|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-573 |
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: 711.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 12 QQTLRAFLKQYSQSASGLLKLSISLGTLNALLMIASCYLLANAAHQVMFEQANLQAVSPLLWPLAGLILVRALLVALSER 91
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 92 VSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKA 171
Cdd:COG4988 81 AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 172 GLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKV 251
Cdd:COG4988 161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 252 AFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQMGTHYHAKLEGISAAADMVDIINQSDA 331
Cdd:COG4988 241 AFLSSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 332 DEHVGSSKLELP-IKHIQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQP 410
Cdd:COG4988 321 AAPAGTAPLPAAgPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 411 LSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQ 490
Cdd:COG4988 401 LSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 491 RIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTE 570
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560
|
...
gi 1952200779 571 QAG 573
Cdd:COG4988 561 KNG 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-554 |
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: 576.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 26 ASGLLKLSISLGTLNALLMIASCYLLANAAHQVMFEQANLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMR 105
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 106 NTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFF 185
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 186 MILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATI 265
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 266 SVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQMGTHYHAKLEGISAAADMVDIINQSDADEHVGSSKLELPIK 345
Cdd:TIGR02857 241 SVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 346 HIQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW 425
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVM 554
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-581 |
0e+00 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 543.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 8 NRAQQQTLRAFLKQYSQSASGLLKLSISLGTLNALLMIASCYLLANAAHQVMFEQANLQAVSPLLWPLAGLILVRALLVA 87
Cdd:PRK11174 2 DKSRQKELTRWLKQQSKPAKRWLNLSILLGFLSGLLLIAQAWLLATILQALIIENIPREALLPPFILLILLFVLRALLAW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 88 LSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQK--GHGATLntLHNGVEALHQYYANYIPSVAYSALIPLAILVMIF 165
Cdd:PRK11174 82 LRERVGFKAGQHIRQQIRQQVLDKLQQLGPAWIQGKpaGSWATL--VLEQVEDMHDFYARYLPQMALAVLVPLLILIAVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 166 PTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGAT 245
Cdd:PRK11174 160 PINWAAGLILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 246 MGVLKVAFLSSFALEFLATISVALVAVIIGFRlFFGTLDFA---------TGFVVLLLAPEFYLPLRQMGTHYHAKLEGI 316
Cdd:PRK11174 240 MEVLRMAFLSSAVLEFFASISIALVAVYFGFS-YLGELNFGhygtgvtlfAGFFVLILAPEFYQPLRDLGTFYHAKAQAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 317 SAAADMVDIINQSDadEHVGSSKLELPIKH---IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCL 393
Cdd:PRK11174 319 GAAESLVTFLETPL--AHPQQGEKELASNDpvtIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 394 LGFHHQANSaISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGF 473
Cdd:PRK11174 397 LGFLPYQGS-LKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 474 DTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYV 553
Cdd:PRK11174 476 DTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWV 555
|
570 580
....*....|....*....|....*...
gi 1952200779 554 MQQGHIVESGQYQQLTEQAGLFAKLVSQ 581
Cdd:PRK11174 556 MQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-579 |
1.03e-148 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 440.76 E-value: 1.03e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 8 NRAQQQTLRaFLKQYSQSASGLLKLSISLGTLNALLMIASCYLLANAAHQVmFEQANLQAVSPLLWPLAGLILVRALLVA 87
Cdd:COG1132 2 SKSPRKLLR-RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDAL-LAGGDLSALLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 88 LSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPT 167
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 168 DYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMG 247
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 248 VLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQMGTHYHAKLEGISAAADMVDIIN 327
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 328 -QSDADEHVGSSKLELPIKHIQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHhQANS-AIS 405
Cdd:COG1132 320 ePPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY-DPTSgRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 406 INEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLS 485
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 486 GGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQY 565
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558
|
570
....*....|....
gi 1952200779 566 QQLTEQAGLFAKLV 579
Cdd:COG1132 559 EELLARGGLYARLY 572
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
33-322 |
8.39e-125 |
|
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: 368.66 E-value: 8.39e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 33 SISLGTLNALLMIASCYLLANAAHQVMFEQANLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKL 112
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 113 SKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHK 192
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 193 AEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAV 272
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1952200779 273 IIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQMGTHYHAKLEGISAAADM 322
Cdd:cd18584 241 YIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
66-581 |
6.87e-102 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 323.71 E-value: 6.87e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 66 QAVSPLLWPLAGLILV----RALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLhNGVEALHQ 141
Cdd:COG2274 189 NQDLSTLWVLAIGLLLallfEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIRE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 142 YYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQL 221
Cdd:COG2274 268 FLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 222 KLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVaVIIGFRLFF------GTLDFATGFVVLLLA 295
Cdd:COG2274 348 KALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVAL-LWLGAYLVIdgqltlGQLIAFNILSGRFLA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 296 PefylpLRQMGTHYhAKLEGISAAADMVDIINQSDADEHVGSSKLELPIK--HIQLNALTFHYPETNEGV-TDINLTLPS 372
Cdd:COG2274 427 P-----VAQLIGLL-QRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLkgDIELENVSFRYPGDSPPVlDNISLTIKP 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 373 SGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAE 452
Cdd:COG2274 501 GERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 453 LDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKD 532
Cdd:COG2274 581 IIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG 660
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1952200779 533 HLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLVSQ 581
Cdd:COG2274 661 RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-581 |
3.93e-101 |
|
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: 317.86 E-value: 3.93e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 14 TLRAFLKQYSQSASGLLkLSISLGTL----NALLMIASCYLLANAAhqvmfeqanlqavspllwpLAGLIL--------V 81
Cdd:COG4987 2 DLLRLLRLLRPHRGRLL-LGVLLGLLtllaGIGLLALSGWLIAAAA-------------------LAPPILnlfvpivgV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 82 RALlvALS-------ER-VSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYI-PSVAY 152
Cdd:COG4987 62 RAF--AIGrtvfrylERlVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLlPLLVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 153 SALIPLAILVMIFpTDYKAGLI----FLLTAPLIPFFMILVGHKAEQlnqeRWQQL-AVLGNYFFDRLQGLTQLKLFNAT 227
Cdd:COG4987 140 LLVILAAVAFLAF-FSPALALVlalgLLLAGLLLPLLAARLGRRAGR----RLAAArAALRARLTDLLQGAAELAAYGAL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 228 KRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDfATGFVVLLLAP----EFYLPLR 303
Cdd:COG4987 215 DRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAAlalfEALAPLP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 304 QMGTHyhakLEGISAAAD-MVDIINQSDADEHVGSSKLELPIKHIQLNALTFHYPETNEGV-TDINLTLPSSGLIAFVGE 381
Cdd:COG4987 294 AAAQH----LGRVRAAARrLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 382 SGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAG 461
Cdd:COG4987 370 SGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVG 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 462 ALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHR 541
Cdd:COG4987 450 LGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR 529
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1952200779 542 LNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLVSQ 581
Cdd:COG4987 530 LAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
41-578 |
5.13e-87 |
|
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: 280.83 E-value: 5.13e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 41 ALLMIASCYLLANAAHQVMF---------EQANLQAVSPLLW-PLA--GLILVRALLVALSERVSNRAALKIKNVMRNTL 108
Cdd:TIGR02203 14 AGLVLAGVAMILVAATESTLaallkplldDGFGGRDRSVLWWvPLVviGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 109 LEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMIL 188
Cdd:TIGR02203 94 FEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 189 VGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVA 268
Cdd:TIGR02203 174 VSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 269 LVAVIIGFRLFFGTL---DFaTGFVVLLLApeFYLPLRQMgTHYHAKLEGISAAADMVDIINQSDADEHVGSSKLELPIK 345
Cdd:TIGR02203 254 VVLFIALFQAQAGSLtagDF-TAFITAMIA--LIRPLKSL-TNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRAIERARG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 346 HIQLNALTFHYPETN-EGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLA 424
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHATFFYRSVAENLRLAKP-DASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAP 503
Cdd:TIGR02203 410 LVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAP 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 504 VLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKL 578
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
36-579 |
1.99e-79 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 261.17 E-value: 1.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 36 LGTLNALLMIASCYLLANAAHQVM----FEQANLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEK 111
Cdd:TIGR02204 21 LAALVALLITAAATLSLPYAVRLMidhgFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 112 LSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGH 191
Cdd:TIGR02204 101 LISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 192 KAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNatkRElnsiSQISDDYRGATMGVLKVAFLSSFALEFLATISVALVA 271
Cdd:TIGR02204 181 RVRKLSRESQDRIADAGSYAGETLGAIRTVQAFG---HE----DAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 272 VIIGFRLFFGTLDFATGFVVL--LLAPEFYLPLRQMGTHYHAKLEG-ISAAADMVDIIN---QSDADEHVGSSKLELPIK 345
Cdd:TIGR02204 254 GAIVGVLWVGAHDVIAGKMSAgtLGQFVFYAVMVAGSIGTLSEVWGeLQRAAGAAERLIellQAEPDIKAPAHPKTLPVP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 346 ---HIQLNALTFHYPETNE--GVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQ 420
Cdd:TIGR02204 334 lrgEIEFEQVNFAYPARPDqpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 AQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLK 500
Cdd:TIGR02204 414 ARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILK 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 501 NAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLV 579
Cdd:TIGR02204 494 DAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLA 572
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
347-582 |
3.94e-78 |
|
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: 246.68 E-value: 3.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPE--TNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLA 424
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPV 504
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 505 LMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLVSQG 582
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
347-578 |
7.62e-78 |
|
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: 245.99 E-value: 7.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGV-TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW 425
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKL 578
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
347-578 |
1.79e-71 |
|
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: 229.42 E-value: 1.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLM 506
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 507 LDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKL 578
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
347-573 |
8.17e-70 |
|
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: 224.80 E-value: 8.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLM 506
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 507 LDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAG 573
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
222-578 |
3.18e-69 |
|
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: 234.71 E-value: 3.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 222 KLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTL---DFAtgFVVLLLApEF 298
Cdd:COG5265 232 KYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMtvgDFV--LVNAYLI-QL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 299 YLPLRQMGTHYHaklEGISAAADM----------VDIINQSDAdehvgsskLELPIK--HIQLNALTFHYPETNEGVTDI 366
Cdd:COG5265 309 YIPLNFLGFVYR---EIRQALADMermfdlldqpPEVADAPDA--------PPLVVGggEVRFENVSFGYDPERPILKGV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 367 NLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKP 446
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 447 DASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAI 526
Cdd:COG5265 458 DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 527 REYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKL 578
Cdd:COG5265 538 REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
38-579 |
3.45e-69 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 234.08 E-value: 3.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 38 TLNALLMIASCYL-LANAAHQVMFEQ-----ANLQAVSPLL--WPLAGLI-LVRALLVAL-SERVSNRaalkiknvMRNT 107
Cdd:PRK13657 19 RLGILLAVANVLLaAATFAEPILFGRiidaiSGKGDIFPLLaaWAGFGLFnIIAGVLVARhADRLAHR--------RRLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 108 LL----EKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSvAYSALIPLAILV-MIFPTDYKAGLIflLTAPLI 182
Cdd:PRK13657 91 VLteyfERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMRE-HLATLVALVVLLpLALFMNWRLSLV--LVVLGI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 183 PFFMI--LVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALE 260
Cdd:PRK13657 168 VYTLIttLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWALASVLNR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 261 FLATISVALVAVI------------------IGF-RLFFGTLDFATGFVVLLlapefylplrqmgthyhaklegISAAAD 321
Cdd:PRK13657 248 AASTITMLAILVLgaalvqkgqlrvgevvafVGFaTLLIGRLDQVVAFINQV----------------------FMAAPK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 322 MVDIINQSDA----DEHVGSSKLELPIKHIQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFH 397
Cdd:PRK13657 306 LEEFFEVEDAvpdvRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 398 HQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLL 477
Cdd:PRK13657 386 DPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 478 GEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQG 557
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
570 580
....*....|....*....|..
gi 1952200779 558 HIVESGQYQQLTEQAGLFAKLV 579
Cdd:PRK13657 546 RVVESGSFDELVARGGRFAALL 567
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
33-319 |
1.69e-68 |
|
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: 223.70 E-value: 1.69e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 33 SISLGTLNALLMIASCYLLANAAhQVMFEQANLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKL 112
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARAL-ARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 113 SKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHK 192
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 193 AEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAV 272
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1952200779 273 IIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQMGTHYHAKLEGISAA 319
Cdd:cd18561 240 VGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAA 286
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
158-578 |
2.74e-66 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 226.44 E-value: 2.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 158 LAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQI 237
Cdd:PRK11176 154 IGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 238 SDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQMgTHYHAKLE-GI 316
Cdd:PRK11176 234 SNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSL-TNVNAQFQrGM 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 317 SAAADMVDIINqSDADEHVGSSKLELPIKHIQLNALTFHYPETNE-GVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLG 395
Cdd:PRK11176 313 AACQTLFAILD-LEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 396 FHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDA-SQAELDEAASKAGALEFITALPDGFD 474
Cdd:PRK11176 392 FYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 475 TLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVM 554
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV 551
|
410 420
....*....|....*....|....
gi 1952200779 555 QQGHIVESGQYQQLTEQAGLFAKL 578
Cdd:PRK11176 552 EDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
347-558 |
7.01e-65 |
|
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: 209.55 E-value: 7.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGV-TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW 425
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHATFFYRSVAENLrlakpdasqaeldeaaskagalefitalpdgfdtllgeqgegLSGGQKQRIALARAFLKNAPVL 505
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGH 558
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
347-579 |
8.16e-62 |
|
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: 204.26 E-value: 8.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHY-PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW 425
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLV 579
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-542 |
5.92e-57 |
|
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: 199.89 E-value: 5.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 19 LKQYSQSASGLLKLSISLGTLNAL----LMIASCYLLANAAHQvmfeqanlqavSPLLWPLAGLILVRALLVALS----- 89
Cdd:TIGR02868 4 ILPLLKPRRRRLALAVLLGALALGsavaLLGVSAWLISRAAEM-----------PPVLYLSVAAVAVRAFGIGRAvfryl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 90 ER-VSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYI-PSVAYSALIPLAILVmIFPT 167
Cdd:TIGR02868 73 ERlVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIvPAGVALVVGAAAVAA-IAVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 168 DYKAGLIF----LLTAPLIPFFMILVGHKAEQLNQ----ERWQQLAvlgnyffDRLQGLTQLKLFNATKRELNSISQISD 239
Cdd:TIGR02868 152 SVPAALILaaglLLAGFVAPLVSLRAARAAEQALArlrgELAAQLT-------DALDGAAELVASGALPAALAQVEEADR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 240 DYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLL---APEFYLPLR---QMGTHYHAKL 313
Cdd:TIGR02868 225 ELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLplaAFEAFAALPaaaQQLTRVRAAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 314 EGISAAADmvdiiNQSDADEHVGSSKLELPIKHIQLNA--LTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFD 391
Cdd:TIGR02868 305 ERIVEVLD-----AAGPVAEGSAPAAGAVGLGKPTLELrdLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 392 CLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPD 471
Cdd:TIGR02868 380 TLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPD 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 472 GFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE----HLINQAIREYAkdhlVLVIAHRL 542
Cdd:TIGR02868 460 GLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAdellEDLLAALSGRT----VVLITHHL 530
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
95-582 |
2.21e-56 |
|
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: 199.73 E-value: 2.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 95 RAALKIKNVMRNTLLEK----LSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPS-----VAYSALIPLAilvmiF 165
Cdd:TIGR01192 78 READRLAHGRRATLLTEafgrIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQhlatfVALFLLIPTA-----F 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 166 PTDYKAGLIFLLTAPLIPFFMILVGHKAEQlnqerwQQLAVLGNY------FFDRLQGLTQLKLFNATKRELNSISQISD 239
Cdd:TIGR01192 153 AMDWRLSIVLMVLGILYILIAKLVMQRTKN------GQAAVEHHYhnvfkhVSDSISNVSVVHSYNRIEAETSALKQFTN 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 240 DYRGATMGVLKVAFLSSFALEFLATISVALVAVI------------------IGF-RLFFGTLDFATGFVVLLLAPEfyl 300
Cdd:TIGR01192 227 NLLSAQYPVLDWWALASGLNRMASTISMMCILVIgtvlvikgelsvgeviafIGFaNLLIGRLDQMSGFITQIFEAR--- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 301 plrqmgthyhAKLEGISAAADMVdiinqSDADEHVGSSKLELPIKHIQLNALTFHYPETNEGVTDINLTLPSSGLIAFVG 380
Cdd:TIGR01192 304 ----------AKLEDFFDLEDSV-----FQREEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 381 ESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKA 460
Cdd:TIGR01192 369 PTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 461 GALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAH 540
Cdd:TIGR01192 449 AAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAH 528
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1952200779 541 RLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLVSQG 582
Cdd:TIGR01192 529 RLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRS 570
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
172-578 |
3.49e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 198.90 E-value: 3.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 172 GLIFLLTAPLIPFFMILVGHKA-EQLNQERwqqlAVLGNYFFDRLQGLTQLKLFNATKRELNSISQ-----ISDDYRGAT 245
Cdd:PRK11160 167 GGILLLLLLLLPLLFYRLGKKPgQDLTHLR----AQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQteqqwLAAQRRQAN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 246 MGVLKVAFLSsFALEFLATISVALVAVIIG--------FRLFFgtldFATGFVVLLLAP--EFYLPLRQMgthyhakleg 315
Cdd:PRK11160 243 LTGLSQALMI-LANGLTVVLMLWLAAGGVGgnaqpgalIALFV----FAALAAFEALMPvaGAFQHLGQV---------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 316 ISAAADMVDIINQSDADEHVGSSKLELPIKHIQLNALTFHYPETNEGV-TDINLTLPSSGLIAFVGESGSGKSTLFDcLL 394
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQ-LL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 395 GFHHQANSA-ISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGaLEFITALPDGF 473
Cdd:PRK11160 387 TRAWDPQQGeILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG-LEKLLEDDKGL 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 474 DTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYV 553
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
410 420
....*....|....*....|....*
gi 1952200779 554 MQQGHIVESGQYQQLTEQAGLFAKL 578
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
346-563 |
2.08e-55 |
|
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: 186.55 E-value: 2.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 346 HIQLNALTFHY-PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLA 424
Cdd:cd03244 2 DIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHATFFYRSVAENLrlakpD----ASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLK 500
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL-----DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 501 NAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESG 563
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
324-581 |
2.59e-55 |
|
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: 198.81 E-value: 2.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 324 DIINQSDADEHVGSSKLELPIKHIQLNALTFHY-PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANS 402
Cdd:TIGR01846 433 DILNSPTEPRSAGLAALPELRGAITFENIRFRYaPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHG 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 403 AISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGE 482
Cdd:TIGR01846 513 QVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 483 GLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVES 562
Cdd:TIGR01846 593 NLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAES 672
|
250
....*....|....*....
gi 1952200779 563 GQYQQLTEQAGLFAKLVSQ 581
Cdd:TIGR01846 673 GRHEELLALQGLYARLWQQ 691
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
347-563 |
9.28e-53 |
|
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: 179.71 E-value: 9.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPET-NEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW 425
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESG 563
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
347-573 |
5.10e-52 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 187.23 E-value: 5.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGV-TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW 425
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPAlENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAG 573
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
154-571 |
7.02e-51 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 186.23 E-value: 7.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 154 ALIPL-AILVMIFPTdykagliFLLTAPLipffmilvGHKAEQLNQERWQQLAVLgnyfFDRLQGLTQLKLFNATKRELN 232
Cdd:TIGR03375 288 VWVPLvAIPLILLPG-------LLLQRPL--------SRLAEESMRESAQRNAVL----VESLSGLETIKALNAEGRFQR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 233 SISQISddyrGATMGV-LKVAFLSSFALEFLATI----SVALVAV----IIGFRLFFGTLDFATgfvvlLLAPEFYLPLR 303
Cdd:TIGR03375 349 RWEQTV----AALARSgLKSRFLSNLATNFAQFIqqlvSVAIVVVgvylISDGELTMGGLIACV-----MLSGRALAPLG 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 304 Q----MGTHYHAKlegisAAADMVDIINQSDADEHVGSSKLELPIKH--IQLNALTFHYPE-TNEGVTDINLTLPSSGLI 376
Cdd:TIGR03375 420 QlaglLTRYQQAK-----TALQSLDELMQLPVERPEGTRFLHRPRLQgeIEFRNVSFAYPGqETPALDNVSLTIRPGEKV 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 377 AFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEA 456
Cdd:TIGR03375 495 AIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 457 ASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVL 536
Cdd:TIGR03375 575 AELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLV 654
|
410 420 430
....*....|....*....|....*....|....*
gi 1952200779 537 VIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQ 571
Cdd:TIGR03375 655 LVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
65-573 |
1.20e-50 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 184.15 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 65 LQAVSPLLWPLAGLILVRALLVALSERVSNRAALKI-----KNVMRNTLLEKLSklgpAYSEQKgHGATLNTLHNGVEAL 139
Cdd:PRK10790 61 LGLVAGLAAAYVGLQLLAAGLHYAQSLLFNRAAVGVvqqlrTDVMDAALRQPLS----AFDTQP-VGQLISRVTNDTEVI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 140 HQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLT 219
Cdd:PRK10790 136 RDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 220 QLKLFNATKRELNSISQISDDYRGATMGVLKvafLSSFALEFLATISVALVavIIGFRLFFGTLDFATGFVVLLLAPEFY 299
Cdd:PRK10790 216 VIQQFRQQARFGERMGEASRSHYMARMQTLR---LDGFLLRPLLSLFSALI--LCGLLMLFGFSASGTIEVGVLYAFISY 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 300 L-----PLRQMGTHYHAKLEGISAAADMVDIINQsdADEHVGSSKLELPIKHIQLNALTFHYPETNEGVTDINLTLPSSG 374
Cdd:PRK10790 291 LgrlnePLIELTTQQSMLQQAVVAGERVFELMDG--PRQQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 375 LIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKpDASQAELD 454
Cdd:PRK10790 369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVW 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 455 EAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHL 534
Cdd:PRK10790 448 QALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTT 527
|
490 500 510
....*....|....*....|....*....|....*....
gi 1952200779 535 VLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAG 573
Cdd:PRK10790 528 LVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
346-559 |
2.50e-50 |
|
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: 173.43 E-value: 2.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 346 HIQLNALTFHYPETNEG--VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQL 423
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAP 503
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 504 VLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHI 559
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
147-579 |
4.71e-49 |
|
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: 181.48 E-value: 4.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 147 IPSVAYSALIPLAILVMI-FPTDYKAGLIFLLTAPLIPFFMILV---GHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLK 222
Cdd:TIGR01193 269 LASTILSLFLDMWILVIVgLFLVRQNMLLFLLSLLSIPVYAVIIilfKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 223 LFNATKRELNSISQISDDYrgatmgvLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVL-------LLA 295
Cdd:TIGR01193 349 SLTSEAERYSKIDSEFGDY-------LNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLgqlitfnALL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 296 PEFYLPLRQMgTHYHAKLEGISAAADM---VDIINQSDADEHVGSSkLELPIKHIQLNALTFHYPETNEGVTDINLTLPS 372
Cdd:TIGR01193 422 SYFLTPLENI-INLQPKLQAARVANNRlneVYLVDSEFINKKKRTE-LNNLNGDIVINDVSYSYGYGSNILSDISLTIKM 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 373 SGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRL-AKPDASQA 451
Cdd:TIGR01193 500 NSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQD 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 452 ELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIReYAK 531
Cdd:TIGR01193 580 EIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL-NLQ 658
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1952200779 532 DHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLV 579
Cdd:TIGR01193 659 DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
41-322 |
4.22e-46 |
|
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: 163.86 E-value: 4.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 41 ALLM-IASCYLLANAAHQVMFEQANLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAY 119
Cdd:cd18781 8 SLLAnIAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRLGPSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 120 SEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQE 199
Cdd:cd18781 88 QEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKIAKKLLSK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 200 RWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLF 279
Cdd:cd18781 168 YWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVAYGGAALGIILALLQFA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1952200779 280 FGTLDFATGFVVLLLAPEFYLPLRQMGTHYHAKLEGISAAADM 322
Cdd:cd18781 248 NGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASDKI 290
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
158-579 |
3.84e-45 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 170.29 E-value: 3.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 158 LAILVMIFPTDYKAGLIFLLTAPLIpFFMILVGHKAEQLNQERWQQ-LAVLGNYFFDRLQGLTQLKLFNATKRELnsisq 236
Cdd:TIGR00958 290 LGLLGFMLWLSPRLTMVTLINLPLV-FLAEKVFGKRYQLLSEELQEaVAKANQVAEEALSGMRTVRSFAAEEGEA----- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 237 isDDYRGATMGVLKVAFLSSFA-LEFLATISVALVAVIIGFrLFFGTLDFATGFV-------VLLLAPEFYLPLRQMGTH 308
Cdd:TIGR00958 364 --SRFKEALEETLQLNKRKALAyAGYLWTTSVLGMLIQVLV-LYYGGQLVLTGKVssgnlvsFLLYQEQLGEAVRVLSYV 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 309 YHAKLEGISAAADMVDIINQSDADEHVGSSKLELPIKHIQLNALTFHYPE--TNEGVTDINLTLPSSGLIAFVGESGSGK 386
Cdd:TIGR00958 441 YSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGK 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 387 STLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFI 466
Cdd:TIGR00958 521 STVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFI 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 467 TALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLInQAIREyAKDHLVLVIAHRLNTVK 546
Cdd:TIGR00958 601 MEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL-QESRS-RASRTVLLIAHRLSTVE 678
|
410 420 430
....*....|....*....|....*....|...
gi 1952200779 547 HADKIYVMQQGHIVESGQYQQLTEQAGLFAKLV 579
Cdd:TIGR00958 679 RADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
343-563 |
1.63e-43 |
|
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: 163.38 E-value: 1.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 343 PIKHIQLNALTFHYPETNEGV-TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISineqpLSDTALADW-Q 420
Cdd:COG4618 327 PKGRLSVENLTVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR-----LDGADLSQWdR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 AQLA-WI---PQHATFFYRSVAENL-RLAKPDASQAEldEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALA 495
Cdd:COG4618 402 EELGrHIgylPQDVELFDGTIAENIaRFGDADPEKVV--AAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 496 RAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREyAKDH--LVLVIAHRLNTVKHADKIYVMQQGHIVESG 563
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
363-512 |
1.77e-38 |
|
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: 138.55 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYR-SVAENL 441
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 442 RLA------KPDASQAELDEAASKAGalefitaLPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTA 512
Cdd:pfam00005 81 RLGlllkglSKREKDARAEEALEKLG-------LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
347-559 |
4.16e-38 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 138.50 E-value: 4.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGV-TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW 425
Cdd:cd03246 1 LEVENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHATFFYRSVAENLrlakpdasqaeldeaaskagalefitalpdgfdtllgeqgegLSGGQKQRIALARAFLKNAPVL 505
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREY-AKDHLVLVIAHRLNTVKHADKIYVMQQGHI 559
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
325-559 |
1.71e-36 |
|
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: 143.26 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 325 IINQSDADEHVgssKLELPIKHIQLNALTFHYPETNEG-VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSA 403
Cdd:TIGR01842 298 LANYPSRDPAM---PLPEPEGHLSVENVTIVPPGGKKPtLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 404 ISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEG 483
Cdd:TIGR01842 375 VRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGAT 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREY-AKDHLVLVIAHRLNTVKHADKIYVMQQGHI 559
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
347-573 |
2.31e-36 |
|
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: 135.76 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPEtNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALAdWQAQLAWI 426
Cdd:COG4555 2 IEVENLSKKYGK-VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQ-HATFFYRSVAENLRLAkpdASQAELDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:COG4555 80 PDeRGLYDRLTVRENIRYF---AELYGLFDEELKKRIEELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAK-DHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLTEQAG 573
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
347-557 |
1.21e-35 |
|
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: 132.59 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYP----ETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINeqplSDTALAdwqAQ 422
Cdd:cd03250 1 ISVEDASFTWDsgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP----GSIAYV---SQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 423 LAWIpQHATffyrsVAENLRLAKP-DAsqaELDEAASKAGALEF-ITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLK 500
Cdd:cd03250 74 EPWI-QNGT-----IRENILFGKPfDE---ERYEKVIKACALEPdLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 501 NAPVLMLDEPTAHLDSQTE-HLINQAIREYAKDH-LVLVIAHRLNTVKHADKIYVMQQG 557
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGrHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
347-584 |
2.09e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.88 E-value: 2.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETnEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsDTALADWQAQLAWI 426
Cdd:COG1131 1 IEVRGLTKRYGDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-ARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFF-YRSVAENLRLAkpdASQAELDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:COG1131 79 PQEPALYpDLTVRENLRFF---ARLYGLPRKEARERIDELLELF--GLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKD-HLVLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQQLTEQA--GLFAKLVSQ 581
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLleDVFLELTGE 233
|
...
gi 1952200779 582 GDA 584
Cdd:COG1131 234 EAR 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
347-559 |
8.62e-34 |
|
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: 126.36 E-value: 8.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPeTNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAlADWQAQLAWI 426
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFFYR-SVAENLRLakpdasqaeldeaaskagalefitalpdgfdtllgeqgeglSGGQKQRIALARAFLKNAPVL 505
Cdd:cd03230 79 PEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKD-HLVLVIAHRLNTV-KHADKIYVMQQGHI 559
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
347-563 |
1.12e-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: 127.53 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHY-PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW 425
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHATFFYRSVAENLrlakpDASQAELDEaaskagalEFITALPdgfdtlLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:cd03369 87 IPQDPTLFSGTIRSNL-----DPFDEYSDE--------EIYGALR------VSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESG 563
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
347-559 |
1.23e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 127.24 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNeGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:COG4619 1 LELEGLSFRVGGKP-ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFFYRSVAENLRLAkPDASQAELDEAAskagALEFITALpdGFDT-LLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:COG4619 80 PQEPALWGGTVRDNLPFP-FQLRERKFDRER----ALELLERL--GLPPdILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKH-ADKIYVMQQGHI 559
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
347-559 |
3.00e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 3.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTaladwQAQLAWI 426
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATF---------------FYRSVAENLRLAKPDASQAelDEAASKAGALEFItalpdgfDTLLGEqgegLSGGQKQR 491
Cdd:COG1121 81 PQRAEVdwdfpitvrdvvlmgRYGRRGLFRRPSRADREAV--DEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 492 IALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAK-DHLVLVIAHRLNTV-KHADKIYVMQQGHI 559
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVrEYFDRVLLLNRGLV 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
307-554 |
3.85e-33 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 135.93 E-value: 3.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 307 THYHAKLEgisAAADMVDIINQSDADEHVGSSKLELPIKHIQLNALTFHYpETNEGV---TDINLTLPSSGLIAFVGESG 383
Cdd:PTZ00265 346 TEYMKSLE---ATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHY-DTRKDVeiyKDLNFTLTEGKTYAFVGESG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 384 SGKSTLFDCLLGFHHQANSAISINE-QPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLA----------------KP 446
Cdd:PTZ00265 422 CGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDG 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 447 DASQAELDEA----ASKAGAL-------------------------------------EFITALPDGFDTLLGEQGEGLS 485
Cdd:PTZ00265 502 NDSQENKNKRnscrAKCAGDLndmsnttdsneliemrknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLS 581
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 486 GGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYA--KDHLVLVIAHRLNTVKHADKIYVM 554
Cdd:PTZ00265 582 GGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
347-563 |
4.78e-33 |
|
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: 127.08 E-value: 4.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETnEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:COG1120 2 LEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATF-FYRSVAENL---------RLAKPDASQAEL-DEAASKAGALEFItalpdgfDTLLGEqgegLSGGQKQRIALA 495
Cdd:COG1120 81 PQEPPApFGLTVRELValgryphlgLFGRPSAEDREAvEEALERTGLEHLA-------DRPVDE----LSGGERQRVLIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 496 RAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLN-TVKHADKIYVMQQGHIVESG 563
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNlAARYADRLVLLKDGRIVAQG 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
347-568 |
9.83e-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: 126.07 E-value: 9.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQL 423
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPvlkDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHAT-----FF--YRSVAENLRLAKPDASQAELDEAASKAGalefitaLPDGFDTLLGEQgegLSGGQKQRIALAR 496
Cdd:COG1124 82 QMVFQDPYaslhpRHtvDRILAEPLRIHGLPDREERIAELLEQVG-------LPPSFLDRYPHQ---LSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 497 AFLKNAPVLMLDEPTAHLD--SQTE--HLINQAIREYakdHL-VLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:COG1124 152 ALILEPELLLLDEPTSALDvsVQAEilNLLKDLREER---GLtYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
365-575 |
9.94e-33 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 134.69 E-value: 9.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLrla 444
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL--- 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 445 KPDASQAELD--EAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLI 522
Cdd:TIGR00957 1381 DPFSQYSDEEvwWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 523 NQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLF 575
Cdd:TIGR00957 1461 QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
352-558 |
2.71e-32 |
|
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: 121.97 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 352 LTFHYPEtNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQhat 431
Cdd:cd00267 5 LSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 432 ffyrsvaenlrlakpdasqaeldeaaskagalefitalpdgfdtllgeqgegLSGGQKQRIALARAFLKNAPVLMLDEPT 511
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952200779 512 AHLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTV-KHADKIYVMQQGH 558
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRtVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
348-563 |
7.08e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 121.39 E-value: 7.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 348 QLNALTFHYPEtNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIP 427
Cdd:cd03214 1 EVENLSVGYGG-RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 428 QhatffyrsvaenlrlakpdasqaeldeAASKAGALEFITAlpdGFDTLlgeqgeglSGGQKQRIALARAFLKNAPVLML 507
Cdd:cd03214 80 Q---------------------------ALELLGLAHLADR---PFNEL--------SGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 508 DEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLN-TVKHADKIYVMQQGHIVESG 563
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
347-563 |
8.72e-32 |
|
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: 121.27 E-value: 8.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTD-INLTLPSSGLIAFVGESGSGKSTLFDCLLGfhhqansaisineqplsdtalaDWQAQLAW 425
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKnLSLELKQGEKIALLGRSGSGKSTLLQLLTG----------------------DLKPQQGE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IpqhatffyrsvaenlRLAKPDASqaELDEAASKAgaLEFITALPDGFDTLLGEQ-GEGLSGGQKQRIALARAFLKNAPV 504
Cdd:cd03247 59 I---------------TLDGVPVS--DLEKALSSL--ISVLNQRPYLFDTTLRNNlGRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 505 LMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESG 563
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
347-561 |
1.43e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.07 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQP---LSDTALADWQ 420
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTalrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDissLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 AQ-LAWIPQhatFF----YRSVAEN----LRLAKPDASQAE--LDEAASKAGALEFITALPDgfdtllgeQgegLSGGQK 489
Cdd:COG1136 85 RRhIGFVFQ---FFnllpELTALENvalpLLLAGVSRKERRerARELLERVGLGDRLDHRPS--------Q---LSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 490 QRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKHADKIYVMQQGHIVE 561
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
348-563 |
2.42e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.10 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 348 QLNALTFHYPEtNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTaladwQAQLAWIP 427
Cdd:cd03235 1 EVEDLTVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 428 QHATF---FYRSVAENLRLA---------KPDASQ-AELDEAASKAGALEFItalpdgfDTLLGEqgegLSGGQKQRIAL 494
Cdd:cd03235 75 QRRSIdrdFPISVRDVVLMGlyghkglfrRLSKADkAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 495 ARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREY-AKDHLVLVIAHRLNTV-KHADKIYVMqQGHIVESG 563
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLL-NRTVVASG 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
365-579 |
7.63e-31 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 128.61 E-value: 7.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAI----------------------------SINEQPLS---- 412
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHivfknehtndmtneqdyqgdeeqnvgmkNVNEFSLTkegg 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 413 ----------------------DTALADWQAQLAWIPQHATFFYRSVAENLRLAKPDASQAELDEAASKAGALEFITALP 470
Cdd:PTZ00265 1266 sgedstvfknsgkilldgvdicDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLP 1345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 471 DGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAK--DHLVLVIAHRLNTVKHA 548
Cdd:PTZ00265 1346 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRS 1425
|
250 260 270
....*....|....*....|....*....|....*..
gi 1952200779 549 DKIYVM----QQGHIVES-GQYQQ-LTEQAGLFAKLV 579
Cdd:PTZ00265 1426 DKIVVFnnpdRTGSFVQAhGTHEElLSVQDGVYKKYV 1462
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
347-563 |
4.40e-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: 117.99 E-value: 4.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPE---TNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQ---PLSDTALADWQ 420
Cdd:cd03257 2 LEVKNLSVSFPTgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 AQLAWIPQHAtffYRS----------VAENLRLAKPDASQAELDEAASKA-----GALEFITALPDGfdtllgeqgegLS 485
Cdd:cd03257 82 KEIQMVFQDP---MSSlnprmtigeqIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPHE-----------LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 486 GGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKH-ADKIYVMQQGHIVES 562
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
.
gi 1952200779 563 G 563
Cdd:cd03257 228 G 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
347-563 |
4.68e-30 |
|
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: 117.82 E-value: 4.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHAT--FFYRSVAE-------NLRLAKPDAsQAELDEAASKAGALEFITALPdgFDtllgeqgegLSGGQKQRIALARA 497
Cdd:COG1122 81 FQNPDdqLFAPTVEEdvafgpeNLGLPREEI-RERVEEALELVGLEHLADRPP--HE---------LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 498 FLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVaELADRVIVLDDGRIVADG 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
348-558 |
6.62e-30 |
|
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: 116.80 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 348 QLNALTFHYPETNEGV-TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHAT--FFYRSVAE-------NLRLAKPDAsQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIALARA 497
Cdd:cd03225 81 FQNPDdqFFGPTVEEevafgleNLGLPEEEI-EERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 498 FLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTVK-HADKIYVMQQGH 558
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
347-563 |
1.36e-29 |
|
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: 122.70 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEG----VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDT---ALADW 419
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 420 QAQLAWIPQH--ATFF-----YRSVAENLRLAKpDASQAELDEAAskAGALEFItALPDGFDTLLGEQgegLSGGQKQRI 492
Cdd:COG1123 341 RRRVQMVFQDpySSLNprmtvGDIIAEPLRLHG-LLSRAERRERV--AELLERV-GLPPDLADRYPHE---LSGGQRQRV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 493 ALARAFLKNAPVLMLDEPTAHLD-SQTEHLINQaIREYAKDH--LVLVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDvSVQAQILNL-LRDLQRELglTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
347-559 |
2.69e-29 |
|
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: 115.28 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQP---LSDTALADWQ 420
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiskLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 A-QLAWIPQhatFF----YRSVAEN----LRLAKPDASQAELD--EAASKAGALEFITALPDgfdtllgeQgegLSGGQK 489
Cdd:cd03255 81 RrHIGFVFQ---SFnllpDLTALENvelpLLLAGVPKKERRERaeELLERVGLGDRLNHYPS--------E---LSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 490 QRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKD--HLVLVIAHRLNTVKHADKIYVMQQGHI 559
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
366-586 |
8.89e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 122.54 E-value: 8.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 366 INLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLrlaK 445
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---D 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 446 P--DASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLIN 523
Cdd:PLN03130 1335 PfnEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ 1414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 524 QAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQL-TEQAGLFAKLV-SQGDAHA 586
Cdd:PLN03130 1415 KTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVqSTGAANA 1479
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
376-586 |
1.75e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 121.62 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 376 IAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLrlaKP--DASQAEL 453
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPfsEHNDADL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 454 DEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH 533
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSC 1421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 534 LVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQ-LTEQAGLFAKLV-SQGDAHA 586
Cdd:PLN03232 1422 TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQElLSRDTSAFFRMVhSTGPANA 1476
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
346-561 |
1.91e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.03 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 346 HIQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAladwqAQ 422
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTaldDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 423 LAWIPQHATFF-YRSVAENLRLA--KPDASQAELDEAASKAGAL----EFITALPDgfdtllgeQgegLSGGQKQRIALA 495
Cdd:COG1116 82 RGVVFQEPALLpWLTVLDNVALGleLRGVPKAERRERARELLELvglaGFEDAYPH--------Q---LSGGMRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 496 RAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAH------RLntvkhADKIYVMQQ--GHIVE 561
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
347-568 |
2.19e-28 |
|
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: 118.85 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYP-ETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLG---FHHQANSAISINEQPLSDTALADWQAQ 422
Cdd:COG1123 5 LEVRDLSVRYPgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 423 LAWIPQHAT--FFYRSVAENLR--LAKPDASQAELDEAASKAgaLEFItalpdGFDTLLGEQGEGLSGGQKQRIALARAF 498
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAeaLENLGLSRAEARARVLEL--LEAV-----GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 499 LKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQQL 568
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
347-561 |
2.90e-28 |
|
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: 112.57 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTaladwQAQL 423
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHATFF-YRSVAEN----LRLAKPDASQA--ELDEAASKAGALEFITALPDgfdtllgeQgegLSGGQKQRIALAR 496
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNvalgLELQGVPKAEAreRAEELLELVGLSGFENAYPH--------Q---LSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 497 AFLKNAPVLMLDEPTAHLDSQTEHLINQAIRE-YAKDHL-VLVIAHRLN-TVKHADKIYVMQQ--GHIVE 561
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiWRETGKtVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
347-539 |
3.43e-28 |
|
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: 111.80 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETnEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDtALADWQAQLAWI 426
Cdd:COG4133 3 LEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PqHATFFYR--SVAENL----RLAKPDASQAELDEAASKAGalefitaLPDGFDTLLGEqgegLSGGQKQRIALARAFLK 500
Cdd:COG4133 81 G-HADGLKPelTVRENLrfwaALYGLRADREAIDEALEAVG-------LAGLADLPVRQ----LSAGQKRRVALARLLLS 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1952200779 501 NAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIA 539
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
347-568 |
4.68e-28 |
|
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: 112.27 E-value: 4.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 P-------QHATFFYRSVAENLRLAKPD---ASQAELDEAASKagALEfITALPDGFDTLLGeqGEGLSGGQKQRIALAR 496
Cdd:cd03260 80 RrrvgmvfQKPNPFPGSIYDNVAYGLRLhgiKLKEELDERVEE--ALR-KAALWDEVKDRLH--ALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 497 AfLKNAP-VLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:cd03260 155 A-LANEPeVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
347-572 |
2.79e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 110.53 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQP---LSDTALADWQAQL 423
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtaLRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHatfFY----RSVAENL---RLAK--------PDASQAEldeaasKAGALEFITALpdGFDTLLGEQGEGLSGGQ 488
Cdd:COG3638 83 GMIFQQ---FNlvprLSVLTNVlagRLGRtstwrsllGLFPPED------RERALEALERV--GLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 489 KQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIA--HRLNTV-KHADKIYVMQQGHIVESGQY 565
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVnlHQVDLArRYADRIIGLRDGRVVFDGPP 231
|
....*..
gi 1952200779 566 QQLTEQA 572
Cdd:COG3638 232 AELTDAV 238
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
347-563 |
3.33e-27 |
|
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: 109.15 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETnEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADWQAQLAWI 426
Cdd:cd03259 1 LELKGLSKTYGSV-RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFF-YRSVAEN----LRLAKPDASQAE--LDEAASKAGALEFITALPDGfdtllgeqgegLSGGQKQRIALARAFL 499
Cdd:cd03259 78 FQDYALFpHLTVAENiafgLKLRGVPKAEIRarVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 500 KNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH---LVLVIAHRLNTVKHADKIYVMQQGHIVESG 563
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELgitTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
250-579 |
3.46e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 114.30 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 250 KVAFLSSFALEFLATISVALVAVIIG-FRLFFGTLDFATGFVVLLLAPEFYLPLRQMGTHYHaklEGISAAADMVDIINQ 328
Cdd:PLN03232 518 KAQLLSAFNSFILNSIPVVVTLVSFGvFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLS---QVVNANVSLQRIEEL 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 329 SDADEHVGSSKLEL----PIKHIQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGfhhqansai 404
Cdd:PLN03232 595 LLSEERILAQNPPLqpgaPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------- 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 405 sinEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPdaSQAELDEAASKAGALEFITALPDGFD-TLLGEQGEG 483
Cdd:PLN03232 666 ---ELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSD--FESERYWRAIDVTALQHDLDLLPGRDlTEIGERGVN 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEH-LINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVES 562
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHqVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
330
....*....|....*..
gi 1952200779 563 GQYQQLTEQAGLFAKLV 579
Cdd:PLN03232 821 GTFAELSKSGSLFKKLM 837
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
347-568 |
5.80e-26 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 106.43 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQA---QL 423
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHATFFYR-SVAENLrlAKPDASQAELDEAASKAGALEFITA--LPDGFDTLLGEqgegLSGGQKQRIALARAFLK 500
Cdd:cd03261 80 GMLFQSGALFDSlTVFENV--AFPLREHTRLSEEEIREIVLEKLEAvgLRGAEDLYPAE----LSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 501 NAPVLMLDEPTAHLDSQTEHLINQAIREY--AKDHLVLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQQL 568
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
347-572 |
7.50e-26 |
|
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: 106.11 E-value: 7.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQP---LSDTALADWQAQL 423
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHATFFYR-SVAENL---RLAK--PDASQAELDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARA 497
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVlsgRLGRrsTWRSLFGLFPKEEKQRALAALERV--GLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 498 FLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIA--HRLNTVK-HADKIYVMQQGHIVESGQYQQLTEQA 572
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVslHQVDLAReYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
347-569 |
2.22e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.84 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNegvTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALAD------WQ 420
Cdd:COG3840 2 LRLDDLTYRYGDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvsmlFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 aqlawipQHATFFYRSVAENLRLA-----KPDASQ-AELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIAL 494
Cdd:COG3840 79 -------ENNLFPHLTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 495 ARAFLKNAPVLMLDEPTAHLD----SQTEHLINQAIREYAKdhLVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLT 569
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGL--TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
347-572 |
3.31e-25 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 104.69 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDT---ALADWQAQL 423
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHATFFYR-SVAENL---RLAKPDASQAELD--EAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARA 497
Cdd:TIGR02315 82 GMIFQHYNLIERlTVLENVlhgRLGYKPTWRSLLGrfSEEDKERALSALERV--GLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 498 FLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIA--HRLNTVK-HADKIYVMQQGHIVESGQYQQLTEQA 572
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIInlHQVDLAKkYADRIVGLKAGEIVFDGAPSELDDEV 237
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
347-563 |
5.46e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.34 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETnEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADWQAQLAWI 426
Cdd:COG3842 6 LELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--TGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQH-ATFFYRSVAEN----LRLAKpdASQAELDEAASKAGAL----EFITALPDgfdtllgeQgegLSGGQKQRIALARA 497
Cdd:COG3842 83 FQDyALFPHLTVAENvafgLRMRG--VPKAEIRARVAELLELvgleGLADRYPH--------Q---LSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 498 FLKNAPVLMLDEPTAHLDSQT-EHLINQaIREyakdhlvlvIAHRLNT----VKH--------ADKIYVMQQGHIVESG 563
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLrEEMREE-LRR---------LQRELGItfiyVTHdqeealalADRIAVMNDGRIEQVG 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
347-557 |
6.91e-25 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 102.79 E-value: 6.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQ---- 422
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 423 LAWIPQHATFFYRSVAENLRLAKPDASQAEldEAASKAGALE-FITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKN 501
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRY--KAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 502 APVLMLDEPTAHLDSQ-TEHLINQAIREYAKD--HLVLVIAHRLNTVKHADKIYVMQQG 557
Cdd:cd03290 159 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
365-568 |
9.35e-25 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 105.95 E-value: 9.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTA----LADWQAQLAWIPQHATFF-YRSVAE 439
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSArgifLPPHRRRIGYVFQEARLFpHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 440 NL----RLAKPDASQAELDEAaskagalefITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLD 515
Cdd:COG4148 97 NLlygrKRAPRAERRISFDEV---------VELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 516 SQTehliNQAIREY---AKDHL---VLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:COG4148 166 LAR----KAEILPYlerLRDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
347-558 |
1.43e-24 |
|
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: 100.72 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPEtNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW- 425
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 --IPQHATFFYRSVAENLRLakpdasqaeldeaaskagalefitalpdgfdtllgeqgeGLSGGQKQRIALARAFLKNAP 503
Cdd:cd03229 80 mvFQDFALFPHLTVLENIAL---------------------------------------GLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 504 VLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKH-ADKIYVMQQGH 558
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
347-563 |
1.74e-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: 102.27 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQP---LSDTALADWQ 420
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTalkDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 AQLAWIPQHATFFY-RSVAEN----LRLAKpdASQAELDEAASKAgaLEFItALPDGFDTLLGEqgegLSGGQKQRIALA 495
Cdd:cd03258 82 RRIGMIFQHFNLLSsRTVFENvalpLEIAG--VPKAEIEERVLEL--LELV-GLEDKADAYPAQ----LSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 496 RAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAK--DHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEG 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
215-579 |
2.00e-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: 108.88 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 215 LQGLTQLKLFN---ATKRELNSISQisddyrgATMGVLK-VAFLSSFAL------EFLATISVALVAVIIGFRlffGTLD 284
Cdd:TIGR00957 503 LNGIKVLKLYAwelAFLDKVEGIRQ-------EELKVLKkSAYLHAVGTftwvctPFLVALITFAVYVTVDEN---NILD 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 285 FATGFVVLLLAPEFYLPLRQMGThyhaKLEGISAAADMVDIINQSDADEHVGSSKLEL-PIKHIQLNALTFH-------- 355
Cdd:TIGR00957 573 AEKAFVSLALFNILRFPLNILPM----VISSIVQASVSLKRLRIFLSHEELEPDSIERrTIKPGEGNSITVHnatftwar 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 356 -YPETNEGVTdinLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISIneqplsdtaladwQAQLAWIPQHATFFY 434
Cdd:TIGR00957 649 dLPPTLNGIT---FSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-------------KGSVAYVPQQAWIQN 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 435 RSVAENLRLAK---PDASQAELdEAASKAGALEFitaLPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPT 511
Cdd:TIGR00957 713 DSLRENILFGKalnEKYYQQVL-EACALLPDLEI---LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 512 AHLDSQT-EHLINQAI--REYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLV 579
Cdd:TIGR00957 789 SAVDAHVgKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
363-571 |
2.10e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.54 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATF-FYRSVAENL 441
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 RL------AKPDASQAELDEAASKAGALEfitalpdgfdtLLGEQGEGLSGGQKQRIALARAFL------KNAPVLMLDE 509
Cdd:PRK13548 98 AMgraphgLSRAEDDALVAAALAQVDLAH-----------LAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 510 PTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLN-TVKHADKIYVMQQGHIVESGQYQQ-LTEQ 571
Cdd:PRK13548 167 PTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEvLTPE 232
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
32-319 |
2.17e-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: 103.40 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 32 LSISLGTLNALLMIASCYLLANAAHQVmFEQANLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEK 111
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLIDDV-IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 112 LSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGH 191
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 192 KAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVA 271
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1952200779 272 VIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQMGTHYHAKLEGISAA 319
Cdd:cd07346 242 LYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
365-563 |
4.23e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 100.81 E-value: 4.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFD---CLLGFHHQANSAISINEQPLSDtalADWQAQLAWIPQHATFF-YRSVAEN 440
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDaisGRVEGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILLpGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 LRLAKPDASQAELDEAASKAgaLEFITALPDGFDTLLGEQG-EGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKK--RVEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1952200779 520 HLINQAIREYAK-DHLVLVIAH--RLNTVKHADKIYVMQQGHIVESG 563
Cdd:cd03234 180 LNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
365-570 |
6.87e-24 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 100.20 E-value: 6.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADWQ---AQLAWIPQHATFFYR-SVAEN 440
Cdd:cd03224 18 GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI--TGLPPHErarAGIGYVPEGRRIFPElTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 LRLA----KPDASQAELDEAaskagaLEFITALPDgfdtLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDS 516
Cdd:cd03224 96 LLLGayarRRAKRKARLERV------YELFPRLKE----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 517 QTEHLINQAIREYAKDHL-VLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQQLTE 570
Cdd:cd03224 166 KIVEEIFEAIRELRDEGVtILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
365-563 |
8.43e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.96 E-value: 8.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATF-FYRSVAENLRL 443
Cdd:COG4559 19 DVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTVEEVVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 444 ------AKPDASQAELDEAASKAGALEfitalpdgfdtLLGEQGEGLSGGQKQRIALARAF--LKNAP-----VLMLDEP 510
Cdd:COG4559 99 graphgSSAAQDRQIVREALALVGLAH-----------LAGRSYQTLSGGEQQRVQLARVLaqLWEPVdggprWLFLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 511 TAHLDSQTEHLINQAIREYAKDHL-VLVIAHRLN-TVKHADKIYVMQQGHIVESG 563
Cdd:COG4559 168 TSALDLAHQHAVLRLARQLARRGGgVVAVLHDLNlAAQYADRILLLHQGRLVAQG 222
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
32-302 |
1.32e-23 |
|
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: 100.80 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 32 LSISLGTLNALLMIASCYLLANAAhQVMFEQANL--QAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLL 109
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVLGRIL-DVLLPDGDPetQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 110 EKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILV 189
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 190 GHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVAL 269
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1952200779 270 VAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPL 302
Cdd:pfam00664 242 ALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
376-579 |
1.56e-23 |
|
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: 99.98 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 376 IAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKpDASQAELDE 455
Cdd:cd03288 50 VGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 456 AASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLV 535
Cdd:cd03288 129 ALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1952200779 536 LVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQA-GLFAKLV 579
Cdd:cd03288 209 VTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
347-563 |
7.59e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.15 E-value: 7.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETnEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADwqAQLAWI 426
Cdd:COG3839 4 LELENVSKSYGGV-EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQ------HATffyrsVAEN----LRLAKpdASQAELDEAASK-AGALEfITAL----PDGfdtllgeqgegLSGGQKQR 491
Cdd:COG3839 81 FQsyalypHMT-----VYENiafpLKLRK--VPKAEIDRRVREaAELLG-LEDLldrkPKQ-----------LSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 492 IALARAFLKNAPVLMLDEPTAHLDSqteHLINQAIREYAKDHlvlviaHRLNT----VKH--------ADKIYVMQQGHI 559
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDA---KLRVEMRAEIKRLH------RRLGTttiyVTHdqveamtlADRIAVMNDGRI 212
|
....
gi 1952200779 560 VESG 563
Cdd:COG3839 213 QQVG 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
250-578 |
1.05e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 103.28 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 250 KVAFLSSFALEFLATISVALVAVIIG-FRLFFGTLDFATGFVVL-----LLAPEFYLP--LRQMGTHYHA--KLEGISAA 319
Cdd:PLN03130 518 KAQLLSAFNSFILNSIPVLVTVVSFGvFTLLGGDLTPARAFTSLslfavLRFPLFMLPnlITQAVNANVSlkRLEELLLA 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 320 ADMVDIINQSdadehvgsskLELPIKHIQLNALTFHYPETNEGVT--DINLTLPSSGLIAFVGESGSGKSTLFDCLLGfh 397
Cdd:PLN03130 598 EERVLLPNPP----------LEPGLPAISIKNGYFSWDSKAERPTlsNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-- 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 398 hqansaisinEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLAKPdaSQAELDEAASKAGALEF-ITALPDGFDTL 476
Cdd:PLN03130 666 ----------ELPPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSP--FDPERYERAIDVTALQHdLDLLPGGDLTE 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 477 LGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSqteHLINQAIREYAKDHL-----VLViAHRLNTVKHADKI 551
Cdd:PLN03130 734 IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA---HVGRQVFDKCIKDELrgktrVLV-TNQLHFLSQVDRI 809
|
330 340
....*....|....*....|....*..
gi 1952200779 552 YVMQQGHIVESGQYQQLTEQAGLFAKL 578
Cdd:PLN03130 810 ILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
363-563 |
1.06e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 95.70 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFH--HQANSAISINEQPLSDTAladWQAQLAWIPQHATFF-YRSVAE 439
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDKRS---FRKIIGYVPQDDILHpTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 440 NLRLAkpdasqAELdeaaskagalefitalpdgfdtllgeqgEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:cd03213 102 TLMFA------AKL----------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1952200779 520 HLINQAIREYAKDH-LVLVIAHRLNT--VKHADKIYVMQQGHIVESG 563
Cdd:cd03213 148 LQVMSLLRRLADTGrTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
365-568 |
1.34e-22 |
|
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: 99.42 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTA----LADWQAQLAWIPQHATFF-YRSVAE 439
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgifLPPEKRRIGYVFQEARLFpHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 440 NLR--LAKPDASQAELDEAAskagalefITALPdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:TIGR02142 95 NLRygMKRARPSERRISFER--------VIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 518 TEHLINQAIREYAkDHL---VLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:TIGR02142 166 RKYEILPYLERLH-AEFgipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
347-559 |
1.92e-22 |
|
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: 95.67 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPEtNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDT--ALADWQAQLA 424
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDkkNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHATFF-YRSVAENLRLA-------KPDASQAELDEAASKAGALEFITALPDGfdtllgeqgegLSGGQKQRIALAR 496
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLApikvkgmSKAEAEERALELLEKVGLADKADAYPAQ-----------LSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 497 AFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTVKH-ADKIYVMQQGHI 559
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
347-563 |
2.20e-22 |
|
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: 95.64 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNegvTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWi 426
Cdd:cd03298 1 VRLDKIRFSYGEQP---MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFFYRSVAENLRLAK-PDASQAELDEAASKAGALEFitalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGLsPGLKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 506 MLDEPTAHLD----SQTEHLINQAIREyaKDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:cd03298 151 LLDEPFAALDpalrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
347-571 |
6.56e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.14 E-value: 6.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNeGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsDTALADWQAQLAWI 426
Cdd:COG1118 3 IEVRNISKRFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQH-ATFFYRSVAEN----LRLAKPdasqaelDEAASKAGALEfitalpdgfdtLLGE-QGEG--------LSGGQKQRI 492
Cdd:COG1118 81 FQHyALFPHMTVAENiafgLRVRPP-------SKAEIRARVEE-----------LLELvQLEGladrypsqLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 493 ALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKD-HLVLVIahrlntVKH--------ADKIYVMQQGHIVESG 563
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVF------VTHdqeealelADRVVVMNQGRIEQVG 216
|
....*...
gi 1952200779 564 QYQQLTEQ 571
Cdd:COG1118 217 TPDEVYDR 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
352-583 |
8.57e-22 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 95.69 E-value: 8.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 352 LTFHYPETNEGV-TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHqANSAISINEQPLSDTALADWQAQLAWIPQHA 430
Cdd:cd03289 8 LTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 431 TFFYRSVAENLrlaKPDA--SQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLD 508
Cdd:cd03289 87 FIFSGTFRKNL---DPYGkwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 509 EPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLVSQGD 583
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSD 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
346-583 |
1.23e-21 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 99.98 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 346 HIQLNALTFHYPETNEGV-TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHhQANSAISINEQPLSDTALADWQAQLA 424
Cdd:TIGR01271 1217 QMDVQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHATFFYRSVAENLrlaKPDA--SQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNA 502
Cdd:TIGR01271 1296 VIPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 503 PVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLVSQG 582
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAA 1452
|
.
gi 1952200779 583 D 583
Cdd:TIGR01271 1453 D 1453
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
347-563 |
1.32e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 94.95 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPlsdTALADWQAQLAWI 426
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP---TRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQ--HATFFYRSVAEN------------LRLAKPDaSQAELDEAASKAGALEFitalpdgFDTLLGEqgegLSGGQKQRI 492
Cdd:PRK15056 84 PQseEVDWSFPVLVEDvvmmgryghmgwLRRAKKR-DRQIVTAALARVDMVEF-------RHRQIGE----LSGGQKKRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 493 ALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREY-AKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESG 563
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
347-564 |
1.59e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEgVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:PRK11231 3 LRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATF-----------FYRSVAENL--RLAKPDasQAELDEAASKAGALEFItalpdgfDTLLGEqgegLSGGQKQRIA 493
Cdd:PRK11231 82 PQHHLTpegitvrelvaYGRSPWLSLwgRLSAED--NARVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 494 LARAFLKNAPVLMLDEPTAHLD--SQTEHLinQAIREY-AKDHLVLVIAHRLNTV-KHADKIYVMQQGHIVESGQ 564
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDinHQVELM--RLMRELnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGT 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
376-570 |
1.90e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 99.47 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 376 IAFVGESGSGKSTLfdcLLGFHHQAN---SAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLrlaKP--DASQ 450
Cdd:PTZ00243 1339 VGIVGRTGSGKSTL---LLTFMRMVEvcgGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASS 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 451 AELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLK--NAPVLMlDEPTAHLDSQTEHLINQAIRE 528
Cdd:PTZ00243 1413 AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkgSGFILM-DEATANIDPALDRQIQATVMS 1491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1952200779 529 YAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTE 570
Cdd:PTZ00243 1492 AFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
364-568 |
2.87e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.54 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 364 TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADwqAQLAWIPQH-ATFFYRSVAENL- 441
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHyALFRHMTVFDNIa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 -------RLAKPDAsqAELDEAASKAgaLEFI--TALPDGFDTllgeqgeGLSGGQKQRIALARAFLKNAPVLMLDEPTA 512
Cdd:PRK10851 97 fgltvlpRRERPNA--AAIKAKVTQL--LEMVqlAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 513 HLDSQTEHLINQAIR---EYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK10851 166 ALDAQVRKELRRWLRqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
352-540 |
2.95e-21 |
|
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: 91.93 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 352 LTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSdtaLADWQAQLAWIPQHAT 431
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 432 --FFYRSVAENLRLAKPDAS--QAELDEAASKAGALEFITALPdgFDtllgeqgegLSGGQKQRIALARAFLKNAPVLML 507
Cdd:cd03226 82 yqLFTDSVREELLLGLKELDagNEQAETVLKDLDLYALKERHP--LS---------LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190
....*....|....*....|....*....|....
gi 1952200779 508 DEPTAHLDSQTEHLINQAIREYAK-DHLVLVIAH 540
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAqGKAVIVITH 184
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
346-563 |
3.26e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.14 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 346 HIQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCllgfhhqansaisIN--EQP---------- 410
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTaldDVSLTIEKGEIFGIIGYSGAGKSTLIRC-------------INllERPtsgsvlvdgv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 411 ----LSDTALADWQAQLAWIPQHatfFY----RSVAEN----LRLAKPDASQ-----AELdeaaskagaLEFI------T 467
Cdd:COG1135 68 dltaLSERELRAARRKIGMIFQH---FNllssRTVAENvalpLEIAGVPKAEirkrvAEL---------LELVglsdkaD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 468 ALPDgfdtllgeQgegLSGGQKQRIALARAfLKNAP-VLMLDEPTAHLDSQTEH----LINQAIREYakdHL-VLVIAHR 541
Cdd:COG1135 136 AYPS--------Q---LSGGQKQRVGIARA-LANNPkVLLCDEATSALDPETTRsildLLKDINREL---GLtIVLITHE 200
|
250 260
....*....|....*....|...
gi 1952200779 542 LNTVKH-ADKIYVMQQGHIVESG 563
Cdd:COG1135 201 MDVVRRiCDRVAVLENGRIVEQG 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
365-563 |
3.42e-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: 92.78 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADWQAQLAWIPQ-HATFFYRSVAEN--- 440
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVPQnYALFPHMTVYKNiay 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 -LRLAKPDASQ--AELDEAAskagalEFItalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:cd03299 95 gLKKRKVDKKEieRKVLEIA------EML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 518 T-EHLINQ---AIREYakDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:cd03299 164 TkEKLREElkkIRKEF--GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVG 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
347-561 |
4.36e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPEtNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGfhhqansaisiNEQPLSDTAlaDW--QAQLA 424
Cdd:COG0488 316 LELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-----------ELEPDSGTV--KLgeTVKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHATFFY--RSVAENLRLAKPDASQAEldeAASKAGALEFItalPDGFDTLLGEqgegLSGGQKQRIALARAFLKNA 502
Cdd:COG0488 382 YFDQHQEELDpdKTVLDELRDGAPGGTEQE---VRGYLGRFLFS---GDDAFKPVGV----LSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 503 PVLMLDEPTAHLDSQTEHLINQAIREY--AkdhlVLVIAH-R--LNTVkhADKIYVMQQGHIVE 561
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALDDFpgT----VLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
363-571 |
4.63e-21 |
|
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: 92.40 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADwqAQLAWIPQH-ATFFYRSVAEN- 440
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHyALFRHMTVFDNv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 ---LRlAKPDASQAELDEAASKAGALEFITALpDGFDTLLGEQgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:cd03296 96 afgLR-VKPRSERPPEAEIRAKVHELLKLVQL-DWLADRYPAQ---LSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 518 TEHLINQAIREYAKD-HL--VLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQ 571
Cdd:cd03296 171 VRKELRRWLRRLHDElHVttVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
365-568 |
4.72e-21 |
|
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: 92.35 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQP---LSDTALADWQAQLAWIPQHATFF-YRSVAEN 440
Cdd:COG1127 23 GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRRRIGMLFQGGALFdSLTVFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 LRLA---KPDASQAELDEAASKAgaLEFItALPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:COG1127 103 VAFPlreHTDLSEAEIRELVLEK--LELV-GLPGAADKMPSE----LSGGMRKRVALARALALDPEILLYDEPTAGLDPI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 518 TEHLINQAIREYaKDHL---VLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:COG1127 176 TSAVIDELIREL-RDELgltSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
348-564 |
4.79e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 92.20 E-value: 4.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 348 QLNALTFHYPETnEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAlADWQAQ--LAW 425
Cdd:TIGR03410 2 EVSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP-PHERARagIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHATFFYR-SVAENLRL---AKPDASQAELDEAaskagaLEFITALPDgfdtLLGEQGEGLSGGQKQRIALARAFLKN 501
Cdd:TIGR03410 80 VPQGREIFPRlTVEENLLTglaALPRRSRKIPDEI------YELFPVLKE----MLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 502 APVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQ 564
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
362-571 |
5.56e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 362 GVT---DINLTLPSsGLI-AFVGESGSGKSTLFDCLLGFHhQANS-AISINEQPLS-DTALADWQAQLAWIPQHATFF-Y 434
Cdd:COG1129 16 GVKaldGVSLELRP-GEVhALLGENGAGKSTLMKILSGVY-QPDSgEILLDGEPVRfRSPRDAQAAGIAIIHQELNLVpN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 435 RSVAENLRLAKPDASQAELDEAASKAGALEFITALpdGFD----TLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEP 510
Cdd:COG1129 94 LSVAENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 511 TAHL-DSQTEHLINQaIREYAKDHL-VLVIAHRLNTVK-HADKIYVMQQGHIVESGQYQQLTEQ 571
Cdd:COG1129 168 TASLtEREVERLFRI-IRRLKAQGVaIIYISHRLDEVFeIADRVTVLRDGRLVGTGPVAELTED 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
347-563 |
6.36e-21 |
|
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: 91.10 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETnEGVTDINLTLPSsGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALAdWQAQLAWI 426
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFFYR-SVAENL----RLAKPDASQ--AELDEAASKAGalefitaLPDGFDTLLGeqgeGLSGGQKQRIALARAFL 499
Cdd:cd03264 78 PQEFGVYPNfTVREFLdyiaWLKGIPSKEvkARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 500 KNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVK-HADKIYVMQQGHIVESG 563
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
367-559 |
1.24e-20 |
|
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: 90.69 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 367 NLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQplSDTALADWQAQLAWIPQ-HATFFYRSVAENLRLA- 444
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQeNNLFAHLTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 445 ----KPDASQAE-LDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:TIGR01277 96 hpglKLNAEQQEkVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1952200779 520 H----LINQAIREyaKDHLVLVIAHRL-NTVKHADKIYVMQQGHI 559
Cdd:TIGR01277 165 EemlaLVKQLCSE--RQRTLLMVTHHLsDARAIASQIAVVSQGKI 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
347-564 |
1.54e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.50 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDtaLADWQaqlawI 426
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSR--LKRRE-----I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQ-----------HATFFYRSVAENLRLA------KPDASQAELDEAASKAGALEFITALPDgfdtllgeqgEgLSGGQK 489
Cdd:COG2884 75 PYlrrrigvvfqdFRLLPDRTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH----------E-LSGGEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 490 QRIALARAFLKNAPVLMLDEPTAHLDSQT-----EHL--INQ---AIreyakdhlvlVIA-HRLNTVKHADK-IYVMQQG 557
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETsweimELLeeINRrgtTV----------LIAtHDLELVDRMPKrVLELEDG 213
|
....*..
gi 1952200779 558 HIVESGQ 564
Cdd:COG2884 214 RLVRDEA 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
365-563 |
1.58e-20 |
|
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: 90.05 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSsGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTA----LADWQAQLAWIPQHATFF-YRSVAE 439
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 440 NLRLAKPDASQAELdeaasKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:cd03297 95 NLAFGLKRKRNRED-----RISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1952200779 520 HLINQAIREYAKD-HL-VLVIAHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:cd03297 168 LQLLPELKQIKKNlNIpVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
62-309 |
1.60e-20 |
|
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: 92.07 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 62 QANLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQ 141
Cdd:cd18544 34 QGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 142 YYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQL 221
Cdd:cd18544 114 LFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 222 KLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLP 301
Cdd:cd18544 194 QLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRP 273
|
....*...
gi 1952200779 302 LRQMGTHY 309
Cdd:cd18544 274 IRDLAEKF 281
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
57-319 |
2.01e-20 |
|
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: 91.83 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 57 QVMFEQANLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGV 136
Cdd:cd18778 28 LVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 137 EALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQ 216
Cdd:cd18778 108 ANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 217 GLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVaVIIGFRLFF-GTLDFATGFVVLLLA 295
Cdd:cd18778 188 GIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLV-LGFGGRLVLaGELTIGDLVAFLLYL 266
|
250 260
....*....|....*....|....
gi 1952200779 296 PEFYLPLRQMGTHYHAKLEGISAA 319
Cdd:cd18778 267 GLFYEPITSLHGLNEMLQRALAGA 290
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
347-563 |
3.95e-20 |
|
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: 88.81 E-value: 3.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAlADWQAQLAWI 426
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFFYRSVAENLRLAK--PDASQAELDEAaskagaLEFItalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPV 504
Cdd:cd03268 79 EAPGFYPNLTARENLRLLArlLGIRKKRIDEV------LDVV-----GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 505 LMLDEPTAHLDSQTEHLINQAIREYAKD-HLVLVIAHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
363-563 |
4.68e-20 |
|
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: 89.42 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDtaladWQAQLAW---------IPQhaTFF 433
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-----LPPHEIArlgigrtfqIPR--LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 434 YRSVAENLRLA------------KPDASQAELDEAAskAGALEFItalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKN 501
Cdd:cd03219 89 ELTVLENVMVAaqartgsglllaRARREEREARERA--EELLERV-----GLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 502 APVLMLDEPTAHLDSQ-TEHLINqAIREYAKDHL-VLVIAHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:cd03219 162 PKLLLLDEPAAGLNPEeTEELAE-LIRELRERGItVLLVEHDMDVVmSLADRVTVLDQGRVIAEG 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
317-582 |
7.83e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 94.08 E-value: 7.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 317 SAAADMVDIINQSDADEHVGSSKLELPIKHIQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGf 396
Cdd:PTZ00243 630 SPSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS- 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 397 hhqaNSAISINEQplsdtaladWQAQ-LAWIPQHATFFYRSVAENL---------RLAkpDA---SQAELDEAAskagal 463
Cdd:PTZ00243 709 ----QFEISEGRV---------WAERsIAYVPQQAWIMNATVRGNIlffdeedaaRLA--DAvrvSQLEADLAQ------ 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 464 efitaLPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLInqaIREYAKDHL---VLVIA- 539
Cdd:PTZ00243 768 -----LGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV---VEECFLGALagkTRVLAt 839
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1952200779 540 HRLNTVKHADKIYVMQQGHIVESGQYQQLTeQAGLFAKLVSQG 582
Cdd:PTZ00243 840 HQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATLAAEL 881
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
365-563 |
1.90e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 87.74 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGF-HHQANSaISINEQPL--SDTALADWQAQLAWIPQHATFF-YRSVAEN 440
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLeEPDSGT-ITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFpHLTVLEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 LRLA-----KPDASQAE------LDeaasKAGALEFITALPDgfdtllgeQgegLSGGQKQRIALARAfLKNAPVLML-D 508
Cdd:COG1126 98 VTLApikvkKMSKAEAEeramelLE----RVGLADKADAYPA--------Q---LSGGQQQRVAIARA-LAMEPKVMLfD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 509 EPTAHLDSQtehLIN---QAIREYAKDHLVLVIahrlntVKH--------ADKIYVMQQGHIVESG 563
Cdd:COG1126 162 EPTSALDPE---LVGevlDVMRDLAKEGMTMVV------VTHemgfarevADRVVFMDGGRIVEEG 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
363-563 |
2.12e-19 |
|
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: 88.17 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADWQ-AQ--LAWIPQHATFFYR-SVA 438
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI--TGLPPHRiARlgIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 ENLRLA--------------KPDASQAELDEAASKAGA-LEFItalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAP 503
Cdd:COG0411 98 ENVLVAaharlgrgllaallRLPRARREEREARERAEElLERV-----GLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 504 VLMLDEPTAHLDSQ-TEHLInQAIREYAKDHL--VLVIAHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:COG0411 173 LLLLDEPAAGLNPEeTEELA-ELIRRLRDERGitILLIEHDMDLVmGLADRIVVLDFGRVIAEG 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
347-563 |
2.15e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.76 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCL-------LGFHHQANSAISINEQPlSDTALADW 419
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKTP-SDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 420 QAQLAWIPQ------HATffyrsVAENLRLAKpdASQAELDEAASKAGALEFITALPdgfdtlLGEQGEG----LSGGQK 489
Cdd:PRK11124 81 RRNVGMVFQqynlwpHLT-----VQQNLIEAP--CRVLGLSKDQALARAEKLLERLR------LKPYADRfplhLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 490 QRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVI-AHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIvTHEVEVArKTASRVVYMENGHIVEQG 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
347-563 |
2.20e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.51 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYP-ETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW 425
Cdd:PRK13632 8 IKVENVSFSYPnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHA--TFFYRSVA-------ENLRLaKPDASQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIALAR 496
Cdd:PRK13632 88 IFQNPdnQFIGATVEddiafglENKKV-PPKKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 497 AFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAK--DHLVLVIAHRLNTVKHADKIYVMQQGHIVESG 563
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
347-563 |
2.51e-19 |
|
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: 86.54 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNeGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADwqAQLAWI 426
Cdd:cd03301 1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQ-HATFFYRSVAEN----LRLAKpdASQAELDEAASKAGALEFItalpdgfDTLLGEQGEGLSGGQKQRIALARAFLKN 501
Cdd:cd03301 78 FQnYALYPHMTVYDNiafgLKLRK--VPKDEIDERVREVAELLQI-------EHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 502 APVLMLDEPTAHLDSqteHLINQAIREYAKDHlvlviaHRLNT----VKH--------ADKIYVMQQGHIVESG 563
Cdd:cd03301 149 PKVFLMDEPLSNLDA---KLRVQMRAELKRLQ------QRLGTttiyVTHdqveamtmADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
347-572 |
5.38e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.38 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNE-GVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAW 425
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQHA--TFFYRSVA-------ENLRLAKPDAsQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIALAR 496
Cdd:PRK13635 86 VFQNPdnQFVGATVQddvafglENIGVPREEM-VERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 497 AFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYaKDHL---VLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQA 572
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQL-KEQKgitVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
346-518 |
5.59e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.84 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 346 HIQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAladwqAQ 422
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPalqDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 423 LAWIPQ-HATFFYRSVAEN----LRLAKpdasqaeLDEAASKAGALEFITalpdgfdtLLGEQGEG------LSGGQKQR 491
Cdd:COG4525 78 RGVVFQkDALLPWLNVLDNvafgLRLRG-------VPKAERRARAEELLA--------LVGLADFArrriwqLSGGMRQR 142
|
170 180
....*....|....*....|....*..
gi 1952200779 492 IALARAFLKNAPVLMLDEPTAHLDSQT 518
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALT 169
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
32-323 |
6.05e-19 |
|
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: 87.48 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 32 LSISLGTLNALLMIASCYLLANAAHQVmFEQANLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEK 111
Cdd:cd18552 3 LAILGMILVAATTAALAWLLKPLLDDI-FVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 112 LSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGH 191
Cdd:cd18552 82 LLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 192 KAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVA 271
Cdd:cd18552 162 RLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 272 VIIGFRLFFGTLDFAT--GFVVLLLApeFYLPLRQMGThYHAKLEGISAAADMV 323
Cdd:cd18552 242 WYGGYQVISGELTPGEfiSFITALLL--LYQPIKRLSN-VNANLQRGLAAAERI 292
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
347-571 |
1.07e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.32 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPetneGVT---DINLTLPSsGLI-AFVGESGSGKSTLFDCLLGFHhQANS-AISINEQPLSDT----ALA 417
Cdd:COG3845 6 LELRGITKRFG----GVVandDVSLTVRP-GEIhALLGENGAGKSTLMKILYGLY-QPDSgEILIDGKPVRIRsprdAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 418 dwqAQLAWIPQHATFFYR-SVAENLRLAKPDASQAELDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALAR 496
Cdd:COG3845 80 ---LGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGRLDRKAARARIRELSERY--GLDVDPDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 497 AFLKNAPVLMLDEPTAHLDSQ-TEHLInQAIREYAKDHL-VLVIAHRLNTVK-HADKIYVMQQGHIVESGQYQQLTEQ 571
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQeADELF-EILRRLAAEGKsIIFITHKLREVMaIADRVTVLRRGKVVGTVDTAETSEE 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
347-563 |
1.63e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.01 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNE-GVTDINLTLPSSGLIAFVGESGSGKST---LFDCLLGFHHQANSAISINEQPLSDTALADWQAQ 422
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 423 LAWIPQHA--TFFYRSVA-------ENLRLAKPDAsQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIA 493
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGddvafglENRAVPRPEM-IKIVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 494 LARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKHADKIYVMQQGHIVESG 563
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
363-568 |
1.86e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 88.59 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSaISINEQPLSDTALADWQAQLAWI------PqhatffYRS 436
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGE-IRFDGQDLDGLSRRALRPLRRRMqvvfqdP------FGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 ----------VAENLRLAKPDASQAELDEAASKAgaLEFITALPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLM 506
Cdd:COG4172 375 lsprmtvgqiIAEGLRVHGPGLSAAERRARVAEA--LEEVGLDPAARHRYPHE----FSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 507 LDEPTAHLDSQTEHLINQAIREYAKDHLV--LVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQREHGLayLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
32-305 |
2.03e-18 |
|
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: 85.92 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 32 LSISLGTLNALLMIASCYLLANA-----AHQVMFEQANLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRN 106
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLLGKAidliiEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 107 TLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFM 186
Cdd:cd18547 83 DLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 187 ILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMgvlKVAFLSSF---ALEFLA 263
Cdd:cd18547 163 KFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASF---KAQFYSGLlmpIMNFIN 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1952200779 264 TISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQM 305
Cdd:cd18547 240 NLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQI 281
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
347-560 |
2.16e-18 |
|
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: 82.48 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPetneGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSdtaladwqaql 423
Cdd:cd03216 1 LELRGITKRFG----GVKaldGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 awipqhatffYRSVAEnlrlakpdasqaeldeaASKAGaLEFITalpdgfdtllgeQgegLSGGQKQRIALARAFLKNAP 503
Cdd:cd03216 66 ----------FASPRD-----------------ARRAG-IAMVY------------Q---LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 504 VLMLDEPTAHL-DSQTEHLINQaIREYAKDHL-VLVIAHRLNTVKH-ADKIYVMQQGHIV 560
Cdd:cd03216 103 LLILDEPTAALtPAEVERLFKV-IRRLRAQGVaVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
357-568 |
2.18e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.68 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 357 PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQA---QLAWIPQH--AT 431
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 432 FFYRS-----VAENLRLAKPDASQAELDEAAS----KAGALE-FITALPDGFdtllgeqgeglSGGQKQRIALARAFLKN 501
Cdd:PRK15079 111 LNPRMtigeiIAEPLRTYHPKLSRQEVKDRVKammlKVGLLPnLINRYPHEF-----------SGGQCQRIGIARALILE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 502 APVLMLDEPTAHLD----SQTEHLINQAIREYAkdhLVLV-IAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK15079 180 PKLIICDEPVSALDvsiqAQVVNLLQQLQREMG---LSLIfIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
347-563 |
2.47e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.39 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCllgfhhqansaisIN--EQP----------- 410
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRC-------------INllERPtsgrvlvdgqd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 411 ---LSDTALADWQAQLAWIPQHatfFY----RSVAEN----LRLAKpdASQAELDEAASKAGALEFITALPDGFDTllge 479
Cdd:PRK11153 69 ltaLSEKELRKARRQIGMIFQH---FNllssRTVFDNvalpLELAG--TPKAEIKARVTELLELVGLSDKADRYPA---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 480 qgeGLSGGQKQRIALARAfLKNAP-VLMLDEPTAHLDSQTEHLINQAIREYAKD-HL-VLVIAHRLNTVKH-ADKIYVMQ 555
Cdd:PRK11153 140 ---QLSGGQKQRVAIARA-LASNPkVLLCDEATSALDPATTRSILELLKDINRElGLtIVLITHEMDVVKRiCDRVAVID 215
|
....*...
gi 1952200779 556 QGHIVESG 563
Cdd:PRK11153 216 AGRLVEQG 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
347-569 |
3.23e-18 |
|
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: 83.71 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPE-TNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHhQANS-AISINEQPLsDTALADWQAQLA 424
Cdd:cd03263 1 LQIRNLTKTYKKgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL-RPTSgTAYINGYSI-RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHATFF-YRSVAENLRLakpdasQAEL-----DEAASKAGALEFITALPDGFDTLLGEqgegLSGGQKQRIALARAF 498
Cdd:cd03263 79 YCPQFDALFdELTVREHLRF------YARLkglpkSEIKEEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 499 LKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLT 569
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
347-552 |
4.10e-18 |
|
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: 83.23 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSD---TALADWQAQL 423
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHATFFY-RSVAENLRLAKpDASQAELDEAASKAGALEFITALPDGFDTLlgeqGEGLSGGQKQRIALARAFLKNA 502
Cdd:cd03292 81 GVVFQDFRLLPdRNVYENVAFAL-EVTGVPPREIRKRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1952200779 503 PVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAhrlntvKHADKIY 552
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA------THAKELV 199
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
347-563 |
5.03e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.51 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPL--SDTALADWQAQLA 424
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WI---PQHATF---FYRSV---AENLRLAKpDASQAELDEAASKAGalefITALPDgfdtllgEQGEGLSGGQKQRIALA 495
Cdd:PRK13636 86 MVfqdPDNQLFsasVYQDVsfgAVNLKLPE-DEVRKRVDNALKRTG----IEHLKD-------KPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 496 RAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKD-HLVLVIA-HRLNTVK-HADKIYVMQQGHIVESG 563
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQG 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
356-539 |
6.08e-18 |
|
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: 82.09 E-value: 6.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 356 YPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPL--SDTALADWQAQLAWIPQHA--T 431
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQRVGLVFQDPddQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 432 FFYRSVAE-------NLRLaKPDASQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIALARAFLKNAPV 504
Cdd:TIGR01166 81 LFAADVDQdvafgplNLGL-SEAEVERRVREALTAVGASGLRERPT-----------HCLSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190
....*....|....*....|....*....|....*
gi 1952200779 505 LMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIA 539
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVIS 183
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
347-563 |
6.52e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 84.02 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNE-GVTDINLTLPSSGLIAFVGESGSGKSTL---FDCLLgfhhQANS-AISINEQplsDTALAD--W 419
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLL----LPTSgKVTVDGL---DTLDEEnlW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 420 QaqlawIPQHA--TF------FYRS-----VA---ENLRLaKPDASQAELDEAASKAGALEFITALPdgfdtllgeqgEG 483
Cdd:TIGR04520 74 E-----IRKKVgmVFqnpdnqFVGAtveddVAfglENLGV-PREEMRKRVDEALKLVGMEDFRDREP-----------HL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKHADKIYVMQQGHIVE 561
Cdd:TIGR04520 137 LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVA 216
|
..
gi 1952200779 562 SG 563
Cdd:TIGR04520 217 EG 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
347-574 |
6.54e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 84.04 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHY----PETNEGVTDINLTLPSSGLIAFVGESGSGKSTL---FDCLL----------GFHHQANSAISINE- 408
Cdd:TIGR04521 1 IKLKNVSYIYqpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLiqhLNGLLkptsgtvtidGRDITAKKKKKLKDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 409 -------------QPLSDTALADwqaqLAWIPQhatffyrsvaeNLRLakpdaSQAELDEAASKAGAL-----EFITALP 470
Cdd:TIGR04521 81 rkkvglvfqfpehQLFEETVYKD----IAFGPK-----------NLGL-----SEEEAEERVKEALELvgldeEYLERSP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 471 dgFDtllgeqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAK--DHLVLVIAHRLNTV-KH 547
Cdd:TIGR04521 141 --FE---------LSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKekGLTVILVTHSMEDVaEY 209
|
250 260 270
....*....|....*....|....*....|...
gi 1952200779 548 ADKIYVMQQGHIVESG------QYQQLTEQAGL 574
Cdd:TIGR04521 210 ADRVIVMHKGKIVLDGtprevfSDVDELEKIGL 242
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
365-560 |
1.18e-17 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 81.99 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPL---SDTALADWQAQLAWIPQ-HATFFYRSVAEN 440
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELhgaSKKQLVQLRRRIGYIFQaHNLLGFLTARQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 LRLAKPDASQAELDEAASKAGALefITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEH 520
Cdd:TIGR02982 103 VQMALELQPNLSYQEARERARAM--LEAV--GLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1952200779 521 LINQAIREYAKDH--LVLVIAHRLNTVKHADKIYVMQQGHIV 560
Cdd:TIGR02982 179 DVVELMQKLAKEQgcTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
363-563 |
1.63e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.89 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHAT----FFYRSVA 438
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSlsfeFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 E------NLRLAKPD-ASQAELDEAASKAGALEFITAlpdGFDTLlgeqgeglSGGQKQRIALARAFLKNAPVLMLDEPT 511
Cdd:PRK09536 99 EmgrtphRSRFDTWTeTDRAAVERAMERTGVAQFADR---PVTSL--------SGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 512 AHLDsqtehlINQAIR------EYAKDHLVLVIA-HRLN-TVKHADKIYVMQQGHIVESG 563
Cdd:PRK09536 168 ASLD------INHQVRtlelvrRLVDDGKTAVAAiHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
352-568 |
1.67e-17 |
|
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: 83.56 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 352 LTFHYPeTNEG----VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSA---ISINEQPLSDTALADWQA--- 421
Cdd:COG0444 7 LKVYFP-TRRGvvkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITsgeILFDGEDLLKLSEKELRKirg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 422 -QLAWIPQHAtffY----------RSVAENLRLAKpDASQAELDEAASKA-------GALEFITALPdgfdtllgeqGEg 483
Cdd:COG0444 86 rEIQMIFQDP---MtslnpvmtvgDQIAEPLRIHG-GLSKAEARERAIELlervglpDPERRLDRYP----------HE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDsqtehLINQA-----IREYAKDH-L-VLVIAHRLNTVKH-ADKIYVMQ 555
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALD-----VTIQAqilnlLKDLQRELgLaILFITHDLGVVAEiADRVAVMY 225
|
250
....*....|...
gi 1952200779 556 QGHIVESGQYQQL 568
Cdd:COG0444 226 AGRIVEEGPVEEL 238
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
363-534 |
1.87e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 81.37 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSA---ISINEQPLsdTALADWQAQLAWIPQHATFF-YRSVA 438
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSAsgeVLLNGRRL--TALPAEQRRIGILFQDDLLFpHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 ENLRLAKPD-----ASQAELDEAASKAGALEFITALPDGfdtllgeqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAH 513
Cdd:COG4136 95 ENLAFALPPtigraQRRARVEQALEEAGLAGFADRDPAT-----------LSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180
....*....|....*....|.
gi 1952200779 514 LDSQTehliNQAIREYAKDHL 534
Cdd:COG4136 164 LDAAL----RAQFREFVFEQI 180
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
347-571 |
2.36e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 82.01 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCL-----L--GFHHQANsaISINEQPL--SDTALA 417
Cdd:COG1117 12 IEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLipGARVEGE--ILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 418 DWQAQLAWIPQHATFFYRSVAEN----LRLAKpDASQAELDEAASKA--GAlefitALPDGFDTLLGEQGEGLSGGQKQR 491
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNvaygLRLHG-IKSKSELDEIVEESlrKA-----ALWDEVKDRLKKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 492 IALARAfLKNAP-VLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAH------RLntvkhADKIYVMQQGHIVESGQ 564
Cdd:COG1117 163 LCIARA-LAVEPeVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFGP 236
|
....*..
gi 1952200779 565 yqqlTEQ 571
Cdd:COG1117 237 ----TEQ 239
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
365-579 |
2.47e-17 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 82.60 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGfhhqansAISINEQPLSDTALADWQAQLAWI-P-----------QHATF 432
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILG-------ELEPSEGKIKHSGRISFSSQFSWImPgtikeniifgvSYDEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 433 FYRSVAEnlrlakpdASQAELDeaaskagalefITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTA 512
Cdd:cd03291 128 RYKSVVK--------ACQLEED-----------ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 513 HLDSQTEHLI-NQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAGLFAKLV 579
Cdd:cd03291 189 YLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
349-559 |
2.49e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.03 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 349 LNALTFHYPEtNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLS----DTALADWQAQLa 424
Cdd:PRK11247 15 LNAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAeareDTRLMFQDARL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 wIPqhatffYRSVAENLRLA-----KPDASQAeLDEAASKAGALEFITALpdgfdtllgeqgeglSGGQKQRIALARAFL 499
Cdd:PRK11247 93 -LP------WKKVIDNVGLGlkgqwRDAALQA-LAAVGLADRANEWPAAL---------------SGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 500 KNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLN-TVKHADKIYVMQQGHI 559
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
15-561 |
2.68e-17 |
|
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: 85.23 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 15 LRAFLKQYSqsasGLLKLSISLGTLNALLMIASCYLLANAAHqvmfeqANLQAVSPLLWPLAGLILVRALLVALSERVSN 94
Cdd:COG4615 4 LRLLLRESR----WLLLLALLLGLLSGLANAGLIALINQALN------ATGAALARLLLLFAGLLVLLLLSRLASQLLLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 95 RAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANyIPSVAYSALIPLAILVMIFptdYKAGLI 174
Cdd:COG4615 74 RLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLA---WLSPPL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 175 FLLTAPLIpFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQ----LKLfNATKREL---NSISQISDDYRgatmg 247
Cdd:COG4615 150 FLLTLVLL-GLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEgfkeLKL-NRRRRRAffdEDLQPTAERYR----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 248 VLKVAFLSSFALEFL--ATISVALVAVIIGFRLFFGTLDFA--TGFVVLLLapefYL--PLRQMGTHYHA---------K 312
Cdd:COG4615 223 DLRIRADTIFALANNwgNLLFFALIGLILFLLPALGWADPAvlSGFVLVLL----FLrgPLSQLVGALPTlsranvalrK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 313 LEGISAAADmvdiiNQSDADEHVGSSKLELPIKHIQLNALTFHYPETNEG----VTDINLTLpSSGLIAF-VGESGSGKS 387
Cdd:COG4615 299 IEELELALA-----AAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegftLGPIDLTI-RRGELVFiVGGNGSGKS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 388 TLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAwipqhATF--FYrsvaenL--RLAKPDAsqAELDEAAS---KA 460
Cdd:COG4615 373 TLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFS-----AVFsdFH------LfdRLLGLDG--EADPARARellER 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 461 GALEFITALPDG-FDTLlgeqgeGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ-----TEHLInQAIReyAKDHL 534
Cdd:COG4615 440 LELDHKVSVEDGrFSTT------DLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfYTELL-PELK--ARGKT 510
|
570 580
....*....|....*....|....*..
gi 1952200779 535 VLVIAHRLNTVKHADKIYVMQQGHIVE 561
Cdd:COG4615 511 VIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
347-563 |
3.54e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHY----PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTA--LADWQ 420
Cdd:PRK13637 3 IKIENLTHIYmegtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvkLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 AQLAWI---PQHATF---FYRSVA---ENLRLakpdaSQAELDEAASKAGAlefITALPdgFDTLLGEQGEGLSGGQKQR 491
Cdd:PRK13637 83 KKVGLVfqyPEYQLFeetIEKDIAfgpINLGL-----SEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 492 IALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGKCELQG 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
363-559 |
4.36e-17 |
|
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: 79.40 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQ-LAWIP----QHATFFYRSV 437
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 438 AENLRLakpdasqaeldeaaskagalefitalpdgfdtllgeqGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:cd03215 96 AENIAL-------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1952200779 518 TEHLINQAIREYAKD-HLVLVIAHRLNTVKH-ADKIYVMQQGHI 559
Cdd:cd03215 139 AKAEIYRLIRELADAgKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
347-564 |
5.31e-17 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 80.56 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALaDWQAQL 423
Cdd:COG4181 9 IELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL--FAL-DEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHATFFYRS--------VAENLRLakPdasqAEL---DEAASKAGAL-------EFITALPdgfdtllgeqgEGLS 485
Cdd:COG4181 86 RLRARHVGFVFQSfqllptltALENVML--P----LELagrRDARARARALlervglgHRLDHYP-----------AQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 486 GGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH---LVLViAHRLNTVKHADKIYVMQQGHIVES 562
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgttLVLV-THDPALAARCDRVLRLRAGRLVED 227
|
..
gi 1952200779 563 GQ 564
Cdd:COG4181 228 TA 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
357-561 |
5.48e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.80 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 357 PETNEGVTDINLTLPSSGLIAFVGESGSGKSTL---FDCLL----------GFHHQANSaisineqplSDTALADWQAQL 423
Cdd:PRK13641 17 PMEKKGLDNISFELEEGSFVALVGHTGSGKSTLmqhFNALLkpssgtitiaGYHITPET---------GNKNLKKLRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQ--HATFFYRSVAENLRLAKPDASQAElDEAASKAgaLEFITALpdGFDTLLGEQGE-GLSGGQKQRIALARAFLK 500
Cdd:PRK13641 88 SLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKEKA--LKWLKKV--GLSEDLISKSPfELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 501 NAPVLMLDEPTAHLDSQTEHLINQAIREYAKD-HLVLVIAHRLNTV-KHADKIYVMQQGHIVE 561
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
363-549 |
6.08e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHhqansaisineQPLSDTALADWQAQLAWIPQHAtffyrSVAENLR 442
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL-----------RPTSGTVRRAGGARVAYVPQRS-----EVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 443 LAKPDASQAEL------------DEAASKAGALEFItalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEP 510
Cdd:NF040873 72 LTVRDLVAMGRwarrglwrrltrDDRAAVDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1952200779 511 TAHLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTVKHAD 549
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGAtVVVVTHDLELVRRAD 186
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
347-563 |
6.47e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.28 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPL--SDTALADWQAQLA 424
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHA--TFFYRSVAE-------NLRLAKpDASQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIALA 495
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEdvafgplNLGLSK-EEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 496 RAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIA-HRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
347-558 |
7.10e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 77.49 E-value: 7.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGfhhqansaisiNEQPLSDTALADWQAQLAWI 426
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-----------ELEPDEGIVTWGSTVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQhatffyrsvaenlrlakpdasqaeldeaaskagalefitalpdgfdtllgeqgegLSGGQKQRIALARAFLKNAPVLM 506
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 507 LDEPTAHLDSQTEHLINQAIREYakDHLVLVIAH-R--LNTVkhADKIYVMQQGH 558
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
361-564 |
1.03e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 80.27 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 361 EGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdtaladwqaqlawipQHATFFYRSvaEN 440
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL----------------EYGDYKYRC--KH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 LRLAKPDASQA---------ELDEAaskagaLEFITALPDG------FDTL-----LGEQGE----GLSGGQKQRIALAR 496
Cdd:COG4167 89 IRMIFQDPNTSlnprlnigqILEEP------LRLNTDLTAEereeriFATLrlvglLPEHANfyphMLSSGQKQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 497 AFLKNAPVLMLDEPTAHLD----SQtehLINQAIREYAKDHLVLV-IAHRLNTVKH-ADKIYVMQQGHIVESGQ 564
Cdd:COG4167 163 ALILQPKIIIADEALAALDmsvrSQ---IINLMLELQEKLGISYIyVSQHLGIVKHiSDKVLVMHQGEVVEYGK 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
365-568 |
1.03e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 84.19 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGfhhqansAISINEQPLSDTALADWQAQLAWI-P-----------QHATF 432
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMG-------ELEPSEGKIKHSGRISFSPQTSWImPgtikdniifglSYDEY 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 433 FYRSVAEnlrlakpdASQAELDeaaskagalefITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTA 512
Cdd:TIGR01271 517 RYTSVIK--------ACQLEED-----------IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 513 HLDSQTEHLI-NQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQL 568
Cdd:TIGR01271 578 HLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
363-571 |
1.12e-16 |
|
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: 79.59 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADWQAQLAWIPQH-ATFFYRSVAEN- 440
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNyALFPHLTVFENi 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 ---LRLAKpdASQAELDEAASKAgaLEFItalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:cd03300 94 afgLRLKK--LPKAEIKERVAEA--LDLV-----QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 518 TEHLINQAIREyakdhlvlvIAHRLNT----VKH--------ADKIYVMQQGHIVESGQYQQLTEQ 571
Cdd:cd03300 165 LRKDMQLELKR---------LQKELGItfvfVTHdqeealtmSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-570 |
1.26e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.89 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 356 YPETNEGVTDINLTLPSSGLIAFVGESGSGKSTL---FDCLLGFHHQAN-------SAISINEQPLSDTALADWQAQLAW 425
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLLELNEEARvegevrlFGRNIYSPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQ---HATFfYRSVAENLRLAKPDASQAELDE----AASKAgalefitALPDGFDTLLGEQGEGLSGGQKQRIALARAF 498
Cdd:PRK14267 93 YPNpfpHLTI-YDNVAIGVKLNGLVKSKKELDErvewALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 499 LKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHR-LNTVKHADKIYVMQQGHIVESGQYQQLTE 570
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
347-563 |
1.67e-16 |
|
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: 79.27 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFF-YRSVAENLRLAkPDASQAELDEAASKAGALEFITALPDGfdTLLGEQGEGLSGGQKQRIALARAFLKNAPVL 505
Cdd:cd03295 81 IQQIGLFpHMTVEENIALV-PKLLKWPKEKIRERADELLALVGLDPA--EFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 506 MLDEPTAHLDSQT-EHLINQAIREYAKDHLVLV-IAHRLN-TVKHADKIYVMQQGHIVESG 563
Cdd:cd03295 158 LMDEPFGALDPITrDQLQEEFKRLQQELGKTIVfVTHDIDeAFRLADRIAIMKNGEIVQVG 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
375-563 |
1.80e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.21 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 375 LIAFVGESGSGKSTLFDCLLGFHHQANSaISINEQPLSDTALADWQAQLAWIPQHAT-FFYRSVAENLRLAKPDASQAEL 453
Cdd:PRK03695 24 ILHLVGPNGAGKSTLLARMAGLLPGSGS-IQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVFQYLTLHQPDKTRTEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 454 DEAAskagaLEFITALPdGFDTLLGEQGEGLSGGQKQRIALARAFLK-------NAPVLMLDEPTAHLDSQTEHLINQAI 526
Cdd:PRK03695 103 VASA-----LNEVAEAL-GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1952200779 527 REYAKDHL-VLVIAHRLN-TVKHADKIYVMQQGHIVESG 563
Cdd:PRK03695 177 SELCQQGIaVVMSSHDLNhTLRHADRVWLLKQGKLLASG 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
347-571 |
2.07e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.82 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHY----PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLS----DTALAD 418
Cdd:PRK13646 3 IRFDNVSYTYqkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 419 WQAQLAWIPQ--HATFFYRSVAENLrLAKPDASQAELDEAASKAgaleFITALPDGFDTLLGEQGE-GLSGGQKQRIALA 495
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREI-IFGPKNFKMNLDEVKNYA----HRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 496 RAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQQLTEQ 571
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDEnkTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
347-564 |
2.60e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.52 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCL-------LGFHHQANSAISINEQPLSDTALADW 419
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGHQFDFSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 420 QAQLAWIPQHATFFYRSVAENL--------RLAKPDAsQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQR 491
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLieapckvlGLSKEQA-REKAMKLLARLRLTDKADRFP-----------LHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 492 IALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVI-AHRLNTVKH-ADKIYVMQQGHIVESGQ 564
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIvTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
348-563 |
2.65e-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: 78.49 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 348 QLNALTFHYPETnEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADWQ-AQL--A 424
Cdd:COG0410 5 EVENLHAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI--TGLPPHRiARLgiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHATFFYR-SVAENLRLAkpdaSQAELDEAASKAgALEFITAL-PDgfdtlLGE----QGEGLSGGQKQRIALARAF 498
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLG----AYARRDRAEVRA-DLERVYELfPR-----LKErrrqRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 499 LKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVtILLVEQNARFAlEIADRAYVLERGRIVLEG 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
363-537 |
3.11e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTalaDWQAQLAWIPQHATFFYRS------ 436
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM---DEEARAKLRAKHVGFVFQSfmlipt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 --VAENLRLakPDASQAElDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHL 514
Cdd:PRK10584 103 lnALENVEL--PALLRGE-SSRQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180
....*....|....*....|....*.
gi 1952200779 515 DSQTEHLINQAIREYAKDH---LVLV 537
Cdd:PRK10584 178 DRQTGDKIADLLFSLNREHgttLILV 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
363-557 |
3.36e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.49 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADWQ-AQLAWIP--QHATFFYR-SVA 438
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--EGLPGHQiARMGVVRtfQHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 ENLRLAK---------------PDASQAELDEAASKAGALEFItalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAP 503
Cdd:PRK11300 99 ENLLVAQhqqlktglfsgllktPAFRRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 504 VLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKH-ADKIYVMQQG 557
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGiSDRIYVVNQG 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
365-561 |
3.53e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.96 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQA-----QL-------AWIPQHATf 432
Cdd:PRK10419 30 NVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQMvfqdsisAVNPRKTV- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 433 fYRSVAENLRlakpdaSQAELDEAASKAGALEFITA--LPDGFDTLLGEQgegLSGGQKQRIALARAFLKNAPVLMLDEP 510
Cdd:PRK10419 109 -REIIREPLR------HLLSLDKAERLARASEMLRAvdLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 511 TAHLDSqteHLINQAIREYAK-----DHLVLVIAHRLNTVKH-ADKIYVMQQGHIVE 561
Cdd:PRK10419 179 VSNLDL---VLQAGVIRLLKKlqqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
363-563 |
4.07e-16 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 78.32 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHA-TFFYRSVAENL 441
Cdd:TIGR03873 17 VDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVEQDSdTAVPLTVRDVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 RLAK-PDASQAELDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEH 520
Cdd:TIGR03873 97 ALGRiPHRSLWAGDSPHDAAVVDRALART--ELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1952200779 521 LINQAIREYAKDHLVLVIA-HRLN-TVKHADKIYVMQQGHIVESG 563
Cdd:TIGR03873 175 ETLALVRELAATGVTVVAAlHDLNlAASYCDHVVVLDGGRVVAAG 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
365-571 |
4.36e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFhhqansaisinEQPLSDTALADWQAQLAWIPQHATFF-YRSVAENLR- 442
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGE-----------LEPDSGEVSIPKGLRIGYLPQEPPLDdDLTVLDTVLd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 443 ---------------LAKPDASQAELDEAA---------------SKAGALefITALpdGFDTLLGEQ--GEgLSGGQKQ 490
Cdd:COG0488 85 gdaelraleaeleelEAKLAEPDEDLERLAelqeefealggweaeARAEEI--LSGL--GFPEEDLDRpvSE-LSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 491 RIALARAFLKNAPVLMLDEPTAHLDSQT-----EHLINqaiREYAkdhlVLVIAH-R--LNTVkhADKIYVMQQGHIVE- 561
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN---YPGT----VLVVSHdRyfLDRV--ATRILELDRGKLTLy 230
|
250
....*....|
gi 1952200779 562 SGQYQQLTEQ 571
Cdd:COG0488 231 PGNYSAYLEQ 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
347-568 |
5.70e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.89 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPEtNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCL-----LGFHHQANSAISINEQ----PLSDTAla 417
Cdd:PRK14239 6 LQVSDLSVYYNK-KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHniysPRTDTV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 418 DWQAQLAWIPQHATFFYRSVAEN----LRLaKPDASQAELDEAASKA--GAlefitALPDGFDTLLGEQGEGLSGGQKQR 491
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFPMSIYENvvygLRL-KGIKDKQVLDEAVEKSlkGA-----SIWDEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 492 IALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
363-568 |
5.74e-16 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 77.58 E-value: 5.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALaDWQAQL--AWIPQHATFFYR-SVAE 439
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLgiGYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 440 NLRLAkpdASQAELDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:cd03218 95 NILAV---LEIRGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 520 HLINQAIREYAKDHL-VLVIAHRL-NTVKHADKIYVMQQGHIVESGQYQQL 568
Cdd:cd03218 170 QDIQKIIKILKDRGIgVLITDHNVrETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
347-563 |
8.47e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEgVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:COG4604 2 IEIKNVSKRYGGKVV-LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFFYR-SVAEnL-----------RLAKPDasQAELDEAaskagaLEF--ITALPDGFdtlLGEqgegLSGGQKQRI 492
Cdd:COG4604 81 RQENHINSRlTVRE-LvafgrfpyskgRLTAED--REIIDEA------IAYldLEDLADRY---LDE----LSGGQRQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 493 ALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH---LVLVIaHRLN-TVKHADKIYVMQQGHIVESG 563
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgktVVIVL-HDINfASCYADHIVAMKDGRVVAQG 218
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
71-306 |
8.99e-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: 78.32 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 71 LLWPLAGLILVRALLVALS---ERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYI 147
Cdd:cd18563 42 LLLLVLGLAGAYVLSALLGilrGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 148 PSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNAT 227
Cdd:cd18563 122 PDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 228 KRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFAT--GFVVLLLapEFYLPLRQM 305
Cdd:cd18563 202 KREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTlvAFLSYLG--MFYGPLQWL 279
|
.
gi 1952200779 306 G 306
Cdd:cd18563 280 S 280
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
365-555 |
1.12e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.29 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRSVAENLRLA 444
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 445 KPDASQAElDEAASKAGALEFitALPDgfdTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQ 524
Cdd:PRK10247 105 WQIRNQQP-DPAIFLDDLERF--ALPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170 180 190
....*....|....*....|....*....|...
gi 1952200779 525 AIREYAKDH--LVLVIAHRLNTVKHADKIYVMQ 555
Cdd:PRK10247 179 IIHRYVREQniAVLWVTHDKDEINHADKVITLQ 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
366-568 |
1.25e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.71 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 366 INLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPL-SDTALADWQAQLAWIPQHATFFY--------RS 436
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIRQLRQHVGFVFqnfnlfphRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 VAENLrLAKPDASQAELDEAASKAGAlefitalpdgfdTLLGEQG---------EGLSGGQKQRIALARAFLKNAPVLML 507
Cdd:PRK11264 102 VLENI-IEGPVIVKGEPKEEATARAR------------ELLAKVGlagketsypRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 508 DEPTAHLDSQTEHLINQAIREYAKDHLVLVI-AHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
362-568 |
1.27e-15 |
|
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: 77.30 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 362 GVTDINLTLpSSGLIaFV--GESGSGKSTLFDCLLGFHHQANSAISINEQP---LSDTALADWQAQ-LAWIPQH-ATFFY 434
Cdd:cd03294 39 GVNDVSLDV-REGEI-FVimGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaaMSRKELRELRRKkISMVFQSfALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 435 RSVAENLRLAKPDASQAELDEAASKAGALEFItALPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHL 514
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELV-GLEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 515 DSqtehlinqAIREYAKDHL----------VLVIAHRLN-TVKHADKIYVMQQGHIVESGQYQQL 568
Cdd:cd03294 192 DP--------LIRREMQDELlrlqaelqktIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
365-564 |
1.34e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.53 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALAD------WQAqlawipqHATFFYRSVA 438
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAErgvgmvFQS-------YALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 EN----LRLAKpdASQAELDEAASKAGAlefITALpdgfDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHL 514
Cdd:PRK11000 94 ENmsfgLKLAG--AKKEEINQRVNQVAE---VLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 515 DSqtehlinqAIR-----EYAKDHlvlviaHRLNT----VKH--------ADKIYVMQQGHIVESGQ 564
Cdd:PRK11000 165 DA--------ALRvqmriEISRLH------KRLGRtmiyVTHdqveamtlADKIVVLDAGRVAQVGK 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
363-563 |
1.35e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAL-ADWQAQLAWIPQHATFFYR-SVAEN 440
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 LRLA---KPDASQAELDEAASKAGALEFITALPDGFdtllgeqGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:PRK10895 99 LMAVlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952200779 518 TEHLINQAIrEYAKDH--LVLVIAHRL-NTVKHADKIYVMQQGHIVESG 563
Cdd:PRK10895 172 SVIDIKRII-EHLRDSglGVLITDHNVrETLAVCERAYIVSQGHLIAHG 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
363-561 |
1.37e-15 |
|
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: 77.15 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQA-----QLAWIPQHATFFYRSV 437
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 438 AENLrLAKPDASQAELDEAASKAGALEFITAL---PDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHL 514
Cdd:TIGR02769 107 VRQI-IGEPLRHLTSLDESEQKARIAELLDMVglrSEDADKLPRQ----LSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1952200779 515 DSQTEHLINQAIREYAKDHLV--LVIAHRLNTV-KHADKIYVMQQGHIVE 561
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTayLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-563 |
1.44e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.88 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 366 INLTLPSSGLIAFVGESGSGKSTL---FDCLLGFHHQANSA--ISINEQPL--SDTALADWQAQLAW-----IPQHATFf 433
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLlrvFNRLIELYPEARVSgeVYLDGQDIfkMDVIELRRRVQMVFqipnpIPNLSIF- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 434 yRSVAENLRLAKPDASQAELDEAASKAgaLEfITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAH 513
Cdd:PRK14247 101 -ENVALGLKLNRLVKSKKELQERVRWA--LE-KAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 514 LDSQTEHLINQAIREYAKDHLVLVIAH-RLNTVKHADKIYVMQQGHIVESG 563
Cdd:PRK14247 177 LDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
340-563 |
1.70e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.99 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 340 LELPIKHiQLNALTFhypetnegvtDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTA---- 415
Cdd:PRK11144 2 LELNFKQ-QLGDLCL----------TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgic 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 416 LADWQAQLAWIPQHATFF--YRsVAENLRLAKPDASQAELDEaaskagalefITALPdGFDTLLGEQGEGLSGGQKQRIA 493
Cdd:PRK11144 71 LPPEKRRIGYVFQDARLFphYK-VRGNLRYGMAKSMVAQFDK----------IVALL-GIEPLLDRYPGSLSGGEKQRVA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 494 LARAFLKNAPVLMLDEPTAHLD--------------SQTehlINQAIreyakdhlvLVIAHRLNTVKH-ADKIYVMQQGH 558
Cdd:PRK11144 139 IGRALLTAPELLLMDEPLASLDlprkrellpylerlARE---INIPI---------LYVSHSLDEILRlADRVVVLEQGK 206
|
....*
gi 1952200779 559 IVESG 563
Cdd:PRK11144 207 VKAFG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
347-568 |
2.28e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVT--DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLA 424
Cdd:PRK13648 8 IVFKNVSFQY-QSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHA--TFFYRSVA-------ENlRLAKPDASQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIALA 495
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKydvafglEN-HAVPYDEMHRRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 496 RAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIA--HRLNTVKHADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
347-577 |
2.54e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.38 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHA--TFFYRSVAENLRLAKPDASqaeLDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPV 504
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGPINLG---LDEETVAHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 505 LMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVI--AHRLNTVKH-ADKIYVMQQGHIVESGQYQQLTEQAGLFAK 577
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
353-568 |
2.81e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 353 TFHYpetNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHhQANSAISINEQPLSDTA---------LADWQAQL 423
Cdd:PRK09984 13 TFNQ---HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI-TGDKSAGSHIELLGRTVqregrlardIRKSRANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHATFFYR-SVAENLRLAKPDASQ-----AELDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARA 497
Cdd:PRK09984 89 GYIFQQFNLVNRlSVLENVLIGALGSTPfwrtcFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 498 FLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLN-TVKHADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
347-563 |
3.73e-15 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 74.71 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHY---PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLG-FHHQANSA----ISINEQPlsdtalAD 418
Cdd:cd03266 2 ITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGlLEPDAGFAtvdgFDVVKEP------AE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 419 WQAQLAWIPQHATFFYR-SVAENLRL------AKPDASQAELDEAASKAGALEFitalpdgfdtlLGEQGEGLSGGQKQR 491
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRlTARENLEYfaglygLKGDELTARLEELADRLGMEEL-----------LDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 492 IALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREY-AKDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
363-570 |
3.95e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.18 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAlaDWQAQLAWIPQ-HATFFYRSVAENL 441
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQsYALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 -------RLAKPDASqAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHL 514
Cdd:PRK11607 113 afglkqdKLPKAEIA-SRVNEMLGLVHMQEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 515 DSQTEHLINQA---IREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTE 570
Cdd:PRK11607 181 DKKLRDRMQLEvvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
366-551 |
4.99e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.93 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 366 INLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAlADWQAQLAWIPQHATFFYR-SVAENLRLA 444
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPElSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 445 KPD--ASQAELDEAASKAGaLEFITALPDGFdtllgeqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLI 522
Cdd:TIGR01189 98 AAIhgGAQRTIEDALAAVG-LTGFEDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180 190
....*....|....*....|....*....|
gi 1952200779 523 NQAIREY-AKDHLVLVIAHRLNTVKHADKI 551
Cdd:TIGR01189 167 AGLLRAHlARGGIVLLTTHQDLGLVEAREL 196
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
376-568 |
5.49e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.62 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 376 IAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALAdwQAQLAWIPQHATFF-YRSVAENLRLA-----KPDAS 449
Cdd:PRK10771 28 VAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFsHLTVAQNIGLGlnpglKLNAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 450 Q-AELDEAASKAGALEFITALPdgfdtllgeqGEgLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEH----LINQ 524
Cdd:PRK10771 106 QrEKLHAIARQMGIEDLLARLP----------GQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQemltLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1952200779 525 AIREyaKDHLVLVIAHRL-NTVKHADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK10771 175 VCQE--RQLTLLMVSHSLeDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
347-580 |
5.99e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.84 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVT---DINLTLPSSGLIAFVGESGSGKSTLFDcLLGFHHQANSAI----SINEQPLSDTALADW 419
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEvlkGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKPTSGTyrvaGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 420 QAQlawipqHATFFYR--------SVAENLRLAkpdASQAELDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQR 491
Cdd:PRK10535 84 RRE------HFGFIFQryhllshlTAAQNVEVP---AVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 492 IALARAFLKNAPVLMLDEPTAHLDSQT-EHLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTE 570
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSgEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVN 232
|
250
....*....|
gi 1952200779 571 QAGLFAKLVS 580
Cdd:PRK10535 233 VAGGTEPVVN 242
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
362-557 |
7.86e-15 |
|
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: 74.01 E-value: 7.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 362 GVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLG----------FHHQansaisinEQPLsDTALADWQAQLA------- 424
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsilVRHD--------GGWV-DLAQASPREILAlrrrtig 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQhatfFYRS---------VAENLRlakpdASQAELDEAASKAGALefITAL----------PDGFdtllgeqgeglS 485
Cdd:COG4778 97 YVSQ----FLRViprvsaldvVAEPLL-----ERGVDREEARARAREL--LARLnlperlwdlpPATF-----------S 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 486 GGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREyAKDHLVLVIA--HRLNTVKH-ADKIYVMQQG 557
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE-AKARGTAIIGifHDEEVREAvADRVVDVTPF 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
350-563 |
8.37e-15 |
|
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: 78.13 E-value: 8.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 350 NALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsDTALADWQAQLAWIPQH 429
Cdd:TIGR01257 933 NLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 430 ATFFYR-SVAENLRLakpdasQAELDEAASKAGALEFITALPD-GFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLML 507
Cdd:TIGR01257 1012 NILFHHlTVAEHILF------YAQLKGRSWEEAQLEMEAMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVL 1085
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 508 DEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVK-HADKIYVMQQGHIVESG 563
Cdd:TIGR01257 1086 DEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSG 1142
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
366-530 |
9.78e-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: 73.30 E-value: 9.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 366 INLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsDTALADWQAQLAWIPQHATFFYR-SVAENLRLA 444
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTlSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 445 KPDASQAELDEAASKAGAlefitalpDGFDTLLGEQgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQ 524
Cdd:cd03231 98 HADHSDEQVEEALARVGL--------NGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
....*.
gi 1952200779 525 AIREYA 530
Cdd:cd03231 167 AMAGHC 172
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
363-570 |
1.19e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGF--HHQANSAISINEQPLSDTALADW-QAQLAWIPQHATFF-YRSVA 438
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVkELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 ENLRLAKPDASQAELDEAASKAGALEFITALPDGFD--TLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHL-D 515
Cdd:PRK13549 101 ENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTASLtE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 516 SQTEHLINqAIREYaKDHLV--LVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLTE 570
Cdd:PRK13549 177 SETAVLLD-IIRDL-KAHGIacIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTE 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
365-575 |
1.26e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.53 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALAdwQAQLAWIPQ-HATFFYRSVAEN--- 440
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQsYALFPHMSLGENvgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 -LRLAKpdASQAELDEAASKAgaLEFITAlpDGFDTLLGEQgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:PRK11432 102 gLKMLG--VPKEERKQRVKEA--LELVDL--AGFEDRYVDQ---ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 520 HLINQAIREyakdhlvlvIAHRLNT----VKH--------ADKIYVMQQGHIVESGQYQQLTEQ-AGLF 575
Cdd:PRK11432 173 RSMREKIRE---------LQQQFNItslyVTHdqseafavSDTVIVMNKGKIMQIGSPQELYRQpASRF 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
320-541 |
2.39e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.00 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 320 ADMVDIINQSDADEHVGSSKLELPIKHIQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQ 399
Cdd:COG4178 336 AGFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPY 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 400 ANSAISINEQplsdtaladwqAQLAWIPQHATFfyrsVAENLR--LAKPDA----SQAELDEAASKAGalefITALPDGF 473
Cdd:COG4178 416 GSGRIARPAG-----------ARVLFLPQRPYL----PLGTLReaLLYPATaeafSDAELREALEAVG----LGHLAERL 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 474 DTllgEQ--GEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHR 541
Cdd:COG4178 477 DE---EAdwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
362-568 |
2.63e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.52 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 362 GVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALadwQAQLAWI----------PQHAT 431
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKK---NKKLKPLrkkvgivfqfPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 432 F--------------FYRSVAENLRLAKPDASQAELDEaaskagalEFITALPdgFDtllgeqgegLSGGQKQRIALARA 497
Cdd:PRK13634 99 FeetvekdicfgpmnFGVSEEDAKQKAREMIELVGLPE--------ELLARSP--FE---------LSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 498 FLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH---LVLViAHRLNTV-KHADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKgltTVLV-THSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
365-564 |
2.67e-14 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 72.50 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAladwQAQLAWIPQHATFFYRSVAENLRLA 444
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----PDRMVVFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 445 ----KPDASQAELDEAASKAGALEFITALPDgfdtllgEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEH 520
Cdd:TIGR01184 79 vdrvLPDLSKSERRAIVEEHIALVGLTEAAD-------KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1952200779 521 LINQAIREYAKDH--LVLVIAHRLN-TVKHADKIYVMQQGHIVESGQ 564
Cdd:TIGR01184 152 NLQEELMQIWEEHrvTVLMVTHDVDeALLLSDRVVMLTNGPAANIGQ 198
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-560 |
2.75e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.20 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 342 LPIKHIQLnalTFH--YPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADW 419
Cdd:COG1101 2 LELKNLSK---TFNpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV--TKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 420 Q-AqlAWI------PQHATFFYRSVAENLRLA---------KPDASQAELDEAAskagalEFITALPDGFDTLLGEQGEG 483
Cdd:COG1101 77 KrA--KYIgrvfqdPMMGTAPSMTIEENLALAyrrgkrrglRRGLTKKRRELFR------ELLATLGLGLENRLDTKVGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLI----NQAIREYakdHL-VLVIAHRLN-TVKHADKIYVMQQG 557
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEEN---NLtTLMVTHNMEqALDYGNRLIMMHEG 225
|
...
gi 1952200779 558 HIV 560
Cdd:COG1101 226 RII 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
366-574 |
3.06e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 366 INLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPL--SDTALADWQAQLAWIPQ--HATFFYRSVAENL 441
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQdpEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 RLAKPDASQAELDEAASKAGALEFITAlpDGFDTllgEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE-H 520
Cdd:PRK13638 100 AFSLRNLGVPEAEITRRVDEALTLVDA--QHFRH---QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRtQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 521 LINQAIREYAKDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQ------YQQLTEQAGL 574
Cdd:PRK13638 175 MIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGApgevfaCTEAMEQAGL 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
366-569 |
4.93e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 366 INLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADWQAQ---LAWIPQHATFF-YRSVAEN- 440
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC--ARLTPAKAHqlgIYLVPQEPLLFpNLSVKENi 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 -LRLAKPDASQAELDEaaskagaleFITALPDGFDtlLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLD-SQT 518
Cdd:PRK15439 108 lFGLPKRQASMQKMKQ---------LLAALGCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 519 EHLINQaIREY-AKDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLT 569
Cdd:PRK15439 177 ERLFSR-IRELlAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLS 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
347-563 |
8.73e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.04 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEG-----VTDINLTLPSSGLIAFVGESGSGKSTL---FDCLLgfhHQANSAISINEQPLSDTA-LA 417
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklaLDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL---IPSEGKVYVDGLDTSDEEnLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 418 DWQAQLAWIPQH------ATFFYRSVA---ENLRLaKPDASQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQ 488
Cdd:PRK13633 82 DIRNKAGMVFQNpdnqivATIVEEDVAfgpENLGI-PPEEIRERVDESLKKVGMYEYRRHAP-----------HLLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 489 KQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKHADKIYVMQQGHIVESG 563
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
347-540 |
9.96e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETnEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLS-----------DTA 415
Cdd:PRK11248 2 LQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaergvvfqNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 416 LADWQAQLAwipqhatffyrSVAENLRLAkpDASQAELDEAASKAGALEFItalpDGFDTLLGEQgegLSGGQKQRIALA 495
Cdd:PRK11248 81 LLPWRNVQD-----------NVAFGLQLA--GVEKMQRLEIAHQMLKKVGL----EGAEKRYIWQ---LSGGQRQRVGIA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952200779 496 RAFLKNAPVLMLDEPTAHLDS----QTEHLINQAIREYAKDhlVLVIAH 540
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAftreQMQTLLLKLWQETGKQ--VLLITH 187
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
347-564 |
1.01e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.56 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSD-TALADWQAQLAW 425
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQH--ATFFYRSVAENLRLA------KPDASQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIALARA 497
Cdd:PRK13644 82 VFQNpeTQFVGRTVEEDLAFGpenlclPPIEIRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 498 FLKNAPVLMLDEPTAHLDSQTEHLINQAIRE-YAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQ 564
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
363-568 |
1.06e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 73.57 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGF----HHQANSAISINEQPLSDTALADWQA----QLAWI-------- 426
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIfqepmtsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 -PQHAtfFYRSVAENLRLAKPdasqaeLDEAASKAGALEFI--TALPDGfDTLLGE---QgegLSGGQKQRIALARAfLK 500
Cdd:COG4172 106 nPLHT--IGKQIAEVLRLHRG------LSGAAARARALELLerVGIPDP-ERRLDAyphQ---LSGGQRQRVMIAMA-LA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 501 NAPVLML-DEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:COG4172 173 NEPDLLIaDEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAEL 244
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
365-540 |
1.34e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALAdwqAQLAWIpQHATFFYR--SVAENLR 442
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA---EACHYL-GHRNAMKPalTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 443 LAKPDASQAELD-EAASKAGALEFITALPDGFdtllgeqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHL 521
Cdd:PRK13539 96 FWAAFLGGEELDiAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|
gi 1952200779 522 INQAIREY-AKDHLVLVIAH 540
Cdd:PRK13539 166 FAELIRAHlAQGGIVIAATH 185
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
365-570 |
1.34e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.51 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLlgfhhQANSAISINEQPLSDTALADWQAQLAWIPQHA--------TFFYRS 436
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCI-----NKLEEITSGDLIVDGLKVNDPKVDERLIRQEAgmvfqqfyLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 VAENL-------RLAKPDASQAELDEAASKAGALEFITALPdgfdtllgeqGEgLSGGQKQRIALARAfLKNAPVLML-D 508
Cdd:PRK09493 94 ALENVmfgplrvRGASKEEAEKQARELLAKVGLAERAHHYP----------SE-LSGGQQQRVAIARA-LAVKPKLMLfD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 509 EPTAHLDSQTEHLINQAIREYAKDHLVLVI-AHRLNTV-KHADKIYVMQQGHIVESGQYQQLTE 570
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIvTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
363-542 |
1.51e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.97 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDC-------LLGFhhQANSAISINEQPLSDTAL--ADWQAQLAWIPQHATFF 433
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGF--RVEGKVTFHGKNLYAPDVdpVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 434 YRSVAENLRL-AKPDASQAELDEAASKAGALefiTALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTA 512
Cdd:PRK14243 104 PKSIYDNIAYgARINGYKGDMDELVERSLRQ---AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190
....*....|....*....|....*....|
gi 1952200779 513 HLDSQTEHLINQAIREYAKDHLVLVIAHRL 542
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
377-562 |
1.98e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 377 AFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALAD-WQAQLAWIPQHATFFYR-SVAENLRLAKPDASQAELD 454
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVPEmTVAENLYLGQLPHKGGIVN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 455 EAASKAGALEFITALPDGFD--TLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ-TEHLInQAIREY-A 530
Cdd:PRK11288 114 RRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAReIEQLF-RVIRELrA 188
|
170 180 190
....*....|....*....|....*....|...
gi 1952200779 531 KDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVES 562
Cdd:PRK11288 189 EGRVILYVSHRMEEIFAlCDAITVFKDGRYVAT 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
363-563 |
2.38e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 71.30 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQP---LSDTALADWQAQLAWIPQ--HATF----- 432
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQdpYASLnprmt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 433 FYRSVAENLRLAKpDASQAELDEAASKAGAL-----EFITALPDGFdtllgeqgeglSGGQKQRIALARAFLKNAPVLML 507
Cdd:COG4608 114 VGDIIAEPLRIHG-LASKAERRERVAELLELvglrpEHADRYPHEF-----------SGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 508 DEPTAHLD----SQTEHLINQAIRE----YakdhlvLVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:COG4608 182 DEPVSALDvsiqAQVLNLLEDLQDElgltY------LFISHDLSVVRHiSDRVAVMYLGKIVEIA 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
347-568 |
3.94e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.15 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVT--DINLTLPSSGLIAFVGESGSGKST---LFDCLLgfhhQANSA-ISINEQPLSDTALADWQ 420
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTlnDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL----EAESGqIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 AQLAWIPQH-------ATFfYRSVA---ENLRLAKPDAsQAELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQ 490
Cdd:PRK13650 81 HKIGMVFQNpdnqfvgATV-EDDVAfglENKGIPHEEM-KERVNEALELVGMQDFKEREP-----------ARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 491 RIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
348-568 |
5.32e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.23 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 348 QLNALTFH--YPEtNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQ----- 420
Cdd:PRK10619 5 KLNVIDLHkrYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 --------AQLAWIPQHATFF-YRSVAENLRLAKPDA---SQAELDEAASKAGALEFITalpdgfDTLLGEQGEGLSGGQ 488
Cdd:PRK10619 84 knqlrllrTRLTMVFQHFNLWsHMTVLENVMEAPIQVlglSKQEARERAVKYLAKVGID------ERAQGKYPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 489 KQRIALARAFLKNAPVLMLDEPTAHLDSQT--EHL-INQAIREYAKDhlVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQ 564
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELvgEVLrIMQQLAEEGKT--MVVVTHEMGFARHvSSHVIFLHQGKIEEEGA 235
|
....
gi 1952200779 565 YQQL 568
Cdd:PRK10619 236 PEQL 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
348-568 |
7.64e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 348 QLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISI--------NEQPLSDTALADW 419
Cdd:PRK10261 17 NLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrrrSRQVIELSEQSAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 420 Q------AQLAWIPQHATFFYRSV-------AENLRLAKpdasQAELDEAASKAGALEFITALPDGfDTLLGEQGEGLSG 486
Cdd:PRK10261 97 QmrhvrgADMAMIFQEPMTSLNPVftvgeqiAESIRLHQ----GASREEAMVEAKRMLDQVRIPEA-QTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 487 GQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHL--VLVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETG 251
|
....*
gi 1952200779 564 QYQQL 568
Cdd:PRK10261 252 SVEQI 256
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
354-563 |
8.05e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.61 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 354 FHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQplsDTALADWQAQLAWIPQHATFF 433
Cdd:PRK11308 22 FKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ---DLLKADPEAQKLLRQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 434 ---YRSVaeNLR------LAKPDASQAELDEAASKAGAL----------EFITALPDGFdtllgeqgeglSGGQKQRIAL 494
Cdd:PRK11308 99 qnpYGSL--NPRkkvgqiLEEPLLINTSLSAAERREKALammakvglrpEHYDRYPHMF-----------SGGQRQRIAI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 495 ARAFLKNAPVLMLDEPTAHLD----SQTEHLINQAIREYakdHLVLV-IAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDvsvqAQVLNLMMDLQQEL---GLSYVfISHDLSVVEHiADEVMVMYLGRCVEKG 237
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
361-563 |
9.18e-13 |
|
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: 68.13 E-value: 9.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 361 EGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISIN-EQPLSD--------TALADWQAQLAW-IPqha 430
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAgLVPWKRrkkflrriGVVFGQKTQLWWdLP--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 431 tffyrsVAENLRLAK------PDASQAELDEaaskagalefITALPDgFDTLLGEQGEGLSGGQKQRIALARAFLKNAPV 504
Cdd:cd03267 112 ------VIDSFYLLAaiydlpPARFKKRLDE----------LSELLD-LEELLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 505 LMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
347-559 |
1.02e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.92 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETN---EGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPL---SDTALADWQ 420
Cdd:PRK11629 6 LQCDNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklSSAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 421 AQ-LAWIPQHATFF-----YRSVAENLRLAKPDASQAeldeaasKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIAL 494
Cdd:PRK11629 86 NQkLGFIYQFHHLLpdftaLENVAMPLLIGKKKPAEI-------NSRALEMLAAV--GLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 495 ARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKHADKIYVMQQGHI 559
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
363-585 |
1.14e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADwQAQLAWIPQHATFFYR-SVAENL 441
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVVPQFDNLDLEfTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 ----RLAKPDASQAEldeaASKAGALEFiTALPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:PRK13536 136 lvfgRYFGMSTREIE----AVIPSLLEF-ARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 518 TEHLINQAIRE-YAKDHLVLVIAHRLNTVKH-ADKIYVMQQGH-IVESGQYQQLTEQAGLFAKLVSQGDAH 585
Cdd:PRK13536 207 ARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGRkIAEGRPHALIDEHIGCQVIEIYGGDPH 277
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
366-570 |
1.28e-12 |
|
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: 70.24 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 366 INLTLPSSGLIAFVGESGSGKSTLFDCLLGF--HHQANSAISINEQPLSDTALADWQAQ-LAWIPQHATFFYR-SVAENL 441
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 RLAKP---DASQAELDEAASKAGALEFITALPDGFDTL-LGEQGeglsGGQKQRIALARAFLKNAPVLMLDEPTAHL-DS 516
Cdd:TIGR02633 100 FLGNEitlPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSLtEK 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 517 QTEHLINqAIREYAKDHLVLV-IAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLTE 570
Cdd:TIGR02633 176 ETEILLD-IIRDLKAHGVACVyISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSE 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
365-564 |
1.31e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 68.62 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTA----LADWQAQLAWIPQ--HATFFYRSVA 438
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQfpESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 ENLRLAKPD--ASQAELDEAASKAGALEFITalpdgfDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDS 516
Cdd:PRK13649 105 KDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1952200779 517 QTEHLINQAIREYAKDHLVLV-IAHRLNTV-KHADKIYVMQQGHIVESGQ 564
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVlVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
361-563 |
1.35e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.28 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 361 EGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSdtaLADWqaqlAWIPQHATFFYR--SVA 438
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH---FGDY----SYRSQRIRMIFQdpSTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 ENLR------LAKPDASQAELD-EAASKA--GALEFITALPDGfdtlLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDE 509
Cdd:PRK15112 100 LNPRqrisqiLDFPLRLNTDLEpEQREKQiiETLRQVGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 510 PTAHLD-SQTEHLINQAIREYAKDHLVLV-IAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:PRK15112 176 ALASLDmSMRSQLINLMLELQEKQGISYIyVTQHLGMMKHiSDQVLVMHQGEVVERG 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
365-584 |
1.80e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSA--------ISINEQPLSD---TALADWQAQLAWIPQHATFF 433
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPrgarvtgdVTLNGEPLAAidaPRLARLRAVLPQAAQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 434 yrSVAENLRLAK-PDASQA-----ELDEAASKAGALEfitalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAP---- 503
Cdd:PRK13547 99 --SAREIVLLGRyPHARRAgalthRDGEIAWQALALA-------GATALVGRDVTTLSGGELARVQFARVLAQLWPphda 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 504 -----VLMLDEPTAHLDSQTEHLINQAIREYAKD-HL-VLVIAHRLN-TVKHADKIYVMQQGHIVESGQYQQLTEQA--- 572
Cdd:PRK13547 170 aqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLTPAhia 249
|
250
....*....|....*
gi 1952200779 573 ---GLFAKLVSQGDA 584
Cdd:PRK13547 250 rcyGFAVRLVDAGDG 264
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
345-568 |
2.00e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.81 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 345 KHIQLNALTFHYPETNE--GVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQ 422
Cdd:PRK13642 3 KILEVENLVFKYEKESDvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 423 LAWIPQHA--TFFYRSVAENLRLAKPDASQ------AELDEAASKAGALEFITALPdgfdtllgeqgEGLSGGQKQRIAL 494
Cdd:PRK13642 83 IGMVFQNPdnQFVGATVEDDVAFGMENQGIpreemiKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 495 ARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYA-KDHL-VLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLtVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
345-561 |
2.13e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 345 KHIQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLA 424
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 425 WIPQHATFFYrsvaenlRLAKPDASQAElDEAASKagALEFI-----TALPDGFDTLLgeqgeGLSGGQKQRIALARAFL 499
Cdd:PRK10522 401 AVFTDFHLFD-------QLLGPEGKPAN-PALVEK--WLERLkmahkLELEDGRISNL-----KLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 500 KNAPVLMLDEPTAHLDSQTEHLINQAIREY--AKDHLVLVIAHRLNTVKHADKIYVMQQGHIVE 561
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLlqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
365-571 |
2.34e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISIN--EQPLSDTALAdWQAQLAWIPQHATFFYR-SVAENL 441
Cdd:PRK09700 23 SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINniNYNKLDHKLA-AQLGIGIIYQELSVIDElTVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 RLAKPDASQ------AELDEAASKAGALEFITALPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHL- 514
Cdd:PRK09700 102 YIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLt 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 515 DSQTEHL---INQAIREYAKdhlVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLTEQ 571
Cdd:PRK09700 178 NKEVDYLfliMNQLRKEGTA---IVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
483-572 |
3.24e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.95 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 483 GLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREY-AKDHLVLVIAHRL-NTVKHADKIYVMQQGHIV 560
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMeHVLEVADEVIVMDKGKIL 255
|
90
....*....|...
gi 1952200779 561 ESGQ-YQQLTEQA 572
Cdd:PRK13631 256 KTGTpYEIFTDQH 268
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
379-570 |
3.59e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 379 VGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAlADWQAQLAWIPQHATF---FyrSVAENLRLAKPDASQAELDE 455
Cdd:PRK13537 39 LGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGVVPQFDNLdpdF--TVRENLLVFGRYFGLSAAAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 456 AASKAGALEFiTALPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIRE-YAKDHL 534
Cdd:PRK13537 116 RALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKT 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 1952200779 535 VLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLTE 570
Cdd:PRK13537 191 ILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-568 |
4.17e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.04 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 366 INLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFYR------SVAE 439
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRpnpfpmSIMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 440 NLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:PRK14271 120 NVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTT 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1952200779 520 HLINQAIREYAKDHLVLVIAHRL-NTVKHADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK14271 200 EKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
347-575 |
5.69e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.66 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAlADwQAQLAWI 426
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AE-NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQH-ATFFYRSVAEN----LRLAK-PDASQAELDEAASKAGALE-FITALPdgfdtllgeqgEGLSGGQKQRIALARAFL 499
Cdd:PRK09452 92 FQSyALFPHMTVFENvafgLRMQKtPAAEITPRVMEALRMVQLEeFAQRKP-----------HQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 500 KNAPVLMLDEPTAHLD----SQTEHLINQAIREyakdhlvLVIahrlnT---VKH--------ADKIYVMQQGHIVESGQ 564
Cdd:PRK09452 161 NKPKVLLLDESLSALDyklrKQMQNELKALQRK-------LGI-----TfvfVTHdqeealtmSDRIVVMRDGRIEQDGT 228
|
250
....*....|..
gi 1952200779 565 YQQLTEQ-AGLF 575
Cdd:PRK09452 229 PREIYEEpKNLF 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
360-568 |
6.91e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 360 NEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHhQANSAISINEQPLSdtaLADWQAQLAWIPQHATFF---YRS 436
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLH---NLNRRQLLPVRHRIQVVFqdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 ----------VAENLRLAKPDASQAELDEAASKAgaLEFITALPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLM 506
Cdd:PRK15134 375 lnprlnvlqiIEEGLRVHQPTLSAAQREQQVIAV--MEEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 507 LDEPTAHLDSQTEHLINQAIREYAKDHLV--LVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
357-563 |
9.03e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.91 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 357 PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTA----LADWQAQLAWIPQ--HA 430
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQfpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 431 TFFYRSVAENLRLAKPDASQAELDEAASKAGALEFItalpdGFDTLLGEQGE-GLSGGQKQRIALARAFLKNAPVLMLDE 509
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 510 PTAHLDSQTEHLINQAIRE-YAKDHLVLVIAHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCG 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
379-571 |
1.24e-11 |
|
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: 65.98 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 379 VGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAladwqAQLAWI----PQHATFFYRSVAEN----LRLAKPDAsq 450
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-----PHLRHInmvfQSYALFPHMTVEENvafgLKMRKVPR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 451 AELDEAASKAgaLEFITalpdgfdtlLGEQGEG----LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQ-- 524
Cdd:TIGR01187 75 AEIKPRVLEA--LRLVQ---------LEEFADRkphqLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLel 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1952200779 525 -AIREYAKDHLVLVIAHRLNTVKHADKIYVMQQGHIVESGQYQQLTEQ 571
Cdd:TIGR01187 144 kTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-568 |
1.40e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.07 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPL---SDTALAD---WQAQLAWIPQHATFF-YRSV 437
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDaikLRKEVGMVFQQPNPFpHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 438 AENLrlAKPDASQAELDEAASKAGALEFI--TALPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLD 515
Cdd:PRK14246 108 YDNI--AYPLKSHGIKEKREIKKIVEECLrkVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 516 SQTEHLINQAIREYAKDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQL 568
Cdd:PRK14246 186 IVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
365-562 |
1.50e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGF--HHQANSAISINEQPLSDTALADWQAQ--------LAWIPqhatffY 434
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCRFKDIRDSEALgiviihqeLALIP------Y 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 435 RSVAENLRLAKPDASQAELD--EAASKAGALEFITALPDGFDTLLGEQGEGlsggQKQRIALARAFLKNAPVLMLDEPTA 512
Cdd:NF040905 93 LSIAENIFLGNERAKRGVIDwnETNRRARELLAKVGLDESPDTLVTDIGVG----KQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 513 HL-DSQTEHLINqAIREYaKDHLV--LVIAHRLNTV-KHADKIYVMQQGHIVES 562
Cdd:NF040905 169 ALnEEDSAALLD-LLLEL-KAQGItsIIISHKLNEIrRVADSITVLRDGRTIET 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
363-563 |
1.54e-11 |
|
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: 63.70 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHqansaisineqplsdtaladwqaqlawipqhatffYRSVAENLR 442
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPK-----------------------------------YEVTEGEIL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 443 LAKPDASQAELDEAASKAGALEF-----ITALPdgFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:cd03217 61 FKGEDITDLPPEERARLGIFLAFqyppeIPGVK--NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1952200779 518 TEHLINQAIREYAKDHL-VLVIAHR---LNTVKhADKIYVMQQGHIVESG 563
Cdd:cd03217 139 ALRLVAEVINKLREEGKsVLIITHYqrlLDYIK-PDRVHVLYDGRIVKSG 187
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
375-578 |
1.62e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.99 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 375 LIAFVGESGSGKSTLFDCLLGFHH---QANSAISINEQPLSDTALadwQAQLAWIPQHATFF-YRSVAENLRLakpdasQ 450
Cdd:TIGR00955 53 LLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKEM---RAISAYVQQDDLFIpTLTVREHLMF------Q 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 451 AEL--DEAASKAGALEFI------TALPDGFDTLLGEQG--EGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEH 520
Cdd:TIGR00955 124 AHLrmPRRVTKKEKRERVdevlqaLGLRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 521 LINQAIREYA-KDHLVLVIAHRLNT--VKHADKIYVMQQGHIVESGQYQQLTEqagLFAKL 578
Cdd:TIGR00955 204 SVVQVLKGLAqKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP---FFSDL 261
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
361-563 |
2.12e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.36 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 361 EGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISI------------NEQP------------------ 410
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIiyhvalcekcgyVERPskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 411 -----LSDTALADWQAQLAWIPQHATFFY--RSVAENLRLAKPDASQaELDEAASKAGALEFITALPDGFDTLLGEqgeg 483
Cdd:TIGR03269 94 vdfwnLSDKLRRRIRKRIAIMLQRTFALYgdDTVLDNVLEALEEIGY-EGKEAVGRAVDLIEMVQLSHRITHIARD---- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH-LVLVIAHRLNTV--KHADKIYVMQQGHIV 560
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHWPEVieDLSDKAIWLENGEIK 248
|
...
gi 1952200779 561 ESG 563
Cdd:TIGR03269 249 EEG 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
348-568 |
2.34e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.42 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 348 QLNALTFHYPetneGVT---DINLTLPSSGLIAFVGESGSGKSTLFDcLLGFHHQANSA-ISINEQPLSDTALADWQAQL 423
Cdd:PRK10575 13 ALRNVSFRVP----GRTllhPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSEGeILLDAQPLESWSSKAFARKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 424 AWIPQHAtffyrSVAENL------------------RLAKPDASQAEldEAASKAGALEFITALPDgfdtllgeqgeGLS 485
Cdd:PRK10575 88 AYLPQQL-----PAAEGMtvrelvaigrypwhgalgRFGAADREKVE--EAISLVGLKPLAHRLVD-----------SLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 486 GGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIA--HRLN-TVKHADKIYVMQQGHIVES 562
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQ 229
|
....*.
gi 1952200779 563 GQYQQL 568
Cdd:PRK10575 230 GTPAEL 235
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
373-552 |
3.80e-11 |
|
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: 62.62 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 373 SGLIAFVGESGSGKSTLFDCLLG--FHHQANSaisiNEQPLSDTALADWQAQLAWIpqhatffyrsvaenlRLAKPDASQ 450
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIIEALKYalTGELPPN----SKGGAHDPKLIREGEVRAQV---------------KLAFENANG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 451 AELdEAASKAGALEFITALPDG-FDTLLGEQGEGLSGGQKQ------RIALARAFLKNAPVLMLDEPTAHLDS-QTEHLI 522
Cdd:cd03240 83 KKY-TITRSLAILENVIFCHQGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESL 161
|
170 180 190
....*....|....*....|....*....|..
gi 1952200779 523 NQAIREYAKDH--LVLVIAHRLNTVKHADKIY 552
Cdd:cd03240 162 AEIIEERKSQKnfQLIVITHDEELVDAADHIY 193
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
347-563 |
4.12e-11 |
|
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: 62.68 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNeGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTAladwQAQLAWI 426
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFfYR--SVAENLR-LA-----KPDASQAELDEAASKAGALEfitalpdgfdtLLGEQGEGLSGGQKQRIALARAF 498
Cdd:cd03269 76 PEERGL-YPkmKVIDQLVyLAqlkglKKEEARRRIDEWLERLELSE-----------YANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 499 LKNAPVLMLDEPTAHLDSQTEHLINQAIREYA-KDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
452-542 |
6.52e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 452 ELDEAASKAGAL-EFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDsqtehlINQ------ 524
Cdd:PRK13409 182 ELLKKVDERGKLdEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQrlnvar 253
|
90
....*....|....*...
gi 1952200779 525 AIREYAKDHLVLVIAHRL 542
Cdd:PRK13409 254 LIRELAEGKYVLVVEHDL 271
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
347-568 |
7.07e-11 |
|
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: 62.39 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGF-HHQANSAISINEQPLSDTAlaDWQAQLAW 425
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLlKPTSGRATVAGHDVVREPR--EVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 426 IPQhatffYRSVA------ENL----RLAkpDASQAELDEAASKAgaLEFItALPDGFDTLLGEqgegLSGGQKQRIALA 495
Cdd:cd03265 78 VFQ-----DLSVDdeltgwENLyihaRLY--GVPGAERRERIDEL--LDFV-GLLEAADRLVKT----YSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 496 RAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQQL 568
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
347-581 |
7.42e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.22 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWI 426
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHA--TFFYRSVAE-------NLRLakpdaSQAELDEAASKAGALEFITALPDgfdtllgEQGEGLSGGQKQRIALARA 497
Cdd:PRK13647 85 FQDPddQVFSSTVWDdvafgpvNMGL-----DKDEVERRVEEALKAVRMWDFRD-------KPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 498 FLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIA-HRLN-TVKHADKIYVMQQGHIVESGQY-----QQLTE 570
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKslltdEDIVE 232
|
250
....*....|.
gi 1952200779 571 QAGLFAKLVSQ 581
Cdd:PRK13647 233 QAGLRLPLVAQ 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
348-540 |
7.60e-11 |
|
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: 64.57 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 348 QLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLG----FHHQANSAISIN------EQPLSDT--- 414
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkdFNGEARPQPGIKvgylpqEPQLDPTktv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 415 ------ALADWQAQLAwipqhatffyRSVAENLRLAKPDAS-------QAELDEAASKAGALEFITALPDGFDTLLGEQG 481
Cdd:TIGR03719 86 renveeGVAEIKDALD----------RFNEISAKYAEPDADfdklaaeQAELQEIIDAADAWDLDSQLEIAMDALRCPPW 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 482 EG----LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDhlVLVIAH 540
Cdd:TIGR03719 156 DAdvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGT--VVAVTH 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-540 |
1.20e-10 |
|
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: 62.04 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 356 YPETNEGVTDINL-----TLPSSGLIAFVGESGSGKSTLFDCLLGfhhqansaisiNEQPLSDTALADwQAQLAWIPQHA 430
Cdd:cd03237 3 YPTMKKTLGEFTLeveggSISESEVIGILGPNGIGKTTFIKMLAG-----------VLKPDEGDIEIE-LDTVSYKPQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 431 TFFYRSVAENLRLAKpdasqaeLDEAASKAgalEFITAL--PDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLD 508
Cdd:cd03237 71 KADYEGTVRDLLSSI-------TKDFYTHP---YFKTEIakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190
....*....|....*....|....*....|....
gi 1952200779 509 EPTAHLDSQTEHLINQAIREYAKDH--LVLVIAH 540
Cdd:cd03237 141 EPSAYLDVEQRLMASKVIRRFAENNekTAFVVEH 174
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
359-572 |
1.65e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 359 TNEGVTDINLTLPS------SGLIafvgesGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALAD-WQAQLAWIP---- 427
Cdd:COG1129 264 VGGVVRDVSFSVRAgeilgiAGLV------GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 428 QHATFFYRSVAENLRLAKPD--ASQAELDEAASKAGALEFITAL---PDGFDTLLGEqgegLSGGQKQRIALARAFLKNA 502
Cdd:COG1129 338 GEGLVLDLSIRENITLASLDrlSRGGLLDRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 503 PVLMLDEPTAHLD--SQTEhlINQAIREYAKDHL-VLVI------AHRLntvkhADKIYVMQQGHIVESGQYQQLTEQA 572
Cdd:COG1129 414 KVLILDEPTRGIDvgAKAE--IYRLIRELAAEGKaVIVIsselpeLLGL-----SDRILVMREGRIVGELDREEATEEA 485
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
359-572 |
1.66e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 359 TNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQ-LAWIPQHatffyR-- 435
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgIVYISED-----Rkr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 436 -------SVAENLRL-AKPDASQA--ELDEAASKAGALEFITALpdGFDTLLGEQGEG-LSGGQKQRIALARAFLKNAPV 504
Cdd:PRK10762 339 dglvlgmSVKENMSLtALRYFSRAggSLKHADEQQAVSDFIRLF--NIKTPSMEQAIGlLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 505 LMLDEPTAHLDSQTEHLINQAIREYAKDHL--VLVIAHRLNTVKHADKIYVMQQGHIveSGQYQqlTEQA 572
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLsiILVSSEMPEVLGMSDRILVMHEGRI--SGEFT--REQA 482
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
363-579 |
1.66e-10 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 61.26 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAqlaWIPQHATFFYRSVAENLR 442
Cdd:TIGR03740 16 VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGS---LIESPPLYENLTARENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 443 -----LAKPDAsqaELDEAASKAGalefitaLPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:TIGR03740 93 vhttlLGLPDS---RIDEVLNIVD-------LTNTGKKKAKQ----FSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 518 TEHLINQAIREYAKDHLVLVI-AHRLNTVKH-ADKIYVMQQGHIVESGQYQQLTEQAGLFAKLV 579
Cdd:TIGR03740 159 GIQELRELIRSFPEQGITVILsSHILSEVQQlADHIGIISEGVLGYQGKINKSENLEKLFVEVV 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
365-563 |
1.86e-10 |
|
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: 61.64 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQA-NSAISINEQPLSDTALADWQAQLAWI-PQHATFFYRSV-AENL 441
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERRGGEDVWELRKRIGLVsPALQLRFPRDEtVLDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 ----------RLAKPDASQAELdeaaskagALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPT 511
Cdd:COG1119 101 vlsgffdsigLYREPTDEQRER--------ARELLELL--GLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 512 AHLDSQTEHLINQAIREYAKD---HLVLViAHRLN----TVKHAdkiYVMQQGHIVESG 563
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEgapTLVLV-THHVEeippGITHV---LLLKDGRVVAAG 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-545 |
1.90e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 338 SKLelpIKHIQLNALTFHYpETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCL---------------LGFHHQans 402
Cdd:PRK14258 2 SKL---IPAIKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelesevrvegrVEFFNQ--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 403 aiSINEQPLSDTALadwQAQLAWIPQHATFFYRSVAENLRLA------KPDASQAELDEAASKAGALEfitalpDGFDTL 476
Cdd:PRK14258 75 --NIYERRVNLNRL---RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKDADLW------DEIKHK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952200779 477 LGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDS----QTEHLI-NQAIREyakDHLVLVIAHRLNTV 545
Cdd:PRK14258 144 IHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPiasmKVESLIqSLRLRS---ELTMVIVSHNLHQV 214
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
72-306 |
1.92e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 62.20 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 72 LWPLAGLILV----RALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYI 147
Cdd:cd18565 53 LWLLGGLTVAafllESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 148 PSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNAT 227
Cdd:cd18565 133 NSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 228 KRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATG-----FVV-LLLAPEFYLP 301
Cdd:cd18565 213 DFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTltvgtLVTfLFYTQRLLWP 292
|
....*
gi 1952200779 302 LRQMG 306
Cdd:cd18565 293 LTRLG 297
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
362-571 |
2.31e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 362 GVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGfhHQANSAISI----NEQPLSDTA---------LA--DWqaqlAWI 426
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPDAGEVhyrmRDGQLRDLYalseaerrrLLrtEW----GFV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHATFFYR-------SVAE-----------NLRLAKPD-ASQAELDEAAskagalefITALPDGFdtllgeqgeglSGG 487
Cdd:PRK11701 95 HQHPRDGLRmqvsaggNIGErlmavgarhygDIRATAGDwLERVEIDAAR--------IDDLPTTF-----------SGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 488 QKQRIALARAfLKNAP--VLMlDEPTAHLDSQTE----HLINQAIREYakdHL-VLVIAHRLNTVKH-ADKIYVMQQGHI 559
Cdd:PRK11701 156 MQQRLQIARN-LVTHPrlVFM-DEPTGGLDVSVQarllDLLRGLVREL---GLaVVIVTHDLAVARLlAHRLLVMKQGRV 230
|
250
....*....|..
gi 1952200779 560 VESGqyqqLTEQ 571
Cdd:PRK11701 231 VESG----LTDQ 238
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
71-306 |
2.64e-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: 61.68 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 71 LLWPLAGLILVRALLVA--------LSERVSNRAALKiknvMRNTLLEKLSKLGPAYseqkghgatLNTLHNG------- 135
Cdd:cd18542 37 LLWLLALLILGVALLRGvfrylqgyLAEKASQKVAYD----LRNDLYDHLQRLSFSF---------HDKARTGdlmsrct 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 136 --VEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNyffd 213
Cdd:cd18542 104 sdVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNT---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 214 RLQ----GLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGF-----RLFFGTLD 284
Cdd:cd18542 180 VLQenltGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYlvingEITLGELV 259
|
250 260
....*....|....*....|..
gi 1952200779 285 FATGFVVLLLapefyLPLRQMG 306
Cdd:cd18542 260 AFISYLWMLI-----WPVRQLG 276
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
355-554 |
3.14e-10 |
|
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: 58.91 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 355 HYPETNegvtdiNLTLPSSGLIAFVGESGSGKSTLFDcllgfhhqansaisineqplsdtaladwqaQLAWIpqhatFFY 434
Cdd:cd03227 9 SYFVPN------DVTFGEGSLTIITGPNGSGKSTILD------------------------------AIGLA-----LGG 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 435 RSVAENlrlaKPDASQAELDEAASKAgalEFITALPdgfdtllgeqgeGLSGGQKQRIALARAF----LKNAPVLMLDEP 510
Cdd:cd03227 48 AQSATR----RRSGVKAGCIVAAVSA---ELIFTRL------------QLSGGEKELSALALILalasLKPRPLYILDEI 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1952200779 511 TAHLDSQTEHLINQAIREYA-KDHLVLVIAHRLNTVKHADKIYVM 554
Cdd:cd03227 109 DRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHI 153
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
347-559 |
3.60e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADwqAQLAWI 426
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQ-HATFFYRSVAEN----LRLAKpdASQAELDE-AASKAGALEFitalpdgfDTLLGEQGEGLSGGQKQRIALARAFLK 500
Cdd:PRK11650 82 FQnYALYPHMSVRENmaygLKIRG--MPKAEIEErVAEAARILEL--------EPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 501 NAPVLMLDEPTAHLDSQtehLINQAIREYAKDHlvlviaHRLNT----VKH--------ADKIYVMQQGHI 559
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAK---LRVQMRLEIQRLH------RRLKTtslyVTHdqveamtlADRVVVMNGGVA 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
347-565 |
3.78e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 58.70 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQplsdtaladwqAQLAWI 426
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 427 PQHAtffYrsvaenlrlakpdasqaeldeaaskagalefitaLPDGfdtLLGEQ-----GEGLSGGQKQRIALARAFLKN 501
Cdd:cd03223 70 PQRP---Y----------------------------------LPLG---TLREQliypwDDVLSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 502 APVLMLDEPTAHLDSQTEHLINQAIREyakdHLVLVI--AHRLNTVKHADKIYvmqqgHIVESGQY 565
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKE----LGITVIsvGHRPSLWKFHDRVL-----DLDGEGGW 166
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
345-578 |
3.79e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.18 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 345 KHIQLNALTFHY----PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQ-------ANSAISINEQPLSD 413
Cdd:PRK13645 5 KDIILDNVSYTYakktPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISetgqtivGDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 414 taLADWQAQLAWIPQHATF--FYRSVAENLRLAkPDASQAELDEAASKAGALEFITALPDGFdtlLGEQGEGLSGGQKQR 491
Cdd:PRK13645 85 --VKRLRKEIGLVFQFPEYqlFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 492 IALARAFLKNAPVLMLDEPTAHLDSQTE----HLINQAIREYAKDhlVLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQ 566
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEedfiNLFERLNKEYKKR--IIMVTHNMDQVlRIADEVIVMHEGKVISIGSPF 236
|
250
....*....|..
gi 1952200779 567 QLTEQAGLFAKL 578
Cdd:PRK13645 237 EIFSNQELLTKI 248
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
363-584 |
5.19e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.89 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHhQANS-AISINEQPLSDTALAdwqaQLAWIP------------QH 429
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL-APDSgEVLWDGEPLDPEDRR----RIGYLPeerglypkmkvgEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 430 ATFFYRsvaenLRLAKPDASQAELDEAASKAGalefitaLPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDE 509
Cdd:COG4152 92 LVYLAR-----LKGLSKAEAKRRADEWLERLG-------LGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 510 PTAHLDSQTEHLINQAIREYA-KDHLVLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQQLTEQAGLFA-KLVSQGDA 584
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGRNTlRLEADGDA 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
363-563 |
8.23e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFH----HQANSAISINEQPLSDTALADwqAQLAWIPQHAtffyRSVA 438
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCALRG--RKIATIMQNP----RSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 ENLRLAKPDASQ--AELDEAASKAGALEFITA--LPDGfDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHL 514
Cdd:PRK10418 93 NPLHTMHTHAREtcLALGKPADDATLTAALEAvgLENA-ARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 515 DSQTEHLINQAIREYAKDHL--VLVIAHRLNTV-KHADKIYVMQQGHIVESG 563
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
363-549 |
1.32e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsDTALADWQAQLAWIpQHATFF--YRSVAEN 440
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFV-GHRSGInpYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 441 LRLAKPDASQA-ELDEAAsKAGALEFITALPDGFdtllgeqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:PRK13540 95 CLYDIHFSPGAvGITELC-RLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180 190
....*....|....*....|....*....|.
gi 1952200779 520 HLINQAIREY-AKDHLVLVIAHRLNTVKHAD 549
Cdd:PRK13540 164 LTIITKIQEHrAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
484-568 |
1.36e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.87 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYaKDHL---VLVIAHRLNTVKH-ADKIYVMQQGHI 559
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL-QQELnmgLLFITHNLSIVRKlADRVAVMQNGRC 235
|
....*....
gi 1952200779 560 VESGQYQQL 568
Cdd:PRK15134 236 VEQNRAATL 244
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
353-568 |
1.68e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 353 TFHYPETN-EGVTDINLTLPSSGLIAFVGESGSGKS-TLFdCLLGFHhQANSAIS----INEQP---LSDTALADWQA-Q 422
Cdd:PRK09473 21 TFSTPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLL-AANGRIGgsatFNGREilnLPEKELNKLRAeQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 423 LAWI---PQHATFFYRSVAENL--------RLAKPDA---SQAELDeAASKAGALEFITALPDGFdtllgeqgeglSGGQ 488
Cdd:PRK09473 99 ISMIfqdPMTSLNPYMRVGEQLmevlmlhkGMSKAEAfeeSVRMLD-AVKMPEARKRMKMYPHEF-----------SGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 489 KQRIALARAFLKNAPVLMLDEPTAHLD----SQTEHLINQAIREYakDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREF--NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYG 244
|
....*
gi 1952200779 564 QYQQL 568
Cdd:PRK09473 245 NARDV 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
363-563 |
1.88e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 57.66 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHH---QANSAISINEQPlSDTALADWQAQLAWIPQHATFF-YRSVA 438
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIP-YKEFAEKYPGEIIYVSEEDVHFpTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 ENLrlakpdasqaeldEAASKAGALEFItalpdgfdtllgeqgEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQT 518
Cdd:cd03233 102 ETL-------------DFALRCKGNEFV---------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952200779 519 EHLINQAIREYAKD-HLVLVIA---HRLNTVKHADKIYVMQQGHIVESG 563
Cdd:cd03233 154 ALEILKCIRTMADVlKTTTFVSlyqASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
363-559 |
1.96e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSA-ISINEQPLSDTALAD-WQAQLAWIP----QHATFFYRS 436
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGeIFIDGKPVKIRNPQQaIAQGIAMVPedrkRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 VAENLRLAKPD--ASQAELDEAASKAGALEFITAL----PDGFDTLlgeqgEGLSGGQKQRIALARAFLKNAPVLMLDEP 510
Cdd:PRK13549 358 VGKNITLAALDrfTGGSRIDDAAELKTILESIQRLkvktASPELAI-----ARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 511 TAHLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTV-KHADKIYVMQQGHI 559
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLVQQGVaIIVISSELPEVlGLSDRVLVMHEGKL 483
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
359-559 |
1.96e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 359 TNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQ-LAWIP----QHATFF 433
Cdd:PRK15439 275 TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARgLVYLPedrqSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 434 YRSVAENLRLAKPDASQAELDEAASKAGALEFITALPDGFDTLlgEQG-EGLSGGQKQRIALARAFLKNAPVLMLDEPTA 512
Cdd:PRK15439 355 DAPLAWNVCALTHNRRGFWIKPARENAVLERYRRALNIKFNHA--EQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952200779 513 HLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTVKH-ADKIYVMQQGHI 559
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
363-563 |
2.07e-09 |
|
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: 56.95 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLfdcllgfhhqansaisineqpLSDTALADWQAQLAWIPQhaTFFYRSVaenLR 442
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---------------------VNEGLYASGKARLISFLP--KFSRNKL---IF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 443 LakpdasqaeldeaaskaGALEFITALPDGFDTLlGEQGEGLSGGQKQRIALARAFLKNAP--VLMLDEPTAHLD-SQTE 519
Cdd:cd03238 65 I-----------------DQLQFLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHqQDIN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1952200779 520 HLINQAIREYAKDHLVLVIAHRLNTVKHADKIYVM------QQGHIVESG 563
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
364-517 |
2.28e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 364 TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSdTALADWQAQLAWIpQHATFFYR--SVAENL 441
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-RQRDEYHQDLLYL-GHQPGIKTelTALENL 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 442 RLAKPDASQAELDEAASkagALEFITALpdGFDTLLGEQgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:PRK13538 96 RFYQRLHGPGDDEALWE---ALAQVGLA--GFEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
347-560 |
2.60e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.97 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETnEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQplsdtALADWQAQ---- 422
Cdd:PRK11614 6 LSFDKVSAHYGKI-QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK-----DITDWQTAkimr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 423 --LAWIPQHATFFYR-SVAENLRLAKPDASQAELDEAASKAGALefitaLPDGFDTLLGEQGEgLSGGQKQRIALARAFL 499
Cdd:PRK11614 80 eaVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVYEL-----FPRLHERRIQRAGT-MSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 500 KNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLV--LVIAHRLNTVKHADKIYVMQQGHIV 560
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTifLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
380-526 |
3.14e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 380 GESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATFFyrSVAENLRLAKPDASQaeldEAASK 459
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADL--STLENLHFLCGLHGR----RAKQM 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 460 AGALEFITALPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAI 526
Cdd:PRK13543 118 PGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
365-563 |
3.44e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.07 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQAQLAWIPQHATF-----FYRSVAE 439
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgditVQELVAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 440 NLRLAKPDASQAELDEAASKAGALEfitalPDGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:PRK10253 105 GRYPHQPLFTRWRKEDEEAVTKAMQ-----ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952200779 520 ----HLINQAIREyaKDHLVLVIAHRLN-TVKHADKIYVMQQGHIVESG 563
Cdd:PRK10253 180 idllELLSELNRE--KGYTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
363-578 |
3.49e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.45 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLG-FHHQANSAISINEQPLSDTALADW-QAQLAWIPQ----HATFFYRS 436
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAQAiRAGIAMVPEdrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 VAENLRLAKPD--ASQAELDEAASKAGALEFI------TALPDGFDTllgeqgeGLSGGQKQRIALARAFLKNAPVLMLD 508
Cdd:TIGR02633 356 VGKNITLSVLKsfCFKMRIDAAAELQIIGSAIqrlkvkTASPFLPIG-------RLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 509 EPTAHLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLTEQAGLFAKL 578
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVaIIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHALTQEQVLAAAL 500
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
68-307 |
3.49e-09 |
|
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: 58.21 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 68 VSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYI 147
Cdd:cd18551 35 SGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 148 PSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNAT 227
Cdd:cd18551 115 PQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 228 KRELNSISQISDDYRGATMGVLKV-AFLSSFAlefLATISVALVAVII--GFRLFFGTLDFAT--GFVVLLlapeFYL-- 300
Cdd:cd18551 195 ERETKRGGEAAERLYRAGLKAAKIeALIGPLM---GLAVQLALLVVLGvgGARVASGALTVGTlvAFLLYL----FQLit 267
|
....*..
gi 1952200779 301 PLRQMGT 307
Cdd:cd18551 268 PLSQLSS 274
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
363-563 |
5.64e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFhhqansaisinEQPLSDTALADWQAQLAWIPQHA---TFFYRSVAE 439
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL-----------VAPDEGVIKRNGKLRIGYVPQKLyldTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 440 NLRLaKPDASQAELDEAASKAGALEfitalpdgfdtLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:PRK09544 89 FLRL-RPGTKKEDILPALKRVQAGH-----------LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952200779 520 ----HLINQAIREYakDHLVLVIAHRLNTV-KHADKIYVMQQgHIVESG 563
Cdd:PRK09544 157 valyDLIDQLRREL--DCAVLMVSHDLHLVmAKTDEVLCLNH-HICCSG 202
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
365-563 |
7.32e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 56.61 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGF-HHQANS-AISINEQPLSDTAlADWQAQ----LAWipQH--------A 430
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpKYEVTSgSILLDGEDILELS-PDERARagifLAF--QYpveipgvsV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 431 TFFYRSVAENLRLAKPDASQAeLDEAASKAGALEfitaLPDGFdtLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEP 510
Cdd:COG0396 95 SNFLRTALNARRGEELSAREF-LKLLKEKMKELG----LDEDF--LDRYVNEGFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 511 TAHLDSQTEHLINQAIREYAKDHL-VLVIAH--R-LNTVKhADKIYVMQQGHIVESG 563
Cdd:COG0396 168 DSGLDIDALRIVAEGVNKLRSPDRgILIITHyqRiLDYIK-PDFVHVLVDGRIVKSG 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
365-540 |
8.98e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSdtaladwqaqlawIPQHatffyRSVAENLrLA 444
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-------------FGRE-----ASLIDAI-GR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 445 KPDASQAEldEAASKAGalefitaLPDGFdTLLGEQGEgLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQ 524
Cdd:COG2401 109 KGDFKDAV--ELLNAVG-------LSDAV-LWLRRFKE-LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170
....*....|....*....
gi 1952200779 525 AIREYAKDH---LVLVIAH 540
Cdd:COG2401 178 NLQKLARRAgitLVVATHH 196
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
58-278 |
9.95e-09 |
|
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: 56.72 E-value: 9.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 58 VMFEQANLQAVSPLLWPLAGLILVRALL----VALSERVSNRAALKIknvmRNTLLEKLSKLGPAYSEQKGHGATLNTLH 133
Cdd:cd18576 25 AALGGGDTASLNQIALLLLGLFLLQAVFsffrIYLFARVGERVVADL----RKDLYRHLQRLPLSFFHERRVGELTSRLS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 134 NGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFD 213
Cdd:cd18576 101 NDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 214 RLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKV-AFLSSFaLEFLATISVALVaVIIGFRL 278
Cdd:cd18576 181 TLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIrALFSSF-IIFLLFGAIVAV-LWYGGRL 244
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
66-309 |
1.10e-08 |
|
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: 56.73 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 66 QAVSPLLWP---LAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQY 142
Cdd:cd18546 33 GDLGVLLLAaaaYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 143 YANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLK 222
Cdd:cd18546 113 LQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 223 LFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPL 302
Cdd:cd18546 193 AFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPI 272
|
....*..
gi 1952200779 303 RQMGTHY 309
Cdd:cd18546 273 QQLSQVF 279
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
365-540 |
1.17e-08 |
|
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: 57.64 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGfhhqansaisiNEQPLSDTAladwqaqlawipqhatffyrSVAENLRLA 444
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITG-----------QEQPDSGTI--------------------EIGETVKLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 445 KPDASQAELD------EAASkaGALEFIT---------ALPDGFDTLLGEQ----GEgLSGGQKQRIALARAFLKNAPVL 505
Cdd:TIGR03719 389 YVDQSRDALDpnktvwEEIS--GGLDIIKlgkreipsrAYVGRFNFKGSDQqkkvGQ-LSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190
....*....|....*....|....*....|....*
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKdhLVLVIAH 540
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNFAG--CAVVISH 498
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
347-571 |
1.17e-08 |
|
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: 57.89 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 347 IQLNALTFHYPETNEGVT----DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINeqpLSDtalaDW--- 419
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVkavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR---VGD----EWvdm 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 420 -----------QAQLAWIPQHATFF-YRSVAENLrlakPDASQAEL-DEAASKAGALEFITAlpdGFD-----TLLGEQG 481
Cdd:TIGR03269 353 tkpgpdgrgraKRYIGILHQEYDLYpHRTVLDNL----TEAIGLELpDELARMKAVITLKMV---GFDeekaeEILDKYP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 482 EGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAI---REYAKDHLVlVIAHRLNTVKH-ADKIYVMQQG 557
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQTFI-IVSHDMDFVLDvCDRAALMRDG 504
|
250
....*....|....
gi 1952200779 558 HIVESGQYQQLTEQ 571
Cdd:TIGR03269 505 KIVKIGDPEEIVEE 518
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
484-554 |
1.34e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 1.34e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDsqtehlINQ------AIREYAK-DHLVLVIAHRLNTVKH-ADKIYVM 554
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLD------IYQrlnvarLIRELAEeGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
435-586 |
1.69e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 435 RSVAENLRL-AKPDASQAE--LDEAASKAGALEFITAL----PDGfDTLLGEqgegLSGGQKQRIALARAFLKNAPVLML 507
Cdd:PRK11288 346 HSVADNINIsARRHHLRAGclINNRWEAENADRFIRSLniktPSR-EQLIMN----LSGGNQQKAILGRWLSEDMKVILL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 508 DEPTAHLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLTEQAGLFAKLVSQGDAH 585
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVaVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQATERQALSLALPRTSAAV 500
|
.
gi 1952200779 586 A 586
Cdd:PRK11288 501 A 501
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
376-540 |
1.85e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 376 IAFVGESGSGKSTLFDCLLGfhhqansaisiNEQPlsDTALADWQAQLAWIPQHATFFYR-SVAENLRLAKPDASQAELD 454
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAG-----------VLKP--DEGEVDPELKISYKPQYIKPDYDgTVEDLLRSITDDLGSSYYK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 455 EaaskagalEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYA--KD 532
Cdd:PRK13409 435 S--------EIIKPL--QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeeRE 504
|
....*...
gi 1952200779 533 HLVLVIAH 540
Cdd:PRK13409 505 ATALVVDH 512
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
363-563 |
1.93e-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: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLsdTALADWQ-AQL--AWIPQHATFFYR-SVA 438
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI--THLPMHKrARLgiGYLPQEASIFRKlTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 439 ENLR----LAKPDASQ--AELDEaaskagalefitalpdgfdtLLGE---------QGEGLSGGQKQRIALARAFLKNAP 503
Cdd:COG1137 97 DNILavleLRKLSKKEreERLEE--------------------LLEEfgithlrksKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 504 VLMLDEPTAHLDSQTEHLINQAIReyakdHL------VLVIAHrlN---TVKHADKIYVMQQGHIVESG 563
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIR-----HLkergigVLITDH--NvreTLGICDRAYIISEGKVLAEG 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
376-540 |
2.46e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 376 IAFVGESGSGKSTLFDCLLGfhhqansaisiNEQPlsDTALADWQAQLAWIPQH-ATFFYRSVAENLRlakpDASQAELD 454
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAG-----------VLKP--DEGEVDEDLKISYKPQYiSPDYDGTVEEFLR----SANTDDFG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 455 EAASKAgalEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYA--KD 532
Cdd:COG1245 432 SSYYKT---EIIKPL--GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAenRG 506
|
....*...
gi 1952200779 533 HLVLVIAH 540
Cdd:COG1245 507 KTAMVVDH 514
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
363-563 |
2.95e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 363 VTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQ---PLSDTALADWQAQLAWIPQ--HATFFYR-- 435
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQdpYASLDPRqt 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 436 ---SVAENLR---LAKPDASQAELDEAASKAGAL-EFITALPDGFdtllgeqgeglSGGQKQRIALARAFLKNAPVLMLD 508
Cdd:PRK10261 420 vgdSIMEPLRvhgLLPGKAAAARVAWLLERVGLLpEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 509 EPTAHLDSQTEHLINQAIREYAKDHLV--LVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
436-559 |
2.95e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 54.74 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 436 SVAENLRLA-------------KPDASQAE-LDEAaskagaLEFItalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKN 501
Cdd:COG4674 101 TVFENLELAlkgdrgvfaslfaRLTAEERDrIEEV------LETI-----GLTDKADRLAGLLSHGQKQWLEIGMLLAQD 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 502 APVLMLDEPTAHL-DSQTEHLiNQAIREYAKDHLVLVIAHRLNTVKH-ADKIYVMQQGHI 559
Cdd:COG4674 170 PKLLLLDEPVAGMtDAETERT-AELLKSLAGKHSVVVVEHDMEFVRQiARKVTVLHQGSV 228
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
462-563 |
3.40e-08 |
|
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: 54.93 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 462 ALEFITALPD-----------GFDTL-LGEQGEGLSGGQKQRIALARAFLKNAP---VLMLDEPTAHLDSQ-TEHLINQA 525
Cdd:cd03271 136 ALEFFENIPKiarklqtlcdvGLGYIkLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHdVKKLLEVL 215
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1952200779 526 IREYAKDHLVLVIAHRLNTVKHADKIYVM------QQGHIVESG 563
Cdd:cd03271 216 QRLVDKGNTVVVIEHNLDVIKCADWIIDLgpeggdGGGQVVASG 259
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
482-554 |
4.50e-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: 54.29 E-value: 4.50e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 482 EGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKD-HLVLVIAHRLNTVKH-ADKIYVM 554
Cdd:cd03236 138 DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDdNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
376-563 |
5.05e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 54.42 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 376 IAFVGESGSGKSTLFDCLlGFHHQANS-AISINEQPLS-------DTALADWQ------AQLAWIPQHatfF----YRSV 437
Cdd:COG4598 37 ISIIGSSGSGKSTFLRCI-NLLETPDSgEIRVGGEEIRlkpdrdgELVPADRRqlqrirTRLGMVFQS---FnlwsHMTV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 438 AEN--------LRLAKpdasqaelDEAASKAGALEFITALPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDE 509
Cdd:COG4598 113 LENvieapvhvLGRPK--------AEAIERAEALLAKVGLADKRDAYPAH----LSGGQQQRAAIARALAMEPEVMLFDE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 510 PTAHLDSQTEHLINQAIREYAKDH-LVLVIAHRLNTVKH-ADKIYVMQQGHIVESG 563
Cdd:COG4598 181 PTSALDPELVGEVLKVMRDLAEEGrTMLVVTHEMGFARDvSSHVVFLHQGRIEEQG 236
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
484-555 |
5.86e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.96 E-value: 5.86e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAK--DHLVLVIAHRLNTVKH-ADKIYVMQ 555
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
374-560 |
6.70e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 374 GLIAFV-GESGSGKSTLFDCLLGFHHQANSAISINEQPLS---DTALADWQAQLAWIPQ-HATFFYRSVAENLRL----- 443
Cdd:PRK10908 28 GEMAFLtGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlkNREVPFLRRQIGMIFQdHHLLMDRTVYDNVAIpliia 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 444 -AKPDASQAELDEAASKAGALEFITALPDGfdtllgeqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLI 522
Cdd:PRK10908 108 gASGDDIRRRVSAALDKVGLLDKAKNFPIQ-----------LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1952200779 523 NQAIREYAKDHL-VLVIAHRLNTV-KHADKIYVMQQGHIV 560
Cdd:PRK10908 177 LRLFEEFNRVGVtVLMATHDIGLIsRRSYRMLTLSDGHLH 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
377-570 |
7.92e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 377 AFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSDTALADWQA--------QLAWIPQhatffyRSVAENLRLAKPDA 448
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEagigiihqELNLIPQ------LTIAENIFLGREFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 449 S---QAELDEAASKAGALEFITALPDGFDTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHL-DSQTEHLINq 524
Cdd:PRK10762 108 NrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFR- 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1952200779 525 AIREY-AKDHLVLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQQLTE 570
Cdd:PRK10762 183 VIRELkSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADLTE 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
365-569 |
1.01e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPL----SDTALADW----QAQLAWIPQhatffyRS 436
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALENGismvHQELNLVLQ------RS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 VAENLRLAKPDASQAELDEAASKAGALEFITALpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHL-D 515
Cdd:PRK10982 90 VMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 516 SQTEHL--INQAIREyaKDHLVLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQQLT 569
Cdd:PRK10982 168 KEVNHLftIIRKLKE--RGCGIVYISHKMEEIfQLCDEITILRDGQWIATQPLAGLT 222
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
75-309 |
1.04e-07 |
|
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: 53.63 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 75 LAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSA 154
Cdd:cd18545 46 FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 155 LIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAeqlnQERWQQ----LAVLGNYFFDRLQGLTQLKLFNATKRE 230
Cdd:cd18545 126 LTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRA----RKAWQRvrkkISNLNAYLHESISGIRVIQSFAREDEN 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 231 LNSISQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQMGTHY 309
Cdd:cd18545 202 EEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFY 280
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
362-563 |
1.65e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.88 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 362 GVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINE---QPLSDTALAD-WQAQLAWIPQH-ATFFYRS 436
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREvRRKKIAMVFQSfALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 VAENLRLAKPDASQAELDEAASKAGALEFItalpdGFDTLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDS 516
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQV-----GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 517 --QTEhLINQAIREYAK-DHLVLVIAHRLN-TVKHADKIYVMQQGHIVESG 563
Cdd:PRK10070 198 liRTE-MQDELVKLQAKhQRTIVFISHDLDeAMRIGDRIAIMQNGEVVQVG 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
361-571 |
2.73e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 361 EGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQPLSD-TALADWQAQLAWIPQ----HATFFYR 435
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlSPRERRRLGVAYIPEdrlgRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 436 SVAENLRL----AKPDASQAELDEAASKAGALEFITAL---PDGFDTLLGeqgeGLSGGQKQRIALARAFLKNAPVLMLD 508
Cdd:COG3845 352 SVAENLILgryrRPPFSRGGFLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 509 EPTAHLDSQTEHLINQAIREyAKDH--LVLVIAHRLNTV-KHADKIYVMQQGHIVESGQYQQLTEQ 571
Cdd:COG3845 428 QPTRGLDVGAIEFIHQRLLE-LRDAgaAVLLISEDLDEIlALSDRIAVMYEGRIVGEVPAAEATRE 492
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
364-557 |
5.53e-07 |
|
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: 50.32 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 364 TDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQA--NSAISINEQPLSDTaladwqaqlawipqhatfFYRSV--AE 439
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKN------------------FQRSTgyVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 440 NLRLAKPDASQAEldeaaskagALEFITALpdgfdtllgeqgEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTE 519
Cdd:cd03232 86 QQDVHSPNLTVRE---------ALRFSALL------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1952200779 520 HLINQAIREYAKDHL-VLVIAHRLNTV--KHADKIYVMQQG 557
Cdd:cd03232 145 YNIVRFLKKLADSGQaILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
364-570 |
6.66e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.92 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 364 TDINLTLPSSGLIAFVGESGSGKSTLFDcLLGFHHQANSAiSI-----NEQPLSDTALADWQAQLAWIPQH-ATFFYRSV 437
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLR-LIGGQIAPDHG-EIlfdgeNIPAMSRSRLYTVRKRMSMLFQSgALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 438 AENLrlAKPDASQAELDEAASKAGALEFITALP-DGFDTLLGEQgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDS 516
Cdd:PRK11831 102 FDNV--AYPLREHTQLPAPLLHSTVMMKLEAVGlRGAAKLMPSE---LSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 517 QTEHLINQAIRE--YAKDHLVLVIAHRLNTVKH-ADKIYVMQQGHIVESGQYQQLTE 570
Cdd:PRK11831 177 ITMGVLVKLISElnSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
376-540 |
1.04e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 376 IAFVGESGSGKSTLFDCLLG----FHHQANSAISIN------EQPLSDT---------ALADWQAQLAWipqhatffYRS 436
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGvdkeFEGEARPAPGIKvgylpqEPQLDPEktvrenveeGVAEVKAALDR--------FNE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 VAENLrlAKPDAsqaELDEAASKAGALEFITALPDGFDtlLGEQGE----------------GLSGGQKQRIALARAFLK 500
Cdd:PRK11819 108 IYAAY--AEPDA---DFDALAAEQGELQEIIDAADAWD--LDSQLEiamdalrcppwdakvtKLSGGERRRVALCRLLLE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1952200779 501 NAPVLMLDEPTAHLDSQTEHLINQAIREYAKDhlVLVIAH 540
Cdd:PRK11819 181 KPDMLLLDEPTNHLDAESVAWLEQFLHDYPGT--VVAVTH 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
484-540 |
1.13e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 1.13e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYakDHLVLVIAH 540
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY--QGTVLLVSH 495
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
477-551 |
1.22e-06 |
|
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: 51.55 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 477 LGEQGEGLSGGQKQRIALARAFLKNA---PVLMLDEPTA--HLDSqTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKI 551
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTglHFDD-IKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYI 901
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
484-552 |
1.23e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.51 E-value: 1.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 484 LSGGQKQRIALARAF----LKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIY 552
Cdd:pfam02463 1078 LSGGEKTLVALALIFaiqkYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
270-531 |
1.48e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 270 VAVIIGFRLFFgtldfatgFVVLLLAPEFYLPLRQMGTHY--------HAKLEGISAAADMVDIINQSDadehvgSSKLE 341
Cdd:TIGR00956 672 FGIIIGFTVFF--------FFVYILLTEFNKGAKQKGEILvfrrgslkRAKKAGETSASNKNDIEAGEV------LGSTD 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 342 LPIKHIQLNALTFHYPETNEGV---TDINLTLPSSG-----------------LIAFVGESGSGKSTLFDCLLGfhhQAN 401
Cdd:TIGR00956 738 LTDESDDVNDEKDMEKESGEDIfhwRNLTYEVKIKKekrvilnnvdgwvkpgtLTALMGASGAGKTTLLNVLAE---RVT 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 402 SAIS------INEQPLSDTaladWQAQLAWIPQHATFFYRS-VAENLR----LAKPDA-SQAELDEAASKAGALEFITAL 469
Cdd:TIGR00956 815 TGVItggdrlVNGRPLDSS----FQRSIGYVQQQDLHLPTStVRESLRfsayLRQPKSvSKSEKMEYVEEVIKLLEMESY 890
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 470 PDGfdtLLGEQGEGLSGGQKQRIALARAFLKNAPVLM-LDEPTAHLDSQTEHLINQAIREYAK 531
Cdd:TIGR00956 891 ADA---VVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD 950
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
474-518 |
1.53e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.53e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1952200779 474 DTLLGEqgegLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQT 518
Cdd:PRK11147 151 DAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
375-516 |
2.06e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 375 LIAFVGESGSGKSTLFDCLLGFHHQAN--SAISINEQPLSDTALAdwqaQLAWIPQHATFF-YRSVAENL------RLAK 445
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK----RTGFVTQDDILYpHLTVRETLvfcsllRLPK 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 446 PDASQAELDEAASKAGALefitALPDGFDTLLGEQG-EGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDS 516
Cdd:PLN03211 172 SLTKQEKILVAESVISEL----GLTKCENTIIGNSFiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
483-564 |
2.25e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.70 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 483 GLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ-TEHLINQAIREYAKDHLVLVIAHRL-NTVKHADKIYVMQQGHIV 560
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKII 244
|
....
gi 1952200779 561 ESGQ 564
Cdd:PRK13651 245 KDGD 248
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
359-563 |
2.49e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.26 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 359 TNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGfhHQANSAI---------SINEQPlsdtalADWQAQLAWIpqh 429
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYKILegdilfkgeSILDLE------PEERAHLGIF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 430 ATFFYR------SVAENLRLA----KPDASQAELDeaaskagALEFITALPDGFDtLLGEQ--------GEGLSGGQKQR 491
Cdd:CHL00131 88 LAFQYPieipgvSNADFLRLAynskRKFQGLPELD-------PLEFLEIINEKLK-LVGMDpsflsrnvNEGFSGGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 492 IALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYA-KDHLVLVIAH--RLNTVKHADKIYVMQQGHIVESG 563
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
375-563 |
2.94e-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: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 375 LIAFVGESGSGKSTLFDCLL----GFHHQANSAISINEQPLSDTaLADWQAQLAWIPQHATFF-YRSVAENL----RLAK 445
Cdd:TIGR00956 89 LTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFpHLTVGETLdfaaRCKT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 446 PDASQAELDE---AASKAGALEFITALPDGFDTLLG-EQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHL 521
Cdd:TIGR00956 168 PQNRPDGVSReeyAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALE 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1952200779 522 INQAIREYAK--DHLVLVIAHRL--NTVKHADKIYVMQQGHIVESG 563
Cdd:TIGR00956 248 FIRALKTSANilDTTPLVAIYQCsqDAYELFDKVIVLYEGYQIYFG 293
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
484-557 |
4.29e-06 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 47.84 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAF----LKNAPVLMLDEPTAHLD-SQTEHLINqAIREYAKDHLVLVIAHRLNTVKHADKIY-VMQQG 557
Cdd:cd03278 114 LSGGEKALTALALLFaifrVRPSPFCVLDEVDAALDdANVERFAR-LLKEFSKETQFIVITHRKGTMEAADRLYgVTMQE 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
484-567 |
6.90e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYA-KDHLVLVIAHRL-NTVKHADKIYVMQQGH--- 558
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMpELLGITDRILVMSNGLvag 471
|
....*....
gi 1952200779 559 IVESGQYQQ 567
Cdd:PRK10982 472 IVDTKTTTQ 480
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
43-284 |
1.00e-05 |
|
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: 47.47 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 43 LMIASCYLLANAAhqvmfeqanlqaVSPLLWPLAGLIL----VR--ALLVALS---ER-VSNRAALKIKNVMRNTLLEKL 112
Cdd:cd18585 11 LLALSGWFISAAA------------LAGLAAPTFNYFTpaagVRgfAITRTAGrygERlVSHDATFRLLSNLRVWFYRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 113 SKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYI-PSVAysALIplAILVMIFPTDY-------KAGLIFLLTAPLIPF 184
Cdd:cd18585 79 EPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLsPPVV--ALL--VILATILFLAFfspalalILLAGLLLAGVVIPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 185 FMILVGHK-AEQLNQERwqqlAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFLA 263
Cdd:cd18585 155 LFYRLGKKiGQQLVQLR----AELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLS 230
|
250 260
....*....|....*....|.
gi 1952200779 264 TISVALVAVIIGFRLFFGTLD 284
Cdd:cd18585 231 GLTVWLVLWLGAPLVQNGALD 251
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
484-563 |
1.13e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.81 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYA-KDHLVLV-IAHRLNTVKH-ADKIYVMQQGHIV 560
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVlITHDLALVAEaAHKIIVMYAGQVV 233
|
...
gi 1952200779 561 ESG 563
Cdd:PRK11022 234 ETG 236
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
344-528 |
1.15e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 344 IKHIQLNALTFHYpetneGVTDINLTlpsSGLIAFVGESGSGKSTLFDCL-LGFHHQANSAISINEQPLSDTALADW--- 419
Cdd:COG0419 2 LLRLRLENFRSYR-----DTETIDFD---DGLNLIVGPNGAGKSTILEAIrYALYGKARSRSKLRSDLINVGSEEASvel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 420 --------------QAQLAWIPQHA-------------TFFYRSVAENLRLAKPDAsQAELDEAASKAGALEFITALPDG 472
Cdd:COG0419 74 efehggkryrierrQGEFAEFLEAKpserkealkrllgLEIYEELKERLKELEEAL-ESALEELAELQKLKQEILAQLSG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 473 FDTLlgeqgEGLSGGQKQRIALARAFlknapVLMLDepTAHLDSQTEHLINQAIRE 528
Cdd:COG0419 153 LDPI-----ETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEE 196
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
478-573 |
1.34e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 478 GEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKD-HLVLVIAHRLNTVKH-ADKIYVMQ 555
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|....*...
gi 1952200779 556 QGHIVESGQYQQLTEQAG 573
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
92-305 |
2.44e-05 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 46.64 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 92 VSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYY-ANYIPSVAYSALIPLAILVMIFpTDYK 170
Cdd:cd18554 69 FAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFItTGLMNIWLDMITIIIAICIMLV-LNPK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 171 AGLIFLLtapLIPFFMILVGH---KAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSISQISDDYRGATMG 247
Cdd:cd18554 148 LTFVSLV---IFPFYILAVKYffgRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALK 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200779 248 VLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQM 305
Cdd:cd18554 225 HTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRL 282
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
365-540 |
2.64e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGFhhqansaisinEQPLSDTAladwqaqlawipqhatffyrSVAENLRLA 444
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ-----------EQPDSGTI--------------------KIGETVKLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 445 KPDASQAELD------EAASkaGALEFIT---------ALPDGFDTLLGEQ----GEgLSGGQKQRIALARAFLKNAPVL 505
Cdd:PRK11819 391 YVDQSRDALDpnktvwEEIS--GGLDIIKvgnreipsrAYVGRFNFKGGDQqkkvGV-LSGGERNRLHLAKTLKQGGNVL 467
|
170 180 190
....*....|....*....|....*....|....*
gi 1952200779 506 MLDEPTAHLDSQTEHLINQAIREYAKdhLVLVIAH 540
Cdd:PRK11819 468 LLDEPTNDLDVETLRALEEALLEFPG--CAVVISH 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
484-556 |
3.47e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 3.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 484 LSGGQKQRIALARAF----LKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIY--VMQQ 556
Cdd:TIGR02168 1090 LSGGEKALTALALLFaifkVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYgvTMQE 1168
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
444-545 |
5.04e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 444 AKPDASqaelDEAASKAGALEFITALPDGF-------DTLLG-----EQGEGL----SGGQKQRIALARAFLKNAPVLML 507
Cdd:PRK15064 104 ALPEMS----EEDGMKVADLEVKFAEMDGYtaearagELLLGvgipeEQHYGLmsevAPGWKLRVLLAQALFSNPDILLL 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1952200779 508 DEPTAHLDSQT----EHLINQaireyaKDHLVLVIAH-R--LNTV 545
Cdd:PRK15064 180 DEPTNNLDINTirwlEDVLNE------RNSTMIIISHdRhfLNSV 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
442-545 |
5.37e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 RLAKPDASQAElDEAASKAGALEFItalPDgfdtLLGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHL 521
Cdd:PLN03073 311 RLELIDAYTAE-ARAASILAGLSFT---PE----MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLW 382
|
90 100
....*....|....*....|....*..
gi 1952200779 522 INQAIREYAKDhlVLVIAHR---LNTV 545
Cdd:PLN03073 383 LETYLLKWPKT--FIVVSHArefLNTV 407
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
365-563 |
7.20e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.56 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTL-FDCLLG----------------FHHQANS-----------AISINEQPLSDTAl 416
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLaFDTIYAegqrryveslsayarqFLGQMDKpdvdsieglspAIAIDQKTTSRNP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 417 adwqaqlawipqHATFfyRSVAE---NLRLAkpdasqaeldeaASKAGALEFITALPD-GFDTL-LGEQGEGLSGGQKQR 491
Cdd:cd03270 92 ------------RSTV--GTVTEiydYLRLL------------FARVGIRERLGFLVDvGLGYLtLSRSAPTLSGGEAQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 492 IALARAFLKN-APVL-MLDEPTAHLDSQTEHLINQAIREYaKDH--LVLVIAHRLNTVKHADKIYVM------QQGHIVE 561
Cdd:cd03270 146 IRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRL-RDLgnTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVA 224
|
..
gi 1952200779 562 SG 563
Cdd:cd03270 225 QG 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
342-528 |
7.38e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 342 LPIkhIQLNALTFHYPETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFdcllgfhhqanSAISINEQPLSDTALADWQA 421
Cdd:PLN03073 506 PPI--ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTIL-----------KLISGELQPSSGTVFRSAKV 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 422 QLAWIPQH-ATFFYRSVAENLRLAK--PDASQAELDEAASKAGalefITAlpdgfdTLLGEQGEGLSGGQKQRIALARAF 498
Cdd:PLN03073 573 RMAVFSQHhVDGLDLSSNPLLYMMRcfPGVPEQKLRAHLGSFG----VTG------NLALQPMYTLSGGQKSRVAFAKIT 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 499 LKNAPVLMLDEPTAHLD---------------------SQTEHLINQAIRE 528
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDldavealiqglvlfqggvlmvSHDEHLISGSVDE 693
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
75-276 |
1.04e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 44.50 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 75 LAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLhNGVEALHQYYAnyipSVAYSA 154
Cdd:cd18566 48 VVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLT----GQALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 155 LIPLAILVMIFptdykaGLIFLLTAPL--IPFFM--------ILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLF 224
Cdd:cd18566 123 LLDLPFVLIFL------GLIWYLGGKLvlVPLVLlglfvlvaILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAM 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1952200779 225 NATKRELNSISQISddyRGATMGVLKVAFLSSFALEFLATISVALVAVIIGF 276
Cdd:cd18566 197 AMEPQMLRRYERLQ---ANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAF 245
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
365-529 |
1.30e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTLFDCLLGfhhqansaisiNEQPlsDTALADW--QAQLAWIPQ-HATFFyrsvAENL 441
Cdd:PRK15064 337 NLNLLLEAGERLAIIGENGVGKTTLLRTLVG-----------ELEP--DSGTVKWseNANIGYYAQdHAYDF----ENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 RLAK--PDASQAELDEAASKA--GALEFitalpdGFDTLlGEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQ 517
Cdd:PRK15064 400 TLFDwmSQWRQEGDDEQAVRGtlGRLLF------SQDDI-KKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
170
....*....|..
gi 1952200779 518 TEHLINQAIREY 529
Cdd:PRK15064 473 SIESLNMALEKY 484
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
366-559 |
1.38e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 366 INLTLPSSGLIAFVGESGSGKSTLFDCLLGfhhqansaisiNEQPLS-DTALADwQAQLAWIPQHATFFYRSVAENL--- 441
Cdd:PRK10636 331 IKLNLVPGSRIGLLGRNGAGKSTLIKLLAG-----------ELAPVSgEIGLAK-GIKLGYFAQHQLEFLRADESPLqhl 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 442 -RLAKPDASQAELDEAASKAGALEFITalpdgfdtllgEQGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEH 520
Cdd:PRK10636 399 aRLAPQELEQKLRDYLGGFGFQGDKVT-----------EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1952200779 521 LINQAIREYakDHLVLVIAHRLNTVKH-ADKIYVMQQGHI 559
Cdd:PRK10636 468 ALTEALIDF--EGALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
484-560 |
1.47e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 1.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKD-HLVLVIAHRLNTV-KHADKIYVMQQGHIV 560
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEgKGVIVISSELPELlGMCDRIYVMNEGRIT 483
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
472-557 |
1.79e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 472 GFDTL-LGEQGEGLSGGQKQRIALARAFL---KNAPVLMLDEPTAHLDSQTEH-LINQAIREYAKDHLVLVIAHRLNTVK 546
Cdd:PRK00635 797 GLDYLpLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKaLIYVLQSLTHQGHTVVIIEHNMHVVK 876
|
90
....*....|.
gi 1952200779 547 HADkiYVMQQG 557
Cdd:PRK00635 877 VAD--YVLELG 885
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
484-568 |
3.40e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.87 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAfLKNAPVLML-DEPTAHLDSQTEHLINQAIREYAKDH--LVLVIAHRLNTVKH-ADKIYVMQQGHI 559
Cdd:PRK15093 159 LTEGECQKVMIAIA-LANQPRLLIaDEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQT 237
|
....*....
gi 1952200779 560 VESGQYQQL 568
Cdd:PRK15093 238 VETAPSKEL 246
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
43-288 |
3.89e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 42.47 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 43 LMIASCYLLA--NAAHQVM---FEQANLQAVSPLLWPLAGLILVRALLVA--------LSERVSNRaalkiknvMRNTLL 109
Cdd:cd18575 5 LLIAAAATLAlgQGLRLLIdqgFAAGNTALLNRAFLLLLAVALVLALASAlrfylvswLGERVVAD--------LRKAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 110 EKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILV 189
Cdd:cd18575 77 AHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 190 GHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSisqisddYRGATMGVLKVAFLSSFALEFLATISVAL 269
Cdd:cd18575 157 GRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQR-------FATAVEAAFAAALRRIRARALLTALVIFL 229
|
250
....*....|....*....
gi 1952200779 270 VAVIIGFRLFFGTLDFATG 288
Cdd:cd18575 230 VFGAIVFVLWLGAHDVLAG 248
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
376-581 |
4.03e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 376 IAFVGESGSGKSTLFDCLLGfhhqansaiSINEQPLSDTALADWQaqLAWIPQHATFFYRSVAENLRLAKPDASQ--AEL 453
Cdd:PRK10636 30 VGLVGKNGCGKSTLLALLKN---------EISADGGSYTFPGNWQ--LAWVNQETPALPQPALEYVIDGDREYRQleAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 454 DEA---------ASKAGALEFITA---------LPDGfdtlLGEQGEGL-------SGGQKQRIALARAFLKNAPVLMLD 508
Cdd:PRK10636 99 HDAnerndghaiATIHGKLDAIDAwtirsraasLLHG----LGFSNEQLerpvsdfSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952200779 509 EPTAHLDSQTEHLINQAIREYAKDhLVLVIAHR--LNTVkhADKIYVMQQGHIVE-SGQYQQLTEQAGlfAKLVSQ 581
Cdd:PRK10636 175 EPTNHLDLDAVIWLEKWLKSYQGT-LILISHDRdfLDPI--VDKIIHIEQQSLFEyTGNYSSFEVQRA--TRLAQQ 245
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
367-540 |
4.17e-04 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 42.57 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 367 NLTL-PSSGLIAFVGESGSGKSTLFDC---LLGF---------------------------------------------- 396
Cdd:cd03241 14 ELELdFEEGLTVLTGETGAGKSILLDAlslLLGGrasadlirsgaekavvegvfdisdeeeakalllelgieddddliir 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 397 ---HHQANSAISINEQPLSDTALADWQAQLAWIP-QHatffyrsvaENLRLAKPDASQAELDEAASKagaLEF-ITALPD 471
Cdd:cd03241 94 reiSRKGRSRYFINGQSVTLKLLRELGSLLVDIHgQH---------DHQNLLNPERQLDLLDGGLDD---VEFlFSTNPG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 472 gfdTLLGEQGEGLSGGQKQRIALA----RAFLKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAH 540
Cdd:cd03241 162 ---EPLKPLAKIASGGELSRLMLAlkaiLARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCITH 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
460-551 |
4.46e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 460 AGALEfITALPDGFDTllgEQGEGLSGGQKQRIALARAF----LKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLV 535
Cdd:TIGR02169 1055 AGGLE-LSAKPKGKPV---QRLEAMSGGEKSLTALSFIFaiqrYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQF 1130
|
90
....*....|....*.
gi 1952200779 536 LVIAHRLNTVKHADKI 551
Cdd:TIGR02169 1131 IVVSLRSPMIEYADRA 1146
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
462-551 |
5.13e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 462 ALEFITALP---DGFDTL---------LGEQGEGLSGGQKQRIALARAFLKNA---PVLMLDEPTA--HLDSqTEHLIN- 523
Cdd:PRK00349 797 ALEFFEAIPkiaRKLQTLvdvglgyikLGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTglHFED-IRKLLEv 875
|
90 100
....*....|....*....|....*....
gi 1952200779 524 -QAIREyaKDHLVLVIAHRLNTVKHADKI 551
Cdd:PRK00349 876 lHRLVD--KGNTVVVIEHNLDVIKTADWI 902
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
32-305 |
6.09e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 42.08 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 32 LSISLGTLNALLMIASCYLLanaahQVMFEQANLQAVSPLLWPLAGLILVRALLVAL----SERVSNRAALKIKNVMRNT 107
Cdd:cd18550 3 LVLLLILLSALLGLLPPLLL-----REIIDDALPQGDLGLLVLLALGMVAVAVASALlgvvQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 108 LLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLtapLIPFFMI 187
Cdd:cd18550 78 LYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLV---LLPLFVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 188 L---VGHKAEQLNQERWQQLAVLGNYFFDRL--QGLTQLKLFNATKRELNSISQISDDYRGATMGVLKVAFLSSFALEFL 262
Cdd:cd18550 155 PtrrVGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLF 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1952200779 263 ATISVALVAVIIGFRLFFGTLDFAT--GFVVLLlaPEFYLPLRQM 305
Cdd:cd18550 235 TAIGPALVYWVGGLLVIGGGLTIGTlvAFTALL--GRLYGPLTQL 277
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
71-323 |
6.65e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 42.11 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 71 LLWPLA----GLILVRALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANY 146
Cdd:cd18564 52 LLLLAAaalvGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 147 IPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVG---HKAEQLNQERWQQLAVLGNyffdrlQGLTQLKL 223
Cdd:cd18564 132 VLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSrriKEASREQRRREGALASVAQ------ESLSAIRV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 224 FNATKRElnsiSQISDDYRGATMGVLKvAFLSSFALEFLATISVA-LVAVIIGFRLFFGTLDFATG---------FVVLL 293
Cdd:cd18564 206 VQAFGRE----EHEERRFARENRKSLR-AGLRAARLQALLSPVVDvLVAVGTALVLWFGAWLVLAGrltpgdllvFLAYL 280
|
250 260 270
....*....|....*....|....*....|
gi 1952200779 294 LApeFYLPLRQMGtHYHAKLEGISAAADMV 323
Cdd:cd18564 281 KN--LYKPVRDLA-KLTGRIAKASASAERV 307
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
484-571 |
6.69e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.00 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 484 LSGGQKQRIALARAFLKNAPVLMLDEPTAHLD--SQTEhlINQAIREYAKDHLVLVI--AHRLNTVKH-ADKIYVMQQGH 558
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvSKEA--IREFLKEYNRERGTTILltSHDMDDIEAlCDRVIVIDHGR 232
|
90
....*....|...
gi 1952200779 559 IVESGQYQQLTEQ 571
Cdd:COG4586 233 IIYDGSLEELKER 245
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
379-559 |
6.97e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 379 VGESGSGKSTLFDCLLGFHHQ--ANSAISINEQPLSDTALADWQAQLAWIPQHATFFYRsVAENLR-------------- 442
Cdd:PRK10938 292 VGPNGAGKSTLLSLITGDHPQgySNDLTLFGRRRGSGETIWDIKKHIGYVSSSLHLDYR-VSTSVRnvilsgffdsigiy 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 443 LAKPDASQAEldeaaskagALEFITALpdGFDTLLGEQG-EGLSGGQkQRIAL-ARAFLKNAPVLMLDEPTAHLDSQTEH 520
Cdd:PRK10938 371 QAVSDRQQKL---------AQQWLDIL--GIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQ 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 521 L----INQAIREyAKDHLVLV----------IAHRLNTVKHADkIYVMQQGHI 559
Cdd:PRK10938 439 LvrrfVDVLISE-GETQLLFVshhaedapacITHRLEFVPDGD-IYRYVQTKL 489
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
472-568 |
1.20e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 472 GFDTL-LGEQGEGLSGGQKQRIALAR---AFLKNapVL-MLDEPTAHLDSQ-TEHLINQAIREYAKDHLVLVIAHRLNTV 545
Cdd:TIGR00630 476 GLDYLsLSRAAGTLSGGEAQRIRLATqigSGLTG--VLyVLDEPSIGLHQRdNRRLINTLKRLRDLGNTLIVVEHDEDTI 553
|
90 100
....*....|....*....|....*....
gi 1952200779 546 KHADKIYVM------QQGHIVESGQYQQL 568
Cdd:TIGR00630 554 RAADYVIDIgpgageHGGEVVASGTPEEI 582
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
364-393 |
1.32e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.17 E-value: 1.32e-03
10 20 30
....*....|....*....|....*....|
gi 1952200779 364 TDINLtlpSSGLIAFVGESGSGKSTLFDCL 393
Cdd:pfam13476 12 QTIDF---SKGLTLITGPNGSGKTTILDAI 38
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
370-464 |
1.52e-03 |
|
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.
Pssm-ID: 410924 [Multi-domain] Cd Length: 179 Bit Score: 39.67 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 370 LPSSGLIAFVGESGSGKSTLFDCLLGF-----HHQANsaISINEQPL--------SDTALADwQAQlawIPQHATFFYRS 436
Cdd:cd19516 8 FPREGLVYVAGATGSGKSTLLAAIYRYilendPPDRK--IITYEDPIefvydgikSKHSIIV-QSQ---IPRHFKSFAKA 81
|
90 100
....*....|....*....|....*....
gi 1952200779 437 VAENLRlAKPDA-SQAELDEAASKAGALE 464
Cdd:cd19516 82 VREALR-RKPSLiGVGELRDQETISAAVE 109
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
357-547 |
1.64e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 41.27 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 357 PETNEGVTDINLTLPSSGLIAFVGESGSGKSTLFDCLLGFHHQANSAISINEQplsdtaladwqAQLAWIPQHATFFYRS 436
Cdd:TIGR00954 462 PNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 437 VAEnlRLAKPDASQAELDEAASKAgALEFITALPDgFDTLLGEQG---------EGLSGGQKQRIALARAFLKNAPVLML 507
Cdd:TIGR00954 531 LRD--QIIYPDSSEDMKRRGLSDK-DLEQILDNVQ-LTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1952200779 508 DEPTAHLDSQTEHLINQAIREYAKDhlVLVIAHRLNTVKH 547
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREFGIT--LFSVSHRKSLWKY 644
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
365-391 |
1.95e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 1.95e-03
10 20
....*....|....*....|....*...
gi 1952200779 365 DINLTLPSSGLIAFVGESGSGKSTL-FD 391
Cdd:PRK00349 18 NIDLDIPRDKLVVFTGLSGSGKSSLaFD 45
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
436-573 |
2.43e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 436 SVAENLRL-AK-----PDASQAELDEAASKAGALEFITALPDGfdtllgeqgegLSGGQKQRIALARAFLKNAPVLMLDE 509
Cdd:NF033858 355 TVRQNLELhARlfhlpAAEIAARVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDE 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 510 PTAHLDSQT-----EHLINQAiREyakDHLVLVIA-HRLNTVKHADKIYVMQQGHIVESGQYQQLTEQAG 573
Cdd:NF033858 424 PTSGVDPVArdmfwRLLIELS-RE---DGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
478-552 |
2.47e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 39.21 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 478 GEQGEGLSGGQKQRIALARAF----LKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHL-VLVIAHRLNTVKHADKIY 552
Cdd:cd03239 89 GKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSqFIVITLKKEMFENADKLI 168
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
75-285 |
2.60e-03 |
|
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: 40.07 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 75 LAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYYANYIPSVAYSA 154
Cdd:cd18548 45 MLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 155 LIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKLFNATKRELNSI 234
Cdd:cd18548 125 IMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERF 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952200779 235 SQISDDYRGATMGVLKVAFLSSFALEFLATISVALVAVIIGFRLFFGTLDF 285
Cdd:cd18548 205 DKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQV 255
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
484-552 |
2.82e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 39.55 E-value: 2.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952200779 484 LSGGQKQRIALARAF----LKNAPVLMLDEPTAHLDSQTEHLINQAIREYAKDHLVLVIAHRLNTVKHADKIY 552
Cdd:cd03272 159 LSGGQKSLVALALIFaiqkCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFY 231
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
484-551 |
3.57e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 3.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952200779 484 LSGGQKQRIALARAFLKNAP---VLMLDEPTA--HLDsQTEHLIN--QAIREyaKDHLVLVIAHRLNTVKHADKI 551
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTglHFH-DIRKLLEvlHRLVD--KGNTVVVIEHNLDVIKTADWI 898
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
376-404 |
4.71e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 4.71e-03
10 20
....*....|....*....|....*....
gi 1952200779 376 IAFVGESGSGKSTLFDCLLGFHHQANSAI 404
Cdd:PRK01889 198 VALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
469-549 |
6.41e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 469 LPDGFDTLLGeqGEGLSGGQKQRIALARAFLKNAPVLMLDEPTAHLD----SQTEHLINQAIREYAKDHLVLVIAHRLNT 544
Cdd:PRK01156 795 MVEGIDSLSG--GEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDedrrTNLKDIIEYSLKDSSDIPQVIMISHHREL 872
|
....*
gi 1952200779 545 VKHAD 549
Cdd:PRK01156 873 LSVAD 877
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
64-270 |
8.92e-03 |
|
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: 38.31 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 64 NLQAVSPLLWPLAGLILVRALLVALSERVSNRAALKIKNVMRNTLLEKLSKLGPAYSEQKGHGATLNTLHNGVEALHQYY 143
Cdd:cd18557 31 DLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200779 144 ANYIPSVAYSALIPLAILVMIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEQLNQERWQQLAVLGNYFFDRLQGLTQLKL 223
Cdd:cd18557 111 TDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1952200779 224 FNATKRELNSIS-QISDDYRGATMGVLKVAFLSSFAlEFLATISVALV 270
Cdd:cd18557 191 FSAEEKEIRRYSeALDRSYRLARKKALANALFQGIT-SLLIYLSLLLV 237
|
|
| |
