglsggERQRIALARVFL--- 487
Cdd:COG4559 88 FPFTVEEVVALGraphgsSAAQDRQIVREALALVGlahlAGRSYQTLSGG---------------EQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 488 ----KDAKIVILDEPTAGLD-AHTEKLLEKAFDELFQNRTVIIIAH--RLSSLYrADKIILIDRGEIRGMGRHEQLL 557
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDlAHQHAVLRLARQLARRGGGVVAVLHdlNLAAQY-ADRILLLHQGRLVAQGTPEEVL 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
337-539 |
2.25e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ-VGYLH 415
Cdd:COG1129 7 MRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 416 QTPFIFPG-SIAENIALGKKGAKGEEIKRAASLAGAHQFIAELpqGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVI 494
Cdd:COG1129 86 QELNLVPNlSVAENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499664576 495 LDEPTAGLDAH-TEKLLE-----KAfdelfQNRTVIIIAHRLSSLYR-ADKI 539
Cdd:COG1129 164 LDEPTASLTEReVERLFRiirrlKA-----QGVAIIYISHRLDEVFEiADRV 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
335-571 |
2.57e-26 |
|
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: 107.77 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYL 414
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPG-SIAENIALGKK--GAKGEEIK-RAASLAG---------AHQFIAELPQGydtkvgeggrglsggERQRIA 481
Cdd:cd03295 81 IQQIGLFPHmTVEENIALVPKllKWPKEKIReRADELLAlvgldpaefADRYPHELSGG---------------QQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 482 LARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLA 558
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILR 225
|
250
....*....|....*
gi 499664576 559 E--NELYRQLITAYR 571
Cdd:cd03295 226 SpaNDFVAEFVGADR 240
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
331-565 |
3.87e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.80 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 331 SPPEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGvplwelkeKDWYD- 409
Cdd:COG3842 2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--------RDVTGl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 -----QVGYLHQTPFIFPG-SIAENIA--LGKKGAKGEEIKRAAS-------LAG-AHQFIAELPQGYDtkvgeggrgls 473
Cdd:COG3842 73 ppekrNVGMVFQDYALFPHlTVAENVAfgLRMRGVPKAEIRARVAellelvgLEGlADRYPHQLSGGQQ----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 474 ggerQRIALARVFLKDAKIVILDEPTAGLDAHT-EKLLEkafdELFQ-----NRTVIIIAHRLS---SLyrADKIILIDR 544
Cdd:COG3842 142 ----QRVALARALAPEPRVLLLDEPLSALDAKLrEEMRE----ELRRlqrelGITFIYVTHDQEealAL--ADRIAVMND 211
|
250 260
....*....|....*....|.
gi 499664576 545 GEIrgmgrhEQLLAENELYRQ 565
Cdd:COG3842 212 GRI------EQVGTPEEIYER 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
345-557 |
4.01e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.55 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 345 IPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQ-TPFIFPG 423
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQhSSLSFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 SIAENIALG------KKGAKGEEIKRAASLAG----AHQFIAELPQGydtkvgeggrglsggERQRIALARVFL------ 487
Cdd:PRK13548 92 TVEEVVAMGraphglSRAEDDALVAAALAQVDlahlAGRDYPQLSGG---------------EQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 488 KDAKIVILDEPTAGLD-AHTEKLLEKAFDelF---QNRTVIIIAH--RLSSLYrADKIILIDRGEIRGMGRHEQLL 557
Cdd:PRK13548 157 GPPRWLLLDEPTSALDlAHQHHVLRLARQ--LaheRGLAVIVVLHdlNLAARY-ADRIVLLHQGRLVADGTPAEVL 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
334-565 |
4.96e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.39 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWEL--KEKDwydqV 411
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLppKDRN----I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPG-SIAENIALGKK--GAKGEEIKR----AASLAG----AHQFIAELPQGydtkvgeggrglsggERQRI 480
Cdd:COG3839 78 AMVFQSYALYPHmTVYENIAFPLKlrKVPKAEIDRrvreAAELLGledlLDRKPKQLSGG---------------QRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAhteKLLEKAFDEL--FQNR---TVIIIAHRLS---SLyrADKIILIDRGEIrgmgr 552
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDA---KLRVEMRAEIkrLHRRlgtTTIYVTHDQVeamTL--ADRIAVMNDGRI----- 212
|
250
....*....|...
gi 499664576 553 hEQLLAENELYRQ 565
Cdd:COG3839 213 -QQVGTPEELYDR 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
334-546 |
1.76e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 112.04 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYIPGK--EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGV-PLWELKEKDWYDQ 410
Cdd:PTZ00265 382 KIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 VGYLHQTPFIFPGSIAENIA---------------LGKKGAKGEEIKRAASLAGA------------------------- 450
Cdd:PTZ00265 462 IGVVSQDPLLFSNSIKNNIKyslyslkdlealsnyYNEDGNDSQENKNKRNSCRAkcagdlndmsnttdsneliemrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 451 -----------------HQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKA 513
Cdd:PTZ00265 542 qtikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270
....*....|....*....|....*....|....*
gi 499664576 514 FDEL--FQNRTVIIIAHRLSSLYRADKIILIDRGE 546
Cdd:PTZ00265 622 INNLkgNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
335-547 |
3.11e-25 |
|
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: 103.76 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLwELKEKDWYD---QV 411
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINElrqKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPG-SIAENIALG----KKGAKGEEIKRAASLAG-------AHQFIAELPQGydtkvgeggrglsggERQR 479
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITLApikvKGMSKAEAEERALELLEkvgladkADAYPAQLSGG---------------QQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 480 IALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ-NRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
335-547 |
4.32e-25 |
|
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: 103.26 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKdwydQVGYL 414
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGR----AIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQT--------PFIFPGSIAENIALGKK--GAKGEEIKR----AASLAG----AHQFIAELPQGydtkvgeggrglsggE 476
Cdd:cd03292 77 RRKigvvfqdfRLLPDRNVYENVAFALEvtGVPPREIRKrvpaALELVGlshkHRALPAELSGG---------------E 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 477 RQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADK--IILIDRGEI 547
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
323-560 |
7.74e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 110.07 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 323 NKRSITWDSPPEIILKQVSHSYIPG-KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWE 401
Cdd:PLN03232 1223 NRPVSGWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 402 LKEKDWYDQVGYLHQTPFIFPGSIAENIalgKKGAKGEEIKRAASLAGAH--QFIAELPQGYDTKVGEGGRGLSGGERQR 479
Cdd:PLN03232 1303 FGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHikDVIDRNPFGLDAEVSEGGENFSVGQRQL 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 480 IALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAE 559
Cdd:PLN03232 1380 LSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
.
gi 499664576 560 N 560
Cdd:PLN03232 1460 D 1460
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
335-558 |
1.12e-24 |
|
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: 102.66 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGK---EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD-- 409
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 -QVGYLHQTPFIFPG-SIAENIALGKK--GAKGEEIKRAA----SLAG----AHQFIAELPQGydtkvgeggrglsggER 477
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEERVlellELVGledkADAYPAQLSGG---------------QK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 478 QRIALARVFLKDAKIVILDEPTAGLDAHTE----KLLEKAFDELfqNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGR 552
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTqsilALLRDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....*.
gi 499664576 553 HEQLLA 558
Cdd:cd03258 225 VEEVFA 230
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
17-304 |
2.48e-24 |
|
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: 103.01 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 17 LVKIALTSFISGGAIIAQAYLIAYIINGAFLAKKgLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLL 96
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD-LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 97 EKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLI 176
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 177 GSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAM 256
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499664576 257 VAVEVGLRLLYGKMEFLQAFFVLLLAPELYLPLRNLGSSFHAGRTAIA 304
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALA 287
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
334-565 |
3.34e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.07 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGvplwelkeKDWY----- 408
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--------RDLFtnlpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 409 --DQVGYLHQTPFIFPG-SIAENIA--LGKKGAKGEEIKRAAS-------LAG-AHQFIAELPQGydtkvgeggrglsgg 475
Cdd:COG1118 73 reRRVGFVFQHYALFPHmTVAENIAfgLRVRPPSKAEIRARVEellelvqLEGlADRYPSQLSGG--------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 476 ERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKafdELFQ-----NRTVIIIAHRLSSLYR-ADKIILIDRGEIrg 549
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRR---WLRRlhdelGGTTVFVTHDQEEALElADRVVVMNQGRI-- 212
|
250
....*....|....*.
gi 499664576 550 mgrhEQLLAENELYRQ 565
Cdd:COG1118 213 ----EQVGTPDEVYDR 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
335-548 |
3.87e-24 |
|
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: 100.35 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPlEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKdWYDQVGYL 414
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPGSIAEN----IALGKKGAKGEEIKRAASLAG-------AHQFIAELPQGydtkvgeggrglsggERQRIALA 483
Cdd:cd03264 78 PQEFGVYPNFTVREfldyIAWLKGIPSKEVKARVDEVLElvnlgdrAKKKIGSLSGG---------------MRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 484 RVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSL-YRADKIILIDRGEIR 548
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLV 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
131-570 |
4.42e-24 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 107.72 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 131 ARYLPQLISAG---IIPLMILVVVLALDLISGI-IMLLTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSgkffELLQGIA 206
Cdd:TIGR00957 432 ATYINMIWSAPlqvILALYFLWLNLGPSVLAGVaVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMN----EILNGIK 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 207 DLKAFGRSKEqvneLKKSGLMFRDATMEVLR-VAFLSA------LALEVLATISTAMVAVEVGLR-LLYGKMEFLQ-AFF 277
Cdd:TIGR00957 508 VLKLYAWELA----FLDKVEGIRQEELKVLKkSAYLHAvgtftwVCTPFLVALITFAVYVTVDENnILDAEKAFVSlALF 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 278 VLLLAPELYLP--LRNL-GSSFHAGRTAIAFSQklwtiiEEKESRVfLNKRSITWDSPPEIILKQVSHSYIPGKE-VLKN 353
Cdd:TIGR00957 584 NILRFPLNILPmvISSIvQASVSLKRLRIFLSH------EELEPDS-IERRTIKPGEGNSITVHNATFTWARDLPpTLNG 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 354 INLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGvplwelkekdwydQVGYLHQTPFIFPGSIAENIALGK 433
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 434 KgakgEEIKRAASLAGAHQFIAEL---PQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEK-L 509
Cdd:TIGR00957 724 A----LNEKYYQQVLEACALLPDLeilPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKhI 799
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 510 LEKAF--DELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLITAY 570
Cdd:TIGR00957 800 FEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTY 862
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
347-551 |
7.56e-24 |
|
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: 99.16 E-value: 7.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPA--EGEILINGVPLwelKEKDWYDQVGYLHQTPFIFPG- 423
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 SIAENI--ALGKKGAKGEEIKRAAslagahqfiaelpqgydtkvgeggrglsggerqrIALArvFLKDAKIVILDEPTAG 501
Cdd:cd03213 98 TVRETLmfAAKLRGLSGGERKRVS----------------------------------IALE--LVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499664576 502 LDAHTEKLLEKAFDEL-FQNRTVIIIAHRLSSL--YRADKIILIDRGEIRGMG 551
Cdd:cd03213 142 LDSSSALQVMSLLRRLaDTGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
330-547 |
7.99e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 100.20 E-value: 7.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 330 DSPPEIILKQVSHSYIPGKE---VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkd 406
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 407 wyDQ--------VGYLHQTPFIFPGSIA-ENIAL-----GKKGAKgeeiKRAASLAG-------AHQFIAELPQGydtkv 465
Cdd:COG4181 82 --DArarlrarhVGFVFQSFQLLPTLTAlENVMLplelaGRRDAR----ARARALLErvglghrLDHYPAQLSGG----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 466 geggrglsggERQRIALARVFLKDAKIVILDEPTAGLDAHTEkllEKAFDELFQ-NR----TVIIIAHRLSSLYRADKII 540
Cdd:COG4181 151 ----------EQQRVALARAFATEPAILFADEPTGNLDAATG---EQIIDLLFElNRergtTLVLVTHDPALAARCDRVL 217
|
....*..
gi 499664576 541 LIDRGEI 547
Cdd:COG4181 218 RLRAGRL 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
341-546 |
9.77e-24 |
|
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: 101.09 E-value: 9.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 341 SHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGvplwelkekdwydQVGYLHQTPFI 420
Cdd:cd03291 43 SNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 421 FPGSIAENIALGKKgakgEEIKRAASLAGAHQF---IAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDE 497
Cdd:cd03291 110 MPGTIKENIIFGVS----YDEYRYKSVVKACQLeedITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499664576 498 PTAGLDAHTEK-LLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGE 546
Cdd:cd03291 186 PFGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
335-557 |
1.07e-23 |
|
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: 100.16 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEG---EIL---INGVPLWELKEKdwy 408
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWELRKR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 409 dqVGY----LHQTpfiFPGSI-AENIAL-GKKGAKG-------EEIKRAASLAG-------AHQFIAELPQGydtkvgeg 468
Cdd:COG1119 80 --IGLvspaLQLR---FPRDEtVLDVVLsGFFDSIGlyreptdEQRERARELLEllglahlADRPFGTLSQG-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 469 grglsggERQRIALARVFLKDAKIVILDEPTAGLD-AHTEKLLEkAFDELFQN--RTVIIIAHRLSSLYRA-DKIILIDR 544
Cdd:COG1119 147 -------EQRRVLIARALVKDPELLILDEPTAGLDlGARELLLA-LLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKD 218
|
250
....*....|...
gi 499664576 545 GEIRGMGRHEQLL 557
Cdd:COG1119 219 GRVVAAGPKEEVL 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
350-556 |
1.09e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.40 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLvklLLGLMRPAE---GEILINGVP-----LWELKEkdwydQVGYLHQTPFIF 421
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTL---LLTFMRMVEvcgGEIRVNGREigaygLRELRR-----QFSMIPQDPVLF 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 422 PGSIAENIALGKKgAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLK-DAKIVILDEPTA 500
Cdd:PTZ00243 1397 DGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATA 1475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 501 GLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQL 556
Cdd:PTZ00243 1476 NIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
331-530 |
1.09e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.72 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 331 SPPEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLwELKE-KDWYD 409
Cdd:COG3845 2 MPPALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSpRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 Q-VGYLHQTPFIFPG-SIAENIALGKKGAKG------EEIKRAASLAGAHQF-------IAELPQGydtkvgeggrglsg 474
Cdd:COG3845 80 LgIGMVHQHFMLVPNlTVAENIVLGLEPTKGgrldrkAARARIRELSERYGLdvdpdakVEDLSVG-------------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499664576 475 gERQRIALARVFLKDAKIVILDEPTAGL-DAHTEKLLE-----KAfdelfQNRTVIIIAHRL 530
Cdd:COG3845 146 -EQQRVEILKALYRGARILILDEPTAVLtPQEADELFEilrrlAA-----EGKSIIFITHKL 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
142-567 |
1.28e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 106.21 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 142 IIPLMILVVVLALDLISGIIMLLTapLIPvFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFgrSKEQVNEL 221
Cdd:PLN03232 429 IVSMVLLYQQLGVASLFGSLILFL--LIP-LQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCY--AWEKSFES 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 222 KKSGLmfRDATMEVLRVA-FLSALALEVLATISTAMVAVEVGL-RLLYGKMEFLQAFFVLLLAPELYLPLRNLGSSFHAG 299
Cdd:PLN03232 504 RIQGI--RNEELSWFRKAqLLSAFNSFILNSIPVVVTLVSFGVfVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 300 RTAIAFSQKlwtiIEEkesrVFLNKRSITWDSPP------EIILKQVSHSY--IPGKEVLKNINLTIKPLEKVAIVGPSG 371
Cdd:PLN03232 582 VNANVSLQR----IEE----LLLSEERILAQNPPlqpgapAISIKNGYFSWdsKTSKPTLSDINLEIPVGSLVAIVGGTG 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 372 AGKSTLVKLLLGLMRPAE-GEILINGvplwelkekdwydQVGYLHQTPFIFPGSIAENIALGKKgAKGEEIKRAASlAGA 450
Cdd:PLN03232 654 EGKTSLISAMLGELSHAEtSSVVIRG-------------SVAYVPQVSWIFNATVRENILFGSD-FESERYWRAID-VTA 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 451 HQFIAELPQGYD-TKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAH-TEKLLEKAFDELFQNRTVIIIAH 528
Cdd:PLN03232 719 LQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTN 798
|
410 420 430
....*....|....*....|....*....|....*....
gi 499664576 529 RLSSLYRADKIILIDRGEIRGMGRHEQLLAENELYRQLI 567
Cdd:PLN03232 799 QLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
330-561 |
1.83e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.07 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 330 DSPPEIILKQVSHSYIPG-KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWY 408
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 409 DQVGYLHQTP---FIfpGSIAE-NIALG--KKGAKGEEIKR----AASLAGAHQFIAELPQgydtkvgeggrGLSGGERQ 478
Cdd:PRK13632 83 KKIGIIFQNPdnqFI--GATVEdDIAFGleNKKVPPKKMKDiiddLAKKVGMEDYLDKEPQ-----------NLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 479 RIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQL 556
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
....*
gi 499664576 557 LAENE 561
Cdd:PRK13632 230 LNNKE 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
335-551 |
2.98e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 97.67 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKdwYDQVGYL 414
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPGSIA-ENIALGKK--GAKGEEIKRAASLAGAHQFIAELPQGYDTKVgeggrglsggeRQRIALARVFLKDAK 491
Cdd:cd03268 78 IEAPGFYPNLTArENLRLLARllGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGM-----------KQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499664576 492 IVILDEPTAGLDAH-TEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMG 551
Cdd:cd03268 147 LLILDEPTNGLDPDgIKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
334-561 |
3.40e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.71 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYIPG----KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILI-NGVPLWELKEKDWY 408
Cdd:PRK13634 2 DITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 409 D---QVGYLHQTP--FIFPGSIAENIALGKK--GAKGEEIKRAAS----LAGahqfiaeLPQGYDTKvgeGGRGLSGGER 477
Cdd:PRK13634 82 PlrkKVGIVFQFPehQLFEETVEKDICFGPMnfGVSEEDAKQKARemieLVG-------LPEELLAR---SPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 478 QRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHE 554
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*..
gi 499664576 555 QLLAENE 561
Cdd:PRK13634 232 EIFADPD 238
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
335-570 |
3.60e-23 |
|
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: 98.46 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWEL---KEkdwydQV 411
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpphKR-----PV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPG-SIAENIALG--KKGAKGEEIKRAAS-------LAG-AHQFIAELPQGydtkvgeggrglsggERQRI 480
Cdd:cd03300 75 NTVFQNYALFPHlTVFENIAFGlrLKKLPKAEIKERVAealdlvqLEGyANRKPSQLSGG---------------QQQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRLS-SLYRADKIILIDRGEIRGMGRHEqll 557
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPE--- 216
|
250
....*....|...
gi 499664576 558 aenELYRQLITAY 570
Cdd:cd03300 217 ---EIYEEPANRF 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
335-551 |
1.24e-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: 96.17 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING--VPLWELKEKDwydqVG 412
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdVTDLPPKDRD----IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPG-SIAENIALGKK--GAKGEEIKRAASLAGAHQFIAELPQGYDTKVgeggrglSGGERQRIALARVFLKD 489
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLKlrKVPKDEIDERVREVAELLQIEHLLDRKPKQL-------SGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 490 AKIVILDEPTAGLDAhteKLLEKAFDEL--FQNR---TVIIIAH-RLSSLYRADKIILIDRGEIRGMG 551
Cdd:cd03301 149 PKVFLMDEPLSNLDA---KLRVQMRAELkrLQQRlgtTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
335-567 |
1.84e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 98.61 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGK---EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD-- 409
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 -QVGylhqtpFIFPG-------SIAENIALGKK--GAKGEEI-KRAASL-------AGAHQFIAELPQGydtkvgeggrg 471
Cdd:COG1135 82 rKIG------MIFQHfnllssrTVAENVALPLEiaGVPKAEIrKRVAELlelvglsDKADAYPSQLSGG----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 472 lsggERQRIALARVFLKDAKIVILDEPTAGLDAHTEK----LLEKAFDELfqNRTVIIIAH------RLsslyrADKIIL 541
Cdd:COG1135 145 ----QKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKDINREL--GLTIVLITHemdvvrRI-----CDRVAV 213
|
250 260
....*....|....*....|....*...
gi 499664576 542 IDRGEIRGMGRHEQLLA--ENELYRQLI 567
Cdd:COG1135 214 LENGRIVEQGPVLDVFAnpQSELTRRFL 241
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
347-559 |
2.02e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 102.30 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGvplwelkekdwydQVGYLHQTPFIFPGSIA 426
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 427 ENIALGkkgAKGEEIkRAASLAGAHQF---IAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLD 503
Cdd:TIGR01271 505 DNIIFG---LSYDEY-RYTSVIKACQLeedIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 504 AHTEK-LLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAE 559
Cdd:TIGR01271 581 VVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
337-548 |
2.40e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINgvplwelkeKDWydQVGYLHQ 416
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGL--RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TPFIFPG-SIAENIALGKKGAK-------------GEEIKRAASLAGAHQFIAELpQGY--DTKVGEGGRGLSGGERQ-- 478
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGDAELRaleaeleeleaklAEPDEDLERLAELQEEFEAL-GGWeaEARAEEILSGLGFPEEDld 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 479 ------------RIALARVFLKDAKIVILDEPTAGLDAHTEKLLEkafdELFQNR--TVIIIAH-R--LSSLyrADKIIL 541
Cdd:COG0488 148 rpvselsggwrrRVALARALLSEPDLLLLDEPTNHLDLESIEWLE----EFLKNYpgTVLVVSHdRyfLDRV--ATRILE 221
|
....*..
gi 499664576 542 IDRGEIR 548
Cdd:COG0488 222 LDRGKLT 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
335-547 |
2.90e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.29 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKekdwyDQVGYL 414
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-----EDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFP-GSIAENIALGKKG---AKGEEIKRAASLAG-AHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKD 489
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGLKGqwrDAALQALAAVGLADrANEWPAALSGG---------------QKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499664576 490 AKIVILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRLS-SLYRADKIILIDRGEI 547
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-562 |
2.96e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWEL-KEKDWYDQVGY 413
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFI-FPG-SIAENIALGKKG--AKGEEIKRAASLAgahqfIAELpqGYDTKVGEGGRGLSGGERQRIALARVFLKD 489
Cdd:PRK13644 82 VFQNPETqFVGrTVEEDLAFGPENlcLPPIEIRKRVDRA-----LAEI--GLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 490 AKIVILDEPTAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENEL 562
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
335-503 |
4.51e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 95.45 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWeLKEKDWYD---QV 411
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKlrrKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPG-SIAENIALG----KKGAKGEEIKRAASL-------AGAHQFIAELPQGydtkvgeggrglsggERQR 479
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLApikvKKMSKAEAEERAMELlervglaDKADAYPAQLSGG---------------QQQR 144
|
170 180
....*....|....*....|....
gi 499664576 480 IALARVFLKDAKIVILDEPTAGLD 503
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALD 168
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
351-551 |
6.28e-22 |
|
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: 94.28 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIK---PLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEK-DWYDQ---VGYLHQTPFIFPG 423
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQqrkIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 -SIAENIALGKKGAKGEEIK-RAASLAGAHQfIAELPQGYDTKVGEGGRglsggerQRIALARVFLKDAKIVILDEPTAG 501
Cdd:cd03297 90 lNVRENLAFGLKRKRNREDRiSVDELLDLLG-LDHLLNRYPAQLSGGEK-------QRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499664576 502 LDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMG 551
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
350-558 |
6.47e-22 |
|
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: 94.81 E-value: 6.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkdwyDQ-----VGYLHQTPFIFPG- 423
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP----HEiarlgIGRTFQIPRLFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 SIAENIALG-------------KKGAKGEEIKRAASLAG-------AHQFIAELPQGydtkvgeggrglsggERQRIALA 483
Cdd:cd03219 91 TVLENVMVAaqartgsglllarARREEREARERAEELLErvgladlADRPAGELSYG---------------QQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 484 RVFLKDAKIVILDEPTAGL-DAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLA 558
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-548 |
6.53e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILInGVPLwelkekdwydQVGYL 414
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPG--SIAENIAlgkKGAKGEEIKRAASLAG--------AHQFIAELPQGydTKVgeggrglsggerqRIALAR 484
Cdd:COG0488 384 DQHQEELDPdkTVLDELR---DGAPGGTEQEVRGYLGrflfsgddAFKPVGVLSGG--EKA-------------RLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 485 VFLKDAKIVILDEPTAGLDAHTEKLLEKAFDElFQNrTVIIIAH-R--LSSLyrADKIILIDRGEIR 548
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
355-551 |
8.06e-22 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 93.77 E-value: 8.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 355 NLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPlwELKEKDWYDQVGYLHQTPFIFPG-SIAENIALG- 432
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS--HTGLAPYQRPVSMLFQENNLFAHlTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 433 KKGAK-----GEEIKRAASLAGAHQFIAELPQgydtkvgeggrGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTE 507
Cdd:TIGR01277 96 HPGLKlnaeqQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499664576 508 K----LLEKAFDElfQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMG 551
Cdd:TIGR01277 165 EemlaLVKQLCSE--RQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
335-560 |
1.02e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 94.05 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYipgKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELkekdwydqvgYL 414
Cdd:COG3840 2 LRLDDLTYRY---GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL----------PP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPF--------IFPG-SIAENIALGKK------GAKGEEIKRAASLAGAHQFIAELP------Qgydtkvgeggrgls 473
Cdd:COG3840 69 AERPVsmlfqennLFPHlTVAQNIGLGLRpglkltAEQRAQVEQALERVGLAGLLDRLPgqlsggQ-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 474 ggeRQRIALARVFLKDAKIVILDEPTAGLD----AHTEKLLEKAFDElfQNRTVIIIAHRLSSLYR-ADKIILIDRGEIR 548
Cdd:COG3840 135 ---RQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIA 209
|
250
....*....|..
gi 499664576 549 GMGRHEQLLAEN 560
Cdd:COG3840 210 ADGPTAALLDGE 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
333-561 |
1.08e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 95.08 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYiPGKE--VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPL-----WELKEK 405
Cdd:PRK13635 4 EIIRVEHISFRY-PDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseetvWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 406 dwydqVGYLHQTP-FIFPGS-IAENIALG--KKGAKGEE-IKR---AASLAGAHQFI----AELPQGydtkvgeggrgls 473
Cdd:PRK13635 83 -----VGMVFQNPdNQFVGAtVQDDVAFGleNIGVPREEmVERvdqALRQVGMEDFLnrepHRLSGG------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 474 ggERQRIALARVFLKDAKIVILDEPTAGLD-AHTEKLLE---KAFDElfQNRTVIIIAHRLSSLYRADKIILIDRGEIRG 549
Cdd:PRK13635 145 --QKQRVAIAGVLALQPDIIILDEATSMLDpRGRREVLEtvrQLKEQ--KGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
250
....*....|..
gi 499664576 550 MGRHEQLLAENE 561
Cdd:PRK13635 221 EGTPEEIFKSGH 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
348-547 |
1.59e-21 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 93.49 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAE---GEILINGVPLwelKEKDWYDQVGYLHQTPFIFPG- 423
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 SIAE------NIALGKKGAKGEEIKRAASLAgahqfiaeLPQGYDTKVGEGGRGLSGGERQ-RIALARVFLKDAKIVILD 496
Cdd:cd03234 97 TVREtltytaILRLPRKSSDAIRKKRVEDVL--------LRDLALTRIGGNLVKGISGGERrRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499664576 497 EPTAGLDAHTEKLLEKAFDELFQ-NRTVIIIAHR-LSSLYRA-DKIILIDRGEI 547
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARrNRIVILTIHQpRSDLFRLfDRILLLSSGEI 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
350-557 |
2.30e-21 |
|
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: 93.17 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELK-EKdwyDQVGYLHQTPFIFPG-SIAE 427
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpEK---RDISYVPQNYALFPHmTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 428 NIALG--KKGAKGEEIKR-----AASLAGAH---QFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIVILDE 497
Cdd:cd03299 91 NIAYGlkKRKVDKKEIERkvleiAEMLGIDHllnRKPETLSGG---------------EQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 498 PTAGLDAHT-EKL---LEKAFDELfqNRTVIIIAHRLS-SLYRADKIILIDRGEIRGMGRHEQLL 557
Cdd:cd03299 156 PFSALDVRTkEKLreeLKKIRKEF--GVTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
229-567 |
2.35e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 99.04 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 229 RDATMEVLRVA-FLSALALEVLATISTAMVAVEVGL-RLLYGKMEFLQAFFVLLLAPELYLPLRNLGSSFHAGRTAIAFS 306
Cdd:PLN03130 509 RDDELSWFRKAqLLSAFNSFILNSIPVLVTVVSFGVfTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 307 QKLwtiiEEkesrVFLNKRSITWDSP------PEIILKQVSHSYIPGKE--VLKNINLTIKPLEKVAIVGPSGAGKSTLV 378
Cdd:PLN03130 589 KRL----EE----LLLAEERVLLPNPplepglPAISIKNGYFSWDSKAErpTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 379 KLLLGLMRP-AEGEILINGvplwelkekdwydQVGYLHQTPFIFPGSIAENIALGKKgAKGEEIKRAASLAGAHQFIAEL 457
Cdd:PLN03130 661 SAMLGELPPrSDASVVIRG-------------TVAYVPQVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLL 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 458 PQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHT-EKLLEKAFDELFQNRTVIIIAHRLSSLYRA 536
Cdd:PLN03130 727 PGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQVFDKCIKDELRGKTRVLVTNQLHFLSQV 806
|
330 340 350
....*....|....*....|....*....|.
gi 499664576 537 DKIILIDRGEIRGMGRHEQLLAENELYRQLI 567
Cdd:PLN03130 807 DRIILVHEGMIKEEGTYEELSNNGPLFQKLM 837
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
356-547 |
5.72e-21 |
|
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: 91.40 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 356 LTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDwyDQVGYLHQTPFIFPG-SIAENIALGKK 434
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 435 -GAKGEEIKRAASLAGAHQFiaelpqGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKA 513
Cdd:cd03298 97 pGLKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 499664576 514 FDELFQNR--TVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:cd03298 171 VLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
347-530 |
6.57e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 92.41 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGL------MRpAEGEILINGvplwelkeKDWYD----------Q 410
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgAR-VEGEILLDG--------EDIYDpdvdvvelrrR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 VGYLHQTPFIFPGSIAENIALG------KKGAKGEEI-----KRAA--------------SLAGAHQfiaelpqgydtkv 465
Cdd:COG1117 94 VGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIveeslRKAAlwdevkdrlkksalGLSGGQQ------------- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 466 geggrglsggerQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRL 530
Cdd:COG1117 161 ------------QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
344-528 |
6.63e-21 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 90.56 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 344 YIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPL-WELKE-KDWYDQVGYLHQTP--F 419
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdYSRKGlLERRQRVGLVFQDPddQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 420 IFPGSIAENIALGKK--GAKGEEIKR----AASLAGAHQFIAELPQ--GYDTKvgeggrglsggerQRIALARVFLKDAK 491
Cdd:TIGR01166 81 LFAADVDQDVAFGPLnlGLSEAEVERrvreALTAVGASGLRERPTHclSGGEK-------------KRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 499664576 492 IVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAH 528
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRaEGMTVVISTH 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
338-565 |
7.97e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.45 E-value: 7.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 338 KQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVP-------LWELKEKdwydq 410
Cdd:PRK13639 5 RDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydkksLLEVRKT----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 VGYLHQTP--FIFPGSIAENIALG--KKGAKGEEIKRAASLAgahqFIAELPQGYDTKVgegGRGLSGGERQRIALARVF 486
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEA----LKAVGMEGFENKP---PHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 487 LKDAKIVILDEPTAGLDAHTEKLLEKAFDELfqNR---TVIIIAHR--LSSLYrADKIILIDRGEIRGMGRHEQLLAENE 561
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDL--NKegiTIIISTHDvdLVPVY-ADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
....
gi 499664576 562 LYRQ 565
Cdd:PRK13639 230 TIRK 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
332-547 |
8.22e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.89 E-value: 8.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 332 PPEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYdQV 411
Cdd:PRK15439 9 PPLLCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH-QL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 G-YL-HQTPFIFPG-SIAENIALGKKgakgeeiKRAASLAGAHQFIAELpqGYDTKVGEGGRGLSGGERQRIALARVFLK 488
Cdd:PRK15439 87 GiYLvPQEPLLFPNlSVKENILFGLP-------KRQASMQKMKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499664576 489 DAKIVILDEPTAGLDAH-TEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:PRK15439 158 DSRILILDEPTASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
346-542 |
8.77e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 346 PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGvplwelkekdwYDQVGYLHQ---TPFIFP 422
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 423 GSIAENIALGKKGAKG-------------EEIKRAASLAG-AHQFIAELPQGydtkvgeggrglsggERQRIALARVFLK 488
Cdd:NF040873 72 LTVRDLVAMGRWARRGlwrrltrddraavDDALERVGLADlAGRQLGELSGG---------------QRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 489 DAKIVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAHRLSSLYRADKIILI 542
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
17-410 |
9.80e-21 |
|
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: 95.64 E-value: 9.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 17 LVKIALTSFISGGAIIAqayLIAyIINGAFLAKKGL--GELWPFFPALFLIVTLRF----SLGYFGEKVGANLASKVTGE 90
Cdd:COG4615 15 LLLALLLGLLSGLANAG---LIA-LINQALNATGAAlaRLLLLFAGLLVLLLLSRLasqlLLTRLGQHAVARLRLRLSRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 91 IRNVLLEKIAALGTkvllpektGELLTLILEGVESLEVYYARyLPQLISAGIIplmILVVVLALDLISGIIMLLTAPLIp 170
Cdd:COG4615 91 ILAAPLERLERIGA--------ARLLAALTEDVRTISQAFVR-LPELLQSVAL---VLGCLAYLAWLSPPLFLLTLVLL- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 171 VFMMLIGSFAEKLAQKQWSSLSRLSGKFFE----LLQGIADLKaFGRSKEQV---NELKKSGLMFRDATMEVLRVaFLSA 243
Cdd:COG4615 158 GLGVAGYRLLVRRARRHLRRAREAEDRLFKhfraLLEGFKELK-LNRRRRRAffdEDLQPTAERYRDLRIRADTI-FALA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 244 LALEVLATIstAMVAVEVGLRLLYGKMEFLQAF-FVLLLapeLYL--PLRNLGSSFHA-GRTAIAFsQKLWTI---IEEK 316
Cdd:COG4615 236 NNWGNLLFF--ALIGLILFLLPALGWADPAVLSgFVLVL---LFLrgPLSQLVGALPTlSRANVAL-RKIEELelaLAAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 317 ESRVFLNKRSITWDSPPEIILKQVSHSYIPGKE----VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEI 392
Cdd:COG4615 310 EPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
410
....*....|....*...
gi 499664576 393 LINGVPLwELKEKDWYDQ 410
Cdd:COG4615 390 LLDGQPV-TADNREAYRQ 406
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
330-540 |
1.11e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.93 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 330 DSPPEIILKQVSHSyIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD 409
Cdd:PRK10247 3 ENSPLLQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 QVGYLHQTPFIFPGSIAENIALGK--KGAKGEEIKRAASLAgahQFiaELPqgyDTKVGEGGRGLSGGERQRIALARVFL 487
Cdd:PRK10247 82 QVSYCAQTPTLFGDTVYDNLIFPWqiRNQQPDPAIFLDDLE---RF--ALP---DTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 488 KDAKIVILDEPTAGLDAHTEKLLEKAFDELF--QNRTVIIIAHRLSSLYRADKII 540
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVI 208
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
343-545 |
1.26e-20 |
|
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: 90.47 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 343 SYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ----VGYLHQTP 418
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 419 FIFPGSIAENIALGKKGAKgEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEP 498
Cdd:cd03290 89 WLLNATVEENITFGSPFNK-QRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499664576 499 TAGLDAH-TEKLLEKAFDELFQN--RTVIIIAHRLSSLYRADKIILIDRG 545
Cdd:cd03290 168 FSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
338-565 |
1.66e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.79 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 338 KQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQT 417
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 418 P--FIFPGSIAENIALG--KKGAKGEEIKR----AASLAGAHQFIAELPQ---GYDTKvgeggrglsggerqRIALARVF 486
Cdd:PRK13652 87 PddQIFSPTVEQDIAFGpiNLGLDEETVAHrvssALHMLGLEELRDRVPHhlsGGEKK--------------RVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 487 LKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN--RTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAENELY 563
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
..
gi 499664576 564 RQ 565
Cdd:PRK13652 233 AR 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
335-565 |
2.21e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.86 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYipGKE-VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING--VPLWELKEKDwydqV 411
Cdd:PRK11432 7 VVLKNITKRF--GSNtVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedVTHRSIQQRD----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPG-SIAENIALGKK--GAKGEEIKRA-------ASLAG-AHQFIAELPQGydtkvgeggrglsggERQRI 480
Cdd:PRK11432 81 CMVFQSYALFPHmSLGENVGYGLKmlGVPKEERKQRvkealelVDLAGfEDRYVDQISGG---------------QQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYR-ADKIILIDRGEIrgMgrheQLL 557
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAvSDTVIVMNKGKI--M----QIG 219
|
....*...
gi 499664576 558 AENELYRQ 565
Cdd:PRK11432 220 SPQELYRQ 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
348-551 |
2.33e-20 |
|
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: 89.65 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKekdwYDQVGYLHQTPFIFPG-SIA 426
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPKmKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 427 EN-IALGK-KGAKGEEIKRAA-------SLAG-AHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIVILD 496
Cdd:cd03269 89 DQlVYLAQlKGLKKEEARRRIdewlerlELSEyANKRVEELSKG---------------NQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 497 EPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMG 551
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
338-548 |
2.51e-20 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 89.72 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 338 KQVSHSYIPGK---EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD----Q 410
Cdd:TIGR02211 5 ENLGKRYQEGKldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 VGYLHQTPFIFPG-SIAENIA----LGKKgAKGEEIKRAASLAGAhqfiaelpQGYDTKVGEGGRGLSGGERQRIALARV 485
Cdd:TIGR02211 85 LGFIYQFHHLLPDfTALENVAmpllIGKK-SVKEAKERAYEMLEK--------VGLEHRINHRPSELSGGERQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 486 FLKDAKIVILDEPTAGLDAHTEKlleKAFDELF-----QNRTVIIIAHRLSSLYRADKIILIDRGEIR 548
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDNNNAK---IIFDLMLelnreLNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
337-564 |
2.98e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.06 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVP-------LWELKEkdwyd 409
Cdd:PRK13636 8 VEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidysrkgLMKLRE----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 QVGYLHQTP--FIFPGSIAENIALG--KKGAKGEEIKRAASLAGAHQFIAELPQgydtkvgEGGRGLSGGERQRIALARV 485
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 486 FLKDAKIVILDEPTAGLD----AHTEKLLEKAFDELfqNRTVIIIAHRLS--SLYrADKIILIDRGEIRGMGRHEQLLAE 559
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDivPLY-CDNVFVMKEGRVILQGNPKEVFAE 232
|
....*
gi 499664576 560 NELYR 564
Cdd:PRK13636 233 KEMLR 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
335-546 |
4.15e-20 |
|
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: 86.73 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPlwelkekdwydQVGYL 414
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQtpfiFPGsiaenialgkkgakGEEIkraaslagahqfiaelpqgydtkvgeggrglsggerqRIALARVFLKDAKIVI 494
Cdd:cd03221 69 EQ----LSG--------------GEKM-------------------------------------RLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 495 LDEPTAGLDAHTEKLLEKAFDELfqNRTVIIIAH-R--LSSLyrADKIILIDRGE 546
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
335-547 |
6.68e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.22 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPG----KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWElKEKDWY-- 408
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDKYir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 409 ---DQVGYLHQTP--FIFPGSIAENIALGKK--GAKGEEIKraaslAGAHQFIAELpqGYDTKVGEGGRGLSGGERQR-I 480
Cdd:PRK13646 82 pvrKRIGMVFQFPesQLFEDTVEREIIFGPKnfKMNLDEVK-----NYAHRLLMDL--GFSRDVMSQSPFQMSGGQMRkI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELF--QNRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSI 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
351-570 |
6.99e-20 |
|
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: 88.94 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDwyDQVGYLHQTPFIFPG-SIAENI 429
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 430 ALGKKGAKGE------EIKRAAS-------LAG-AHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIVIL 495
Cdd:cd03296 96 AFGLRVKPRSerppeaEIRAKVHellklvqLDWlADRYPAQLSGG---------------QRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 496 DEPTAGLDAHTEK----LLEKAFDELfqNRTVIIIAHRLS-SLYRADKIILIDRGEIrgmgrhEQLLAENELYRQLITAY 570
Cdd:cd03296 161 DEPFGALDAKVRKelrrWLRRLHDEL--HVTTVFVTHDQEeALEVADRVVVMNKGRI------EQVGTPDEVYDHPASPF 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
342-559 |
8.49e-20 |
|
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: 88.26 E-value: 8.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 342 HSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkdwYDQV----GYLHQT 417
Cdd:cd03224 7 NAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP---HERAragiGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 418 PFIFPG-SIAENIALGKKGAKGEEIK-------------------RAASLAGAHQfiaelpqgydtkvgeggrglsgger 477
Cdd:cd03224 84 RRIFPElTVEENLLLGAYARRRAKRKarlervyelfprlkerrkqLAGTLSGGEQ------------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 478 QRIALARVFLKDAKIVILDEPTAGLdahTEKLLEKAFDELFQNR----TVIIIAHRLS-SLYRADKIILIDRGEIRGMGR 552
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGL---APKIVEEIFEAIRELRdegvTILLVEQNARfALEIADRAYVLERGRVVLEGT 215
|
....*..
gi 499664576 553 HEQLLAE 559
Cdd:cd03224 216 AAELLAD 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
347-572 |
1.11e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.65 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAE-----GEILING-VPLWELKE--KDWYDQVGYLHQTP 418
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTaRSLSQQKGliRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 419 FIFPG-SIAENIALGKKGAKGEeiKRAASLAGAHQFIAELpqGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDE 497
Cdd:PRK11264 95 NLFPHrTVLENIIEGPVIVKGE--PKEEATARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 498 PTAGLDAHTEKLLEKAFDELFQ-NRTVIIIAHRLsSLYR--ADKIILIDRGEIRGMGRHEQLLA--ENELYRQLITAYRG 572
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEM-SFARdvADRAIFMDQGRIVEQGPAKALFAdpQQPRTRQFLEKFLL 249
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
347-504 |
1.12e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.54 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRP---AEGEILINGVPLWELK-EKDwydQVGYLHQTPFIFP 422
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPaEQR---RIGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 423 G-SIAENIALG-----KKGAKGEEIKRA---ASLAG-AHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKI 492
Cdd:COG4136 90 HlSVGENLAFAlpptiGRAQRRARVEQAleeAGLAGfADRDPATLSGG---------------QRARVALLRALLAEPRA 154
|
170
....*....|..
gi 499664576 493 VILDEPTAGLDA 504
Cdd:COG4136 155 LLLDEPFSKLDA 166
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
334-566 |
1.98e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYIPGK----EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILIN--GVP--LWELKE- 404
Cdd:PRK13645 6 DIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPanLKKIKEv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 405 KDWYDQVGYLHQTP--FIFPGSIAENIALG--KKGAKGEEI-KRAASLAGahqfIAELPQGYdtkVGEGGRGLSGGERQR 479
Cdd:PRK13645 86 KRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvNLGENKQEAyKKVPELLK----LVQLPEDY---VKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 480 IALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN--RTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQL 556
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEI 238
|
250
....*....|
gi 499664576 557 LAENELYRQL 566
Cdd:PRK13645 239 FSNQELLTKI 248
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
17-289 |
2.76e-19 |
|
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: 88.08 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 17 LVKIALTSFISGGAIIAQAYLIAYIINGAF-LAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVL 95
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 96 LEKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMML 175
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 176 IGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTA 255
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 499664576 256 MVAVEVGLRLLYGKMEFLQAFFVLLLAPELYLPL 289
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
347-547 |
3.05e-19 |
|
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: 85.56 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ-VGYL----HQTPFIF 421
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 422 PGSIAENIALGkkgakgeeikraASLAGAHQfiaelpqgydtkvgeggrglsggerQRIALARVFLKDAKIVILDEPTAG 501
Cdd:cd03215 92 DLSVAENIALS------------SLLSGGNQ-------------------------QKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499664576 502 LDAHTEKLLEKAFDELF-QNRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:cd03215 135 VDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
335-562 |
5.32e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.10 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYL 414
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTP--FIFPGSIAENIALG--KKGAKGEEIKR----AASLAGAHQFIAELPQ--GYDTKvgeggrglsggerQRIALAR 484
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERrveeALKAVRMWDFRDKPPYhlSYGQK-------------KRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 485 VFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRLS-SLYRADKIILIDRGEIRGMG-----RHEQLL 557
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIV 231
|
....*
gi 499664576 558 AENEL 562
Cdd:PRK13647 232 EQAGL 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
354-558 |
1.31e-18 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 87.47 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 354 INLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD----QVGYLHQTPFIFPG-SIAEN 428
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpekrRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 429 IALGKKGAKGEEikRAASLAGAHQFIaelpqGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEK 508
Cdd:TIGR02142 96 LRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 509 ----LLEKAFDELfqNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLA 558
Cdd:TIGR02142 169 eilpYLERLHAEF--GIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
355-558 |
1.56e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.02 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 355 NLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGV----------PlwelkekdwydqVGYLHQTPFIFPG- 423
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrP------------VSMLFQENNLFSHl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 SIAENIALGK------KGAKGEEIKRAASLAGAHQFIAELPqgydtkvgeggRGLSGGERQRIALARVFLKDAKIVILDE 497
Cdd:PRK10771 87 TVAQNIGLGLnpglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 498 PTAGLD----AHTEKLLEKAFDElfQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLA 558
Cdd:PRK10771 156 PFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
342-547 |
1.73e-18 |
|
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: 83.73 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 342 HSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLM--RPAEGEILINGVplwELKEKDWYDQ----VGYLH 415
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGE---DITDLPPEERarlgIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 416 QTPFIFPG-SIAENIALGKKGAKGEEIKRaaslagahqfiAELPQgydtkvgeggrglsggerqrialarVFLKDAKIVI 494
Cdd:cd03217 84 QYPPEIPGvKNADFLRYVNEGFSGGEKKR-----------NEILQ-------------------------LLLLEPDLAI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 495 LDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAH--RLSSLYRADKIILIDRGEI 547
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRI 183
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
335-557 |
1.84e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.76 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPgKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLW--ELKEKDWYDQVG 412
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPGSIA-ENIALGK---KGAKGEEIKRAAS-------LAG-AHQFIAELPQGydtkvgeggrglsggERQRI 480
Cdd:PRK09493 81 MVFQQFYLFPHLTAlENVMFGPlrvRGASKEEAEKQARellakvgLAErAHHYPSELSGG---------------QQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLL 557
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
335-555 |
1.94e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.54 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKD---WYDQV 411
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQT-PFIFPGSIAENIA--LGKKGAKGEEIKRAASLA--------GAHQFIAELPQGydtkvgeggrglsggERQRI 480
Cdd:PRK10908 82 GMIFQDhHLLMDRTVYDNVAipLIIAGASGDDIRRRVSAAldkvglldKAKNFPIQLSGG---------------EQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELfqNR---TVIIIAHRLSSLYRAD-KIILIDRGEIRGmGRHEQ 555
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF--NRvgvTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
347-528 |
2.42e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVplwELKEKDWYDQVGYL-HQTPFIFPGSI 425
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAEACHYLgHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 AENIAL--GKKGAKGEEIKRAASLAGAHQfIAELPQGYdtkvgeggrgLSGGERQRIALARVFLKDAKIVILDEPTAGLD 503
Cdd:PRK13539 91 AENLEFwaAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*.
gi 499664576 504 AHTEKLLEKAFDE-LFQNRTVIIIAH 528
Cdd:PRK13539 160 AAAVALFAELIRAhLAQGGIVIAATH 185
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
342-539 |
2.92e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.44 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 342 HSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLL--LGLMRP---AEGEILINGVPLWELKEK--DWYDQVGYL 414
Cdd:PRK14239 12 SVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPRTDtvDLRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPGSIAENIALGK--KGAKGEEIKRAA---SLAGAHQFIAELPQGYDTKVGEGGRGLsggerQRIALARVFLKD 489
Cdd:PRK14239 92 FQQPNPFPMSIYENVVYGLrlKGIKDKQVLDEAvekSLKGASIWDEVKDRLHDSALGLSGGQQ-----QRVCIARVLATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499664576 490 AKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHrlsSLYRADKI 539
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-565 |
3.43e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEK--DWYDQVGYLHQTP--FIFPG 423
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQDPeqQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 SIAENIALGKK--GAKGEEIKR----AASLAGA----HQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIV 493
Cdd:PRK13638 94 DIDSDIAFSLRnlGVPEAEITRrvdeALTLVDAqhfrHQPIQCLSHG---------------QKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 494 ILDEPTAGLD-AHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAENELYRQ 565
Cdd:PRK13638 159 LLDEPTAGLDpAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAMEQ 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
334-562 |
3.89e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.14 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYIPGK----EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEI---LINGVPLWELKEKD 406
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 407 WYD---------------------QVGYLHQtpF----IFPGSIAENIALGKKG---AKGEEIKRAA---SLAGahqfia 455
Cdd:PRK13651 82 KVLeklviqktrfkkikkikeirrRVGVVFQ--FaeyqLFEQTIEKDIIFGPVSmgvSKEEAKKRAAkyiELVG------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 456 eLPQGYDTKvgeGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRLSS-L 533
Cdd:PRK13651 154 -LDESYLQR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNvL 229
|
250 260 270
....*....|....*....|....*....|....*
gi 499664576 534 YRADKIILIDRGEIRGMG------RHEQLLAENEL 562
Cdd:PRK13651 230 EWTKRTIFFKDGKIIKDGdtydilSDNKFLIENNM 264
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
350-540 |
4.39e-18 |
|
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: 85.49 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRP---AEGEILINGVPLWELKEKDWYD----QVGYLHQTPFifp 422
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDPM--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 423 GS----------IAENIALGKKGAKGEEIKRAAS------LAGAHQFIAELP------QgydtkvgeggrglsggeRQRI 480
Cdd:COG0444 97 TSlnpvmtvgdqIAEPLRIHGGLSKAEARERAIEllervgLPDPERRLDRYPhelsggM-----------------RQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAHTEK----LLEKAFDELfqNRTVIIIAHRLSSLYR-ADKII 540
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAqilnLLKDLQREL--GLAILFITHDLGVVAEiADRVA 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
348-547 |
5.34e-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: 83.54 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING-VPlwelkekdWYDQVGYLHQTPFIFPG--- 423
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVP--------WKRRKKFLRRIGVVFGQktq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 -----SIAENIALGK---KGAKGEEIKRAASLAGAHQFIAELpqgyDTKVgeggrgLSGGERQRI--ALARVFLKDAKIV 493
Cdd:cd03267 106 lwwdlPVIDSFYLLAaiyDLPPARFKKRLDELSELLDLEELL----DTPV------RQLSLGQRMraEIAAALLHEPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
337-548 |
6.09e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.39 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPlweLKEKDwYDQVGYLHQ 416
Cdd:COG4152 4 LKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPED-RRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TPFIFPG-SIAENIA-LGK-KGAKGEEIKRAAS-------LAG-AHQFIAELPQGydtkvgeggrglsggERQRIALARV 485
Cdd:COG4152 79 ERGLYPKmKVGEQLVyLARlKGLSKAEAKRRADewlerlgLGDrANKKVEELSKG---------------NQQKVQLIAA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 486 FLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRLSSLYR-ADKIILIDRGEIR 548
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEElCDRIVIINKGRKV 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
333-528 |
1.04e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.99 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYIPG---KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLwelkEKDWYD 409
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV----TGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 QvGYLHQTPFIFPG-SIAENIALG---KKGAKGEEIKRAAS------LAGAHQ-FIAELPQGydtkvgeggrglsggERQ 478
Cdd:COG4525 78 R-GVVFQKDALLPWlNVLDNVAFGlrlRGVPKAERRARAEEllalvgLADFARrRIWQLSGG---------------MRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499664576 479 RIALARVFLKDAKIVILDEPTAGLDAHT----EKLLEKAFDElfQNRTVIIIAH 528
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTreqmQELLLDVWQR--TGKGVFLITH 193
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
335-563 |
1.23e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.82 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYL 414
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFI--------------FPGSiaenialgkKGAKGEE----IKRAASLAG----AHQFIAELPQGydtkvgeggrgl 472
Cdd:COG4604 81 RQENHInsrltvrelvafgrFPYS---------KGRLTAEdreiIDEAIAYLDledlADRYLDELSGG------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 473 sggERQRIALARVFLKDAKIVILDEPTAGLD-AH---TEKLLEKAFDELfqNRTVIIIAHRL--SSLYrADKIILIDRGE 546
Cdd:COG4604 140 ---QRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHsvqMMKLLRRLADEL--GKTVVIVLHDInfASCY-ADHIVAMKDGR 213
|
250 260
....*....|....*....|
gi 499664576 547 IRGMGRHEQLLAE---NELY 563
Cdd:COG4604 214 VVAQGTPEEIITPevlSDIY 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
334-565 |
1.36e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGY 413
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFIFPG-SIAENIALGKK---------GAKGEEI---------------KRAASLAGAHQfiaelpqgydtkvgeg 468
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYGRSpwlslwgrlSAEDNARvnqameqtrinhladRRLTDLSGGQR---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 469 grglsggerQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRLSSLYR-ADKIILIDRGE 546
Cdd:PRK11231 145 ---------QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRyCDHLVVLANGH 215
|
250
....*....|....*....
gi 499664576 547 IRGMGRHEQLLAEnELYRQ 565
Cdd:PRK11231 216 VMAQGTPEEVMTP-GLLRT 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
340-547 |
1.87e-17 |
|
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: 82.55 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 340 VSHSYIPG--------KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDwydQV 411
Cdd:TIGR02769 8 VTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ---RR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIF---PGS----------IAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRglsggerQ 478
Cdd:TIGR02769 85 AFRRDVQLVFqdsPSAvnprmtvrqiIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQL-------Q 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499664576 479 RIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
335-552 |
2.05e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.31 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDwyDQVGYL 414
Cdd:PRK11000 4 VTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPG-SIAENIALGKK--GAKGEEIKR-----AASLAGAHqFIAELPQgydtkvgeggrGLSGGERQRIALARVF 486
Cdd:PRK11000 81 FQSYALYPHlSVAENMSFGLKlaGAKKEEINQrvnqvAEVLQLAH-LLDRKPK-----------ALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 487 LKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAH-RLSSLYRADKIILIDRGEIRGMGR 552
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
347-527 |
2.23e-17 |
|
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: 80.48 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKdWYDQVGYLHQTPFIFPG-SI 425
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLGHLPGLKPElSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 AENI----------------ALGKKGAKGEEIKRAASLAGAHQfiaelpqgydtkvgeggrglsggerQRIALARVFLKD 489
Cdd:TIGR01189 91 LENLhfwaaihggaqrtiedALAAVGLTGFEDLPAAQLSAGQQ-------------------------RRLALARLWLSR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 499664576 490 AKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIA 527
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLT 183
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
351-562 |
2.23e-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: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMrPAEGEILINGVPLWELKEKDWYDQVGYLHQ---TPFIFPGsiAE 427
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQqqsPPFAMPV--FQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 428 NIALG--KKGAKGEEIKRAASLAGA-------HQFIAELPQGydtkvgeggrglsggERQRIALARVFLK-------DAK 491
Cdd:COG4138 89 YLALHqpAGASSEAVEQLLAQLAEAlgledklSRPLTQLSGG---------------EWQRVRLAAVLLQvwptinpEGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 492 IVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAHRLS-SLYRADKIILIDRGEIRGMGRHEQLLAENEL 562
Cdd:COG4138 154 LLLLDEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPENL 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
333-562 |
2.72e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVG 412
Cdd:PRK09536 2 PMIDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQ-TPFIFPGSIAENIALGKKGAKGE----------EIKRAASLAGAHQF----IAELPQGydtkvgeggrglsggER 477
Cdd:PRK09536 81 SVPQdTSLSFEFDVRQVVEMGRTPHRSRfdtwtetdraAVERAMERTGVAQFadrpVTSLSGG---------------ER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 478 QRIALARVFLKDAKIVILDEPTAGLDA-HTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQ 555
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDInHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPAD 225
|
....*..
gi 499664576 556 LLAENEL 562
Cdd:PRK09536 226 VLTADTL 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
353-516 |
2.92e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.62 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 353 NINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkDWYDQVGYL-HQ-------TPFifpgs 424
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLgHQpgiktelTAL----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 425 iaEN--IALGKKGAKGEEIKRAA----SLAG-----AHQfiaeLPQGydtkvgeggrglsggerQ--RIALARVFLKDAK 491
Cdd:PRK13538 93 --ENlrFYQRLHGPGDDEALWEAlaqvGLAGfedvpVRQ----LSAG-----------------QqrRVALARLWLTRAP 149
|
170 180
....*....|....*....|....*
gi 499664576 492 IVILDEPTAGLDAHTEKLLEKAFDE 516
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
330-551 |
4.25e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.72 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 330 DSPPEIILKQVSHSYiPGKE--VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDW 407
Cdd:PRK13648 3 DKNSIIVFKNVSFQY-QSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 408 YDQVGYLHQTP-FIFPGSIA--------ENIALGKKGAKgEEIKRAASLAGAHQFIAELPQGydtkvgeggrgLSGGERQ 478
Cdd:PRK13648 82 RKHIGIVFQNPdNQFVGSIVkydvafglENHAVPYDEMH-RRVSEALKQVDMLERADYEPNA-----------LSGGQKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 479 RIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRLSSLYRADKIILIDRGEIRGMG 551
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
351-559 |
4.92e-17 |
|
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: 81.15 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD----QVGYLHQTPFIFPG-SI 425
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 AENIALG---------KKGAKGEEIKRAASLAG-AHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIVIL 495
Cdd:cd03294 120 LENVAFGlevqgvpraEREERAAEALELVGLEGwEHKYPDELSGG---------------MQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 496 DEPTAGLDAHTEKLLEkafDELFQ-----NRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAE 559
Cdd:cd03294 185 DEAFSALDPLIRREMQ---DELLRlqaelQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
337-547 |
5.08e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.39 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYIPGKE---VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkdwyDQVGY 413
Cdd:PRK10535 7 LKDIRRSYPSGEEqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA----DALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQT--PFIFPG-------SIAENIALGKKGAKGEeikRAASLAGAHQFIAELpqGYDTKVGEGGRGLSGGERQRIALAR 484
Cdd:PRK10535 83 LRREhfGFIFQRyhllshlTAAQNVEVPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 485 VFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAHRLSSLYRADKIILIDRGEI 547
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
335-547 |
6.60e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.29 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKE-----VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVP------LWELK 403
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 404 EKdwydqVGYLHQTP--FIFPGSIAENIALGKK--GAKGEEIKR----AASLAGAHQFIAELPQgydtkvgeggrGLSGG 475
Cdd:PRK13633 85 NK-----AGMVFQNPdnQIVATIVEEDVAFGPEnlGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 476 ERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRLSSLYRADKIILIDRGEI 547
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
342-547 |
8.01e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.11 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 342 HSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGlmRPA----EGEILINGVPLWELKEkdwyDQ-----VG 412
Cdd:COG0396 7 HVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSILLDGEDILELSP----DEraragIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPG-SIAE--NIALGKKgaKGEEIKRAASLAGAHQFIAELpqGYDT----------------Kvgeggrgls 473
Cdd:COG0396 81 LAFQYPVEIPGvSVSNflRTALNAR--RGEELSAREFLKLLKEKMKEL--GLDEdfldryvnegfsggekK--------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 474 ggerqRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAH--RLSSLYRADKIILIDRGEI 547
Cdd:COG0396 148 -----RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRI 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
339-531 |
8.72e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 339 QVSHSYIPGK---EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWEL----KEKDWYDQV 411
Cdd:PRK11629 10 NLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPGSIA-ENIAL----GKKgakgeeiKRAASLAGAHQFIAELpqGYDTKVGEGGRGLSGGERQRIALARVF 486
Cdd:PRK11629 90 GFIYQFHHLLPDFTAlENVAMplliGKK-------KPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499664576 487 LKDAKIVILDEPTAGLDAHTEKLLEKAFDEL--FQNRTVIIIAHRLS 531
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
332-563 |
9.62e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.30 E-value: 9.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 332 PPEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWEL-KEKdwyDQ 410
Cdd:PRK09452 12 SPLVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpAEN---RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 VGYLHQTPFIFPG-SIAENIALGKKGAK--GEEIK------------------RAASLAGAHQfiaelpqgydtkvgegg 469
Cdd:PRK09452 88 VNTVFQSYALFPHmTVFENVAFGLRMQKtpAAEITprvmealrmvqleefaqrKPHQLSGGQQ----------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 470 rglsggerQRIALARVFLKDAKIVILDEPTAGLDAhteKLLEKAFDELFQ-----NRTVIIIAH-RLSSLYRADKIILID 543
Cdd:PRK09452 151 --------QRVAIARAVVNKPKVLLLDESLSALDY---KLRKQMQNELKAlqrklGITFVFVTHdQEEALTMSDRIVVMR 219
|
250 260
....*....|....*....|
gi 499664576 544 RGEIrgmgrhEQLLAENELY 563
Cdd:PRK09452 220 DGRI------EQDGTPREIY 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
347-529 |
1.07e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.32 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGL--------MRPAEGEILingvplwelkekdwydqvgYLHQTP 418
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVL-------------------FLPQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 419 FIFPGSIAENIA--LGKKGAKGEEIKRAASLAGAHQFIAELPQGYD-TKVGEGGRGlsggerQRIALARVFLKDAKIVIL 495
Cdd:COG4178 436 YLPLGTLREALLypATAEAFSDAELREALEAVGLGHLAERLDEEADwDQVLSLGEQ------QRLAFARLLLHKPDWLFL 509
|
170 180 190
....*....|....*....|....*....|....
gi 499664576 496 DEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHR 529
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
347-573 |
1.13e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.81 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkdWYDQVGYLHQTPFIFPG-SI 425
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFPHmTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 AENIALGKKG---AKGEEIKRAA---SLAGAHQFIAELPQgydtkvgeggrGLSGGERQRIALARVFLKDAKIVILDEPT 499
Cdd:PRK11607 109 EQNIAFGLKQdklPKAEIASRVNemlGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 500 AGLDahtEKLLEKAFDELFQ-----NRTVIIIAH-RLSSLYRADKIILIDRGEIRGMGRHEqllaenELYRQLITAYRGE 573
Cdd:PRK11607 178 GALD---KKLRDRMQLEVVDilervGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE------EIYEHPTTRYSAE 248
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
22-296 |
1.29e-16 |
|
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: 80.54 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 22 LTSFISGGAIIAQAYLIAYIINGAFLAKKgLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIAA 101
Cdd:cd18552 6 LGMILVAATTAALAWLLKPLLDDIFVEKD-LEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 102 LGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAE 181
Cdd:cd18552 85 LPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 182 KLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVAVEV 261
Cdd:cd18552 165 KISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYG 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 499664576 262 GLRLLYGKM---EFLqAFFVLLLApeLYLPLRNLGSSF 296
Cdd:cd18552 245 GYQVISGELtpgEFI-SFITALLL--LYQPIKRLSNVN 279
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
346-564 |
1.35e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.53 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 346 PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMrPA---EGEILINGvplwELKE-KDWYD--QVG--YLHQ- 416
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDG----EVCRfKDIRDseALGivIIHQe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 ---TPFIfpgSIAENIALGKKGAKGEEIKRAASLAGAHQFIA-----ELPqgyDTKVgeggRGLSGGERQRIALARVFLK 488
Cdd:NF040905 87 lalIPYL---SIAENIFLGNERAKRGVIDWNETNRRARELLAkvgldESP---DTLV----TDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 489 DAKIVILDEPTAGL-DAHTEKLLE--KAFDElfQNRTVIIIAHRLSSLYR-ADKI-ILIDRGEIRGMGRHEQLLAENELY 563
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAALLDllLELKA--QGITSIIISHKLNEIRRvADSItVLRDGRTIETLDCRADEVTEDRII 234
|
.
gi 499664576 564 R 564
Cdd:NF040905 235 R 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
336-557 |
1.62e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 336 ILKQVSHSyIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYL- 414
Cdd:PRK10575 13 ALRNVSFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPGSIAENIALGK---KGAKG-------EEIKRAASLAG----AHQFIAELPQGydtkvgeggrglsggERQRI 480
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGRypwHGALGrfgaadrEKVEEAISLVGlkplAHRLVDSLSGG---------------ERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLD-AHTEKLLeKAFDELFQNR--TVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQL 556
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDiAHQVDVL-ALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEL 235
|
.
gi 499664576 557 L 557
Cdd:PRK10575 236 M 236
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
17-297 |
1.76e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 80.25 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 17 LVKIALTSFISGGAIIAQAYLIAYIINGAFLAKKGLGELWPFFP---ALFLIVTLRFSLGYFGEKVGANLASKVTGEIRN 93
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLlvlGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 94 VLLEKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFM 173
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 174 MLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRV-AFLSALaLEVLATI 252
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLwATFFPL-LTFLTSL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499664576 253 STAMVAVEVGLRLLYGKMEF--LQAFFVLLLapELYLPLRNLGSSFH 297
Cdd:cd18563 240 GTLIVWYFGGRQVLSGTMTLgtLVAFLSYLG--MFYGPLQWLSRLNN 284
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
348-551 |
2.20e-16 |
|
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: 78.34 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING--VPLWELkekdwydQVGylhqtpfiFPGSI 425
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGL-------GGG--------FNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 A--ENIALGK--KGAKGEEIKRAAslagahQFI---AELPQGYDTKVGEGGRGLSGgerqRIALARVFLKDAKIVILDEP 498
Cdd:cd03220 100 TgrENIYLNGrlLGLSRKEIDEKI------DEIiefSELGDFIDLPVKTYSSGMKA----RLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 499 TAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRLSSLYR-ADKIILIDRGEIRGMG 551
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
350-547 |
2.86e-16 |
|
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: 78.93 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkdwydqvgylH-----------QTP 418
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP----------HriarlgiartfQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 419 FIFPG-SIAENIALG----------------KKGAKGEE--IKRAASLAG-------AHQFIAELPQGydtkvgeggrgl 472
Cdd:COG0411 89 RLFPElTVLENVLVAaharlgrgllaallrlPRARREEReaRERAEELLErvgladrADEPAGNLSYG------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 473 sggERQRIALARVFLKDAKIVILDEPTAGLdAHTEK-----LLEKAFDElfQNRTVIIIAHRLSSLYR-ADKIILIDRGE 546
Cdd:COG0411 157 ---QQRRLEIARALATEPKLLLLDEPAAGL-NPEETeelaeLIRRLRDE--RGITILLIEHDMDLVMGlADRIVVLDFGR 230
|
.
gi 499664576 547 I 547
Cdd:COG0411 231 V 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
335-566 |
2.92e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.46 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKE-VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRP---AEGEILINGVPL-----WELKEK 405
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLtaktvWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 406 dwydqVGYLHQTP---FIfPGSIAENIALG--KKGAKGEEIKR----AASLAGAHQFIAELPQgydtkvgeggrGLSGGE 476
Cdd:PRK13640 86 -----VGIVFQNPdnqFV-GATVGDDVAFGleNRAVPRPEMIKivrdVLADVGMLDYIDSEPA-----------NLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 477 RQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHE 554
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPV 228
|
250
....*....|..
gi 499664576 555 QLLAENELYRQL 566
Cdd:PRK13640 229 EIFSKVEMLKEI 240
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
331-559 |
3.07e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 331 SPPEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLwELKEKDWYDQ 410
Cdd:PRK13536 38 STVAIDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-PARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 VGYLHQTPFIFPG-SIAENIALGKK--GAKGEEIKraASLAGAHQFiAELPQGYDTKVGEGGRGLSggerQRIALARVFL 487
Cdd:PRK13536 116 IGVVPQFDNLDLEfTVRENLLVFGRyfGMSTREIE--AVIPSLLEF-ARLESKADARVSDLSGGMK----RRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 488 KDAKIVILDEPTAGLDAHTEKLL-EKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAE 559
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
349-556 |
3.53e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.13 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 349 EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDwyDQVGYLHQTPFIFPG-SIAE 427
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 428 NIALG------KKGAKGEEIKRAAS-------LAG-AHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIV 493
Cdd:PRK10851 94 NIAFGltvlprRERPNAAAIKAKVTqllemvqLAHlADRYPAQLSGG---------------QKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAH-RLSSLYRADKIILIDRGEIRGMGRHEQL 556
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
346-546 |
4.15e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 346 PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMrPA---EGEILINGVPLWELKEKDwYDQVG--YLHQTPFI 420
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRD-TERAGiaIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 421 FPG-SIAENIALGKKGAKGEEIKRAASLAGAHQFIAELpqGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPT 499
Cdd:PRK13549 94 VKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499664576 500 AGL-DAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGE 546
Cdd:PRK13549 172 ASLtESETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
350-551 |
4.36e-16 |
|
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: 77.41 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGV-----PLwELKEKdwydqVGYLHQTPFIFPG- 423
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdvvkePA-EARRR-----LGFVSDSTGLYDRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 SIAENIAL--GKKGAKGEEIKRA----ASLAGAHQFI----AELPQGydtkvgeggrglsggERQRIALARVFLKDAKIV 493
Cdd:cd03266 94 TARENLEYfaGLYGLKGDELTARleelADRLGMEELLdrrvGGFSTG---------------MRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDEL-FQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMG 551
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-547 |
5.05e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 349 EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMR-----PAEGEILINGVPLWELKEKDWYDQVGYLHQTPFIFPG 423
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 -SIAENIALGKKgaKGEEIKRAASLAGAHQFIAELPQGYD---TKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPT 499
Cdd:PRK14247 97 lSIFENVALGLK--LNRLVKSKKELQERVRWALEKAQLWDevkDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499664576 500 AGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEI 547
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQI 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
353-566 |
5.69e-16 |
|
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: 79.76 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 353 NINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGvplwelkeKDWYD------------QVGYLHQTPFI 420
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG--------EVLQDsargiflpphrrRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 421 FPG-SIAENIALGKKGAKGEEikRAASLAGA----------HQFIAELPQGydtkvgeggrglsggERQRIALARVFLKD 489
Cdd:COG4148 89 FPHlSVRGNLLYGRKRAPRAE--RRISFDEVvellgighllDRRPATLSGG---------------ERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 490 AKIVILDEPTAGLDAHTeK-----LLEKAFDELfqNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAENELY 563
Cdd:COG4148 152 PRLLLMDEPLAALDLAR-KaeilpYLERLRDEL--DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
...
gi 499664576 564 RQL 566
Cdd:COG4148 229 PLA 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
347-558 |
6.44e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 80.62 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGL--MRPAEGEILIN----------GVP---------------- 398
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyvERPskvgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 399 ----LWELKEKDWYD---QVGYLHQTPFIFPG--SIAENI--ALGKKGAKGEE-IKRAASLagahqfIAELPQGYdtKVG 466
Cdd:TIGR03269 92 eevdFWNLSDKLRRRirkRIAIMLQRTFALYGddTVLDNVleALEEIGYEGKEaVGRAVDL------IEMVQLSH--RIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 467 EGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAH---RLSSLyrADKIIL 541
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHwpeVIEDL--SDKAIW 241
|
250
....*....|....*..
gi 499664576 542 IDRGEIRGMGRHEQLLA 558
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVA 258
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
366-559 |
6.45e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 79.07 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 366 IVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYdqVGYLHQTPFIFPG-SIAENIALGKK--GAKGEEIK 442
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH--INMVFQSYALFPHmTVEENVAFGLKmrKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 443 -------RAASLAG-AHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAF 514
Cdd:TIGR01187 79 prvlealRLVQLEEfADRKPHQLSGG---------------QQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499664576 515 DELfQNR---TVIIIAHRLS-SLYRADKIILIDRGEIRGMGRHEQLLAE 559
Cdd:TIGR01187 144 KTI-QEQlgiTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
349-556 |
8.00e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 76.64 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 349 EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLweLKE-KDWYDQVGYLHQTPFIFPGSIA- 426
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREpREVRRRIGIVFQDLSVDDELTGw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 427 ENIALGKK--GAKGEEIK-RAASL---AGAHQFIAELPQGYDTKVgeggrglsggeRQRIALARVFLKDAKIVILDEPTA 500
Cdd:cd03265 92 ENLYIHARlyGVPGAERReRIDELldfVGLLEAADRLVKTYSGGM-----------RRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499664576 501 GLDAHTE----KLLEKAFDElfQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQL 556
Cdd:cd03265 161 GLDPQTRahvwEYIEKLKEE--FGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
351-545 |
8.36e-16 |
|
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: 76.74 E-value: 8.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkdwyDQVgYLHQTPFIFPG-SIAENI 429
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP----DRM-VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 430 ALG--------KKGAKGEEIKRAASLAG----AHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIVILDE 497
Cdd:TIGR01184 76 ALAvdrvlpdlSKSERRAIVEEHIALVGlteaADKRPGQLSGG---------------MKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499664576 498 PTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRL-SSLYRADKIILIDRG 545
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
342-562 |
8.64e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 76.94 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 342 HSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkdwyDQ-----VGYLHQ 416
Cdd:COG0410 10 HAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP----HRiarlgIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TPFIFPG-SIAENIALG----KKGAKGEEIK----------------RAASLAGAHQfiaelpqgydtkvgeggrglsgg 475
Cdd:COG0410 86 GRRIFPSlTVEENLLLGayarRDRAEVRADLervyelfprlkerrrqRAGTLSGGEQ----------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 476 erQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELfqNR---TVIII---AHRLSSLyrADKIILIDRGEIRG 549
Cdd:COG0410 143 --QMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL--NRegvTILLVeqnARFALEI--ADRAYVLERGRIVL 216
|
250
....*....|...
gi 499664576 550 MGRHEQLLAENEL 562
Cdd:COG0410 217 EGTAAELLADPEV 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
339-552 |
1.12e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.05 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 339 QVSHSYI--PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLwelkeKDWYDQVGYLHQ 416
Cdd:PRK11248 3 QISHLYAdyGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TPFIFP-GSIAENIALG---------KKGAKGEEIKRAASLAGAHQ-FIAELPQGydtkvgeggrglsggERQRIALARV 485
Cdd:PRK11248 78 NEGLLPwRNVQDNVAFGlqlagvekmQRLEIAHQMLKKVGLEGAEKrYIWQLSGG---------------QRQRVGIARA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 486 FLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN--RTVIIIAHRL-SSLYRADKIILIDRGEIRGMGR 552
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITHDIeEAVFMATELVLLSPGPGRVVER 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
346-535 |
1.22e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 346 PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ-VGYLHQTPFIFPG- 423
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgVAIIYQELHLVPEm 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 SIAENIALGKKGAKGEEIKRAASLAGAHQFIAELpqGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLD 503
Cdd:PRK11288 95 TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190
....*....|....*....|....*....|...
gi 499664576 504 AHTEKLLEKAFDEL-FQNRTVIIIAHRLSSLYR 535
Cdd:PRK11288 173 AREIEQLFRVIRELrAEGRVILYVSHRMEEIFA 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
335-551 |
1.34e-15 |
|
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: 76.00 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPG-KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKeKDWYDQVGY 413
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR-KAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFIFPG-SIAENIAL---------GKKGAKGEEIKRAASLAG-AHQFIAELPQGydtkvgeggrglsggERQRIAL 482
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkglpkSEIKEEVELLLRVLGLTDkANKRARTLSGG---------------MKRKLSL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 483 ARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMG 551
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIG 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
347-514 |
1.37e-15 |
|
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: 75.61 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEkDWYDQVGYL-HQTPFIFPGSI 425
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLgHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 AENI--------------ALGKKGAKGEEIKRAASLAGAHQfiaelpqgydtkvgeggrglsggerQRIALARVFLKDAK 491
Cdd:cd03231 91 LENLrfwhadhsdeqveeALARVGLNGFEDRPVAQLSAGQQ-------------------------RRVALARLLLSGRP 145
|
170 180
....*....|....*....|...
gi 499664576 492 IVILDEPTAGLDAHTEKLLEKAF 514
Cdd:cd03231 146 LWILDEPTTALDKAGVARFAEAM 168
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-547 |
1.53e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.66 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPG----KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ 410
Cdd:COG1101 2 LELKNLSKTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 VGYLHQTPFI--FPG-SIAENIALGKKGAKGEEIKRAASLAGAHQF---IAELPQGY----DTKVgeggrgLSGGERQRI 480
Cdd:COG1101 82 IGRVFQDPMMgtAPSmTIEENLALAYRRGKRRGLRRGLTKKRRELFrelLATLGLGLenrlDTKV------GLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499664576 481 ALARVF--LKDAKIVILDEPTAGLDAHTEKLLEKAFDELF--QNRTVIIIAHRLS-SLYRADKIILIDRGEI 547
Cdd:COG1101 156 ALSLLMatLTKPKLLLLDEHTAALDPKTAALVLELTEKIVeeNNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
337-546 |
1.69e-15 |
|
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: 79.59 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILIN-GVplwelkekdwydQVGYLH 415
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGI------------KVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 416 QTPFIFPG-SIAENI-----------------------------ALGKKGAKGEEIKRAAslaGAHQF-----IA----E 456
Cdd:TIGR03719 75 QEPQLDPTkTVRENVeegvaeikdaldrfneisakyaepdadfdKLAAEQAELQEIIDAA---DAWDLdsqleIAmdalR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 457 LPQGyDTKVGEGGRGLSggerQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDElFQNrTVIIIAHRLSSLYRA 536
Cdd:TIGR03719 152 CPPW-DADVTKLSGGER----RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTHDRYFLDNV 224
|
250
....*....|.
gi 499664576 537 DKIIL-IDRGE 546
Cdd:TIGR03719 225 AGWILeLDRGR 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
335-566 |
1.76e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.08 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKE--VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVG 412
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTP-FIFPGSIAE-NIALG--KKGAKGEEIK----RAASLAGAHQFI----AELPQGydtkvgeggrglsggERQRI 480
Cdd:PRK13650 85 MVFQNPdNQFVGATVEdDVAFGleNKGIPHEEMKervnEALELVGMQDFKerepARLSGG---------------QKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLA 558
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
....*...
gi 499664576 559 ENELYRQL 566
Cdd:PRK13650 230 RGNDLLQL 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
348-571 |
2.05e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING--VPLWELkekdwydQVGYLHQtpfiFPGsi 425
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvSALLEL-------GAGFHPE----LTG-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 AENIALGKK--GAKGEEIKRA----ASLAGAHQFIaelpqgyDTKVgeggrglsggerQ--------RIALARVFLKDAK 491
Cdd:COG1134 106 RENIYLNGRllGLSRKEIDEKfdeiVEFAELGDFI-------DQPV------------KtyssgmraRLAFAVATAVDPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 492 IVILDEPTAGLDAH-TEKLLEKaFDELFQN-RTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAEnelYRQLIT 568
Cdd:COG1134 167 ILLVDEVLAVGDAAfQKKCLAR-IRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA---YEALLA 242
|
...
gi 499664576 569 AYR 571
Cdd:COG1134 243 GRE 245
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-567 |
2.46e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 76.24 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 344 YIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMR------PAEGEILINGVPLWELKEKDWYDQVGYLHQT 417
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 418 PFIFPG-SIAENIA--LGKKGAKGE-EIKRAasLAGAHQFIAELPQGYDtKVGEGGRGLSGGERQRIALARVFLKDAKIV 493
Cdd:PRK14246 99 PNPFPHlSIYDNIAypLKSHGIKEKrEIKKI--VEECLRKVGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 494 ILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLA--ENELYRQLI 567
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTspKNELTEKYV 252
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-304 |
3.11e-15 |
|
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: 76.42 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 22 LTSFISGGAIIAQAYLIAYIINGAFLAKKGLGELWPFFPALFLIVTLRfSLGYFGEKVGANLAS-KVTGEIRNVLLEKIA 100
Cdd:cd18778 6 LCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLR-ALLNFLRIYLNHVAEqKVVADLRSDLYDKLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 101 ALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFA 180
Cdd:cd18778 85 RLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 181 EKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVaVE 260
Cdd:cd18778 165 RPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLV-LG 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499664576 261 VGLRL-LYGKMEF--LQAFFVLLLApeLYLPLRNLGSSFHAGRTAIA 304
Cdd:cd18778 244 FGGRLvLAGELTIgdLVAFLLYLGL--FYEPITSLHGLNEMLQRALA 288
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
340-547 |
3.31e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.88 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 340 VSHSY--------IPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD-- 409
Cdd:PRK10419 9 LSHHYahgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 -QVGYLHQTPfifPG------SIAENIA--------LGKKG--AKGEEIKRAASLAGAHqfIAELPQgydtkvgeggrGL 472
Cdd:PRK10419 89 rDIQMVFQDS---ISavnprkTVREIIReplrhllsLDKAErlARASEMLRAVDLDDSV--LDKRPP-----------QL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 473 SGGERQRIALARVFLKDAKIVILDEPTAGLDAHTE----KLLEKafdelFQNRT---VIIIAHRLSSLYR-ADKIILIDR 544
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQagviRLLKK-----LQQQFgtaCLFITHDLRLVERfCQRVMVMDN 227
|
...
gi 499664576 545 GEI 547
Cdd:PRK10419 228 GQI 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
333-559 |
3.89e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.31 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYIP-GKEVLK---NINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEilingvpLWELKEKDWY 408
Cdd:TIGR03269 278 PIIKVRNVSKRYISvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE-------VNVRVGDEWV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 409 DQ--------------VGYLHQTPFIFP-GSIAENIA----------LGKKGA------KGEEIKRAASLagAHQFIAEL 457
Cdd:TIGR03269 351 DMtkpgpdgrgrakryIGILHQEYDLYPhRTVLDNLTeaiglelpdeLARMKAvitlkmVGFDEEKAEEI--LDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 458 PQGydtkvgeggrglsggERQRIALARVFLKDAKIVILDEPTAGLDAHTE----KLLEKAFDELfqNRTVIIIAHRLS-S 532
Cdd:TIGR03269 429 SEG---------------ERHRVALAQVLIKEPRIVILDEPTGTMDPITKvdvtHSILKAREEM--EQTFIIVSHDMDfV 491
|
250 260
....*....|....*....|....*..
gi 499664576 533 LYRADKIILIDRGEIRGMGRHEQLLAE 559
Cdd:TIGR03269 492 LDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
337-546 |
3.99e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 78.23 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ-VGYLH 415
Cdd:PRK10982 1 MSNISKSF-PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 416 QT-PFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVgeGGRGLSGGERQRIALARVFLKDAKIVI 494
Cdd:PRK10982 80 QElNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRA--KVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 495 LDEPTAGLdahTEKLLEKAFD--ELFQNR--TVIIIAHRLSSLYR-ADKIILIDRGE 546
Cdd:PRK10982 158 MDEPTSSL---TEKEVNHLFTiiRKLKERgcGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
354-562 |
4.23e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 354 INLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMrPAEGEILINGVPLWELKEKDWYDQVGYLHQ---TPFIFPG------S 424
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQqqtPPFAMPVfqyltlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 425 IAENIALGKKGAKGEEIKRAASLAGA-HQFIAELPQGydtkvgeggrglsggERQRIALARVFLK-------DAKIVILD 496
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGLDDKlGRSVNQLSGG---------------EWQRVRLAAVVLQvwpdinpAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 497 EPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAENEL 562
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCqQGIAVVMSSHDLNHTLRhADRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
335-564 |
5.02e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.93 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIP----GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKE----KD 406
Cdd:PRK13643 2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 407 WYDQVGYLHQTP--FIFPGSIAENIALGKK--GAKGEEIKRAAS-----LAGAHQFIAELPqgydtkvgeggRGLSGGER 477
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQnfGIPKEKAEKIAAeklemVGLADEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 478 QRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQ 555
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
....*....
gi 499664576 556 LLAENELYR 564
Cdd:PRK13643 231 VFQEVDFLK 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
335-547 |
5.40e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.38 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSY-IPGKEV--LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDwydqv 411
Cdd:PRK11153 2 IELKNISKVFpQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 gyL----HQTPFIFPG-------SIAENIALGKK--GAKGEEIK-RAASL-------AGAHQFIAELPQGydtkvgeggr 470
Cdd:PRK11153 77 --LrkarRQIGMIFQHfnllssrTVFDNVALPLElaGTPKAEIKaRVTELlelvglsDKADRYPAQLSGG---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 471 glsggERQRIALARVFLKDAKIVILDEPTAGLDAHTEK----LLEKAFDELfqNRTVIIIAHRLSSLYR-ADKIILIDRG 545
Cdd:PRK11153 145 -----QKQRVAIARALASNPKVLLCDEATSALDPATTRsileLLKDINREL--GLTIVLITHEMDVVKRiCDRVAVIDAG 217
|
..
gi 499664576 546 EI 547
Cdd:PRK11153 218 RL 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-558 |
6.48e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.13 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEG-----EILINGVPLWELKEK-DWYDQVGYLHQTPFI 420
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 421 FPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTA 500
Cdd:PRK14271 113 FPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 501 GLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLA 558
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
333-535 |
8.78e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.13 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ-V 411
Cdd:PRK09700 4 PYISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQT-PFIFPGSIAENIALGKKGAK---GEEI---KRAASLAGAHQFIAELPQGYDTKVgeggRGLSGGERQRIALAR 484
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIGRHLTKkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKV----ANLSISHKQMLEIAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 485 VFLKDAKIVILDEPTAGLdahTEKLLEKAFDELFQNRT----VIIIAHRLSSLYR 535
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQLRKegtaIVYISHKLAEIRR 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
331-533 |
9.40e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 9.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 331 SPPEIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ 410
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 VGYLHQTPFIFPGSIAENIALGKKGAKG--------------EEIKRAASLAGAHQFIAELPQGydtkvgeggrglsggE 476
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDVVMMGRYGHMGwlrrakkrdrqivtAALARVDMVEFRHRQIGELSGG---------------Q 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499664576 477 RQRIALARVFLKDAKIVILDEPTAGLDAHTE----KLLEKAFDElfqNRTVIIIAHRLSSL 533
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEariiSLLRELRDE---GKTMLVSTHNLGSV 205
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
356-557 |
1.20e-14 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 73.35 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 356 LTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPlwelkEKDWYDQVGYL---HQTPFIFPGSIAENIALG 432
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVpqrHEFAWDFPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 433 KKG--------------AKGEEIKRAASLAGAHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIVILDEP 498
Cdd:TIGR03771 76 RTGhigwlrrpcvadfaAVRDALRRVGLTELADRPVGELSGG---------------QRQRVLVARALATRPSVLLLDEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499664576 499 TAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRL-SSLYRADKIILIDrGEIRGMGRHEQLL 557
Cdd:TIGR03771 141 FTGLDMPTQELLTELFIELAGAgTAILMTTHDLaQAMATCDRVVLLN-GRVIADGTPQQLQ 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-572 |
1.35e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.72 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 342 HSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKL---LLGLMRPA--EGEILINGVPLW--ELKEKDWYDQVGYL 414
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIYspDVDPIEVRREVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPG-SIAENIALG---------------------KKGAKGEEIK-----RAASLAGAHQfiaelpqgydtkvge 467
Cdd:PRK14267 91 FQYPNPFPHlTIYDNVAIGvklnglvkskkeldervewalKKAALWDEVKdrlndYPSNLSGGQR--------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 468 ggrglsggerQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGE 546
Cdd:PRK14267 156 ----------QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGK 225
|
250 260
....*....|....*....|....*...
gi 499664576 547 IRGMGRHEQLL--AENELYRQLITAYRG 572
Cdd:PRK14267 226 LIEVGPTRKVFenPEHELTEKYVTGALG 253
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
335-566 |
2.35e-14 |
|
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: 72.58 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPL--WELKEKDwYDQVG 412
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItkLPMHKRA-RLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPG-SIAENIAL---GKKGAKGEEIKRAASLAG-------AHQFIAELPQGydtkvgeggrglsggERQRIA 481
Cdd:cd03218 79 YLPQEASIFRKlTVEENILAvleIRGLSKKEREEKLEELLEefhithlRKSKASSLSGG---------------ERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 482 LARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ-NRTVIIIAHRLS-SLYRADKIILIDRGEIRGMGRHEQlLAE 559
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEE-IAA 222
|
....*..
gi 499664576 560 NELYRQL 566
Cdd:cd03218 223 NELVRKV 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
350-563 |
2.87e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.12 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILI----NGVPLWELKEKDWYDQ------------VGY 413
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITNPYSkkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTP--FIFPGSIAENIALGKKgAKGEEIKRAASLAGAHQFIAELPQGYdtkVGEGGRGLSGGERQRIALARVFLKDAK 491
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 492 IVILDEPTAGLDAHTEK-LLEKAFDELFQNRTVIIIAHRLSS-LYRADKIILIDRGEIRGMGRHEQLLAENELY 563
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
335-547 |
3.02e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.32 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPG----KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVP---------LWE 401
Cdd:PRK13641 3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetgnknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 402 LKEKdwydqVGYLHQTP--FIFPGSIAENIALGKK--GAKGEEIKRAA-----------SLAGAHQFiaELPQGydtkvg 466
Cdd:PRK13641 83 LRKK-----VSLVFQFPeaQLFENTVLKDVEFGPKnfGFSEDEAKEKAlkwlkkvglseDLISKSPF--ELSGG------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 467 eggrglsggERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDElFQ--NRTVIIIAHRLSSLYR-ADKIILID 543
Cdd:PRK13641 150 ---------QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD-YQkaGHTVILVTHNMDDVAEyADDVLVLE 219
|
....
gi 499664576 544 RGEI 547
Cdd:PRK13641 220 HGKL 223
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
337-528 |
3.29e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.76 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSyIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILInGVPLwelkEKDWYDQvgylHQ 416
Cdd:PRK11147 322 MENVNYQ-IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL----EVAYFDQ----HR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TPFIFPGSIAENIALGKK----GAKGEEI-----------KRA----ASLAGAHQfiaelpqgydtkvgeggrglsgger 477
Cdd:PRK11147 392 AELDPEKTVMDNLAEGKQevmvNGRPRHVlgylqdflfhpKRAmtpvKALSGGER------------------------- 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499664576 478 QRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDElFQNrTVIIIAH 528
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS-YQG-TVLLVSH 495
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
350-548 |
3.51e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.12 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKD----WYDQVGYLHQTPFIFPGSI 425
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 A-ENIALGKKgAKGEEIKRaaSLAGAHQFIAELpqGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDA 504
Cdd:PRK10584 105 AlENVELPAL-LRGESSRQ--SRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499664576 505 HTEkllEKAFDELFQ-NR----TVIIIAHRLSSLYRADKIILIDRGEIR 548
Cdd:PRK10584 180 QTG---DKIADLLFSlNRehgtTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
335-543 |
5.25e-14 |
|
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: 69.88 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEIlingvplwelkEKDWYDQVGYL 414
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPGSIAENIAL--GKKGAKGEEikraaslagahqfiaelpqgydtkvgeggrglsggerQRIALARVFLKDAKI 492
Cdd:cd03223 70 PQRPYLPLGTLREQLIYpwDDVLSGGEQ-------------------------------------QRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499664576 493 VILDEPTAGLDAHTE-KLLEKAFDELFqnrTVIIIAHRLSSLYRADKIILID 543
Cdd:cd03223 113 VFLDEATSALDEESEdRLYQLLKELGI---TVISVGHRPSLWKFHDRVLDLD 161
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
335-562 |
6.83e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.08 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGK----EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLW-ELKEKDWYD 409
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITsTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 ---QVGYLHQTP--FIFPGSIAENIALGKK--GAKGEEIKRAA-----------SLAGAHQFiaELPQGydtkvgeggrg 471
Cdd:PRK13649 83 irkKVGLVFQFPesQLFEETVLKDVAFGPQnfGVSQEEAEALAreklalvgiseSLFEKNPF--ELSGG----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 472 lsggERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRLSSLYR-ADKIILIDRGEIRG 549
Cdd:PRK13649 150 ----QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVL 225
|
250
....*....|...
gi 499664576 550 MGRHEQLLAENEL 562
Cdd:PRK13649 226 SGKPKDIFQDVDF 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
333-535 |
7.40e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYIPGKeVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLlGLMRPAEGEILINGVPlwELKEKDWYD--- 409
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRV--EFFNQNIYErrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 -------QVGYLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIAL 482
Cdd:PRK14258 82 nlnrlrrQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 483 ARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFD--ELFQNRTVIIIAHRLSSLYR 535
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSR 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
351-535 |
1.03e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKL------LLGLMRpAEGEILINGvplwelkeKDWYDQ----------VGYL 414
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFR-VEGKVTFHG--------KNLYAPdvdpvevrrrIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFIFPGSIAENIALGKK--GAKG---EEIKRAASLAGahqfiaeLPQGYDTKVGEGGRGLSGGERQRIALARVFLKD 489
Cdd:PRK14243 97 FQKPNPFPKSIYDNIAYGARinGYKGdmdELVERSLRQAA-------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499664576 490 AKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR 535
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAAR 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
347-546 |
1.04e-13 |
|
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: 73.71 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPA--EGEILINGVPLWELKEKDWYDQ-VGYLHQTPFIFPG 423
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 -SIAENIALGKK-GAKGEEIKRAASLAGAHQFIAELpQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAG 501
Cdd:TIGR02633 93 lSVAENIFLGNEiTLPGGRMAYNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499664576 502 L-DAHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGE 546
Cdd:TIGR02633 172 LtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
346-557 |
1.76e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.16 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 346 PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPA---EGEILINGVPL--WELKEKDwydqvGYLHQTPFI 420
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIdaKEMRAIS-----AYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 421 FPGSIAE-------------NIALGKKGAKGEEIKRAASLAGAHQFIaelpqgydTKVGEGGRGLSGGERQRIALARVFL 487
Cdd:TIGR00955 111 IPTLTVRehlmfqahlrmprRVTKKEKRERVDEVLQALGLRKCANTR--------IGVPGRVKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 488 KDAKIVILDEPTAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRLSS-LYRA-DKIILIDRGEIRGMGRHEQLL 557
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSSeLFELfDKIILMAEGRVAYLGSPDQAV 255
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
347-549 |
2.09e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ-VGYL----HQTPFIF 421
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgIAYVpedrKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 422 PGSIAENIALG--KKGAKGEEIKRAASLAGAHQFIAEL---PQGYDTKVGEggrglsggerQRIALARVFLKDAKIVILD 496
Cdd:COG1129 344 DLSIRENITLAslDRLSRGGLLDRRRERALAEEYIKRLrikTPSPEQPVGNlsg----gnqQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499664576 497 EPTAGLD--AHTE--KLLEKAFDelfQNRTVIIIahrlSS-----LYRADKIILIDRGEIRG 549
Cdd:COG1129 420 EPTRGIDvgAKAEiyRLIRELAA---EGKAVIVI----SSelpelLGLSDRILVMREGRIVG 474
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
348-545 |
2.16e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLM--RPAEGEilingvplWELKEKDWYDQVgylhqtpfifpgSI 425
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGC--------VDVPDNQFGREA------------SL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 AENIALGKKGAKGEEIKRAASLAGAHQFIA---ELPQGydtkvgeggrglsggERQRIALARVFLKDAKIVILDEPTAGL 502
Cdd:COG2401 103 IDAIGRKGDFKDAVELLNAVGLSDAVLWLRrfkELSTG---------------QKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499664576 503 DAHTEKLLEKAFDELFQNR--TVIIIAHRlSSLYRA---DKIILIDRG 545
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAgiTLVVATHH-YDVIDDlqpDLLIFVGYG 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
349-566 |
2.50e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 349 EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMR-----PAEGEILINGVPLWELKEKDWYD---QVGYL-HQTPF 419
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksaGSHIELLGRTVQREGRLARDIRKsraNTGYIfQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 420 IFPGSIAENIALGKKG--------------AKGEEIKRAASLAG----AHQFIAELPQGydtkvgeggrglsggERQRIA 481
Cdd:PRK09984 98 VNRLSVLENVLIGALGstpfwrtcfswftrEQKQRALQALTRVGmvhfAHQRVSTLSGG---------------QQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 482 LARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRLS-SLYRADKIILIDRGEIRGMGRHEQLLA 558
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDN 242
|
250
....*....|
gi 499664576 559 E--NELYRQL 566
Cdd:PRK09984 243 ErfDHLYRSI 252
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
22-296 |
2.59e-13 |
|
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: 70.88 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 22 LTSFISGGAIIAQAYLIAYIINGAFLAKKG-LGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIA 100
Cdd:cd18544 6 LLLLLATALELLGPLLIKRAIDDYIVPGQGdLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 101 ALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFA 180
Cdd:cd18544 86 RLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 181 EKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVAVE 260
Cdd:cd18544 166 RKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWY 245
|
250 260 270
....*....|....*....|....*....|....*...
gi 499664576 261 VGLRLLYGKMEF--LQAFfvLLLAPELYLPLRNLGSSF 296
Cdd:cd18544 246 GGGQVLSGAVTLgvLYAF--IQYIQRFFRPIRDLAEKF 281
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
348-567 |
6.09e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.12 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING-VPlwelkekdWYDQVGYLHQTPFIFpG--- 423
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVP--------FKRRKEFARRIGVVF-Gqrs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 ------SIAENIALGKkgakgeEI---------KRAASLAGA-------HQFIAELPQGydtkvgeggrglsggerQR-- 479
Cdd:COG4586 106 qlwwdlPAIDSFRLLK------AIyripdaeykKRLDELVELldlgellDTPVRQLSLG-----------------QRmr 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 480 --IALArvFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR--TVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHE 554
Cdd:COG4586 163 ceLAAA--LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLE 240
|
250
....*....|...
gi 499664576 555 QLLAENELYRQLI 567
Cdd:COG4586 241 ELKERFGPYKTIV 253
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
337-530 |
6.18e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ-VGYLH 415
Cdd:PRK10762 7 LKGIDKAF-PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 416 QTPFIFPG-SIAENIALGKK------GAKGEEIKRAAS--LA------GAHQFIAELPQGydtkvgeggrglsggERQRI 480
Cdd:PRK10762 86 QELNLIPQlTIAENIFLGREfvnrfgRIDWKKMYAEADklLArlnlrfSSDKLVGELSIG---------------EQQMV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499664576 481 ALARVFLKDAKIVILDEPTAGL-DAHTEKLLeKAFDEL-FQNRTVIIIAHRL 530
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELkSQGRGIVYISHRL 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
348-557 |
7.74e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 7.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQTPfIFPGSIA- 426
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA-TTPGDITv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 427 -ENIALGK----------KGAKGEEIKRAASLAGahqfIAELP-QGYDTkvgeggrgLSGGERQRIALARVFLKDAKIVI 494
Cdd:PRK10253 99 qELVARGRyphqplftrwRKEDEEAVTKAMQATG----ITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 495 LDEPTAGLD-AHTEKLLEkAFDELFQNR--TVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLL 557
Cdd:PRK10253 167 LDEPTTWLDiSHQIDLLE-LLSELNREKgyTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
347-549 |
7.93e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 7.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ-VGYL----HQTPFIF 421
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIpedrLGRGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 422 PGSIAENIALG----KKGAKGEEIKRAASLAGAHQFIAEL---PQGYDTKVGEggrglsggerQRIALARVFLKDAKIVI 494
Cdd:COG3845 350 DMSVAENLILGryrrPPFSRGGFLDRKAIRAFAEELIEEFdvrTPGPDTPARSlsg----gnqQKVILARELSRDPKLLI 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499664576 495 LDEPTAGLDA------HtEKLLEKAfDelfQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRG 549
Cdd:COG3845 426 AAQPTRGLDVgaiefiH-QRLLELR-D---AGAAVLLISEDLDEILAlSDRIAVMYEGRIVG 482
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
353-531 |
9.66e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 69.38 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 353 NINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD---QVGYLHQTPFifpGS----- 424
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDPY---ASlnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 425 -----IAENIALGKKGAKGEEIKRAASL--------AGAHQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAK 491
Cdd:COG4608 113 tvgdiIAEPLRIHGLASKAERRERVAELlelvglrpEHADRYPHEFSGG---------------QRQRIGIARALALNPK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499664576 492 IVILDEPTAGLD----AHTEKLLEKAFDELfqNRTVIIIAHRLS 531
Cdd:COG4608 178 LIVCDEPVSALDvsiqAQVLNLLEDLQDEL--GLTYLFISHDLS 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
347-573 |
9.83e-13 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 68.07 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPL--WELKEKDWYDqVGYLHQTPFIFPG- 423
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIthLPMHERARLG-IGYLPQEASIFRKl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 SIAENI----ALGKKGAKGEEIKRAASLAGAHQF--IAELPQGydtkvgeggrGLSGGERQRIALARVFLKDAKIVILDE 497
Cdd:TIGR04406 92 TVEENImavlEIRKDLDRAEREERLEALLEEFQIshLRDNKAM----------SLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 498 PTAGLDAHTEKLLEKAFDELFQ-NRTVIIIAHRL-SSLYRADKIILIDRGEIRGMGRHEQLLAeNELYRQLitaYRGE 573
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVrETLDICDRAYIISDGKVLAEGTPAEIVA-NEKVRRV---YLGE 235
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
17-277 |
1.27e-12 |
|
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: 68.58 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 17 LVKIALTSFISGGAIIAQAYLIAYIINGAFLAKKG-----LGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEI 91
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGgggvdFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 92 RNVLLEKIAAlgtkvlLP------EKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLT 165
Cdd:cd18547 81 RKDLFEKLQR------LPlsyfdtHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 166 APLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMevlRVAFLSAL- 244
Cdd:cd18547 155 VPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASF---KAQFYSGLl 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 499664576 245 --ALEVLATISTAMVAVEVGLRLLYGKMEF--LQAFF 277
Cdd:cd18547 232 mpIMNFINNLGYVLVAVVGGLLVINGALTVgvIQAFL 268
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
335-530 |
1.74e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEIlingvplwelkEKDWYDQVGYL 414
Cdd:PRK09544 5 VSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 415 HQTPFI---FPGSIAENIALgKKGAKGEEIKRAASLAGAHQFIAELPQ---GYDTkvgeggrglsggerQRIALARVFLK 488
Cdd:PRK09544 73 PQKLYLdttLPLTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQklsGGET--------------QRVLLARALLN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499664576 489 DAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRL 530
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
348-528 |
2.21e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIkPLEKV-AIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD---QVGYLHQTPFIFPG 423
Cdd:PRK11831 20 RCIFDNISLTV-PRGKItAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 -SIAENIA--LGKKGAKGEEIKR--------AASLAGAHQFI-AELPQGydtkvgeggrglsggERQRIALARVFLKDAK 491
Cdd:PRK11831 99 mNVFDNVAypLREHTQLPAPLLHstvmmkleAVGLRGAAKLMpSELSGG---------------MARRAALARAIALEPD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499664576 492 IVILDEPTAGLDAHTEKLLEKAFDELfqNR----TVIIIAH 528
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISEL--NSalgvTCVVVSH 202
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
331-574 |
2.87e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 331 SPPEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWElKEKDWYDQ 410
Cdd:PRK13537 4 SVAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 VGYLHQTPFIFPG-SIAENIALGKK--GAKGEEIKraASLAGAHQFiAELPQGYDTKVGEGGRGLSggerQRIALARVFL 487
Cdd:PRK13537 82 VGVVPQFDNLDPDfTVRENLLVFGRyfGLSAAAAR--ALVPPLLEF-AKLENKADAKVGELSGGMK----RRLTLARALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 488 KDAKIVILDEPTAGLDAHTEKLL-EKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAEN----- 560
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIESEigcdv 234
|
250
....*....|....*
gi 499664576 561 -ELYRQLITAYRGEV 574
Cdd:PRK13537 235 iEIYGPDPVALRDEL 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
351-572 |
3.42e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.52 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD----QVGYLHQTPFIFPG-SI 425
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 AENIALGKK--GAKGEEIKRAASLAGAHQFIAELPQGYDTKVgeggrglSGGERQRIALARVFLKDAKIVILDEPTAGLD 503
Cdd:PRK10070 124 LDNTAFGMElaGINAEERREKALDALRQVGLENYAHSYPDEL-------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499664576 504 A--HTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLaENELYRQLITAYRG 572
Cdd:PRK10070 197 PliRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL-NNPANDYVRTFFRG 267
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
351-569 |
5.79e-12 |
|
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: 68.17 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMrPAEGEILINGVPLWELKEKDWYD-----QVGYlhQTPFifpGS- 424
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPlrrrmQVVF--QDPF---GSl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 425 ---------IAENIALGKKGAKGEEI-KRAASL--------AGAHQFIAELPQGydtkvgeggrglsggERQRIALARVF 486
Cdd:COG4172 376 sprmtvgqiIAEGLRVHGPGLSAAERrARVAEAleevgldpAARHRYPHEFSGG---------------QRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 487 LKDAKIVILDEPTAGLDAHTEK----LLEkafdELfQNR---TVIIIAHRLS---SLyrADKIILIDRGEIRGMGRHEQL 556
Cdd:COG4172 441 ILEPKLLVLDEPTSALDVSVQAqildLLR----DL-QREhglAYLFISHDLAvvrAL--AHRVMVMKDGKVVEQGPTEQV 513
|
250
....*....|....*
gi 499664576 557 LA--ENELYRQLITA 569
Cdd:COG4172 514 FDapQHPYTRALLAA 528
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
335-565 |
8.19e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.79 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING--VPLWELKEKDwydqVG 412
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEPADRD----IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPG-SIAENIALGKK--GAKGEEIKR----AASLAGAHQFI----AELPQGydtkvgeggrglsggERQRIA 481
Cdd:PRK11650 80 MVFQNYALYPHmSVRENMAYGLKirGMPKAEIEErvaeAARILELEPLLdrkpRELSGG---------------QRQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 482 LARVFLKDAKIVILDEPTAGLDAhteKLlekafdeLFQNRTVIIIAHR---LSSLY----------RADKIILIDRGEIr 548
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDA---KL-------RVQMRLEIQRLHRrlkTTSLYvthdqveamtLADRVVVMNGGVA- 213
|
250
....*....|....*..
gi 499664576 549 gmgrhEQLLAENELYRQ 565
Cdd:PRK11650 214 -----EQIGTPVEVYEK 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
350-506 |
1.04e-11 |
|
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: 64.76 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILIN----GVPLWELKEKDWY----DQVGYLHQtpF-- 419
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREILalrrRTIGYVSQ--Flr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 420 IFPGSIAENIALGKKGAKGEEIKRAASLAGA--HQFiaELPQ------------GydtkvgeggrglsggERQRIALARV 485
Cdd:COG4778 104 VIPRVSALDVVAEPLLERGVDREEARARAREllARL--NLPErlwdlppatfsgG---------------EQQRVNIARG 166
|
170 180
....*....|....*....|.
gi 499664576 486 FLKDAKIVILDEPTAGLDAHT 506
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAAN 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
348-568 |
1.36e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRpAEGEILINGVPLWELKEKDwydQVGYLHQTPFIF--PGS- 424
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQ---LLPVRHRIQVVFqdPNSs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 425 ----------IAENIALGKK----GAKGEEIKRAASLAG-----AHQFIAELPQGydtkvgeggrglsggERQRIALARV 485
Cdd:PRK15134 375 lnprlnvlqiIEEGLRVHQPtlsaAQREQQVIAVMEEVGldpetRHRYPAEFSGG---------------QRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 486 FLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTV--IIIAHRLsSLYRA--DKIILIDRGEIRGMGRHEQLLA--E 559
Cdd:PRK15134 440 LILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDL-HVVRAlcHQVIVLRQGEVVEQGDCERVFAapQ 518
|
....*....
gi 499664576 560 NELYRQLIT 568
Cdd:PRK15134 519 QEYTRQLLA 527
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
333-547 |
1.92e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.35 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYIP-GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGvplwelkeKDWYDQV 411
Cdd:TIGR01257 927 PGVCVKNLVKIFEPsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG--------KDIETNL 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 GYLHQTPFIFPgsiAENIaLGKKGAKGEEIKRAASLAGAHQFIAELPQ-------GYDTKVGEGGRGLSGGERQRIALAR 484
Cdd:TIGR01257 999 DAVRQSLGMCP---QHNI-LFHHLTVAEHILFYAQLKGRSWEEAQLEMeamledtGLHHKRNEEAQDLSGGMQRKLSVAI 1074
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 485 VFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSL-YRADKIILIDRGEI 547
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRL 1138
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
334-554 |
2.23e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 64.26 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING-----------VPLWEL 402
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpseKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 403 KEKdwydqVGYLHQTPFIFPG-SIAENI--------ALGKKGAKGEEIKRAASLA---GAHQFIAELPQGydtkvgeggr 470
Cdd:COG4161 81 RQK-----VGMVFQQYNLWPHlTVMENLieapckvlGLSKEQAREKAMKLLARLRltdKADRFPLHLSGG---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 471 glsggERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR-TVIIIAHRLSSLYR-ADKIILIDRGEIR 548
Cdd:COG4161 146 -----QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRII 220
|
....*.
gi 499664576 549 GMGRHE 554
Cdd:COG4161 221 EQGDAS 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
357-543 |
2.32e-11 |
|
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: 63.97 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 357 TIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGvplwelkekdwyDQVGYLHQTPFI-FPGSIAENIAlgkkg 435
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL------------DTVSYKPQYIKAdYEGTVRDLLS----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 436 akgEEIKRAASLAgahQFIAEL--PQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKA 513
Cdd:cd03237 84 ---SITKDFYTHP---YFKTEIakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|...
gi 499664576 514 FDELFQN--RTVIIIAHR-LSSLYRADKIILID 543
Cdd:cd03237 158 IRRFAENneKTAFVVEHDiIMIDYLADRLIVFE 190
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
348-547 |
4.72e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIkPLEKVAIV-GPSGAGKSTLVKLLLGLMRPAEGEIlingvplWELKekdwydQVGYLHQTPFIFPGSIA 426
Cdd:PTZ00243 673 KVLLRDVSVSV-PRGKLTVVlGATGSGKSTLLQSLLSQFEISEGRV-------WAER------SIAYVPQQAWIMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 427 ENIALGKkgakgEEikRAASLAGAHQF------IAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTA 500
Cdd:PTZ00243 739 GNILFFD-----EE--DAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499664576 501 GLDAHT-EKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDRGEI 547
Cdd:PTZ00243 812 ALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
351-556 |
7.94e-11 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 63.18 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLweLKEKDWYDQ-VGYLHQTPFIFPGSIA-EN 428
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRKVRRsIGIVPQYASVDEDLTGrEN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 429 IAL--GKKGAKGEEI-KRAASLAgaHQFiaELPQGYDTKVGEGGRGLSggerQRIALARVFLKDAKIVILDEPTAGLDAH 505
Cdd:TIGR01188 87 LEMmgRLYGLPKDEAeERAEELL--ELF--ELGEAADRPVGTYSGGMR----RRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499664576 506 TEKLLEKAFDELFQ-NRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQL 556
Cdd:TIGR01188 159 TRRAIWDYIRALKEeGVTILLTTHYMEEADKlCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
337-546 |
1.02e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 337 LKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGE-ILINGVplwelkekdwydQVGYLH 415
Cdd:PRK11819 9 MNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGI------------KVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 416 QTPFIFPG-SIAENIALGKKGAKG-----EEI---------------KRAASL------AGAHQF-----IA----ELPQ 459
Cdd:PRK11819 77 QEPQLDPEkTVRENVEEGVAEVKAaldrfNEIyaayaepdadfdalaAEQGELqeiidaADAWDLdsqleIAmdalRCPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 460 GyDTKVgeggRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKaFDELFQNrTVIIIAH-RlsslYRADK 538
Cdd:PRK11819 157 W-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQ-FLHDYPG-TVVAVTHdR----YFLDN 225
|
250
....*....|..
gi 499664576 539 I---IL-IDRGE 546
Cdd:PRK11819 226 VagwILeLDRGR 237
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
347-551 |
1.53e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 347 GKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLG-LMRPAE-------GEILINGVPLWELKEKDWYDQVGYLHQTP 418
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 419 F-IFPGSIAENIALG------KKGA----KGEEIKRAASLAGAhqfiaelpqgyDTKVGEGGRGLSGGERQRIALARVFL 487
Cdd:PRK13547 93 QpAFAFSAREIVLLGrypharRAGAlthrDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 488 K---------DAKIVILDEPTAGLD-AHTEKLLEKAFDELFQ-NRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMG 551
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARhADRIAMLADGAIVAHG 237
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
349-573 |
2.11e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.73 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 349 EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLwELKEKDWYDQ-VGYLHQTPF-------- 419
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSQrIRMIFQDPStslnprqr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 420 ---IFPGSIAENIALgkkgakgEEIKRAASLAGAHQFIAELPQgydtKVGEGGRGLSGGERQRIALARVFLKDAKIVILD 496
Cdd:PRK15112 106 isqILDFPLRLNTDL-------EPEQREKQIIETLRQVGLLPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 497 EPTAGLDAHTEKLLEKAFDELFQNRTV--IIIAHRLSSL-YRADKIILIDRGEIRGMGRHEQLLAE--NELYRQLITAYR 571
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMkHISDQVLVMHQGEVVERGSTADVLASplHELTKRLIAGHF 254
|
..
gi 499664576 572 GE 573
Cdd:PRK15112 255 GE 256
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
353-555 |
2.13e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 353 NINLTIkPLEKV-AIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD----QVGYLHQTPFIFPG-SIA 426
Cdd:PRK11144 16 TVNLTL-PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPpekrRIGYVFQDARLFPHyKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 427 ENIALGKKGAKGEEIKRAASLAGAHQFIAELPqgydtkvgeggRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDA-- 504
Cdd:PRK11144 95 GNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpr 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499664576 505 HTEKL--LEKAFDELfqNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQ 555
Cdd:PRK11144 164 KRELLpyLERLAREI--NIPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
342-547 |
4.09e-10 |
|
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: 60.35 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 342 HSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGlmRPA----EGEILINGVPLWELKEKDWYDQVGYL-HQ 416
Cdd:TIGR01978 7 HVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPDERARAGLFLaFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TPFIFPG-------SIAENIALGKKGAKG-------EEIKRAASLAG-----AHQFIAELPQGYDTKvgeggrglsgger 477
Cdd:TIGR01978 85 YPEEIPGvsnleflRSALNARRSARGEEPldlldfeKLLKEKLALLDmdeefLNRSVNEGFSGGEKK------------- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 478 qRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAH--RLSSLYRADKIILIDRGEI 547
Cdd:TIGR01978 152 -RNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLRePDRSFLIITHyqRLLNYIKPDYVHVLLDGRI 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
351-561 |
5.08e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.49 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPL-----WELKEKdwydqVGYLHQTP---FIfP 422
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtaenvWNLRRK-----IGMVFQNPdnqFV-G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 423 GSIAENIALG--KKGAKGEE-IKRAASLAGAHQFIaelpqGYDTKvgeGGRGLSGGERQRIALARVFLKDAKIVILDEPT 499
Cdd:PRK13642 97 ATVEDDVAFGmeNQGIPREEmIKRVDEALLAVNML-----DFKTR---EPARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 500 AGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAENE 561
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
22-293 |
6.56e-10 |
|
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: 60.52 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 22 LTSFISGGAIIAQAYLIAYIINGAFLAKKgLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIAA 101
Cdd:cd18542 6 LALLLATALNLLIPLLIRRIIDSVIGGGL-RELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 102 LGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAE 181
Cdd:cd18542 85 LSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 182 KLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVAVEV 261
Cdd:cd18542 165 PAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVG 244
|
250 260 270
....*....|....*....|....*....|....
gi 499664576 262 GLRLLYGKMEF--LQAFFVLLLApeLYLPLRNLG 293
Cdd:cd18542 245 GYLVINGEITLgeLVAFISYLWM--LIWPVRQLG 276
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
330-566 |
8.06e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.55 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 330 DSPPEIILKQVSHSYIPGKEvLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING-----VPLWELKE 404
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 405 K--------DWydqvGYLHQTP-------FIFPGSIAENI-ALGKK--GakgeEIKRAAS-------LAGAHqfIAELPQ 459
Cdd:PRK11701 81 AerrrllrtEW----GFVHQHPrdglrmqVSAGGNIGERLmAVGARhyG----DIRATAGdwlerveIDAAR--IDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 460 GYDTKVgeggrglsggeRQRIALARVFLKDAKIVILDEPTAGLD----AHTEKLLEKAFDELfqNRTVIIIAHRLsSLYR 535
Cdd:PRK11701 151 TFSGGM-----------QQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVREL--GLAVVIVTHDL-AVAR 216
|
250 260 270
....*....|....*....|....*....|....
gi 499664576 536 --ADKIILIDRGEIRGMGRHEQLLAE-NELYRQL 566
Cdd:PRK11701 217 llAHRLLVMKQGRVVESGLTDQVLDDpQHPYTQL 250
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
334-566 |
1.08e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPlweLKEKDWYDqvgY 413
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---VTAEQPED---Y 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LHQTPFIF-----------PGSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGydtkvgeggrglsggERQRIAL 482
Cdd:PRK10522 396 RKLFSAVFtdfhlfdqllgPEGKPANPALVEKWLERLKMAHKLELEDGRISNLKLSKG---------------QKKRLAL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 483 ARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYRADKIILIDRGEIRGMGRHEQLLAEN 560
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASR 540
|
....*.
gi 499664576 561 ELYRQL 566
Cdd:PRK10522 541 DAVART 546
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
350-503 |
2.27e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 350 VLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPlweLKEKDWYDQVGYLHQTPFIFPG-SIAEN 428
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT---ATRGDRSRFMAYLGHLPGLKADlSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 429 IALgKKGAKGEEIKRAASLAGAhqfIAELPQGYDTKVgeggRGLSGGERQRIALARVFLKDAKIVILDEPTAGLD 503
Cdd:PRK13543 103 LHF-LCGLHGRRAKQMPGSALA---IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
335-551 |
2.33e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING-----------VPLWELK 403
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 404 EKdwydqVGYLHQTPFIFPG-SIAENI--------ALGKKGAKGEEIKRAASL---AGAHQFIAELPQGydtkvgeggrg 471
Cdd:PRK11124 82 RN-----VGMVFQQYNLWPHlTVQQNLieapcrvlGLSKDQALARAEKLLERLrlkPYADRFPLHLSGG----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 472 lsggERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR-TVIIIAHRLSSLYR-ADKIILIDRGEIRG 549
Cdd:PRK11124 146 ----QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
..
gi 499664576 550 MG 551
Cdd:PRK11124 222 QG 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
335-392 |
3.37e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 3.37e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEI 392
Cdd:PRK15064 320 LEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
25-268 |
3.62e-09 |
|
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: 58.19 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 25 FISGGAIIAQAYLIAYIINGafLAKKGL--GELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIAAL 102
Cdd:cd18541 9 ILVDLLQLLIPRIIGRAIDA--LTAGTLtaSQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 103 GTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAEK 182
Cdd:cd18541 87 SPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 183 LAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRV-AFLSALaLEVLATISTAMVavev 261
Cdd:cd18541 167 RFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVdALFFPL-IGLLIGLSFLIV---- 241
|
....*..
gi 499664576 262 glrLLYG 268
Cdd:cd18541 242 ---LWYG 245
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
349-558 |
4.11e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.67 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 349 EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLHQ-------TPFIF 421
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQlrllrtrLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 422 PG-------SIAENI--------ALGKKGAKGEEIKRAASLAgahqfIAELPQGydtkvgEGGRGLSGGERQRIALARVF 486
Cdd:PRK10619 99 QHfnlwshmTVLENVmeapiqvlGLSKQEARERAVKYLAKVG-----IDERAQG------KYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 487 LKDAKIVILDEPTAGLD----AHTEKLLEKAFDElfqNRTVIIIAHRLS-SLYRADKIILIDRGEIRGMGRHEQLLA 558
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDpelvGEVLRIMQQLAEE---GKTMVVVTHEMGfARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
342-547 |
4.89e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 342 HSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGlmRPA----EGEILINGVPLWELkEKDWYDQVGYL--H 415
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDL-EPEERAHLGIFlaF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 416 QTPFIFPG-------SIAENIALGKKGAKG-------EEIKRAASLAGA-----HQFIAELPQGYDTKvgeggrglsgge 476
Cdd:CHL00131 91 QYPIEIPGvsnadflRLAYNSKRKFQGLPEldpleflEIINEKLKLVGMdpsflSRNVNEGFSGGEKK------------ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 477 rqRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVIIIAH--RLSSLYRADKIILIDRGEI 547
Cdd:CHL00131 159 --RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKI 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
335-573 |
1.13e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.06 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING-----VPLWELKEKDwyd 409
Cdd:PRK10895 4 LTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHARARRG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 qVGYLHQTPFIFPG-----------SIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYDTKvgeggrglsggerq 478
Cdd:PRK10895 80 -IGYLPQEASIFRRlsvydnlmavlQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERR-------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 479 RIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRT-VIIIAHRL-SSLYRADKIILIDRGEIRGMGRHEQL 556
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEI 224
|
250
....*....|....*..
gi 499664576 557 LAENELYRqlitAYRGE 573
Cdd:PRK10895 225 LQDEHVKR----VYLGE 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
332-503 |
1.62e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.42 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 332 PPEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGV-----PLWELKEKD 406
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPMHKRARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 407 wydqVGYLHQTPFIFPG-SIAENIA-------LGKKG--AKGEEI-----------KRAASLAGahqfiaelpqgydtkv 465
Cdd:COG1137 80 ----IGYLPQEASIFRKlTVEDNILavlelrkLSKKEreERLEELleefgithlrkSKAYSLSG---------------- 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 499664576 466 geggrglsgGERQRIALARVFLKDAKIVILDEPTAGLD 503
Cdd:COG1137 140 ---------GERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
24-268 |
2.98e-08 |
|
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: 55.13 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 24 SFISGGAIIAQAYLIAYIINGAFLAKKGLGELWPFFpALFLIVTL-----RFSLGYFGEKVGANLaskvtgeiRNVLLEK 98
Cdd:cd18551 8 SLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLV-ALFLLQAVlsalsSYLLGRTGERVVLDL--------RRRLWRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 99 IAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGS 178
Cdd:cd18551 79 LLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 179 FAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFG-------RSKEQVNELKKSGlmfrdatmevLRVAFLSALaLEVLAT 251
Cdd:cd18551 159 RIRKASKRAQDALGELSAALERALSAIRTVKASNaeeretkRGGEAAERLYRAG----------LKAAKIEAL-IGPLMG 227
|
250
....*....|....*....
gi 499664576 252 IST--AMVAVevglrLLYG 268
Cdd:cd18551 228 LAVqlALLVV-----LGVG 241
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
97-300 |
3.51e-08 |
|
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: 55.18 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 97 EKIAALGTKVLLPEKTGELLTLILEGVESLEVYYAR-YLPQLISAGIIPLMILVVV---LALDLISGIIMLLTAPLIPVF 172
Cdd:cd18585 76 RKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRvLSPPVVALLVILATILFLAffsPALALILLAGLLLAGVVIPLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 173 MMLIG-SFAEKLAQKQwsslSRLSGKFFELLQGIADLKAFGRSKEQVNELKKS-----GLMFRDATMEVLRVAfLSALAL 246
Cdd:cd18585 156 FYRLGkKIGQQLVQLR----AELRTELVDGLQGMAELLIFGALERQRQQLEQLsdaliKEQRRLARLSGLSQA-LMILLS 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 247 EVLATISTAMVAVEVGLRLLYGKMEFLQAFFVL----LLAPelyLPL--RNLGSSFHAGR 300
Cdd:cd18585 231 GLTVWLVLWLGAPLVQNGALDGALLAMLVFAVLasfeAVAP---LPLafQYLGETRAAAR 287
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
339-547 |
4.08e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 339 QVSHSYIPgkeVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILIngvplwelkEKDWydQVGYLHQTP 418
Cdd:PRK11147 10 WLSFSDAP---LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY---------EQDL--IVARLQQDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 419 fifP----GSIAENIALGKKgAKGEEIKRAASL-------------------------AGAHQF---------------- 453
Cdd:PRK11147 76 ---PrnveGTVYDFVAEGIE-EQAEYLKRYHDIshlvetdpseknlnelaklqeqldhHNLWQLenrinevlaqlgldpd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 454 --IAELPQGYDTKVgeggrglsggerqriALARVFLKDAKIVILDEPTAGLDAHTEKLLEKaFDELFQNrTVIIIAHRLS 531
Cdd:PRK11147 152 aaLSSLSGGWLRKA---------------ALGRALVSNPDVLLLDEPTNHLDIETIEWLEG-FLKTFQG-SIIFISHDRS 214
|
250
....*....|....*..
gi 499664576 532 SLYR-ADKIILIDRGEI 547
Cdd:PRK11147 215 FIRNmATRIVDLDRGKL 231
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
16-294 |
4.15e-08 |
|
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: 54.78 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 16 YLVKIALTSFISGGAIIAQAYLIAYIINgAFLAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVL 95
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAID-EYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 96 LEKIAALGTKVLLPEKTGELLTLILEGVESLEvyyarylpQLISAGIIPL--------MILVVVLALDLISGIIMLLTAP 167
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLS--------DLLSNGLINLipdlltlvGIVIIMFSLNVRLALVTLAVLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 168 LIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALE 247
Cdd:cd18545 152 LLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499664576 248 VLATISTAMVAVEVGLRLLYGKMEF--LQAFFvlllapeLYL-----PLRNLGS 294
Cdd:cd18545 232 LISALGTALVYWYGGKLVLGGAITVgvLVAFI-------GYVgrfwqPIRNLSN 278
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
354-531 |
4.18e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.10 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 354 INLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD---QVGYLHQTPF--IFPG-SIAE 427
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsDIQMIFQDPLasLNPRmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 428 NIA---------LGKKGAKgEEIKRAASLAG-AHQFIAELPQGYDtkvgeggrglsGGERQRIALARVFLKDAKIVILDE 497
Cdd:PRK15079 120 IIAeplrtyhpkLSRQEVK-DRVKAMMLKVGlLPNLINRYPHEFS-----------GGQCQRIGIARALILEPKLIICDE 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 499664576 498 PTAGLD----AHTEKLLEKAFDELfqNRTVIIIAHRLS 531
Cdd:PRK15079 188 PVSALDvsiqAQVVNLLQQLQREM--GLSLIFIAHDLA 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
348-545 |
4.70e-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: 53.40 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLG--LMRPAEGEILINGVPLwelkEKDWYDQVGYLHQTPFIFPGSI 425
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPL----DKNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 426 AEnialgkkgakgEEIKRAASLAGAHQfiaelpqgYDTKvgeggrglsggerqRIALARVFLKDAKIVILDEPTAGLDAH 505
Cdd:cd03232 96 VR-----------EALRFSALLRGLSV--------EQRK--------------RLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499664576 506 TE----KLLEKAFDElfqNRTVIIIAHRLSS--LYRADKIILIDRG 545
Cdd:cd03232 143 AAynivRFLKKLADS---GQAILCTIHQPSAsiFEKFDRLLLLKRG 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
336-539 |
6.03e-08 |
|
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: 53.91 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 336 ILKQVSHSYIPGKEVLKNINlTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEG---------EILIN--GVPLWELKE 404
Cdd:cd03236 2 LEDEPVHRYGPNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILDEfrGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 405 KDWYDQVG------YLHQTPFIFPGSIAENIALGKKGAKGEEIKRAASLAGA-HQFIAELPQGydtkvgeggrglsggER 477
Cdd:cd03236 81 KLLEGDVKvivkpqYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHVlDRNIDQLSGG---------------EL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 478 QRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ-NRTVIIIAHRLSSL-YRADKI 539
Cdd:cd03236 146 QRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLAVLdYLSDYI 209
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
360-546 |
8.31e-08 |
|
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: 51.61 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 360 PLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILIngvplwelkekdwydqvgylhqtpfifpgsiaenialgkkgakge 439
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 440 eikraasLAGAHQFIAELPQGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFD---- 515
Cdd:smart00382 36 -------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499664576 516 ---ELFQNRTVIIIAHRLSSL------YRADKIILIDRGE 546
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLgpallrRRFDRRIVLLLIL 148
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
345-547 |
1.02e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 52.65 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 345 IPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPA---EGEILINGVPLWELKEKdwydqvgylhqtpfiF 421
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK---------------Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 422 PGSIAENIALGKKGAK---GEEIKRAASLAGaHQFIAELPQGyDTKvgeggrglsggerqRIALARVFLKDAKIVILDEP 498
Cdd:cd03233 82 PGEIIYVSEEDVHFPTltvRETLDFALRCKG-NEFVRGISGG-ERK--------------RVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499664576 499 TAGLDAHTE----KLLEKAFDELfqnRTVIIIahrlsSLYRA--------DKIILIDRGEI 547
Cdd:cd03233 146 TRGLDSSTAleilKCIRTMADVL---KTTTFV-----SLYQAsdeiydlfDKVLVLYEGRQ 198
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
331-518 |
1.40e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 331 SPPEIILKQVSHSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING---VPLWELKEKDW 407
Cdd:PLN03073 505 GPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAkvrMAVFSQHHVDG 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 408 YDqvgyLHQTPFI-----FPGSIAENIA--LGKKGAKGE-EIKRAASLAGAHQfiaelpqgydtkvgeggrglsggerQR 479
Cdd:PLN03073 585 LD----LSSNPLLymmrcFPGVPEQKLRahLGSFGVTGNlALQPMYTLSGGQK-------------------------SR 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 480 IALARVFLKDAKIVILDEPTAGLD---------------------AHTEKLLEKAFDELF 518
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDldavealiqglvlfqggvlmvSHDEHLISGSVDELW 695
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
353-573 |
1.95e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.30 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 353 NINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWEL--------------------KEKDWYDQV- 411
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghqiarmgvvrtfqhvrlfREMTVIENLl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 --GYLHQTPFIFPGSI-------AENIALGKKGAKGEEI-------KRAASLAGAHQfiaelpqgydtkvgeggrglsgg 475
Cdd:PRK11300 103 vaQHQQLKTGLFSGLLktpafrrAESEALDRAATWLERVgllehanRQAGNLAYGQQ----------------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 476 erQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQ--NRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGR 552
Cdd:PRK11300 160 --RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGT 237
|
250 260
....*....|....*....|.
gi 499664576 553 HEQlLAENElyrQLITAYRGE 573
Cdd:PRK11300 238 PEE-IRNNP---DVIKAYLGE 254
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
61-293 |
2.29e-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: 52.90 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 61 ALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISA 140
Cdd:cd18564 59 ALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 141 GIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNE 220
Cdd:cd18564 139 LLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERR 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 221 LKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVAVEVGLRLLYGKMEF--LQAFFVLLLApeLYLPLRNLG 293
Cdd:cd18564 219 FARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPgdLLVFLAYLKN--LYKPVRDLA 291
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
357-540 |
2.38e-07 |
|
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: 53.63 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 357 TIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILingvplWELK--------EKDWYDQV-GYLHQT-PFIFPGSIA 426
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD------EDLKisykpqyiSPDYDGTVeEFLRSAnTDDFGSSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 427 EN-IAlgkKGAKGEEI--KRAASLAGAhqfiaELpqgydtkvgeggrglsggerQRIALARVFLKDAKIVILDEPTAGLD 503
Cdd:COG1245 436 KTeII---KPLGLEKLldKNVKDLSGG-----EL--------------------QRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499664576 504 AHTEKLLEKAFDELFQNR--TVIIIAHRLSSL-YRADKII 540
Cdd:COG1245 488 VEQRLAVAKAIRRFAENRgkTAMVVDHDIYLIdYISDRLM 527
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
21-304 |
2.75e-07 |
|
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: 52.48 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 21 ALTSFISGGAIIAQAYLIAYIINGAfLAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIA 100
Cdd:cd18543 5 LLAALLATLAGLAIPLLTRRAIDGP-IAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 101 ALGTKVLLPEKTGELLTLILEGVESLEVYYArYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIpvfmMLIGSFA 180
Cdd:cd18543 84 RLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPL----VLVARRF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 181 EK-------LAQKQWSSLSrlsGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATIS 253
Cdd:cd18543 159 RRryfpasrRAQDQAGDLA---TVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499664576 254 TAMVAVEVGLRLLYGKM---EFLqAFFVLLLApeLYLPLRNLGSSFHAGRTAIA 304
Cdd:cd18543 236 LAAVLALGGWLVANGSLtlgTLV-AFSAYLTM--LVWPVRMLGWLLAMAQRARA 286
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
357-546 |
3.42e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 357 TIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILingvplWELK--------EKDWYDQVG-YLHQTPFIFPGS--- 424
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELKisykpqyiKPDYDGTVEdLLRSITDDLGSSyyk 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 425 --IAENIALgkkgakgEEI--KRAASLAGAhqfiaELpqgydtkvgeggrglsggerQRIALARVFLKDAKIVILDEPTA 500
Cdd:PRK13409 435 seIIKPLQL-------ERLldKNVKDLSGG-----EL--------------------QRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499664576 501 GLDAHTEKLLEKAFDELFQNR--TVIIIAHRLSSL-YRADKIILIDrGE 546
Cdd:PRK13409 483 HLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMIdYISDRLMVFE-GE 530
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
61-296 |
3.50e-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: 52.04 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 61 ALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIAALGTKVLLPEKTGELLTLILEGVESLEVYYARYLPQLISA 140
Cdd:cd18554 51 MFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 141 GIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNE 220
Cdd:cd18554 131 MITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQ 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 221 LKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVAVEVGLRLLYGKMEF--LQAFFVLLlaPELYLPLRNLGSSF 296
Cdd:cd18554 211 FDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVgtLVAFVGYM--ERMYSPLRRLVNSF 286
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
333-539 |
4.03e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYIPGKEVLKNInLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEIliNGVPLWE--LKE------ 404
Cdd:PRK13409 72 PEELEEEPVHRYGVNGFKLYGL-PIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEPSWDevLKRfrgtel 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 405 ----KDWYD-------QVGYLHQTPFIFPGSIAENIA-LGKKGAKGEEIKRAASLAGAHQFIAELPQGydtkvgeggrgl 472
Cdd:PRK13409 149 qnyfKKLYNgeikvvhKPQYVDLIPKVFKGKVRELLKkVDERGKLDEVVERLGLENILDRDISELSGG------------ 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 473 sggERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIAHRLSSL-YRADKI 539
Cdd:PRK13409 217 ---ELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLdYLADNV 281
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
368-537 |
4.74e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 368 GPSGAGKSTLVKLLLGLMRPAEGEILINGVPLwelkEKD---WYDQVGYLHQTPFIFPG-SIAENIALGKKGAKGE-EIK 442
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDlctYQKQLCFVGHRSGINPYlTLRENCLYDIHFSPGAvGIT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 443 RAASLAGAHQFIaELPQGydtkvgeggrGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHT-EKLLEKAFDELFQNR 521
Cdd:PRK13540 110 ELCRLFSLEHLI-DYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSlLTIITKIQEHRAKGG 178
|
170
....*....|....*.
gi 499664576 522 TVIIIAHRLSSLYRAD 537
Cdd:PRK13540 179 AVLLTSHQDLPLNKAD 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
342-549 |
7.85e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 342 HSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPA-EGEILINGVPLWELKEKDWYDQ-VGYL---HQ 416
Cdd:PRK13549 269 DPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNPQQAIAQgIAMVpedRK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TPFIFPG-SIAENIALG--KKGAKGEEIKRAASLAGAHQFIAELpqgydtKVGEGGRGLSGGER-----QRIALARVFLK 488
Cdd:PRK13549 349 RDGIVPVmGVGKNITLAalDRFTGGSRIDDAAELKTILESIQRL------KVKTASPELAIARLsggnqQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 489 DAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIahrLSS-----LYRADKIILIDRGEIRG 549
Cdd:PRK13549 423 NPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIV---ISSelpevLGLSDRVLVMHEGKLKG 485
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
348-569 |
9.44e-07 |
|
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: 51.61 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKS----TLVKLLLGLMRPAEGEILINGVPLWELKEKDWY----DQVGylhqtpF 419
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIA------M 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 420 IF--PGS-----------IAENIALgKKGAKGEE-------------IKRAASLAGA--HQfiaeLPQGydtkvgeggrg 471
Cdd:COG4172 97 IFqePMTslnplhtigkqIAEVLRL-HRGLSGAAararalellervgIPDPERRLDAypHQ----LSGG----------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 472 lsggERQRIALARVFLKDAKIVILDEPTAGLDAHTE----KLLekafDELfQNRT---VIIIAHRLSSLYR-ADKIILID 543
Cdd:COG4172 161 ----QRQRVMIAMALANEPDLLIADEPTTALDVTVQaqilDLL----KDL-QRELgmaLLLITHDLGVVRRfADRVAVMR 231
|
250 260
....*....|....*....|....*...
gi 499664576 544 RGEIRGMGRHEQLLAE-NELY-RQLITA 569
Cdd:COG4172 232 QGEIVEQGPTAELFAApQHPYtRKLLAA 259
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
351-503 |
1.10e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.73 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWE---LKEKDWYDQVGYLHQTPF--IFP--- 422
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPYgsLNPrkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 423 -GSIAE-----NIALGKKgakgeeiKRAASlagAHQFIAEL---PQGYDtkvgEGGRGLSGGERQRIALARVFLKDAKIV 493
Cdd:PRK11308 111 vGQILEeplliNTSLSAA-------ERREK---ALAMMAKVglrPEHYD----RYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170
....*....|
gi 499664576 494 ILDEPTAGLD 503
Cdd:PRK11308 177 VADEPVSALD 186
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
333-572 |
1.28e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYipGK-EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLwelkeKDWydqv 411
Cdd:PRK11614 4 VMLSFDKVSAHY--GKiQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-----TDW---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 412 gylhQTPFIFPGSIA---------------ENIALG----KKGAKGEEIKRAASLagahqfiaeLPQGYDTKVgEGGRGL 472
Cdd:PRK11614 73 ----QTAKIMREAVAivpegrrvfsrmtveENLAMGgffaERDQFQERIKWVYEL---------FPRLHERRI-QRAGTM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 473 SGGERQRIALARVFLKDAKIVILDEPTAGLdahTEKLLEKAFDELFQNR----TVIIIAHRLS-SLYRADKIILIDRGEI 547
Cdd:PRK11614 139 SGGEQQMLAIGRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEQLReqgmTIFLVEQNANqALKLADRGYVLENGHV 215
|
250 260
....*....|....*....|....*
gi 499664576 548 RGMGRHEQLLAeNELYRqliTAYRG 572
Cdd:PRK11614 216 VLEDTGDALLA-NEAVR---SAYLG 236
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
479-544 |
1.59e-06 |
|
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: 49.14 E-value: 1.59e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 479 RIALARVFLKDAKIVILDEPTAGLDA-HTEKLLEKAFDEL--FQNRTVIIIAHRLSSLYRADKIILIDR 544
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERksQKNFQLIVITHDEELVDAADHIYRVEK 197
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
342-406 |
1.93e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 1.93e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 342 HSYIPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGL--MRPAEGEILINGVPLWELKEKD 406
Cdd:PRK09580 8 HVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPED 74
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
348-547 |
2.85e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLL----GLMRPAEGEILINGVPLWELKeKDWYDQVGYLHQTPFIFPG 423
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIK-KHYRGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 -SIAEN----IALGKKGAKGEEIKR---AASLAGAHQFIAELPQGYDTKVGEGGRGLSGG-ERQRIALARVFLKDAKIVI 494
Cdd:TIGR00956 153 lTVGETldfaARCKTPQNRPDGVSReeyAKHIADVYMATYGLSHTRNTKVGNDFVRGVSGgERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499664576 495 LDEPTAGLDAHTEklLEkaFDELFQNRTVIIIAHRLSSLYRA--------DKIILIDRGEI 547
Cdd:TIGR00956 233 WDNATRGLDSATA--LE--FIRALKTSANILDTTPLVAIYQCsqdayelfDKVIVLYEGYQ 289
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
348-558 |
3.43e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.88 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPA--EGEILINGVPLwelkEKDWYDQVGYLHQTPFIFPG-S 424
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP----TKQILKRTGFVTQDDILYPHlT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 425 IAENIALGKKGAKGEEIKRAASLAGAHQFIAEL--PQGYDTKVGEGGRGLSGG-ERQRIALARVFLKDAKIVILDEPTAG 501
Cdd:PLN03211 157 VRETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNSFIRGISGgERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 502 LDAHTEKLLEKAFDELFQN-RTVIIIAHRLSS-LYRA-DKIILIDRGEIRGMGRHEQLLA 558
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKgKTIVTSMHQPSSrVYQMfDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
333-531 |
3.46e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 333 PEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLG-----------LM--RPAEGEIlingvpL 399
Cdd:PRK10938 259 PRIVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFgrRRGSGET------I 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 400 WELKEKdwydqVGY----LHQTpFIFPGSIAENIALGKKGAKGeeIKRAASLAG---AHQFIAELpqGYDTKVGEGGRGL 472
Cdd:PRK10938 332 WDIKKH-----IGYvsssLHLD-YRVSTSVRNVILSGFFDSIG--IYQAVSDRQqklAQQWLDIL--GIDKRTADAPFHS 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499664576 473 SGGERQRIAL-ARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELF-QNRTVII------------IAHRLS 531
Cdd:PRK10938 402 LSWGQQRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLfvshhaedapacITHRLE 474
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
352-547 |
3.72e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.78 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 352 KNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVplwELKEKDWYDQV----GYL----HQTPFIFPG 423
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSPLDAVkkgmAYItesrRDNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 424 SIAENIAL-------GKKGAKG-----EEIKRAAS--------LAGAHQFIAELPQGYDTKVGeggrglsggerqriaLA 483
Cdd:PRK09700 357 SIAQNMAIsrslkdgGYKGAMGlfhevDEQRTAENqrellalkCHSVNQNITELSGGNQQKVL---------------IS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 484 RVFLKDAKIVILDEPTAGLD--AHTE--KLLEKAFDElfqNRTVIIIAHRLSSLYRA-DKIILIDRGEI 547
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDvgAKAEiyKVMRQLADD---GKVILMVSSELPEIITVcDRIAVFCEGRL 487
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
354-555 |
4.00e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 354 INLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYL----HQTPFIFPG-SIAEN 428
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLcpedRKAEGIIPVhSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 429 IALGKKGAK---GEEIKRAASLAGAHQFIAEL----PQGyDTKVGEGGRGLSggerQRIALARVFLKDAKIVILDEPTAG 501
Cdd:PRK11288 352 INISARRHHlraGCLINNRWEAENADRFIRSLniktPSR-EQLIMNLSGGNQ----QKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 502 LD--AHTEkLLEKAFDELFQNRTVIIIAHRLSS-LYRADKIILIDRGEIRGMGRHEQ 555
Cdd:PRK11288 427 IDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEvLGVADRIVVMREGRIAGELAREQ 482
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
335-528 |
6.69e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.78 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 335 IILKQVSHSYipGKEVL-KNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILI-NGVplwelkekdwydQVG 412
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 413 YLHQTPFIFPG--SIAENIA-------LGKKgakgeEIKRAASLA-----GAHQ--FIAELPQGydtkvgeggrglsggE 476
Cdd:TIGR03719 389 YVDQSRDALDPnkTVWEEISggldiikLGKR-----EIPSRAYVGrfnfkGSDQqkKVGQLSGG---------------E 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499664576 477 RQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDElFQNrTVIIIAH 528
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLN-FAG-CAVVISH 498
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
358-543 |
7.05e-06 |
|
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: 46.80 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 358 IKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVplwelkekdwydqvgylhqTPFIFPGSIaenialgkkgak 437
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI-------------------TPVYKPQYI------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 438 geeikraaSLAGAhqfiaELpqgydtkvgeggrglsggerQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDEL 517
Cdd:cd03222 71 --------DLSGG-----EL--------------------QRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 499664576 518 FQN--RTVIIIAHRLSSL-YRADKIILID 543
Cdd:cd03222 118 SEEgkKTALVVEHDLAVLdYLSDRIHVFE 146
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
330-545 |
7.54e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 330 DSPPEIILKQVSHSYIpgkEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPA--EGEILINGVPlwelKEKDW 407
Cdd:PLN03140 878 DMPAEMKEQGVTEDRL---QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP----KKQET 950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 408 YDQV-GYLHQTPFIFPG-SIAENIA------LGKKGAKGE------EIKRAASLAGAHQFIAELP--QGYDTKvgeggrg 471
Cdd:PLN03140 951 FARIsGYCEQNDIHSPQvTVRESLIysaflrLPKEVSKEEkmmfvdEVMELVELDNLKDAIVGLPgvTGLSTE------- 1023
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 472 lsggERQRIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAF-DELFQNRTVIIIAHRLS-SLYRA-DKIILIDRG 545
Cdd:PLN03140 1024 ----QRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSiDIFEAfDELLLMKRG 1096
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
25-239 |
8.07e-06 |
|
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: 47.86 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 25 FISGGAIIAQAYLIAYIINGAFLAKkGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIAALGT 104
Cdd:cd18576 6 LLSSAIGLVFPLLAGQLIDAALGGG-DTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 105 KVLLPEKTGELLTLILEGVESLEVYYARYLPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAEKLA 184
Cdd:cd18576 85 SFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499664576 185 QKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNElkksglmFRDATMEVLRVA 239
Cdd:cd18576 165 KKVQDELAEANTIVEETLQGIRVVKAFTREDYEIER-------YRKALERVVKLA 212
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
22-268 |
8.07e-06 |
|
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: 47.94 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 22 LTSFISGGAIIAQAYLIAYIINgAFLAKKGLGELWPFFPALFLIVTLR--------FSLGYFGEKVGANLASKVtgeIRN 93
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLID-TIIKGGDLDVLNELALILLAIYLLQsvftfvryYLFNIAGERIVARLRRDL---FSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 94 VLLEKIAALGTKvllpeKTGELLTLILEGVESLevyyARYLPQLISAGIIPLMILVVVLALDLIS----GIIMLLTAPLI 169
Cdd:cd18557 79 LLRQEIAFFDKH-----KTGELTSRLSSDTSVL----QSAVTDNLSQLLRNILQVIGGLIILFILswklTLVLLLVIPLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 170 PVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNelkksglMFRDATMEVLRVAFLSALALEVL 249
Cdd:cd18557 150 LIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIR-------RYSEALDRSYRLARKKALANALF 222
|
250
....*....|....*....
gi 499664576 250 ATISTAMVAVEVGLRLLYG 268
Cdd:cd18557 223 QGITSLLIYLSLLLVLWYG 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
333-399 |
8.57e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 8.57e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 333 PEIILKQVSHSYiPGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEI-LINGVPL 399
Cdd:PRK10636 311 PLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKL 377
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
134-296 |
9.09e-06 |
|
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: 47.87 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 134 LPQLISAGIIPLMILVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFGR 213
Cdd:cd18546 117 LVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 214 SKEQVNELKKSGLMFRDATMEVLRVAFLSALALEVLATISTAMVAVEVGLRLLYGKMEF--LQAFfvLLLAPELYLPLRN 291
Cdd:cd18546 197 ERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVgvLVAF--LLYLRRFFAPIQQ 274
|
....*
gi 499664576 292 LGSSF 296
Cdd:cd18546 275 LSQVF 279
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
479-560 |
1.59e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 479 RIALARVFLKDAKIVILDEPTAGLDAHTEKLLEkafDELFQ-NRTVIIIAH-R--LSSL--YRADkiilIDRGEIR---- 548
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLE---DVLNErNSTMIIISHdRhfLNSVctHMAD----LDYGELRvypg 235
|
90 100
....*....|....*....|.
gi 499664576 549 ---------GMGRhEQLLAEN 560
Cdd:PRK15064 236 nydeymtaaTQAR-ERLLADN 255
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
364-539 |
4.43e-05 |
|
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: 46.32 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 364 VAIVGPSGAGKSTLVKLLLGLMRPAEGEIliNGVPLW----------ELKE--KDWYDQ-------VGYLHQTPFIFPGS 424
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDY--DEEPSWdevlkrfrgtELQDyfKKLANGeikvahkPQYVDLIPKVFKGT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 425 IAEniALGKKGAKG--EEIKRAASLAGA-HQFIAELPQGydtkvgeggrglsggERQRIALARVFLKDAKIVILDEPTAG 501
Cdd:COG1245 180 VRE--LLEKVDERGklDELAEKLGLENIlDRDISELSGG---------------ELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499664576 502 LDAHtEKL-LEKAFDELFQ-NRTVIIIAHRLSSL-YRADKI 539
Cdd:COG1245 243 LDIY-QRLnVARLIRELAEeGKYVLVVEHDLAILdYLADYV 282
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
351-540 |
5.09e-05 |
|
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: 44.24 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIkPLEK-VAIVGPSGAGKSTLVKLLLglmrPAEGEILINGVPlwelkEKDWYDQVGYLHQTPFIFPGSIaENI 429
Cdd:cd03238 11 LQNLDVSI-PLNVlVVVTGVSGSGKSTLVNEGL----YASGKARLISFL-----PKFSRNKLIFIDQLQFLIDVGL-GYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 430 ALGKKgakgeeikrAASLAGAHQfiaelpqgydtkvgeggrglsggerQRIALARVFLKDAK--IVILDEPTAGLDAHT- 506
Cdd:cd03238 80 TLGQK---------LSTLSGGEL-------------------------QRVKLASELFSEPPgtLFILDEPSTGLHQQDi 125
|
170 180 190
....*....|....*....|....*....|....
gi 499664576 507 EKLLEKAFDELFQNRTVIIIAHRLSSLYRADKII 540
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
478-540 |
5.24e-05 |
|
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: 45.30 E-value: 5.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 478 QRIALARVFLKDAK---IVILDEPTAGLDAHTEKLLEKAFDELFQN-RTVIIIAHRLSSLYRADKII 540
Cdd:cd03271 176 QRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNLDVIKCADWII 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
349-549 |
6.35e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 349 EVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQ------------------ 410
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARglvylpedrqssglylda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 411 ------VGYLHQTPFIFPGSIAENI-------ALGKKGAKGEEIKRaaSLAGAHQfiaelpqgydtkvgeggrglsgger 477
Cdd:PRK15439 357 plawnvCALTHNRRGFWIKPARENAvleryrrALNIKFNHAEQAAR--TLSGGNQ------------------------- 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 478 QRIALARVFLKDAKIVILDEPTAGLD----AHTEKLLEKAFDelfQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRG 549
Cdd:PRK15439 410 QKVLIAKCLEASPQLLIVDEPTRGVDvsarNDIYQLIRSIAA---QNVAVLFISSDLEEIEQmADRVLVMHQGEISG 483
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
478-540 |
9.72e-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: 45.39 E-value: 9.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 478 QRIALARVFLKDAK---IVILDEPTAGLdaHTE---KLLEKAFDELFQNRTVIIIAHRLSSLYRADKII 540
Cdd:TIGR00630 836 QRIKLAKELSKRSTgrtLYILDEPTTGL--HFDdikKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYII 902
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
335-394 |
1.19e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 1.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499664576 335 IILKQVSHSYipGKEVL-KNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILI 394
Cdd:PRK11819 325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
334-544 |
1.19e-04 |
|
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: 42.73 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 334 EIILKQVSHSYIPgkevlknINLTIKPLEKVAIVGPSGAGKSTLVklllglmrpaegeilingvplwelkekdwyDQVGY 413
Cdd:cd03227 1 KIVLGRFPSYFVP-------NDVTFGEGSLTIITGPNGSGKSTIL------------------------------DAIGL 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 414 LhqtpfifpgSIAENIALGKKGAKGEEIKRAASLAGAHQFIAELPQGYdtkvgeggrglsggeRQRIALARVF----LKD 489
Cdd:cd03227 44 A---------LGGAQSATRRRSGVKAGCIVAAVSAELIFTRLQLSGGE---------------KELSALALILalasLKP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 490 AKIVILDEPTAGLDA-HTEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKIILIDR 544
Cdd:cd03227 100 RPLYILDEIDRGLDPrDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
14-223 |
1.23e-04 |
|
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: 44.36 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 14 KGYLVKIALTSFISGGAIIAQAYLIAYIINGaFLAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRN 93
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDD-IIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 94 VLLEKIAALGTKVLLPEKTGELLTLILEgveslevyyARYLPQLISAGII-----PLMILVVVLALDLISGIIMLLTAPL 168
Cdd:cd18570 80 GYFKHLLKLPLSFFETRKTGEIISRFND---------ANKIREAISSTTIslfldLLMVIISGIILFFYNWKLFLITLLI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499664576 169 IPVFMMLIGSFA---EKLAQKQWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKK 223
Cdd:cd18570 151 IPLYILIILLFNkpfKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEK 208
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
32-259 |
1.40e-04 |
|
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: 43.93 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 32 IAQAYLIAYIINgAFLAKKGLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRNVLLEKIAALGTKVLlpEK 111
Cdd:cd18548 16 LLLPTLMADIID-EGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEI--DK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 112 --TGELLTLILEGVESLEVYYARYLPQLISAgiiPLMI---LVVVLALDLISGIIMLLTAPLIPVFMMLIGSFAEKLAQK 186
Cdd:cd18548 93 fgTSSLITRLTNDVTQVQNFVMMLLRMLVRA---PIMLigaIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499664576 187 QWSSLSRLSGKFFELLQGIADLKAFGRSKEQVNELKKSGLMFRDATMEVLRV-AFLSALaleVLATISTAMVAV 259
Cdd:cd18548 170 VQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLmALLNPL---MMLIMNLAIVAI 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
346-549 |
2.54e-04 |
|
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: 43.66 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 346 PGKEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPA-EGEILINGVPLWELKEKDWYDQ----VGYLHQTPFI 420
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAgiamVPEDRKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 421 FPG-SIAENIALG---------------KKGAKGEEIKRAaSLAGAHQF--IAELPQGydtkvgeggrglsggERQRIAL 482
Cdd:TIGR02633 351 VPIlGVGKNITLSvlksfcfkmridaaaELQIIGSAIQRL-KVKTASPFlpIGRLSGG---------------NQQKAVL 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499664576 483 ARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNR-TVIIIAHRLSS-LYRADKIILIDRGEIRG 549
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELAEvLGLSDRVLVIGEGKLKG 483
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
353-530 |
2.56e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.56 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 353 NINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRP---AEGEILINGVPLWELKEKDW----YDQVGYLHQTPF--IFP- 422
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELnklrAEQISMIFQDPMtsLNPy 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 423 GSIAENIA--------LGKKGAKGEEIKR--AASLAGAHQFIAELPQGYDTKVGeggrglsggerQRIALARVFLKDAKI 492
Cdd:PRK09473 114 MRVGEQLMevlmlhkgMSKAEAFEESVRMldAVKMPEARKRMKMYPHEFSGGMR-----------QRVMIAMALLCRPKL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499664576 493 VILDEPTAGLD----AHTEKLLEKAFDELfqNRTVIIIAHRL 530
Cdd:PRK09473 183 LIADEPTTALDvtvqAQIMTLLNELKREF--NTAIIMITHDL 222
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
351-572 |
6.31e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYDQVGYLhqtpfifpgsiaENIA 430
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 431 LG--KKGAKGEEIK----RAASLAGAHQFIAELPQGYDTKVgeggrglsggeRQRIALARVFLKDAKIVILDEP-TAGLD 503
Cdd:PRK13545 108 LKglMMGLTKEKIKeiipEIIEFADIGKFIYQPVKTYSSGM-----------KSRLGFAISVHINPDILVIDEAlSVGDQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 504 AHTEKLLEKAFDELFQNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQLLAEnelYRQLITAYRG 572
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDH---YDEFLKKYNQ 243
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
351-386 |
7.00e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 7.00e-04
10 20 30
....*....|....*....|....*....|....*....
gi 499664576 351 LKNINLTIkPLEK-VAIVGPSGAGKSTLVK--LLLGLMR 386
Cdd:COG0178 621 LKNVDVEI-PLGVlTCVTGVSGSGKSTLVNdiLYPALAR 658
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
351-378 |
7.39e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 7.39e-04
10 20
....*....|....*....|....*....
gi 499664576 351 LKNINLTIkPLEK-VAIVGPSGAGKSTLV 378
Cdd:PRK00349 625 LKNVDVEI-PLGKfTCVTGVSGSGKSTLI 652
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
358-392 |
9.41e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 9.41e-04
10 20 30
....*....|....*....|....*....|....*
gi 499664576 358 IKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEI 392
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
351-378 |
1.20e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 1.20e-03
10 20
....*....|....*....|....*....
gi 499664576 351 LKNINLTIkPLEK-VAIVGPSGAGKSTLV 378
Cdd:COG0178 16 LKNIDVDI-PRNKlVVITGLSGSGKSSLA 43
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
330-549 |
1.35e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 330 DSPPEIILKQVSHSYIPGkevLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELKEKDWYD 409
Cdd:PRK10762 250 DKAPGEVRLKVDNLSGPG---VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 410 Q-VGYLHQTP----FIFPGSIAENI---ALGKKGAKGEEIKRAASLAGAHQFIaelpQGYDTKVGEGGRGLSGGE---RQ 478
Cdd:PRK10762 327 NgIVYISEDRkrdgLVLGMSVKENMsltALRYFSRAGGSLKHADEQQAVSDFI----RLFNIKTPSMEQAIGLLSggnQQ 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499664576 479 RIALARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRTVIIIahrLSS-----LYRADKIILIDRGEIRG 549
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL---VSSempevLGMSDRILVMHEGRISG 475
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
348-569 |
1.37e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 41.61 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKS-TLVKLLLGLMRPA----EGEILINGVPLWELKEKDWY----DQVGYLHQTP 418
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 419 FI-------FPGSIAENIAL----GKKGAKGEeIKRAASLAGAHQ-------FIAELPQGydtkvgeggrglsggERQRI 480
Cdd:PRK15134 102 MVslnplhtLEKQLYEVLSLhrgmRREAARGE-ILNCLDRVGIRQaakrltdYPHQLSGG---------------ERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 481 ALARVFLKDAKIVILDEPTAGLD----AHTEKLLEKAFDELfqNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQ 555
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDvsvqAQILQLLRELQQEL--NMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAAT 243
|
250
....*....|....*.
gi 499664576 556 LLA--ENELYRQLITA 569
Cdd:PRK15134 244 LFSapTHPYTQKLLNS 259
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
478-540 |
2.18e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 2.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 478 QRIALARVFLKDAK---IVILDEPTAGLdaHTE---KLLeKAFDELF-QNRTVIIIAHRLSSLYRADKII 540
Cdd:COG0178 833 QRVKLASELSKRSTgktLYILDEPTTGL--HFHdirKLL-EVLHRLVdKGNTVVVIEHNLDVIKTADWII 899
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
364-392 |
2.68e-03 |
|
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: 39.30 E-value: 2.68e-03
10 20
....*....|....*....|....*....
gi 499664576 364 VAIVGPSGAGKSTLVKLLLGLMRPAEGEI 392
Cdd:cd01854 88 SVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
337-392 |
2.73e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 2.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 337 LKQVSHSYipGKEV-LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEI 392
Cdd:NF033858 4 LEGVSHRY--GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV 58
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
363-403 |
2.91e-03 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 38.81 E-value: 2.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 499664576 363 KVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELK 403
Cdd:COG1100 5 KIVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTNGVTIDKKE 45
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
478-540 |
3.66e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 3.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 478 QRIALARVFLKDAK---IVILDEPTAGLDAH-TEKLLEKAFDELFQNRTVIIIAHRLSSLYRADKII 540
Cdd:PRK00635 816 QRLKLAYELLAPSKkptLYVLDEPTTGLHTHdIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
14-212 |
4.23e-03 |
|
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: 39.42 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 14 KGYLVKIALTSFISGGAIIAQAYLIAYIINGAFLAKKgLGELWPFFPALFLIVTLRFSLGYFGEKVGANLASKVTGEIRN 93
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGN-LNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 94 VLLEKIAALGTKVLLPEKTGELLTLIlegvESLevyyaRYLPQLIS----AGIIPLMILVVVLALDLIS----GIIMLLT 165
Cdd:cd18555 80 DFFEHLLKLPYSFFENRSSGDLLFRA----NSN-----VYIRQILSnqviSLIIDLLLLVIYLIYMLYYspllTLIVLLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499664576 166 APLIPVFMMLIGSFAEKLAQKQWSSLSRLSGKFFELLQGIADLKAFG 212
Cdd:cd18555 151 GLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLG 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
351-556 |
4.69e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.84 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING----------VPLWELKEKDWYDQVG----YLHQ 416
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGadmaMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 417 TPF-----IFP--GSIAENIALgKKGAKGEEIKRAAS-------LAGAHQFIAELPQgydtkvgeggrGLSGGERQRIAL 482
Cdd:PRK10261 112 EPMtslnpVFTvgEQIAESIRL-HQGASREEAMVEAKrmldqvrIPEAQTILSRYPH-----------QLSGGMRQRVMI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499664576 483 ARVFLKDAKIVILDEPTAGLDAHTEKLLEKAFDELFQNRT--VIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQL 556
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| guanyl_kin |
TIGR03263 |
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ... |
366-382 |
4.71e-03 |
|
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 213788 Cd Length: 179 Bit Score: 38.24 E-value: 4.71e-03
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
351-396 |
5.61e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.45 E-value: 5.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 499664576 351 LKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILING 396
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG 385
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
358-556 |
6.76e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 39.61 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 358 IKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWElKEKDWYDQVGYLHQTPFIfpgsiaENIALGK---- 433
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGRehly 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 434 -----KGAKGEEIKRAASLAgahqfIAELpqGYDTKVGEGGRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTEK 508
Cdd:TIGR01257 2035 lyarlRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499664576 509 LLEKAFDELF-QNRTVIIIAHRLSSLYR-ADKIILIDRGEIRGMGRHEQL 556
Cdd:TIGR01257 2108 MLWNTIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
366-382 |
7.34e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 38.15 E-value: 7.34e-03
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
356-388 |
8.39e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 8.39e-03
10 20 30
....*....|....*....|....*....|...
gi 499664576 356 LTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPA 388
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPA 49
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
348-510 |
9.10e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.54 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 348 KEVLKNINLTIKPLEKVAIVGPSGAGKSTLVKLLLGLMRPAEGEILINGVPLWELkEKDWYDQVGylHQTPFIFPGSIAE 427
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-AKPYCTYIG--HNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499664576 428 NIALGKKGAKGEEIKRAAslagAHQFiaELPQGYDTKVgeggRGLSGGERQRIALARVFLKDAKIVILDEPTAGLDAHTE 507
Cdd:PRK13541 90 NLKFWSEIYNSAETLYAA----IHYF--KLHDLLDEKC----YSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
...
gi 499664576 508 KLL 510
Cdd:PRK13541 160 DLL 162
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
364-394 |
9.15e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 38.77 E-value: 9.15e-03
10 20 30
....*....|....*....|....*....|.
gi 499664576 364 VAIVGPSGAGKSTLVKLLLGLMRPAEGEILI 394
Cdd:COG3451 207 TLILGPSGSGKSFLLKLLLLQLLRYGARIVI 237
|
|
| |
