|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-574 |
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: 724.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 12 QQSLRAFLKRQSKPAGAWLKLSIALGTFNAILMIAGAYLLAQTIHNVMFEGASLSQVTHFLWPLAGIILLRALFLAISER 91
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 92 LSAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKA 171
Cdd:COG4988 81 AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 172 GLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKI 251
Cdd:COG4988 161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 252 AFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADMVTILNAPLP 331
Cdd:COG4988 241 AFLSSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 332 EQSQQHETKFEEHISSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKP 411
Cdd:COG4988 321 AAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 412 LDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQ 491
Cdd:COG4988 401 LSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 492 RIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQ 571
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560
|
...
gi 658756163 572 QQG 574
Cdd:COG4988 561 KNG 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
28-555 |
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: 596.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 28 AWLKLSIALGTFNAILMIAGAYLLAQTIHNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQT 107
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 108 LLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMI 187
Cdd:TIGR02857 83 LLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 188 LVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISV 267
Cdd:TIGR02857 163 LIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 268 ALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADMVTILNA-PLPEQSQqhETKFEEHIS 346
Cdd:TIGR02857 243 ALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAaPRPLAGK--APVTAAPAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAW 426
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPIL 506
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVM 555
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: 578.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 8 NRAQQQSLRAFLKRQSKPAGAWLKLSIALGTFNAILMIAGAYLLAQTIHNVMFEGASLSQVTHFLWPLAGIILLRALFLA 87
Cdd:PRK11174 2 DKSRQKELTRWLKQQSKPAKRWLNLSILLGFLSGLLLIAQAWLLATILQALIIENIPREALLPPFILLILLFVLRALLAW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 88 ISERLSAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQG--ATLntVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIF 165
Cdd:PRK11174 82 LRERVGFKAGQHIRQQIRQQVLDKLQQLGPAWIQGKPAGswATL--VLEQVEDMHDFYARYLPQMALAVLVPLLILIAVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 166 PTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHAT 245
Cdd:PRK11174 160 PINWAAGLILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 246 LGVLKIAFLSSFALEFLATISVALVAVIIGFRlFFGTLDFA---------TGFVVLLLAPEFYLPLRQLGSHYHARLQGI 316
Cdd:PRK11174 240 MEVLRMAFLSSAVLEFFASISIALVAVYFGFS-YLGELNFGhygtgvtlfAGFFVLILAPEFYQPLRDLGTFYHAKAQAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 317 SAAADMVTILNAPLPEQSQQHETKFEEHISSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLG 396
Cdd:PRK11174 319 GAAESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 397 FHP-QviEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFD 475
Cdd:PRK11174 399 FLPyQ--GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 476 TLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVM 555
Cdd:PRK11174 477 TPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVM 556
|
570 580
....*....|....*....|....*.
gi 658756163 556 QNGEIAQQGTYSQLEQQQGAFKSLLN 581
Cdd:PRK11174 557 QDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-587 |
2.34e-152 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 450.00 E-value: 2.34e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 14 SLRAFLKRQSKPAGAWLKLSIALGTFNAILMIAGAYLLAQTIhNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLS 93
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRII-DALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 94 AYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGL 173
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 174 IFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAF 253
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 254 LSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADMVTILNAPLPEQ 333
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 334 SQQHETKFEEHISSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPqVIE-QISINNKPL 412
Cdd:COG1132 326 DPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD-PTSgRILIDGVDI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 413 DATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQR 492
Cdd:COG1132 405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 493 IALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQ 572
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
570
....*....|....*
gi 658756163 573 QGAFKSLLNLQAQGA 587
Cdd:COG1132 565 GGLYARLYRLQFGEE 579
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
33-322 |
1.54e-129 |
|
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: 380.99 E-value: 1.54e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 33 SIALGTFNAILMIAGAYLLAQTIHNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTKL 112
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 113 THLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSK 192
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 193 AEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVAV 272
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 658756163 273 IIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADM 322
Cdd:cd18584 241 YIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-584 |
1.13e-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: 326.02 E-value: 1.13e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 3 TNPRPNRAQQQSLRAFLKRQSKPAGAWLKLSIALGTFNAILMIAGAYLLAQTIHNVMFegaslSQVTHFLWPLA----GI 78
Cdd:COG2274 131 TPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLP-----NQDLSTLWVLAigllLA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 79 ILLRALFLAISERLSAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDgVEALHDYYAKYLPGVAYSALIPL 158
Cdd:COG2274 206 LLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 159 AILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKIS 238
Cdd:COG2274 285 IFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 239 DDFRHATLGVLKIAFLSSFALEFLATISVALVaVIIGFRLFF------GTLDFATGFVVLLLAPefylpLRQLGSHYhAR 312
Cdd:COG2274 365 AKYLNARFKLRRLSNLLSTLSGLLQQLATVAL-LWLGAYLVIdgqltlGQLIAFNILSGRFLAP-----VAQLIGLL-QR 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 313 LQGISAAADMV-TILNAPlPEQSQQHETKFEEHIS-SININNLNFTYP-NSNEGIKNINLTLPAKGLVAVVGASGSGKST 389
Cdd:COG2274 438 FQDAKIALERLdDILDLP-PEREEGRSKLSLPRLKgDIELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKST 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 390 LFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINT 469
Cdd:COG2274 517 LLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEA 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 470 LENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNA 549
Cdd:COG2274 597 LPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA 676
|
570 580 590
....*....|....*....|....*....|....*
gi 658756163 550 SNILVMQNGEIAQQGTYSQLEQQQGAFKSLLNLQA 584
Cdd:COG2274 677 DRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-582 |
1.57e-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: 319.02 E-value: 1.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 15 LRAFLkRQSKPAGAWLKLSIALGT----FNAILMIAGAYLLAQTihnvmfegASLSQVTHFLWPLAGIillRalFLAIS- 89
Cdd:COG4987 3 LLRLL-RLLRPHRGRLLLGVLLGLltllAGIGLLALSGWLIAAA--------ALAPPILNLFVPIVGV---R--AFAIGr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 90 ------ERL-SAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAK-YLPGVAYSALIPLAIL 161
Cdd:COG4987 69 tvfrylERLvSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRvLLPLLVALLVILAAVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 162 VVIFpTDYKAGLI----FLLTAPLIPFFMILVGSKAEAlnqkRWQQL-AVLGNYFFDRVQGLTQLKLFNATQQELKQIAK 236
Cdd:COG4987 149 FLAF-FSPALALVlalgLLLAGLLLPLLAARLGRRAGR----RLAAArAALRARLTDLLQGAAELAAYGALDRALARLDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 237 ISDDFRHATLGVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLDfATGFVVLLLAP----EFYLPLRQLGSHYHar 312
Cdd:COG4987 224 AEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAAlalfEALAPLPAAAQHLG-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 313 lQGISAAADMVTILNAPLPEQSQQHETKFEEHiSSININNLNFTYPNSNEGI-KNINLTLPAKGLVAVVGASGSGKSTLF 391
Cdd:COG4987 301 -RVRAAARRLNELLDAPPAVTEPAEPAPAPGG-PSLELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 392 DCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLE 471
Cdd:COG4987 379 ALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 472 NGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASN 551
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDR 538
|
570 580 590
....*....|....*....|....*....|.
gi 658756163 552 ILVMQNGEIAQQGTYSQLEQQQGAFKSLLNL 582
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
70-583 |
1.71e-82 |
|
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: 269.28 E-value: 1.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 70 HFLW--PLA--GIILLRALFLAISERLSAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAK 145
Cdd:TIGR02203 51 SVLWwvPLVviGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 146 YLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFN 225
Cdd:TIGR02203 131 AFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 226 ATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTL---DFaTGFVVLLLApeFYLPL 302
Cdd:TIGR02203 211 GQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLtagDF-TAFITAMIA--LIRPL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 303 RQLgSHYHARLQ-GISAAADMVTILNAPlPEQsQQHETKFEEHISSININNLNFTYP-NSNEGIKNINLTLPAKGLVAVV 380
Cdd:TIGR02203 288 KSL-TNVNAPMQrGLAAAESLFTLLDSP-PEK-DTGTRAIERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 381 GASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPA-ATQLELEQAAH 459
Cdd:TIGR02203 365 GRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALA 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 460 QAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVI 539
Cdd:TIGR02203 445 AAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 658756163 540 AHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLLNLQ 583
Cdd:TIGR02203 525 AHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
348-583 |
1.17e-77 |
|
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: 245.53 E-value: 1.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPN--SNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIA 425
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPI 505
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 506 LVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLLNLQ 583
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
348-579 |
8.58e-77 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 243.29 E-value: 8.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI-KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAW 426
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPIL 506
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSL 579
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
348-574 |
5.84e-76 |
|
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: 240.98 E-value: 5.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWI 427
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILV 507
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 508 LDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQG 574
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
348-583 |
2.92e-74 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 236.74 E-value: 2.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWI 427
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILV 507
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 508 LDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLLNLQ 583
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
71-583 |
2.50e-72 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 242.62 E-value: 2.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 71 FLW-PLA--GIILLRALFLAISERLSAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVhdgvealhDYYAKYL 147
Cdd:PRK11176 64 LKWmPLVviGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRI--------TYDSEQV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 148 PGVAYSALIP--------LAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLT 219
Cdd:PRK11176 136 ASSSSGALITvvregasiIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 220 QLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFY 299
Cdd:PRK11176 216 EVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALM 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 300 LPLRQLgSHYHARLQ-GISAAADMVTILNAplpEQSQQHETKFEEHIS-SININNLNFTYPNSNE-GIKNINLTLPAKGL 376
Cdd:PRK11176 296 RPLKSL-TNVNAQFQrGMAACQTLFAILDL---EQEKDEGKRVIERAKgDIEFRNVTFTYPGKEVpALRNINFKIPAGKT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAA-TQLELE 455
Cdd:PRK11176 372 VALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 456 QAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHL 535
Cdd:PRK11176 452 EAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRT 531
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 658756163 536 VLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLLNLQ 583
Cdd:PRK11176 532 SLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
33-319 |
4.33e-72 |
|
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: 232.94 E-value: 4.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 33 SIALGTFNAILMIAGAYLLAQTIhNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTKL 112
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARAL-ARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 113 THLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSK 192
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 193 AEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVAV 272
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 658756163 273 IIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAA 319
Cdd:cd18561 240 VGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAA 286
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
222-587 |
1.64e-71 |
|
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: 240.88 E-value: 1.64e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 222 KLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTL---DFAtgFVVLLLApEF 298
Cdd:COG5265 232 KYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMtvgDFV--LVNAYLI-QL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 299 YLPLRQLGSHYHARLQGISAAADMVTIL----------NAPlPEQSQQHETKFEehissininNLNFTYPNSNEGIKNIN 368
Cdd:COG5265 309 YIPLNFLGFVYREIRQALADMERMFDLLdqppevadapDAP-PLVVGGGEVRFE---------NVSFGYDPERPILKGVS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 369 LTLPAKGLVAVVGASGSGKSTLFDCLLGFHpQVIE-QISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKP 447
Cdd:COG5265 379 FEVPAGKTVAIVGPSGAGKSTLARLLFRFY-DVTSgRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 448 AATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAI 527
Cdd:COG5265 458 DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 528 NKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLLNLQAQGA 587
Cdd:COG5265 538 REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEE 597
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
348-559 |
4.99e-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: 210.32 E-value: 4.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNS-NEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAW 426
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFYQSISDNIkiakpaatqleleqaahqagaldfintlengfdtligeqgegLSGGQKQRIALARAFLKQAPIL 506
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGE 559
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
153-583 |
8.64e-65 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 222.27 E-value: 8.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 153 SALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELK 232
Cdd:TIGR02204 142 NALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 233 QiakisddFRHATLGVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATG---------FVvlLLAPEFYLPLR 303
Cdd:TIGR02204 222 R-------FGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGkmsagtlgqFV--FYAVMVAGSIG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 304 QLgSHYHARLQGISAAAD-MVTILNA----PLPEQSQQHETKFEEHISsinINNLNFTYPNSNE--GIKNINLTLPAKGL 376
Cdd:TIGR02204 293 TL-SEVWGELQRAAGAAErLIELLQAepdiKAPAHPKTLPVPLRGEIE---FEQVNFAYPARPDqpALDGLNLTVRPGET 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQ 456
Cdd:TIGR02204 369 VALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 457 AAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLV 536
Cdd:TIGR02204 449 AARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTT 528
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 658756163 537 LVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLLNLQ 583
Cdd:TIGR02204 529 LIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
72-586 |
5.41e-64 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 220.60 E-value: 5.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 72 LWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLT----KLTHLGPSYIEQHGQGATLNTVHDGVEALH----DYY 143
Cdd:PRK13657 55 IFPLLAAWAGFGLFNIIAGVLVARHADRLAHRRRLAVLTeyfeRIIQLPLAWHSQRGSGRALHTLLRGTDALFglwlEFM 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 144 AKYLpgvaySALIPLAILV-VIFPTDYKAGLIflLTAPLIPFFMI--LVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQ 220
Cdd:PRK13657 135 REHL-----ATLVALVVLLpLALFMNWRLSLV--LVVLGIVYTLIttLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 221 LKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVAVI------------------IGF-RLFFG 281
Cdd:PRK13657 208 VQSYNRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRAASTITMLAILVLgaalvqkgqlrvgevvafVGFaTLLIG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 282 TLDFATGFVVLLLAPEfylplrqlgshyhARLQgisaaaDMVTILNAPLPEQSQQHETKFEEHISSININNLNFTYPNSN 361
Cdd:PRK13657 288 RLDQVVAFINQVFMAA-------------PKLE------EFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 362 EGIKNINLTLPAKGLVAVVGASGSGKSTLFDCL-LGFHPQViEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISD 440
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqRVFDPQS-GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIED 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 441 NIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTE 520
Cdd:PRK13657 428 NIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 521 QLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLlnLQAQG 586
Cdd:PRK13657 508 AKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL--LRAQG 571
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
41-580 |
8.41e-61 |
|
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: 211.67 E-value: 8.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 41 AILMIAGAYLLAQTIHNVmfegASLSQVTHFLWPLAGIillrALFLAISERLSAYAALKIKSAMRQTLLTK----LTHLG 116
Cdd:TIGR01192 32 AAITIAEPILFGRIIDAI----SSKSDVLPTLALWAGF----GVFNTIAYVLVAREADRLAHGRRATLLTEafgrIISMP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 117 PSYIEQHGQGATLNTVHDGVEALHDYYAKYL-----PGVAYSALIPLAilvviFPTDYKAGLIFLLTAPLIPFFMILVGS 191
Cdd:TIGR01192 104 LSWHQQRGTSNALHTLLRATETLFGLWLEFMrqhlaTFVALFLLIPTA-----FAMDWRLSIVLMVLGILYILIAKLVMQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 192 KAEAlnqkrwQQLAVLGNY------FFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATI 265
Cdd:TIGR01192 179 RTKN------GQAAVEHHYhnvfkhVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWALASGLNRMASTI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 266 SVALVAVI------------------IGF-RLFFGTLDFATGFVVLLLAPEfylplrqlgshyhARLQGISAAADMVTIL 326
Cdd:TIGR01192 253 SMMCILVIgtvlvikgelsvgeviafIGFaNLLIGRLDQMSGFITQIFEAR-------------AKLEDFFDLEDSVFQR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 327 NAP--LPEQSQQhetkfeehISSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQ 404
Cdd:TIGR01192 320 EEPadAPELPNV--------KGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 405 ISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEG 484
Cdd:TIGR01192 392 ILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 LSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQG 564
Cdd:TIGR01192 472 LSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKG 551
|
570
....*....|....*.
gi 658756163 565 TYSQLEQQQGAFKSLL 580
Cdd:TIGR01192 552 SFQELIQKDGRFYKLL 567
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
348-583 |
8.64e-60 |
|
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: 198.86 E-value: 8.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTY-PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAW 426
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPIL 506
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLLNLQ 583
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-543 |
2.80e-59 |
|
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: 206.44 E-value: 2.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 24 KPAGAWLKLSIALGT----FNAILMIAGAYLL--AQTIHNVMFEGASLSQVTHFlwplaGIilLRALFLAIsERLSAY-A 96
Cdd:TIGR02868 9 KPRRRRLALAVLLGAlalgSAVALLGVSAWLIsrAAEMPPVLYLSVAAVAVRAF-----GI--GRAVFRYL-ERLVGHdA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 97 ALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAK-YLPGVAYSALIPLAILV--VIFPTdykAGL 173
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRvIVPAGVALVVGAAAVAAiaVLSVP---AAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 174 IF----LLTAPLIPFFMILVGSKAE-ALNQKRWQQLAVLgnyfFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGV 248
Cdd:TIGR02868 158 ILaaglLLAGFVAPLVSLRAARAAEqALARLRGELAAQL----TDALDGAAELVASGALPAALAQVEEADRELTRAERRA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 249 LKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADMVTILNA 328
Cdd:TIGR02868 234 AAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 329 PLPEQSQQHETK--FEEHISSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQIS 406
Cdd:TIGR02868 314 AGPVAEGSAPAAgaVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 407 INNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLS 486
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLS 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 487 GGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRL 543
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
102-586 |
1.07e-57 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 203.41 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 102 SAMRQTLltklthlgpSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPL 181
Cdd:PRK10790 107 AALRQPL---------SAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 182 IPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFnatQQELKQIAKISDDFRHATLGVLKIAFLSSFALEF 261
Cdd:PRK10790 178 VLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF---RQQARFGERMGEASRSHYMARMQTLRLDGFLLRP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 262 LATISVALVavIIGFRLFFGTLDFATGFVVLLLAPEFYL-----PLRQLGSHYHARLQGISAAADMVTILNAPlpeqsQQ 336
Cdd:PRK10790 255 LLSLFSALI--LCGLLMLFGFSASGTIEVGVLYAFISYLgrlnePLIELTTQQSMLQQAVVAGERVFELMDGP-----RQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 337 HETKFEEHISS--ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDA 414
Cdd:PRK10790 328 QYGNDDRPLQSgrIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 415 TSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQ-----LELEQAAhqagalDFINTLENGFDTLIGEQGEGLSGGQ 489
Cdd:PRK10790 408 LSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEqvwqaLETVQLA------ELARSLPDGLYTPLGEQGNNLSVGQ 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 490 KQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQL 569
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQL 561
|
490
....*....|....*..
gi 658756163 570 EQQQGAFKSLLNLQAQG 586
Cdd:PRK10790 562 LAAQGRYWQMYQLQLAG 578
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
172-579 |
3.31e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 198.90 E-value: 3.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 172 GLIFLLTAPLIPFFMILVGSKA-EALNQKRwqqlAVLGNYFFDRVQGLTQLKLFNATQQELKQIAK-----ISDDFRHAT 245
Cdd:PRK11160 167 GGILLLLLLLLPLLFYRLGKKPgQDLTHLR----AQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQteqqwLAAQRRQAN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 246 LGVLKIAFLSsFALEFLATISVALVAVIIG--------FRLFFgtldFATgfvvlLLAPEFYLPL----RQLGshyharl 313
Cdd:PRK11160 243 LTGLSQALMI-LANGLTVVLMLWLAAGGVGgnaqpgalIALFV----FAA-----LAAFEALMPVagafQHLG------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 314 QGISAAADMVTILNAP----LPEQSQQHETKfeehiSSININNLNFTYPNSNEG-IKNINLTLPAKGLVAVVGASGSGKS 388
Cdd:PRK11160 306 QVIASARRINEITEQKpevtFPTTSTAAADQ-----VSLTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALLGRTGCGKS 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 389 TLFDcLLGFHPQVIE-QISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGaLDFI 467
Cdd:PRK11160 381 TLLQ-LLTRAWDPQQgEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG-LEKL 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 468 NTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVK 547
Cdd:PRK11160 459 LEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLE 538
|
410 420 430
....*....|....*....|....*....|..
gi 658756163 548 NASNILVMQNGEIAQQGTYSQLEQQQGAFKSL 579
Cdd:PRK11160 539 QFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
347-564 |
5.54e-56 |
|
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: 188.18 E-value: 5.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTYPNS-NEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIA 425
Cdd:cd03245 2 RIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPI 505
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 506 LVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQG 564
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
347-565 |
9.47e-56 |
|
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: 187.70 E-value: 9.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTY-PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIA 425
Cdd:cd03244 2 DIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLFYQSISDNIKIAKpAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPI 505
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 506 LVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
153-575 |
5.18e-53 |
|
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: 192.39 E-value: 5.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 153 SALI--PLAI--LVVIFptdYKAGLIFLLTAPLIPFfMILVGskaeALNQKRWQQLAVLGN--------YFFDRVQGLTQ 220
Cdd:TIGR03375 265 TALIdlPFALlfLLVIA---IIGGPLVWVPLVAIPL-ILLPG----LLLQRPLSRLAEESMresaqrnaVLVESLSGLET 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 221 LKLFNAT-------QQELKQIAKISDDFRHATlgvlkiAFLSSFALEFLATISVALVAV----IIGFRLFFGTLDFATgf 289
Cdd:TIGR03375 337 IKALNAEgrfqrrwEQTVAALARSGLKSRFLS------NLATNFAQFIQQLVSVAIVVVgvylISDGELTMGGLIACV-- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 290 vvlLLAPEFYLPLRQLgSHYHARLQGISAAADMV-TILNAPLPEQSQQHETKFEEHISSININNLNFTYPNSN-EGIKNI 367
Cdd:TIGR03375 409 ---MLSGRALAPLGQL-AGLLTRYQQAKTALQSLdELMQLPVERPEGTRFLHRPRLQGEIEFRNVSFAYPGQEtPALDNV 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 368 NLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKP 447
Cdd:TIGR03375 485 SLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAP 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 448 AATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAI 527
Cdd:TIGR03375 565 YADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRL 644
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 658756163 528 NKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQ-LEQQQGA 575
Cdd:TIGR03375 645 KRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQvLEALRKG 693
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
324-583 |
6.89e-53 |
|
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: 192.26 E-value: 6.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 324 TILNAPLpEQSQQHETKFEEHISSININNLNFTY-PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVI 402
Cdd:TIGR01846 433 DILNSPT-EPRSAGLAALPELRGAITFENIRFRYaPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQH 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 403 EQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQG 482
Cdd:TIGR01846 512 GQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 483 EGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQ 562
Cdd:TIGR01846 592 ANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAE 671
|
250 260
....*....|....*....|.
gi 658756163 563 QGTYSQLEQQQGAFKSLLNLQ 583
Cdd:TIGR01846 672 SGRHEELLALQGLYARLWQQQ 692
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
352-560 |
1.05e-52 |
|
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: 179.59 E-value: 1.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 352 NLNFTYPNSNEG--IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQ 429
Cdd:cd03248 16 NVTFAYPTRPDTlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 430 TPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLD 509
Cdd:cd03248 96 EPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658756163 510 EPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEI 560
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
173-580 |
7.08e-51 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 186.85 E-value: 7.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 173 LIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQiakisddFRHATLGVLKIA 252
Cdd:TIGR00958 305 MVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASR-------FKEALEETLQLN 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 253 FLSSFA-LEFLATISVALVAVIIGFrLFFGTLDFATGFV-------VLLLAPEFYLPLRQLGSHYHARLQGISAAADMVT 324
Cdd:TIGR00958 378 KRKALAyAGYLWTTSVLGMLIQVLV-LYYGGQLVLTGKVssgnlvsFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 325 ILNAPlPEQSQQHETKFEEHISSININNLNFTYPN--SNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVI 402
Cdd:TIGR00958 457 YLDRK-PNIPLTGTLAPLNLEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 403 EQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQG 482
Cdd:TIGR00958 536 GQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 483 EGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNhlVLVIAHRLNTVKNASNILVMQNGEIAQ 562
Cdd:TIGR00958 616 SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRT--VLLIAHRLSTVERADQILVLKKGSVVE 693
|
410
....*....|....*...
gi 658756163 563 QGTYSQLEQQQGAFKSLL 580
Cdd:TIGR00958 694 MGTHKQLMEDQGCYKHLV 711
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
282-583 |
3.60e-49 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 179.52 E-value: 3.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 282 TLDFATGFVVLL-------LAPEFYLPLRQLGSHYHARLQGISAAADMVTILNAPLPEQSqqhetkfeehiSSININNLN 354
Cdd:PRK10789 252 TLGQLTSFVMYLglmiwpmLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGR-----------GELDVNIRQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 355 FTYP-NSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFdCLLGFHPQVIE-QISINNKPLDATSMSTLQNAIAWIPQTPT 432
Cdd:PRK10789 321 FTYPqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRHFDVSEgDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 433 LFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPT 512
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 513 AHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLLNLQ 583
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
42-322 |
1.28e-48 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 170.80 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 42 ILMIAGAYLLAQTIHNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTKLTHLGPSYIE 121
Cdd:cd18781 10 LANIAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRLGPSYQE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 122 QHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRW 201
Cdd:cd18781 90 KVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKIAKKLLSKYW 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 202 QQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVAVIIGFRLFFG 281
Cdd:cd18781 170 GSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVAYGGAALGIILALLQFANG 249
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 658756163 282 TLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADM 322
Cdd:cd18781 250 SISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASDKI 290
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
173-581 |
5.08e-47 |
|
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: 175.70 E-value: 5.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 173 LIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIakisdDFRHATLgvLKIA 252
Cdd:TIGR01193 299 LLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKI-----DSEFGDY--LNKS 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 253 FLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVL-------LLAPEFYLPLRQLgSHYHARLQGISAAADMVT- 324
Cdd:TIGR01193 372 FKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLgqlitfnALLSYFLTPLENI-INLQPKLQAARVANNRLNe 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 325 ILNAPLPEQSQQHETKFEEHISSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQ 404
Cdd:TIGR01193 451 VYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 405 ISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKI-AKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGE 483
Cdd:TIGR01193 531 ILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGS 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 484 GLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYaKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQ 563
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
|
410
....*....|....*...
gi 658756163 564 GTYSQLEQQQGAFKSLLN 581
Cdd:TIGR01193 690 GSHDELLDRNGFYASLIH 707
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
347-565 |
2.11e-44 |
|
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: 166.08 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTYPNSNEGI-KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIA 425
Cdd:COG4618 330 RLSVENLTVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLFYQSISDNIkiAK-PAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAP 504
Cdd:COG4618 410 YLPQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 505 ILVLDEPTAHLDSQTEQLIQQAInKYAKNH--LVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAI-RALKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
348-560 |
1.61e-39 |
|
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: 142.36 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI-KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAW 426
Cdd:cd03246 1 LEVENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFYQSISDNIkiakpaatqleleqaahqagaldfintlengfdtligeqgegLSGGQKQRIALARAFLKQAPIL 506
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAI-NKYAKNHLVLVIAHRLNTVKNASNILVMQNGEI 560
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 ... |
348-565 |
8.14e-39 |
|
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: 149.81 E-value: 8.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI-KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAW 426
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPTlRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPIL 506
Cdd:TIGR01842 397 LPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAINKY-AKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGE 536
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
347-565 |
3.26e-38 |
|
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: 139.85 E-value: 3.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTY-PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIA 425
Cdd:cd03369 6 EIEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLFYQSISDNikiakpaatqleleqaahqagaLDFIN--TLENGFDTL-IGEQGEGLSGGQKQRIALARAFLKQ 502
Cdd:cd03369 86 IIPQDPTLFSGTIRSN----------------------LDPFDeySDEEIYGALrVSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 503 APILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
348-559 |
9.52e-38 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 138.37 E-value: 9.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNE----GIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqviEqisinnkpLDATS-MSTLQN 422
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG------E--------LEKLSgSVSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 423 AIAWIPQTPTLFYQSISDNIKIAKP----------AATQLELEqaahqagaldfINTLENGFDTLIGEQGEGLSGGQKQR 492
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPfdeeryekviKACALEPD-----------LEILPDGDLTEIGEKGINLSGGQKQR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 493 IALARAFLKQAPILVLDEPTAHLDSQTEQ-LIQQAINKYAKNH-LVLVIAHRLNTVKNASNILVMQNGE 559
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
348-564 |
1.65e-36 |
|
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: 134.36 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI-KNINLTLPAKGLVAVVGASGSGKSTLFDCLLG-FHPQVIEqISINNKPLdATSMSTLQNAIA 425
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGE-ITLDGVPV-SDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLFYQSISDNIkiakpaatqleleqaahqagaldfintlengfdtligeqGEGLSGGQKQRIALARAFLKQAPI 505
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 506 LVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQG 564
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
348-565 |
2.12e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSmstlqNAIAWI 427
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTL---------------FYQSISdNIKIAKPAATQLeLEQAAHQAGALDFIntlengfDTLIGEqgegLSGGQKQR 492
Cdd:COG1121 81 PQRAEVdwdfpitvrdvvlmgRYGRRG-LFRRPSRADREA-VDEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 493 IALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAK-NHLVLVIAHRLNTV-KNASNILVMqNGEIAQQGT 565
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGP 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
348-582 |
2.21e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 139.78 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTY---PNSnEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHP------------------------- 399
Cdd:PTZ00265 1166 IEIMDVNFRYisrPNV-PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 400 --------QVIEQISINNKPLDATS---------------------MSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAAT 450
Cdd:PTZ00265 1245 deeqnvgmKNVNEFSLTKEGGSGEDstvfknsgkilldgvdicdynLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 451 QLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAIN-- 528
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdi 1404
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 529 KYAKNHLVLVIAHRLNTVKNASNILVMQN----GEIAQ-QGTYSQ-LEQQQGAFKSLLNL 582
Cdd:PTZ00265 1405 KDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEElLSVQDGVYKKYVKL 1464
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
364-513 |
3.38e-34 |
|
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: 126.99 E-value: 3.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQ-SISDNI 442
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 443 KIA------KPAATQLELEQAAHQAGALDFIntlengfDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTA 513
Cdd:pfam00005 81 RLGlllkglSKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
350-560 |
3.98e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.78 E-value: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQ 429
Cdd:COG4619 3 LEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 430 TPTLFYQSISDNIkiakPAATQLElEQAAHQAGALDFINTLenGFDTLIGEQG-EGLSGGQKQRIALARAFLKQAPILVL 508
Cdd:COG4619 82 EPALWGGTVRDNL----PFPFQLR-ERKFDRERALELLERL--GLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 509 DEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAH------RLntvknASNILVMQNGEI 560
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
350-559 |
1.30e-33 |
|
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: 125.43 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPNsNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQ 429
Cdd:cd00267 2 IENLSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 430 tptlfyqsisdnikiakpaatqleleqaahqagaldfintlengfdtligeqgegLSGGQKQRIALARAFLKQAPILVLD 509
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658756163 510 EPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHRLNTVKNASN-ILVMQNGE 559
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRtVIIVTHDPELAELAADrVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
350-564 |
2.17e-33 |
|
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: 125.63 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPNsNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQ 429
Cdd:cd03214 2 VENLSVGYGG-RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 430 tptlfyqsisdnikiakpaatqleleqAAHQAGALDFintLENGFDTLigeqgeglSGGQKQRIALARAFLKQAPILVLD 509
Cdd:cd03214 81 ---------------------------ALELLGLAHL---ADRPFNEL--------SGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 510 EPTAHLDSQTEQLIQQAINKYAK--NHLVLVIAHRLN-TVKNASNILVMQNGEIAQQG 564
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
348-574 |
9.03e-33 |
|
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: 126.13 E-value: 9.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGF-HPQViEQISINNKPLDATSmSTLQNAIAW 426
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlKPDS-GSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFY-QSISDNIKIAKPAAtQLELEQAAHQAGALDFINTLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPI 505
Cdd:COG4555 79 LPDERGLYDrLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 506 LVLDEPTAHLDSQTEQLIQQAINKYAK-NHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQLEQQQG 574
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
364-579 |
1.49e-32 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 133.92 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIK 443
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 444 IAKPAATQlELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLI 523
Cdd:TIGR00957 1382 PFSQYSDE-EVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 524 QQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSL 579
Cdd:TIGR00957 1461 QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
350-564 |
1.80e-32 |
|
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: 124.18 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATsmstlQNAIAWIPQ 429
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 430 TPTL---------------------FYQSISdniKIAKPAATQLeLEQAahqaGALDFIntlengfDTLIGEqgegLSGG 488
Cdd:cd03235 76 RRSIdrdfpisvrdvvlmglyghkgLFRRLS---KADKAKVDEA-LERV----GLSELA-------DRQIGE----LSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 489 QKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKY-AKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQG 564
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
348-560 |
2.13e-32 |
|
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: 122.51 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNsNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNaIAWI 427
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLFYQ-SISDNIKiakpaatqleleqaahqagaldfintlengfdtligeqgegLSGGQKQRIALARAFLKQAPIL 506
Cdd:cd03230 79 PEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAINKYAK-NHLVLVIAHRLNTVKN-ASNILVMQNGEI 560
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
348-565 |
7.91e-32 |
|
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: 123.62 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNsNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdaTSMSTLQNA--IA 425
Cdd:COG1120 2 LEAENLSVGYGG-RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL--ASLSRRELArrIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTL-F--------------YQSIsdnikIAKPAATQLEL-EQAAHQAGALDFINTLengFDTLigeqgeglSGGQ 489
Cdd:COG1120 79 YVPQEPPApFgltvrelvalgrypHLGL-----FGRPSAEDREAvEEALERTGLEHLADRP---VDEL--------SGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 490 KQRIALARAFLKQAPILVLDEPTAHLD--SQTE--QLIQQaINKyAKNHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQG 564
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDlaHQLEvlELLRR-LAR-ERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQG 220
|
.
gi 658756163 565 T 565
Cdd:COG1120 221 P 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
348-565 |
6.50e-31 |
|
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: 120.52 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWI 427
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPT--LFYQSISDNI---------------KIAKPAATQLELEQAAHQagaldfiNTLEngfdtligeqgegLSGGQK 490
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVafgpenlglpreeirERVEEALELVGLEHLADR-------PPHE-------------LSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 491 QRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHRLNTV-KNASNILVMQNGEIAQQGT 565
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVaELADRVIVLDDGRIVADGT 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
348-572 |
1.42e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.40 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNaIAWI 427
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLF-YQSISDNIKIAKPA--ATQLELEQAAHQAgaLDFINtLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAP 504
Cdd:COG1131 79 PQEPALYpDLTVRENLRFFARLygLPRKEARERIDEL--LELFG-LTDAADRKVGT----LSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 505 ILVLDEPTAHLDSQTEQLIQQAINKYAK-NHLVLVIAHRLNTV-KNASNILVMQNGEIAQQGTYSQLEQQ 572
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
348-587 |
1.00e-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: 123.09 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPN-SNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQ---VIEQISINNKPLDATSMSTLQNA 423
Cdd:COG1123 5 LEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 IAWIPQTPT--LFYQSISDNIKIAkpaatqLELEQAAHQAGALDFINTLEN-GFDTLIGEQGEGLSGGQKQRIALARAFL 500
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEA------LENLGLSRAEARARVLELLEAvGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 501 KQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQLEQQQGAFK 577
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQALA 238
|
250
....*....|
gi 658756163 578 SLLNLQAQGA 587
Cdd:COG1123 239 AVPRLGAARG 248
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
313-559 |
2.22e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 124.37 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 313 LQGISAAADMVTILN-APLPEQSQQHETKfeEHISSININNLNFTYPNSN--EGIKNINLTLPAKGLVAVVGASGSGKST 389
Cdd:PTZ00265 349 MKSLEATNSLYEIINrKPLVENNDDGKKL--KDIKKIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKST 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 390 LFDCLLGFHPQVIEQISINNK-PLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQLE-LEQ----------- 456
Cdd:PTZ00265 427 ILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEaLSNyynedgndsqe 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 457 --------AAHQAGAL-------------------------------------DFINTLENGFDTLIGEQGEGLSGGQKQ 491
Cdd:PTZ00265 507 nknkrnscRAKCAGDLndmsnttdsneliemrknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQ 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 492 RIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAIN--KYAKNHLVLVIAHRLNTVKNASNILVMQNGE 559
Cdd:PTZ00265 587 RISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
348-564 |
4.65e-29 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 114.91 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPN---SNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNK---PLDATSMSTLQ 421
Cdd:cd03257 2 LEVKNLSVSFPTgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 422 NAIAWIPQ------TPTL-FYQSISDNIKIAKPAATQLELEQAAHQAgaLDFINTLENGFDTLIGEqgegLSGGQKQRIA 494
Cdd:cd03257 82 KEIQMVFQdpmsslNPRMtIGEQIAEPLRIHGKLSKKEARKEAVLLL--LVGVGLPEEVLNRYPHE----LSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 495 LARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKN-ASNILVMQNGEIAQQG 564
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
350-559 |
1.39e-28 |
|
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: 113.33 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPNSNE-GIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIP 428
Cdd:cd03225 2 LKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 429 QTPT--LFYQSISDNIKIAkPAATQL---ELEQAAHQAGALDFINTLEngfDTLIGEqgegLSGGQKQRIALARAFLKQA 503
Cdd:cd03225 82 QNPDdqFFGPTVEEEVAFG-LENLGLpeeEIEERVEEALELVGLEGLR---DRSPFT----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 504 PILVLDEPTAHLDSQTEQLIQQAINKY-AKNHLVLVIAHRLNTVKN-ASNILVMQNGE 559
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
348-560 |
2.33e-28 |
|
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: 112.58 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI---KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTL---- 420
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 421 QNAIAWIPQTPTLF-YQSISDNIKIAKPAATQL--ELEQAAHQAgaLDFINtLENGFDTLIGEqgegLSGGQKQRIALAR 497
Cdd:cd03255 81 RRHIGFVFQSFNLLpDLTALENVELPLLLAGVPkkERRERAEEL--LERVG-LGDRLNHYPSE----LSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 498 AFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAK--NHLVLVIAHRLNTVKNASNILVMQNGEI 560
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
377-589 |
3.48e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 120.47 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLFDCLLgfhpQVIE----QISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKiakPAA--T 450
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALF----RIVElekgRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID---PFSehN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 451 QLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKY 530
Cdd:PLN03232 1338 DADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREE 1417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 531 AKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQG-AFKSLlnLQAQGANN 589
Cdd:PLN03232 1418 FKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRM--VHSTGPAN 1475
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
348-569 |
3.74e-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: 112.66 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFtYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIE-----QISINNKPLDATSMS--TL 420
Cdd:cd03260 1 IELRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 421 QNAIAWIPQTPTLFYQSISDNIKIA------KPAATQLELEQAAHQAGALDfintlENGFDTLigeQGEGLSGGQKQRIA 494
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALRKAALW-----DEVKDRL---HALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 495 LARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNAS-NILVMQNGEIAQQGTYSQL 569
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVAdRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
348-527 |
4.64e-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: 111.79 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIK---NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSmstlqNAI 424
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 425 AWIPQTPTLF-YQSISDNIKI---AKPAATQLELEQAAHqagALDFINtLENGFDTLIGEqgegLSGGQKQRIALARAFL 500
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALgleLQGVPKAEARERAEE---LLELVG-LSGFENAYPHQ----LSGGMRQRVALARALA 147
|
170 180
....*....|....*....|....*..
gi 658756163 501 KQAPILVLDEPTAHLDSQTEQLIQQAI 527
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEEL 174
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
215-580 |
2.32e-27 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 118.12 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 215 VQGLTQLKLFNATQQELKQIAKIsddfRHATLGVLKI-AFLSSFAL------EFLATISVALVAVIIGFRlffGTLDFAT 287
Cdd:TIGR00957 503 LNGIKVLKLYAWELAFLDKVEGI----RQEELKVLKKsAYLHAVGTftwvctPFLVALITFAVYVTVDEN---NILDAEK 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 288 GFVVLLLAPEFYLPLRQLGSHYHARLQG-ISAAADMVTILNAPLPEQSQQHETKFEEHISSININNLNFTYPNSNEGIKN 366
Cdd:TIGR00957 576 AFVSLALFNILRFPLNILPMVISSIVQAsVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITVHNATFTWARDLPPTLN 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 367 -INLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQIsinnkpldatsmsTLQNAIAWIPQTPTLFYQSISDNIKIA 445
Cdd:TIGR00957 656 gITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFG 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 446 KPaaTQLELEQAAHQAGAL--DfINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLI 523
Cdd:TIGR00957 723 KA--LNEKYYQQVLEACALlpD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 524 QQAI---NKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLL 580
Cdd:TIGR00957 800 FEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
32-302 |
3.08e-27 |
|
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: 111.20 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 32 LSIALGTFNAILMIAGAYLLAQTI-HNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLT 110
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVLGRILdVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 111 KLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVG 190
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 191 SKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALV 270
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 658756163 271 AVIIGFRLFFGTLDFATGFVVLLLAPEFYLPL 302
Cdd:pfam00664 243 LWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
350-564 |
3.10e-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: 109.53 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIAWIPQ 429
Cdd:cd03259 3 LKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR--DVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 430 TPTLF-YQSISDNI----KIAKPAATqlELEQAAHQAGALdfintleNGFDTLIGEQGEGLSGGQKQRIALARAFLKQAP 504
Cdd:cd03259 80 DYALFpHLTVAENIafglKLRGVPKA--EIRARVRELLEL-------VGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 505 ILVLDEPTAHLDSQTEQLIQQAINKYAKNH---LVLVIAHRLNTVKNASNILVMQNGEIAQQG 564
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELgitTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
348-580 |
3.17e-27 |
|
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: 110.77 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI-KNINLTLPAKGLVAVVGASGSGKSTL----FDCLLGFHPQ-VIEQISINNKPLdatsmSTLQ 421
Cdd:cd03288 20 IKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFDGKiVIDGIDISKLPL-----HTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 422 NAIAWIPQTPTLFYQSISDNIKIAKpAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLK 501
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 502 QAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQL-EQQQGAFKSLL 580
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLlAQEDGVFASLV 253
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
348-563 |
3.86e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 109.75 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI---KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvIE-----QISINNKPLDATSMST 419
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-----LDrptsgEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 420 L----QNAIAWIPQTPTLF-YQSISDNIKIA-----KPAAtqlELEQAAHQAgaLDFINtLENGFDTLIGEqgegLSGGQ 489
Cdd:COG1136 80 LarlrRRHIGFVFQFFNLLpELTALENVALPlllagVSRK---ERRERAREL--LERVG-LGDRLDHRPSQ----LSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 490 KQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAK--NHLVLVIAHRLNTVKNASNILVMQNGEIAQQ 563
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
76-580 |
6.64e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 116.61 E-value: 6.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 76 AGIILLRALFLAISERLSAYAALKIKSAMRQTLLT-------KLTHLGPsyiEQHGQGATLNTVHDGVEALHDYyAKYLP 148
Cdd:PLN03232 344 AFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAaifhkslRLTHEAR---KNFASGKVTNMITTDANALQQI-AEQLH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 149 GVaYSALIPLAILVVIFPTDYKAGLIF--LLTAPLIPFFMILVgSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNA 226
Cdd:PLN03232 420 GL-WSAPFRIIVSMVLLYQQLGVASLFgsLILFLLIPLQTLIV-RKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAW 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 227 TQQELKQIAKISDD----FRHATLgvlkiafLSSFALEFLATISVALVAVIIG-FRLFFGTLDFATGFVVLLLAPEFYLP 301
Cdd:PLN03232 498 EKSFESRIQGIRNEelswFRKAQL-------LSAFNSFILNSIPVVVTLVSFGvFVLLGGDLTPARAFTSLSLFAVLRSP 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 302 LRQLGSHYHA---------RLQGISAAADMVTILNAPLpeqsqqhetkfEEHISSININNLNFTYPN--SNEGIKNINLT 370
Cdd:PLN03232 571 LNMLPNLLSQvvnanvslqRIEELLLSEERILAQNPPL-----------QPGAPAISIKNGYFSWDSktSKPTLSDINLE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 371 LPAKGLVAVVGASGSGKSTLFDCLLGFHPqvieqisinnkPLDATSMsTLQNAIAWIPQTPTLFYQSISDNIKIAkpaaT 450
Cdd:PLN03232 640 IPVGSLVAIVGGTGEGKTSLISAMLGELS-----------HAETSSV-VIRGSVAYVPQVSWIFNATVRENILFG----S 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 451 QLELEQ--AAHQAGALDFINTLENGFD-TLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQ-TEQLIQQA 526
Cdd:PLN03232 704 DFESERywRAIDVTALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSC 783
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 658756163 527 INKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLL 580
Cdd:PLN03232 784 MKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
377-589 |
6.77e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 116.76 E-value: 6.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLFDCLLgfhpQVIE----QISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKiakP--AAT 450
Cdd:PLN03130 1268 VGIVGRTGAGKSSMLNALF----RIVElergRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD---PfnEHN 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 451 QLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKY 530
Cdd:PLN03130 1341 DADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREE 1420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 531 AKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQG-AFKSLlnLQAQGANN 589
Cdd:PLN03130 1421 FKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGsAFSKM--VQSTGAAN 1478
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
32-319 |
1.42e-26 |
|
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: 109.95 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 32 LSIALGTFNAILMIAGAYLLAQTIHNVmFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTK 111
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLIDDV-IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 112 LTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGS 191
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 192 KAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVA 271
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 658756163 272 VIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAA 319
Cdd:cd07346 242 LYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
233-580 |
1.50e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 115.61 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 233 QIAKISDD----FRHATLgvlkiafLSSFALEFLATISVALVAVIIG-FRLFFGTLDFATGFVVLLLAPEFYLPLRQLGS 307
Cdd:PLN03130 504 KVQTVRDDelswFRKAQL-------LSAFNSFILNSIPVLVTVVSFGvFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPN 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 308 HYHA---------RLQGISAAADMVTILNAPLpeqsqqhetkfEEHISSININNLNFTYPNSNE--GIKNINLTLPAKGL 376
Cdd:PLN03130 577 LITQavnanvslkRLEELLLAEERVLLPNPPL-----------EPGLPAISIKNGYFSWDSKAErpTLSNINLDVPVGSL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLFDCLLGFHPqvieqisinnkPLDATSMsTLQNAIAWIPQTPTLFYQSISDNIKIAKPAaTQLELEQ 456
Cdd:PLN03130 646 VAIVGSTGEGKTSLISAMLGELP-----------PRSDASV-VIRGTVAYVPQVSWIFNATVRDNILFGSPF-DPERYER 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 457 AAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEqliQQAINKYAKNHL- 535
Cdd:PLN03130 713 AIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG---RQVFDKCIKDELr 789
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 658756163 536 ----VLViAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLL 580
Cdd:PLN03130 790 gktrVLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLM 837
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
348-525 |
1.52e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.64 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEG---IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSmstlqNAI 424
Cdd:COG1116 8 LELRGVSKRFPTGGGGvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 425 AWIPQTPTLF-YQSISDNIKIAkPAATQLELEQAAHQAGALdfintLE----NGF-DTLIGEqgegLSGGQKQRIALARA 498
Cdd:COG1116 83 GVVFQEPALLpWLTVLDNVALG-LELRGVPKAERRERAREL-----LElvglAGFeDAYPHQ----LSGGMRQRVAIARA 152
|
170 180
....*....|....*....|....*..
gi 658756163 499 FLKQAPILVLDEPTAHLDSQTEQLIQQ 525
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQD 179
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
348-581 |
4.17e-26 |
|
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: 107.20 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI---KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAI 424
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpvlKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 425 AWIPQTP--------TLfYQSISDNIKIAKPAATQLELEQAAHQAGaldfintLENGFDTLIGEQgegLSGGQKQRIALA 496
Cdd:COG1124 82 QMVFQDPyaslhprhTV-DRILAEPLRIHGLPDREERIAELLEQVG-------LPPSFLDRYPHQ---LSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 497 RAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQLEQ-- 571
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAgp 230
|
250
....*....|
gi 658756163 572 QQGAFKSLLN 581
Cdd:COG1124 231 KHPYTRELLA 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
348-559 |
8.27e-26 |
|
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: 104.19 E-value: 8.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMST--LQNAIA 425
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLF-YQSISDNIkiakpaatqleleqaahqagaldfintlengfdtligeqGEGLSGGQKQRIALARAFLKQAP 504
Cdd:cd03229 80 MVFQDFALFpHLTVLENI---------------------------------------ALGLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 505 ILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKN-ASNILVMQNGE 559
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
348-569 |
2.74e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.45 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSnegIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMStlQNAIAWI 427
Cdd:COG3840 2 LRLDDLTYRYGDF---PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLFYQ-SISDNIKIA-----KPAATQLE-LEQAAHQAGaldfintLENGFDTLIGEqgegLSGGQKQRIALARAFL 500
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGlrpglKLTAEQRAqVEQALERVG-------LAGLLDRLPGQ----LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 501 KQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQL 569
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
365-540 |
8.39e-25 |
|
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: 102.17 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 365 KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDAtSMSTLQNAIAWIPQTPTLF-YQSISDNI- 442
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKpELTVRENLr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 443 ---KIAKPAATQLELEQAAHQAGaldfintLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQT 519
Cdd:COG4133 98 fwaALYGLRADREAIDEALEAVG-------LAGLADLPVRQ----LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180
....*....|....*....|.
gi 658756163 520 EQLIQQAINKYAKNHLVLVIA 540
Cdd:COG4133 167 VALLAELIAAHLARGGAVLLT 187
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
350-560 |
1.72e-24 |
|
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: 101.56 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdatSMSTLQNAIAWIPQ 429
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 430 TPT--LFYQSISDNIKIAKPAATqLELEQAAHQAGALDfINTLE--NGFDtligeqgegLSGGQKQRIALARAFLKQAPI 505
Cdd:cd03226 79 DVDyqLFTDSVREELLLGLKELD-AGNEQAETVLKDLD-LYALKerHPLS---------LSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 506 LVLDEPTAHLDSQTEQLIQQAINKYAK-NHLVLVIAHRLNTVKNASNILV-MQNGEI 560
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKVCDRVLlLANGAI 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
348-565 |
6.04e-24 |
|
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: 100.87 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpnSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIAWI 427
Cdd:cd03299 1 LKVENLSKDW--KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK--DITNLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLF-YQSISDNIK--IAKPAATQLELEQAAHQ-AGALdfintlenGFDTLIGEQGEGLSGGQKQRIALARAFLKQA 503
Cdd:cd03299 77 PQNYALFpHMTVYKNIAygLKKRKVDKKEIERKVLEiAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 504 PILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVI--AHRLNTVKNASN-ILVMQNGEIAQQGT 565
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhvTHDFEEAWALADkVAIMLNGKLIQVGK 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
346-569 |
8.10e-24 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 100.52 E-value: 8.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNA-- 423
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 -IAWIPQTPTL-------------------FYQSI-----SDNIKIAKPAATQLELEQAAHQ-AGALdfintlengfdtl 477
Cdd:COG3638 81 rIGMIFQQFNLvprlsvltnvlagrlgrtsTWRSLlglfpPEDRERALEALERVGLADKAYQrADQL------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 478 igeqgeglSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIA--HRLNTVKN-ASNILV 554
Cdd:COG3638 148 --------SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVnlHQVDLARRyADRIIG 219
|
250
....*....|....*
gi 658756163 555 MQNGEIAQQGTYSQL 569
Cdd:COG3638 220 LRDGRVVFDGPPAEL 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
348-569 |
1.19e-23 |
|
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: 99.96 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI---KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNA- 423
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtalKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 --IAWIPQTPTLFYQ-SISDNI----KIAKPAATQLElEQAAHqagALDFINtLENGFDTLIGEqgegLSGGQKQRIALA 496
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENValplEIAGVPKAEIE-ERVLE---LLELVG-LEDKADAYPAQ----LSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 497 RAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAK--NHLVLVIAHRLNTVKNASN-ILVMQNGEIAQQGTYSQL 569
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDrVAVMEKGEVVEEGTVEEV 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
348-558 |
1.54e-23 |
|
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: 98.94 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNK----PLDATSMSTLQNA 423
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesePSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 IAWIPQTPTLFYQSISDNIKIAKPAATQLEleQAAHQAGALD-FINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQ 502
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRY--KAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 503 APILVLDEPTAHLDSQ-TEQLIQQAINKYAKN--HLVLVIAHRLNTVKNASNILVMQNG 558
Cdd:cd03290 159 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
369-564 |
2.60e-23 |
|
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: 98.33 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 369 LTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNkpLDATSMSTLQNAIAWIPQTPTLF-YQSISDNIKIAKP 447
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRPVSMLFQENNLFaHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 448 AATQLELEQAAHQAGALDfintlENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAI 527
Cdd:cd03298 97 PGLKLTAEDRQAIEVALA-----RVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658756163 528 NKY---AKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQG 564
Cdd:cd03298 172 LDLhaeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
366-564 |
2.64e-23 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 98.14 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 366 NINLTLPAkGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS----MSTLQNAIAWIPQTPTLF-YQSISD 440
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 441 NIKIAKPAATQLELEQAAHQAGALdfintleNGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTE 520
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDL-------LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658756163 521 QLIQQAINKYAK--NHLVLVIAHRLNTV-KNASNILVMQNGEIAQQG 564
Cdd:cd03297 168 LQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
32-319 |
2.80e-23 |
|
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: 100.15 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 32 LSIALGTFNAILMIAGAYLLAQTI-HNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLT 110
Cdd:cd18544 3 LALLLLLLATALELLGPLLIKRAIdDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 111 KLTHLGPSYIEQHGQGATL-NTVHDgVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILV 189
Cdd:cd18544 83 HIQRLPLSFFDRTPVGRLVtRVTND-TEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 190 GSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVAL 269
Cdd:cd18544 162 RKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALAL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 658756163 270 VAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAA 319
Cdd:cd18544 242 VLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASA 291
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
377-581 |
3.32e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 104.86 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLfdcLLGFHpQVIE----QISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKiakP--AAT 450
Cdd:PTZ00243 1339 VGIVGRTGSGKSTL---LLTFM-RMVEvcggEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD---PflEAS 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 451 QLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVL-DEPTAHLDSQTEQLIQQAINK 529
Cdd:PTZ00243 1412 SAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMS 1491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658756163 530 YAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQL-EQQQGAFKSLLN 581
Cdd:PTZ00243 1492 AFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVE 1544
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
348-565 |
4.65e-23 |
|
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: 103.06 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEG----IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS---MSTL 420
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 421 QNAIAWIPQTPT--LF-----YQSISDNIKIAKPAATQlELEQAAHQAgaLDFINTLENGFDTLIGEqgegLSGGQKQRI 493
Cdd:COG1123 341 RRRVQMVFQDPYssLNprmtvGDIIAEPLRLHGLLSRA-ERRERVAEL--LERVGLPPDLADRYPHE----LSGGQRQRV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 494 ALARAFLKQAPILVLDEPTAHLD-SQTEQLIQQaINKYAKNH--LVLVIAHRLNTVKN-ASNILVMQNGEIAQQGT 565
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDvSVQAQILNL-LRDLQRELglTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
348-565 |
7.19e-23 |
|
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: 98.68 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTY----PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTL---FDCLLgfHPQ----VIEQISINNKplDATS 416
Cdd:TIGR04521 1 IKLKNVSYIYqpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLiqhLNGLL--KPTsgtvTIDGRDITAK--KKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 417 MSTLQNAIAWIPQTP--TLFYQSISDNIkiakpA-------ATQLELEQAAHQAgaLDFIntlenGFDTLIGEQGE-GLS 486
Cdd:TIGR04521 77 LKDLRKKVGLVFQFPehQLFEETVYKDI-----AfgpknlgLSEEEAEERVKEA--LELV-----GLDEEYLERSPfELS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 487 GGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAK--NHLVLVIAHRLNTV-KNASNILVMQNGEIAQQ 563
Cdd:TIGR04521 145 GGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKekGLTVILVTHSMEDVaEYADRVIVMHKGKIVLD 224
|
..
gi 658756163 564 GT 565
Cdd:TIGR04521 225 GT 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
347-565 |
1.67e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.07 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTYPNSNeGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvIE-----QISINNKPLDaTSMSTLQ 421
Cdd:COG1118 2 SIEVRNISKRFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-----LEtpdsgRIVLNGRDLF-TNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 422 NAIAWIPQTPTLF-YQSISDNI------------KIAKPAATQLELEQAAHqagaldfintLENGFDTligeQgegLSGG 488
Cdd:COG1118 75 RRVGFVFQHYALFpHMTVAENIafglrvrppskaEIRARVEELLELVQLEG----------LADRYPS----Q---LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 489 QKQRIALARAFLKQAPILVLDEPTAHLDSQT----EQLIQQAINKYaknHLVLVI-------AHRLntvknASNILVMQN 557
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVrkelRRWLRRLHDEL---GGTTVFvthdqeeALEL-----ADRVVVMNQ 209
|
....*...
gi 658756163 558 GEIAQQGT 565
Cdd:COG1118 210 GRIEQVGT 217
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
32-323 |
2.01e-22 |
|
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: 97.88 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 32 LSIALGTFNAILMIAGAYLLAQTIhNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTK 111
Cdd:cd18552 3 LAILGMILVAATTAALAWLLKPLL-DDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 112 LTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGS 191
Cdd:cd18552 82 LLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 192 KAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVA 271
Cdd:cd18552 162 RLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 658756163 272 VIIGFRLFFGTLDFAT--GFVVLLLApeFYLPLRQLGShYHARLQGISAAADMV 323
Cdd:cd18552 242 WYGGYQVISGELTPGEfiSFITALLL--LYQPIKRLSN-VNANLQRGLAAAERI 292
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
368-564 |
3.58e-22 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 94.93 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 368 NLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIAWIPQTPTLF-YQSISDNIKIA- 445
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFaHLTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 446 KP-----AATQLELEQAAHQAGALDFINTLENGfdtligeqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTE 520
Cdd:TIGR01277 96 HPglklnAEQQEKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658756163 521 QLIQQAINKYA---KNHLVLVIAHRLNTVKNASNILVMQNGEIAQQG 564
Cdd:TIGR01277 165 EEMLALVKQLCserQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
348-573 |
4.40e-22 |
|
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: 95.44 E-value: 4.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS----------- 416
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrklrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 417 ------------MSTLQN----AIAWIPQTPTLFYQSISDNIKIAKPAATQLELEQAAHQagaldfintlengfdtlige 480
Cdd:TIGR02315 82 gmifqhynlierLTVLENvlhgRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQ-------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 481 QGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIA--HRLNTVKN-ASNILVMQN 557
Cdd:TIGR02315 142 RADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIInlHQVDLAKKyADRIVGLKA 221
|
250
....*....|....*.
gi 658756163 558 GEIAQQGTYSQLEQQQ 573
Cdd:TIGR02315 222 GEIVFDGAPSELDDEV 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
348-565 |
4.56e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 96.21 E-value: 4.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNS-NEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLG-FHPQVIEqISINNKPLDATSMSTLQNAIA 425
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQSGE-IKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTP--TLFYQSISDNI------KIAKPAATQLELEQAAHQAGALDFINtlengfdtligEQGEGLSGGQKQRIALAR 497
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIafglenKKVPPKKMKDIIDDLAKKVGMEDYLD-----------KEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 498 AFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAK--NHLVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
346-565 |
5.95e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 97.48 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIA 425
Cdd:COG3842 4 PALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR--DVTGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLF-YQSISDNI----KIAKPAATQLElEQAAHqagALDFINtLEnGF-DTLIGEqgegLSGGQKQRIALARAF 499
Cdd:COG3842 81 MVFQDYALFpHLTVAENVafglRMRGVPKAEIR-ARVAE---LLELVG-LE-GLaDRYPHQ----LSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 500 LKQAPILVLDEPTAHLDSQT-EQL------IQQAINKYAknhlVLV---------IAHRlntvknasnILVMQNGEIAQQ 563
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLrEEMreelrrLQRELGITF----IYVthdqeealaLADR---------IAVMNDGRIEQV 217
|
..
gi 658756163 564 GT 565
Cdd:COG3842 218 GT 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
348-572 |
8.34e-22 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 94.56 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNA---I 424
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 425 AWIPQTPTLF-YQSISDNIKIAKPAATQ-----LELEQAAHQAGALDFINTLenGFDTLIGEQGEGLSGGQKQRIALARA 498
Cdd:cd03256 81 GMIFQQFNLIeRLSVLENVLSGRLGRRStwrslFGLFPKEEKQRALAALERV--GLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 499 FLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIA--HRLNTVK-NASNILVMQNGEIAQQGTYSQLEQQ 572
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVslHQVDLAReYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-569 |
2.02e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.31 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNE-GIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAW 426
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPtlfyqsisDN----IKIAKPAATQLE------------LEQAAHQAGALDFINtlengfdtligEQGEGLSGGQK 490
Cdd:PRK13635 86 VFQNP--------DNqfvgATVQDDVAFGLEnigvpreemverVDQALRQVGMEDFLN-----------REPHRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 491 QRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAIN--KYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQ 568
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
.
gi 658756163 569 L 569
Cdd:PRK13635 227 I 227
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
35-319 |
2.58e-21 |
|
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: 94.53 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 35 ALGTFNAILMIAGAYLLAQT-----IHNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLL 109
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWlirelVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 110 TKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILV 189
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 190 GSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVAL 269
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 658756163 270 VAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAA 319
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGA 290
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
348-565 |
3.96e-21 |
|
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: 93.26 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNE-GIKNINLTLPAKGLVAVVGASGSGKSTL---FDCLL----GfhpqvieQISINN-KPLDATSMS 418
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLlptsG-------KVTVDGlDTLDEENLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 419 TLQNAIAWIPQTPtlfyqsisDN-------------------------IKIAKPAATQLELEQAAHQAGALdfintleng 473
Cdd:TIGR04520 74 EIRKKVGMVFQNP--------DNqfvgatveddvafglenlgvpreemRKRVDEALKLVGMEDFRDREPHL--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 474 fdtligeqgegLSGGQKQRIALARAfLKQAP-ILVLDEPTAHLDSQTEQLIQQAINK-YAKNHL-VLVIAHRLNTVKNAS 550
Cdd:TIGR04520 137 -----------LSGGQKQRVAIAGV-LAMRPdIIILDEATSMLDPKGRKEVLETIRKlNKEEGItVISITHDMEEAVLAD 204
|
250
....*....|....*
gi 658756163 551 NILVMQNGEIAQQGT 565
Cdd:TIGR04520 205 RVIVMNKGKIVAEGT 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
350-569 |
4.26e-21 |
|
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: 92.18 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPN-SNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdATSMSTLQNAIAWIP 428
Cdd:cd03263 3 IRNLTKTYKKgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 429 QTPTLF-YQSISDNIKI-----AKPAAT-QLELEQAAHQAGALDFINtlengfdTLIGEqgegLSGGQKQRIALARAFLK 501
Cdd:cd03263 82 QFDALFdELTVREHLRFyarlkGLPKSEiKEEVELLLRVLGLTDKAN-------KRART----LSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 502 QAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQL 569
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
346-580 |
5.58e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 93.02 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPldaTSMSTLQNAIA 425
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP---TRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTL---FYQSISDNI-----------KIAKPAATQLeLEQAAHQAGALDFINtlengfdTLIGEqgegLSGGQKQ 491
Cdd:PRK15056 82 YVPQSEEVdwsFPVLVEDVVmmgryghmgwlRRAKKRDRQI-VTAALARVDMVEFRH-------RQIGE----LSGGQKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 492 RIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKY-AKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQG------ 564
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGptettf 229
|
250
....*....|....*.
gi 658756163 565 TYSQLEQqqgAFKSLL 580
Cdd:PRK15056 230 TAENLEL---AFSGVL 242
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
346-565 |
7.53e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 94.37 E-value: 7.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIA 425
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR--DVTDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLF-YQSISDNI----KIAK-PAAtqlELEQAAHQAGALdfintLEngfdtlIGEQGE----GLSGGQKQRIAL 495
Cdd:COG3839 79 MVFQSYALYpHMTVYENIafplKLRKvPKA---EIDRRVREAAEL-----LG------LEDLLDrkpkQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 496 ARAFLKQAPILVLDEPTAHLDSQT-EQL------IQQAInkyaKNHLVLV---------IAHRlntvknasnILVMQNGE 559
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKLrVEMraeikrLHRRL----GTTTIYVthdqveamtLADR---------IAVMNDGR 211
|
....*.
gi 658756163 560 IAQQGT 565
Cdd:COG3839 212 IQQVGT 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
348-569 |
8.18e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.99 E-value: 8.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLD--ATSMSTLQNAIA 425
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTP--TLFYQSISDNIKIAkPAATQL---ELEQAAHQAGALDFINTLENgfdtligEQGEGLSGGQKQRIALARAFL 500
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDVSFG-AVNLKLpedEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 501 KQAPILVLDEPTAHLDSQTEQLIQQAINKYAKN-HLVLVIA-HRLNTVK-NASNILVMQNGEIAQQGTYSQL 569
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
348-565 |
1.09e-20 |
|
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: 91.59 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLlgfhPQVIE----QISINNKPLDATSMSTLQNA 423
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI----NRLIEptsgEIFIDGEDIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 IAWIPQTPTLF-YQSISDNIKIAkpaATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQ 502
Cdd:cd03295 77 IGYVIQQIGLFpHMTVEENIALV---PKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 503 APILVLDEPTAHLDSQT-EQL------IQQAINKyaknhLVLVIAHRLN-TVKNASNILVMQNGEIAQQGT 565
Cdd:cd03295 154 PPLLLMDEPFGALDPITrDQLqeefkrLQQELGK-----TIVFVTHDIDeAFRLADRIAIMKNGEIVQVGT 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
253-580 |
1.10e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 96.90 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 253 FLSSFALEFLATISVALVAVIIgFRLFFGTLDFAtgfVVLLLAPEfylplRQLGSH---YHARLQGISAAADMV------ 323
Cdd:TIGR01271 312 FFSGFFVVFLSVVPYALIKGII-LRRIFTTISYC---IVLRMTVT-----RQFPGAiqtWYDSLGAITKIQDFLckeeyk 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 324 ------TILNAPLPEQSQQHETKFEEHISSININNLNFTYPNSNEGI-------------KNINLTLPAKGLVAVVGASG 384
Cdd:TIGR01271 383 tleynlTTTEVEMVNVTASWDEGIGELFEKIKQNNKARKQPNGDDGLffsnfslyvtpvlKNISFKLEKGQLLAVAGSTG 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 385 SGKSTLFDCLLGfhpqvieqisiNNKPLDATSMSTlqNAIAWIPQTPTLFYQSISDNIKIAKP----------AATQLEL 454
Cdd:TIGR01271 463 SGKSSLLMMIMG-----------ELEPSEGKIKHS--GRISFSPQTSWIMPGTIKDNIIFGLSydeyrytsviKACQLEE 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 455 EqaahqagaldfINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLI-QQAINKYAKN 533
Cdd:TIGR01271 530 D-----------IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSN 598
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 658756163 534 HLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLL 580
Cdd:TIGR01271 599 KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
364-580 |
1.45e-20 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 92.23 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvieqisinnkPLDATSMSTLQNA-IAWIPQTPTLFYQSISDNI 442
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILG--------------ELEPSEGKIKHSGrISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 443 kIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTE-Q 521
Cdd:cd03291 119 -IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEkE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 522 LIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLL 580
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
348-573 |
1.67e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 90.64 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNA---I 424
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 425 AWIPQTPTLFYQ-SISDNIkiAKPAATQLELEQAAHQAGALDFINT--LENGFDTLIGEqgegLSGGQKQRIALARAFLK 501
Cdd:cd03261 80 GMLFQSGALFDSlTVFENV--AFPLREHTRLSEEEIREIVLEKLEAvgLRGAEDLYPAE----LSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 502 QAPILVLDEPTAHLDSQTEQLIQQAINKY--AKNHLVLVIAHRLNTV-KNASNILVMQNGEIAQQGTYSQLEQQQ 573
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
348-560 |
2.37e-20 |
|
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: 89.51 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS--MSTLQNAIA 425
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKknINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLF-YQSISDNIKIAkPAATQLELEQAAhQAGALDFINT--LENGFDTLIGEqgegLSGGQKQRIALARAFLKQ 502
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLA-PIKVKGMSKAEA-EERALELLEKvgLADKADAYPAQ----LSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 503 APILVLDEPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHRLNTVKNASN-ILVMQNGEI 560
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREVADrVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
352-564 |
2.57e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 89.15 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 352 NLNFTYPNSNEG-----IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFH--PQVIEQISINNKPLDatsMSTLQNAI 424
Cdd:cd03213 8 NLTVTVKSSPSKsgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLD---KRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 425 AWIPQtptlfyqsisDNIKIAkpaatQLELEQAahqagaLDFINTLEngfdtligeqgeGLSGGQKQRIALARAFLKQAP 504
Cdd:cd03213 85 GYVPQ----------DDILHP-----TLTVRET------LMFAAKLR------------GLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 505 ILVLDEPTAHLDSQTEQLIQQAINKYAK-NHLVLVIAHRLNT--VKNASNILVMQNGEIAQQG 564
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
364-557 |
3.01e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.46 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIE---QISINNKPLDAtsMSTLQNAIAWIPQTPTLF-YQSIS 439
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSasgEVLLNGRRLTA--LPAEQRRIGILFQDDLLFpHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 440 DNIKIAKPAATQLELEQAAHQAgALDFINtLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQT 519
Cdd:COG4136 95 ENLAFALPPTIGRAQRRARVEQ-ALEEAG-LAGFADRDPAT----LSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658756163 520 ---------EQLIQQAINkyaknhlVLVIAHRLNTVKNASNILVMQN 557
Cdd:COG4136 169 raqfrefvfEQIRQRGIP-------ALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
348-564 |
3.35e-20 |
|
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: 89.17 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSnEGIKNINLTLPAkGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDAtSMSTLQNAIAWI 427
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTlFYQSIS-----DNIKIAKPAATQLELEQAAHqagALDFINtLENGFDTLIGeqgeGLSGGQKQRIALARAFLKQ 502
Cdd:cd03264 78 PQEFG-VYPNFTvreflDYIAWLKGIPSKEVKARVDE---VLELVN-LGDRAKKKIG----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 503 APILVLDEPTAHLDSqtEQ------LIQQAinkyAKNHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQG 564
Cdd:cd03264 149 PSILIVDEPTAGLDP--EErirfrnLLSEL----GEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
347-565 |
4.71e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.83 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAW 426
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTL-FYQSISDNIKI------AKPAATQLELEQAAHQAGALDFINTLengFDTligeqgegLSGGQKQRIALARAf 499
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMgraphgLSRAEDDALVAAALAQVDLAHLAGRD---YPQ--------LSGGEQQRVQLARV- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 500 LKQ-------APILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLN-TVKNASNILVMQNGEIAQQGT 565
Cdd:PRK13548 149 LAQlwepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
348-560 |
8.27e-20 |
|
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: 88.23 E-value: 8.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdatsmSTLQ-NAIAW 426
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-----SDLRgRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFYQ--------SISDNIKIAkpaatqLELEQAAHQ------AGALDFINtLENGFDTLigeqGEGLSGGQKQR 492
Cdd:cd03292 76 LRRKIGVVFQdfrllpdrNVYENVAFA------LEVTGVPPReirkrvPAALELVG-LSHKHRAL----PAELSGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 493 IALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIA-HRLNTVKNASN-ILVMQNGEI 560
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtHAKELVDTTRHrVIALERGKL 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
347-581 |
1.04e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.53 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLlgfhpQVIE-----QISINNKPLDaTSMSTLQ 421
Cdd:PRK11124 2 SIQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-----NLLEmprsgTLNIAGNHFD-FSKTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 422 NAIAWIPQTPTLFYQ--------SISDNIkIAKPAATqLELEQAAHQAGALDFINTLE-NGFDTLIGEQgegLSGGQKQR 492
Cdd:PRK11124 75 KAIRELRRNVGMVFQqynlwphlTVQQNL-IEAPCRV-LGLSKDQALARAEKLLERLRlKPYADRFPLH---LSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 493 IALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVI-AHRLNTV-KNASNILVMQNGEIAQQGTYSQLE 570
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIvTHEVEVArKTASRVVYMENGHIVEQGDASCFT 229
|
250
....*....|..
gi 658756163 571 Q-QQGAFKSLLN 581
Cdd:PRK11124 230 QpQTEAFKNYLS 241
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
18-510 |
1.06e-19 |
|
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: 92.55 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 18 FLKRQSKPAGAWLKLSIALGTFNAIlmiAGAYLLAqTIHNVMFEGASLSqvTHFLWPLAGIILLRALFLAISERLSAYAA 97
Cdd:COG4615 3 LLRLLLRESRWLLLLALLLGLLSGL---ANAGLIA-LINQALNATGAAL--ARLLLLFAGLLVLLLLSRLASQLLLTRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 98 LKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYyAKYLPGVAYSALIPLAILVVIFptdYKAGLIFLL 177
Cdd:COG4615 77 QHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQA-FVRLPELLQSVALVLGCLAYLA---WLSPPLFLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 178 TAPLI----PFFMILVGSKAEALNQKRWQQlAVLGNYFFDRVQGLTQLKLFNATQQEL--KQIAKISDDFRHATLGVLKI 251
Cdd:COG4615 153 TLVLLglgvAGYRLLVRRARRHLRRAREAE-DRLFKHFRALLEGFKELKLNRRRRRAFfdEDLQPTAERYRDLRIRADTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 252 aFLSSFAleFLATISVALVAVIIGFRLFFGTLDFA--TGFVVLLLapefYL--PLRQLGSHYHARLQGISAAADMVTI-- 325
Cdd:COG4615 232 -FALANN--WGNLLFFALIGLILFLLPALGWADPAvlSGFVLVLL----FLrgPLSQLVGALPTLSRANVALRKIEELel 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 326 -LNAPLPEQSQQHETKFEEHISSININNLNFTYPNSNEG----IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQ 400
Cdd:COG4615 305 aLAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegftLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 401 VIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSI-SDNIKIAKPAATQLELEQAAHQAgaldfinTLENG-FDTLi 478
Cdd:COG4615 385 ESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRLLgLDGEADPARARELLERLELDHKV-------SVEDGrFSTT- 456
|
490 500 510
....*....|....*....|....*....|..
gi 658756163 479 geqgeGLSGGQKQRIALARAFLKQAPILVLDE 510
Cdd:COG4615 457 -----DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
348-577 |
1.18e-19 |
|
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: 89.14 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNS-NEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFhPQVIEQISINNKPLDATSMSTLQNAIAW 426
Cdd:cd03289 3 MTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFYQSISDNIKIAKPAATQlELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPIL 506
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDE-EIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFK 577
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFK 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
337-577 |
1.29e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 93.44 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 337 HETKFEEHISSININNLNFTYPNSNEGI-KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEqISINNKPLDAT 415
Cdd:TIGR01271 1207 HAQKCWPSGGQMDVQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE-IQIDGVSWNSV 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 416 SMSTLQNAIAWIPQTPTLFYQSISDNIKIAKPAATQlELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIAL 495
Cdd:TIGR01271 1286 TLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDE-EIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 496 ARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQLEQQQGA 575
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSL 1444
|
..
gi 658756163 576 FK 577
Cdd:TIGR01271 1445 FK 1446
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
32-321 |
1.46e-19 |
|
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: 89.38 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 32 LSIALGTFNAILMIAGAYLLAQTIhNVMFEGAS------LSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMR 105
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLLGKAI-DLIIEGLGggggvdFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 106 QTLLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFF 185
Cdd:cd18547 82 KDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 186 MILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATlgvLKIAFLSSF---ALEFL 262
Cdd:cd18547 162 TKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKAS---FKAQFYSGLlmpIMNFI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 263 ATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYhARLQGISAAAD 321
Cdd:cd18547 239 NNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQI-NSLQSALAGAE 296
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
347-569 |
1.88e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.07 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTY----PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTL---FDCLLGFHPQVIE--QISINNKPLDaTSM 417
Cdd:PRK13646 2 TIRFDNVSYTYqkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLiqnINALLKPTTGTVTvdDITITHKTKD-KYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 418 STLQNAIAWIPQTP--TLFYQSISDNIkIAKPAATQLELEQAAHQAGALdfinTLENGFDTLIGEQGE-GLSGGQKQRIA 494
Cdd:PRK13646 81 RPVRKRIGMVFQFPesQLFEDTVEREI-IFGPKNFKMNLDEVKNYAHRL----LMDLGFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 495 LARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYA--KNHLVLVIAHRLNTV-KNASNILVMQNGEIAQQGTYSQL 569
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
346-585 |
2.22e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.15 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYPNSNEgIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIA 425
Cdd:PRK11231 1 MTLRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTlfyqsISDNIKIAKPAA----------TQLELEQAAHQAGALDfintlENGFDTLIGEQGEGLSGGQKQRIAL 495
Cdd:PRK11231 80 LLPQHHL-----TPEGITVRELVAygrspwlslwGRLSAEDNARVNQAME-----QTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 496 ARAFLKQAPILVLDEPTAHLD--SQTE--QLIQQaINKYAKNhlVLVIAHRLNTV-KNASNILVMQNGEIAQQGTYSQLe 570
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDinHQVElmRLMRE-LNTQGKT--VVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEV- 225
|
250
....*....|....*
gi 658756163 571 QQQGAFKSLLNLQAQ 585
Cdd:PRK11231 226 MTPGLLRTVFDVEAE 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
348-572 |
2.86e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.32 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWI 427
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTP--TLFYQSISDNIKIAkPAATQLELEQAAHQAGALdfINTLenGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPI 505
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFG-PINLGLDEETVAHRVSSA--LHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 506 LVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVI--AHRLNTVKN-ASNILVMQNGEIAQQGTYSQLEQQ 572
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
350-569 |
3.28e-19 |
|
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: 86.72 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPNSnEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNA---IAW 426
Cdd:cd03224 3 VENLNAGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR--DITGLPPHERAragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFYQ-SISDNIKIA------KPAATQLE--------LEQAAHQAGALdfintlengfdtligeqgegLSGGQKQ 491
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGayarrrAKRKARLErvyelfprLKERRKQLAGT--------------------LSGGEQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 492 RIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAK----------N-HLVLVIAHRLntvknasniLVMQNGEI 560
Cdd:cd03224 140 MLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDegvtillveqNaRFALEIADRA---------YVLERGRV 210
|
....*....
gi 658756163 561 AQQGTYSQL 569
Cdd:cd03224 211 VLEGTAAEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
350-585 |
3.37e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPnSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqVIE----QISINNkplDATsmstlqnaIA 425
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG----ELEpdsgEVSIPK---GLR--------IG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLF-YQSISDNIK----------------IAKPAATQLELEQAAHQAGALDFIN--TLEN---------GFDTL 477
Cdd:COG0488 65 YLPQEPPLDdDLTVLDTVLdgdaelraleaeleelEAKLAEPDEDLERLAELQEEFEALGgwEAEAraeeilsglGFPEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 478 IGEQ--GEgLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYakNHLVLVIAH-R--LNTVknASNI 552
Cdd:COG0488 145 DLDRpvSE-LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY--PGTVLVVSHdRyfLDRV--ATRI 219
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 658756163 553 LVMQNGEIAQ-QGTYS--------QLEQQQGAFKSLLNLQAQ 585
Cdd:COG0488 220 LELDRGKLTLyPGNYSayleqraeRLEQEAAAYAKQQKKIAK 261
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
348-561 |
3.45e-19 |
|
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: 86.61 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSN---EGIKNINLTLPAKGLVAVVGASGSGKSTLFDcLLGFHPQVIE-QISINNKPLDATSMSTLQNA 423
Cdd:TIGR02982 2 ISIRNLNHYYGHGSlrkQVLFDINLEINPGEIVILTGPSGSGKTTLLT-LIGGLRSVQEgSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 ---IAWIPQTPTLF-YQSISDNIKIAKPAATQLELEQAAHQAGALdfintLEN-GFDTLIGEQGEGLSGGQKQRIALARA 498
Cdd:TIGR02982 81 rrrIGYIFQAHNLLgFLTARQNVQMALELQPNLSYQEARERARAM-----LEAvGLGDHLNYYPHNLSGGQKQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 499 FLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKNASNILVMQNGEIA 561
Cdd:TIGR02982 156 LVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQgcTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
347-565 |
3.48e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.37 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTYPNSnEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIAW 426
Cdd:PRK10851 2 SIEIANIKKSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLF-YQSISDNI---------------KIAKPAATQL-ELEQAAHqagaldfintLENGFDTligeqgeGLSGGQ 489
Cdd:PRK10851 79 VFQHYALFrHMTVFDNIafgltvlprrerpnaAAIKAKVTQLlEMVQLAH----------LADRYPA-------QLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 490 KQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKY---AKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
348-559 |
4.07e-19 |
|
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: 84.04 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNsNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvieqisinnkpldatsmstlqnaiAWI 427
Cdd:cd03221 1 IELENLSKTYGG-KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG----------------------------ELE 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLfyqSISDNIKIAKpaatqleLEQaahqagaldfintlengfdtligeqgegLSGGQKQRIALARAFLKQAPILV 507
Cdd:cd03221 52 PDEGIV---TWGSTVKIGY-------FEQ----------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 508 LDEPTAHLDSQTEQLIQQAINKYakNHLVLVIAH-R--LNTVknASNILVMQNGE 559
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
366-569 |
5.13e-19 |
|
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: 89.00 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 366 NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPL-DATSMSTL---QNAIAWIPQTPTLF-YQSISD 440
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFLpphRRRIGYVFQEARLFpHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 441 NI----KIAKPAATQLELEQAahqagaldfINTLenGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLD 516
Cdd:COG4148 97 NLlygrKRAPRAERRISFDEV---------VELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 517 SQT--------EQLIQQAinkyaknHL-VLVIAH------RLntvknASNILVMQNGEIAQQGTYSQL 569
Cdd:COG4148 166 LARkaeilpylERLRDEL-------DIpILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEV 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
348-560 |
5.63e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.87 E-value: 5.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvIE-----QISINNKPLdaTSMStlQN 422
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG-----EErptsgQVLVNGQDL--SRLK--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 423 AIAW-------IPQ-TPTLFYQSISDNIKIA-----KPAAtqlELEQAAHQAgaLDFINtLENGFDTLIGEqgegLSGGQ 489
Cdd:COG2884 73 EIPYlrrrigvVFQdFRLLPDRTVYENVALPlrvtgKSRK---EIRRRVREV--LDLVG-LSDKAKALPHE----LSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 490 KQRIALARAFLKQAPILVLDEPTAHLDSQT-EQLIQ--QAINKYAKNhlVLVIAHRLNTVKNA-SNILVMQNGEI 560
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETsWEIMEllEEINRRGTT--VLIATHDLELVDRMpKRVLELEDGRL 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
347-565 |
6.00e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.41 E-value: 6.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTY----PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNkpLDAT----SMS 418
Cdd:PRK13637 2 SIKIENLTHIYmegtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITdkkvKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 419 TLQNAIAWIPQTP--TLFYQSISDNIKIAkPAATQLELEQ------AAHQAGALDFINTLENG-FDtligeqgegLSGGQ 489
Cdd:PRK13637 80 DIRKKVGLVFQYPeyQLFEETIEKDIAFG-PINLGLSEEEienrvkRAMNIVGLDYEDYKDKSpFE---------LSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 490 KQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAK--NHLVLVIAHRLNTV-KNASNILVMQNGEIAQQGT 565
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
348-571 |
6.71e-19 |
|
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: 86.19 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDA------------- 414
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekelyelrrri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 415 ----------TSMSTLQNaIAWipqtPTLFYQSISDNIkIAKPAATQLE---LEQAAHQagaldfintlengfdtLIGEq 481
Cdd:COG1127 85 gmlfqggalfDSLTVFEN-VAF----PLREHTDLSEAE-IRELVLEKLElvgLPGAADK----------------MPSE- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 482 gegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQT----EQLIQQaINKyaKNHL-VLVIAHRLNTVKN-ASNILVM 555
Cdd:COG1127 142 ---LSGGMRKRVALARALALDPEILLYDEPTAGLDPITsaviDELIRE-LRD--ELGLtSVVVTHDLDSAFAiADRVAVL 215
|
250
....*....|....*.
gi 658756163 556 QNGEIAQQGTYSQLEQ 571
Cdd:COG1127 216 ADGKIIAEGTPEELLA 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
348-560 |
6.73e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.68 E-value: 6.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTY----PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNA 423
Cdd:COG1101 2 LELKNLSKTFnpgtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--DVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 iAWI------PQTPTLFYQSISDNIKIA---------KPAATQLELEQAAHQAGALDfiNTLENGFDTLIGEqgegLSGG 488
Cdd:COG1101 80 -KYIgrvfqdPMMGTAPSMTIEENLALAyrrgkrrglRRGLTKKRRELFRELLATLG--LGLENRLDTKVGL----LSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 489 QKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKY-AKNHL-VLVIAHRLN-TVKNASNILVMQNGEI 560
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLtTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
349-571 |
8.98e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 85.65 E-value: 8.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 349 NINNLNFTYPNSnEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdaTSMSTLQNA---IA 425
Cdd:TIGR03410 2 EVSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI--TKLPPHERAragIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLFYQ-SISDNIKiakpaaTQLELEQAAHQAgALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAP 504
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLL------TGLAALPRRSRK-IPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 505 ILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQLEQ 571
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDE 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
348-565 |
1.13e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.94 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWI 427
Cdd:COG4559 2 LEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTL-FYQSISDNIKI------AKPAATQLELEQAAHQAGALDFINTLengFDTLigeqgeglSGGQKQRIALARAfL 500
Cdd:COG4559 81 PQHSSLaFPFTVEEVVALgraphgSSAAQDRQIVREALALVGLAHLAGRS---YQTL--------SGGEQQRVQLARV-L 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 501 KQ--------APILVLDEPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHRLN-TVKNASNILVMQNGEIAQQGT 565
Cdd:COG4559 149 AQlwepvdggPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGgVVAVLHDLNlAAQYADRILLLHQGRLVAQGT 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
350-560 |
1.17e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.88 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvIEQISINNKPLDATSMSTLQNAIAWIPQ 429
Cdd:PRK11247 15 LNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-----LETPSAGELLAGTAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 430 TPTLF-YQSISDNIKIA-----KPAATQleleqaahqagALDFIntlenGFDTLIGEQGEGLSGGQKQRIALARAFLKQA 503
Cdd:PRK11247 89 DARLLpWKKVIDNVGLGlkgqwRDAALQ-----------ALAAV-----GLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 504 PILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLN-TVKNASNILVMQNGEI 560
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
367-569 |
1.21e-18 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 87.86 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 367 INLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS----MSTLQNAIAWIPQTPTLF-YQSISDN 441
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgifLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 442 I----KIAKPAATQLELEQaahqagaldFINTLenGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS 517
Cdd:TIGR02142 96 LrygmKRARPSERRISFER---------VIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 518 QTEQLIQQAINKYAK--NHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQL 569
Cdd:TIGR02142 165 PRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
365-561 |
1.77e-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: 82.86 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 365 KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS-MSTLQNAIAWIPQtptlfyqsisdnik 443
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 444 iakpaatqleleqaahqagaldfintlengfdtligeqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHL-DSQTEQL 522
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALtPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658756163 523 IQQAINKYAKNHLVLVIAHRLNTVKN-ASNILVMQNGEIA 561
Cdd:cd03216 122 FKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
348-572 |
2.49e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNsNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvieQIsinnkPLDATSM---STLQnaI 424
Cdd:COG0488 316 LELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-------EL-----EPDSGTVklgETVK--I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 425 AWIPQTPTLFY--QSISDNIKIAKPAATQLELeqaahqagaldfINTLEN-GF-----DTLIGEqgegLSGGQKQRIALA 496
Cdd:COG0488 381 GYFDQHQEELDpdKTVLDELRDGAPGGTEQEV------------RGYLGRfLFsgddaFKPVGV----LSGGEKARLALA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 497 RAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNhlVLVIAH-R--LNTVknASNILVMQNGEIAQ-QGTYSQLEQQ 572
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGT--VLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDDYLEK 520
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
364-568 |
3.50e-18 |
|
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: 84.03 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdaTSMSTLQNAIAWIP---QTPTLFYQ-SIS 439
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI--TGLPPHEIARLGIGrtfQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 440 DNIKIA------------KPAATQLELEQAAHQAgaLDFINtLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILV 507
Cdd:cd03219 94 ENVMVAaqartgsglllaRARREEREARERAEEL--LERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 508 LDEPTAHLDSQ-TEQLIQ--QAINkyAKNHLVLVIAHRLNTVKNASN-ILVMQNGEIAQQGTYSQ 568
Cdd:cd03219 167 LDEPAAGLNPEeTEELAEliRELR--ERGITVLLVEHDMDVVMSLADrVTVLDQGRVIAEGTPDE 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
364-564 |
3.65e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 83.86 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFD---CLLGFHPQVIEQISINNKPLDATSMstlQNAIAWIPQ----------- 429
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDaisGRVEGGGTTSGQILFNGQPRKPDQF---QKCVAYVRQddillpgltvr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 430 -----TPTLFYQSISDNiKIAKPAATQLELEQAAHQAGALDFIntlengfdtligeqgEGLSGGQKQRIALARAFLKQAP 504
Cdd:cd03234 100 etltyTAILRLPRKSSD-AIRKKRVEDVLLRDLALTRIGGNLV---------------KGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 505 ILVLDEPTAHLDSQTEQLIQQAINKYAK-NHLVLVIAH--RLNTVKNASNILVMQNGEIAQQG 564
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
346-525 |
4.19e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 84.32 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFH---PQV-IE-QISINNKPLDATSMS-- 418
Cdd:COG1117 10 PKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdliPGArVEgEILLDGEDIYDPDVDvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 419 TLQNAIAWIPQTPTLFYQSISDNI-------KIAKPAatqlEL----EQAAHQAGALDFINtlengfDTLiGEQGEGLSG 487
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVayglrlhGIKSKS----ELdeivEESLRKAALWDEVK------DRL-KKSALGLSG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 658756163 488 GQKQRIALARAFLKQAPILVLDEPTAHLD----SQTEQLIQQ 525
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILE 199
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
377-580 |
5.00e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.48 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIAWIPQTPTLF-YQSISDNIKIA-KP-----AA 449
Cdd:PRK10771 28 VAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRPVSMLFQENNLFsHLTVAQNIGLGlNPglklnAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 450 TQLELEQAAHQAGaldfintLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQ----LIQQ 525
Cdd:PRK10771 106 QREKLHAIARQMG-------IEDLLARLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQemltLVSQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 526 AINKyaKNHLVLVIAHRL-NTVKNASNILVMQNGEIAQQGTYSQLEQQQGAFKSLL 580
Cdd:PRK10771 175 VCQE--RQLTLLMVSHSLeDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
364-566 |
6.32e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 88.30 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvieQISINNKPLDAtsmstlQNAIAWIPQTPTLFYQSISDNIK 443
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-------QFEISEGRVWA------ERSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 444 IAKPaatqlelEQAAHQAGALDF------INTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS 517
Cdd:PTZ00243 743 FFDE-------EDAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658756163 518 QTEQLIQQAINKYAKNHLVLVIA-HRLNTVKNASNILVMQNGEIAQQGTY 566
Cdd:PTZ00243 816 HVGERVVEECFLGALAGKTRVLAtHQVHVVPRADYVVALGDGRVEFSGSS 865
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
346-565 |
1.16e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 83.70 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYPNSNEGI-KNINLTLPAKGLVAVVGASGSGKST---LFDCLLGFHPQVIEQISINNKPLDATSMSTLQ 421
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPAlNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 422 NAIAWIPQTP--TLFYQSISD-------NIKIAKPAATQLeLEQAAHQAGALDFINTlengfdtligeQGEGLSGGQKQR 492
Cdd:PRK13640 84 EKVGIVFQNPdnQFVGATVGDdvafgleNRAVPRPEMIKI-VRDVLADVGMLDYIDS-----------EPANLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 493 IALARAFLKQAPILVLDEPTAHLD----SQTEQLIQQAINKyaKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
347-565 |
1.29e-17 |
|
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: 82.39 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTYPNSnEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIAW 426
Cdd:cd03296 2 SIEVRNVSKRFGDF-VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLF-YQSISDNI----KIAKPAATQLELEQAAHQAGALDFIntlenGFDTLIGEQGEGLSGGQKQRIALARAFLK 501
Cdd:cd03296 79 VFQHYALFrHMTVFDNVafglRVKPRSERPPEAEIRAKVHELLKLV-----QLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 502 QAPILVLDEPTAHLDSQTEQLIQQAINK-YAKNHL--VLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRlHDELHVttVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
348-565 |
1.98e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.97 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI---KNINLTLPAKGLVAVVGASGSGKSTLFDC--LL-----GfhpqvieQISINNKPLDATSM 417
Cdd:COG1135 2 IELENLSKTFPTKGGPVtalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCinLLerptsG-------SVLVDGVDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 418 STLQNA---IAWIPQTPTLFYQ-SISDNIkiAKPaatqLEL-----EQAAHQAGALdfintLEngfdtLIGEQGEG---- 484
Cdd:COG1135 75 RELRAArrkIGMIFQHFNLLSSrTVAENV--ALP----LEIagvpkAEIRKRVAEL-----LE-----LVGLSDKAdayp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 --LSGGQKQRIALARAfLKQAP-ILVLDEPTAHLDSQTEQ----LIQQaINKyaKNHL-VLVIAHRLNTVKN-ASNILVM 555
Cdd:COG1135 139 sqLSGGQKQRVGIARA-LANNPkVLLCDEATSALDPETTRsildLLKD-INR--ELGLtIVLITHEMDVVRRiCDRVAVL 214
|
250
....*....|
gi 658756163 556 QNGEIAQQGT 565
Cdd:COG1135 215 ENGRIVEQGP 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
347-581 |
2.75e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.60 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINN------KPLDATSMSTL 420
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 421 QNAIAWIPQTPTLF-YQSISDNIkIAKPAATqLELEQAAHQAGALDFINTLEngfdtlIGEQGEG----LSGGQKQRIAL 495
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENL-IEAPCKV-LGLSKEQAREKAMKLLARLR------LTDKADRfplhLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 496 ARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVI-AHRLNTV-KNASNILVMQNGEIAQQGTYSQLEQ-Q 572
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIvTHEVEFArKVASQVVYMEKGRIIEQGDASHFTQpQ 232
|
....*....
gi 658756163 573 QGAFKSLLN 581
Cdd:COG4161 233 TEAFAHYLS 241
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
348-564 |
3.13e-17 |
|
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: 80.76 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNsNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIAWI 427
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLF-----YQSISDNIKIAKpaATQLELEQAAHQAGALDFIntlengfDTLIGEQGEGLSGGQKQRIALARAFLKQ 502
Cdd:cd03301 78 FQNYALYphmtvYDNIAFGLKLRK--VPKDEIDERVREVAELLQI-------EHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 503 APILVLDEPTAHLDSQTEQLIQQAINKYAKNH---LVLVIAHRLNTVKNASNILVMQNGEIAQQG 564
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLgttTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
348-575 |
3.26e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPL--DATSMSTLQNAIA 425
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTP--TLFYQSISD-------NIKIAKpAATQLELEQAAHQAGALDFINTLENGfdtligeqgegLSGGQKQRIALA 496
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEdvafgplNLGLSK-EEVEKRVKEALKAVGMEGFENKPPHH-----------LSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 497 RAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIA-HRLNTV-KNASNILVMQNGEIAQQGT----YSQLE 570
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTpkevFSDIE 229
|
....*
gi 658756163 571 QQQGA 575
Cdd:PRK13639 230 TIRKA 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
346-541 |
5.55e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.06 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYPNSNEG---IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTlqn 422
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 423 aiAWIPQTPTLF-YQSISDNI----KIAKpaatqleLEQAAHQAGALDFIntlengfdTLIGEQGEG------LSGGQKQ 491
Cdd:COG4525 79 --GVVFQKDALLpWLNVLDNVafglRLRG-------VPKAERRARAEELL--------ALVGLADFArrriwqLSGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658756163 492 RIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINK-YAKNH-LVLVIAH 541
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDvWQRTGkGVFLITH 193
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
331-565 |
6.89e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.98 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 331 PEQSQQHETKFEEHissininNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCL---------------L 395
Cdd:PRK14243 1 TSTLNGTETVLRTE-------NLNVYY-GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndlipgfrvegkV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 396 GFHPQvieqiSINNKPLDATSmstLQNAIAWIPQTPTLFYQSISDNI----KIAKPAATQLEL-EQAAHQAGALDFINtl 470
Cdd:PRK14243 73 TFHGK-----NLYAPDVDPVE---VRRRIGMVFQKPNPFPKSIYDNIaygaRINGYKGDMDELvERSLRQAALWDEVK-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 471 engfDTLiGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNAS 550
Cdd:PRK14243 143 ----DKL-KQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVS 217
|
250
....*....|....*
gi 658756163 551 NILVMQNGEIAQQGT 565
Cdd:PRK14243 218 DMTAFFNVELTEGGG 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
363-565 |
8.21e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 80.77 E-value: 8.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 363 GIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQN----AIAWIPQTPTLF-YQS 437
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 438 ISDNIKIAKPAATQLELEQAAHQAGALDFINtLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS 517
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVG-LEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 518 ------QTEQLIQQAinKYAKNhlVLVIAHRLN-TVKNASNILVMQNGEIAQQGT 565
Cdd:cd03294 194 lirremQDELLRLQA--ELQKT--IVFITHDLDeALRLGDRIAIMKDGRLVQVGT 244
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
347-565 |
1.34e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.05 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTY----PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTL---FDCLL----GF---------HPQVIEQIS 406
Cdd:PRK13631 21 ILRVKNLYCVFdekqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLvthFNGLIkskyGTiqvgdiyigDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 407 INNKPLDATSMSTLQNAIAWIPQTP--TLFYQSISDNIKIAKPAATQLELEqaAHQAGALdFINTLenGFDTLIGEQGE- 483
Cdd:PRK13631 101 TNPYSKKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE--AKKLAKF-YLNKM--GLDDSYLERSPf 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 484 GLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAI-NKYAKNHLVLVIAHRL-NTVKNASNILVMQNGEIA 561
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKIL 255
|
....
gi 658756163 562 QQGT 565
Cdd:PRK13631 256 KTGT 259
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
348-569 |
1.44e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 79.88 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPN--------SNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMST 419
Cdd:COG4167 5 LEVRNLSKTFKYrtglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 420 LQNAIAWIPQTPTlfyQSISDNIKIAK----PA--ATQLELEQAAHQagaldFINTLEngfdtLIGEQGEG-------LS 486
Cdd:COG4167 85 RCKHIRMIFQDPN---TSLNPRLNIGQileePLrlNTDLTAEEREER-----IFATLR-----LVGLLPEHanfyphmLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 487 GGQKQRIALARAFLKQAPILVLDEPTAHLD-SQTEQLI------QQAIN-KYaknhlvLVIAHRLNTVKNAS-NILVMQN 557
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDmSVRSQIInlmlelQEKLGiSY------IYVSQHLGIVKHISdKVLVMHQ 225
|
250
....*....|..
gi 658756163 558 GEIAQQGTYSQL 569
Cdd:COG4167 226 GEVVEYGKTAEV 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
347-560 |
1.45e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTY----PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTL---FDCLLGFHPQVIE----QISIN--NKPLD 413
Cdd:PRK13641 2 SIKFENVDYIYspgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLmqhFNALLKPSSGTITiagyHITPEtgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 414 AtsmstLQNAIAWIPQTP--TLFYQSISDNIKIAkPAATQLELEQAAHQAgaLDFINTLenGFDT-LIGEQGEGLSGGQK 490
Cdd:PRK13641 82 K-----LRKKVSLVFQFPeaQLFENTVLKDVEFG-PKNFGFSEDEAKEKA--LKWLKKV--GLSEdLISKSPFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 491 QRIALARAFLKQAPILVLDEPTAHLDSQT-EQLIQQAINKYAKNHLVLVIAHRLNTV-KNASNILVMQNGEI 560
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKL 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
364-555 |
1.98e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 77.66 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQ---------------VIEQISINNK-PL---DATSMSTLQNAI 424
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPtsgtvrraggarvayVPQRSEVPDSlPLtvrDLVAMGRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 425 AWIPQTptlfyqsisdnikiakpAATQLELEQAAHQAGALDFintLENGFDTLigeqgeglSGGQKQRIALARAFLKQAP 504
Cdd:NF040873 88 LWRRLT-----------------RDDRAAVDDALERVGLADL---AGRQLGEL--------SGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658756163 505 ILVLDEPTAHLDSQTEQLIQQAINKY-AKNHLVLVIAHRLNTVKNASNILVM 555
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
350-573 |
2.35e-16 |
|
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: 82.29 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPNSNEGIKNINLT-LP-AKglVAVVGASGSGKSTLFDCLLG----FHPQVIEQISIN-----NKP-LDATsM 417
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSfFPgAK--IGVLGLNGAGKSTLLRIMAGvdkdFNGEARPQPGIKvgylpQEPqLDPT-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 418 STLQNAIAWIPQTPTLF--YQSISDniKIAKP-------AATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEG---- 484
Cdd:TIGR03719 84 TVRENVEEGVAEIKDALdrFNEISA--KYAEPdadfdklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDAdvtk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 LSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNhlVLVIAH-R--LNTVknASNILVMQNGE-I 560
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGT--VVAVTHdRyfLDNV--AGWILELDRGRgI 237
|
250
....*....|....
gi 658756163 561 AQQGTYSQ-LEQQQ 573
Cdd:TIGR03719 238 PWEGNYSSwLEQKQ 251
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
360-572 |
2.65e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.53 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 360 SNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIAWIPQTPTLF-YQSI 438
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTHRSIQQRDICMVFQSYALFpHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 439 SDNI-------KIAKPaatqlELEQAAHQAGAL-DFIntlenGFDTLIGEQgegLSGGQKQRIALARAFLKQAPILVLDE 510
Cdd:PRK11432 96 GENVgyglkmlGVPKE-----ERKQRVKEALELvDLA-----GFEDRYVDQ---ISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 511 PTAHLDSQTEQLIQQAINKYAK--NHLVLVIAHRLNTVKNASN-ILVMQNGEIAQQGTYSQLEQQ 572
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDtVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
342-565 |
4.34e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.64 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 342 EEHIssININNLNFTYpNSNEG--IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMST 419
Cdd:PRK13648 4 KNSI--IVFKNVSFQY-QSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 420 LQNAIAWIPQTP-TLFYQSIsdnikIAKPAATQLELEQAAHQ------AGALDFINTLENGFDtligeQGEGLSGGQKQR 492
Cdd:PRK13648 81 LRKHIGIVFQNPdNQFVGSI-----VKYDVAFGLENHAVPYDemhrrvSEALKQVDMLERADY-----EPNALSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 493 IALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIA--HRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
330-542 |
5.07e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 330 LPEQSQQHETKFEEHISSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISInn 409
Cdd:COG4178 345 ADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 410 kPLDATSMstlqnaiaWIPQTP---------TLFYQSISDNIkiakpaaTQLELEQAAHQAGALDFINTLENgfdtligE 480
Cdd:COG4178 423 -PAGARVL--------FLPQRPylplgtlreALLYPATAEAF-------SDAELREALEAVGLGHLAERLDE-------E 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658756163 481 Q--GEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHR 542
Cdd:COG4178 480 AdwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-541 |
5.75e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTL---FDCLLGFHP--QVIEQISINNKPLDATSMSTLQ 421
Cdd:PRK14267 4 AIETVNLRVYY-GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLLELNEeaRVEGEVRLFGRNIYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 422 --NAIAWIPQTPTLF-----YQSISDNIKIAKPAATQLEL----EQAAHQAGALDFINTLENGFDTligeqgeGLSGGQK 490
Cdd:PRK14267 83 vrREVGMVFQYPNPFphltiYDNVAIGVKLNGLVKSKKELdervEWALKKAALWDEVKDRLNDYPS-------NLSGGQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658756163 491 QRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAH 541
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
348-552 |
7.93e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.51 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCL--LG-FHPQVIEQISINNKPLDATSMST----L 420
Cdd:PRK14239 6 LQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPEVTITGSIVYNGHNIYSPRTdtvdL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 421 QNAIAWIPQTPTLFYQSISDN------IKIAKPAATQLE-LEQAAHQAGALDFINtlengfDTLiGEQGEGLSGGQKQRI 493
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENvvyglrLKGIKDKQVLDEaVEKSLKGASIWDEVK------DRL-HDSALGLSGGQQQRV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 494 ALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLntvKNASNI 552
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM---QQASRI 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
348-569 |
8.01e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 8.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNE--GIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIA 425
Cdd:PRK13642 5 LEVENLVFKYEKESDvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTP--TLFYQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLEngFDTligEQGEGLSGGQKQRIALARAFLKQA 503
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD--FKT---REPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 504 PILVLDEPTAHLD----SQTEQLIQQAINKYaknHL-VLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQL 569
Cdd:PRK13642 160 EIIILDESTSMLDptgrQEIMRVIHEIKEKY---QLtVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
364-560 |
9.97e-16 |
|
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: 75.55 E-value: 9.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNA-IAWIPQTPtlfyqsisdni 442
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDR----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 443 kiakpaatqleleqaaHQAGALDFINTLENgfdTLIGEQgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQL 522
Cdd:cd03215 85 ----------------KREGLVLDLSVAEN---IALSSL---LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658756163 523 IQQAINKYA-KNHLVLVIAHRLNTVKNASN-ILVMQNGEI 560
Cdd:cd03215 143 IYRLIRELAdAGKAVLLISSELDELLGLCDrILVMYEGRI 182
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
352-564 |
1.21e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.35 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 352 NLNFTYPNSnEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGF-HPQ---VIEQisinNKPLDATS--MSTLQNAIA 425
Cdd:PRK13638 6 DLWFRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLlRPQkgaVLWQ----GKPLDYSKrgLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTP--TLFYQSISDNIKIAKPAATQLELEQAAHQAGALdfintlengfdTLIGEQG------EGLSGGQKQRIALAR 497
Cdd:PRK13638 81 TVFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEAL-----------TLVDAQHfrhqpiQCLSHGQKKRVAIAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 498 AFLKQAPILVLDEPTAHLDSQTE-QLIQQAINKYAKNHLVLVIAHRLNTVKNASN-ILVMQNGEIAQQG 564
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRtQMIAIIRRIVAQGNHVIISSHDIDLIYEISDaVYVLRQGQILTHG 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
367-527 |
1.40e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.61 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 367 INLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMStLQNAIAWIPQTPTLFYQ-SISDNIKIA 445
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGIKTTlSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 446 KPAATQLELEQAAHQAGAldfintleNGFDTLIGEQgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQ 525
Cdd:cd03231 98 HADHSDEQVEEALARVGL--------NGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
..
gi 658756163 526 AI 527
Cdd:cd03231 167 AM 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
365-573 |
1.59e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 365 KNINLTLpAKGLV-AVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNA-IAWIPQTPTLF-YQSISDN 441
Cdd:COG1129 21 DGVSLEL-RPGEVhALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVpNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 442 IKIAKPAATQLELEQAAHQAGALDFINTLenGFD----TLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHL-D 516
Cdd:COG1129 100 IFLGREPRRGGLIDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLtE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 517 SQTEQLIQQaINKY-AKNHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQLEQQQ 573
Cdd:COG1129 174 REVERLFRI-IRRLkAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELTEDE 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
348-565 |
1.62e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 76.66 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWI 427
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLfyqsisdNIKIakpaaTQLEL---------------EQAAHQAGALDFIN--TLENGF-DTLigeqgeglSGGQ 489
Cdd:COG4604 81 RQENHI-------NSRL-----TVRELvafgrfpyskgrltaEDREIIDEAIAYLDleDLADRYlDEL--------SGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 490 KQRIALARAFLKQAPILVLDEPTAHLD----SQTEQLIQQAINKYAKNhLVLVIaHRLNTVKN-ASNILVMQNGEIAQQG 564
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKT-VVIVL-HDINFASCyADHIVAMKDGRVVAQG 218
|
.
gi 658756163 565 T 565
Cdd:COG4604 219 T 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
348-564 |
1.74e-15 |
|
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: 75.33 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIAWI 427
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLF-YQSISDNIKIAkpaATQLELEQAAHQAgALDFINtLENGFDTLIGeqgeGLSGGQKQRIALARAFLKQAPIL 506
Cdd:cd03268 78 IEAPGFYpNLTARENLRLL---ARLLGIRKKRIDE-VLDVVG-LKDSAKKKVK----GFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAINKYAKN-HLVLVIAHRLNTV-KNASNILVMQNGEIAQQG 564
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-541 |
1.79e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.49 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYPNSnEGIKNINLTLPAKGLVAVVGASGSGKSTL---FDCLLGFHPQ--VIEQISINNKPLDATSMSTL 420
Cdd:PRK14247 2 NKIEIRDLKVSFGQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLlrvFNRLIELYPEarVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 421 QNAIAWIPQTPT-----LFYQSISDNIKIAKPAATQLELEQAAHQAgaLDFINTLENGFDTLIGEQGEgLSGGQKQRIAL 495
Cdd:PRK14247 81 RRRVQMVFQIPNpipnlSIFENVALGLKLNRLVKSKKELQERVRWA--LEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 658756163 496 ARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAH 541
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
41-306 |
2.37e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 76.78 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 41 AILMIAGA-------YLLAQTIHNVmFEGASLSQVTHFLWP----LAGIILLRALFLAISERLSAYAALKIKSAMRQTLL 109
Cdd:cd18563 5 FLLMLLGTalglvppYLTKILIDDV-LIQLGPGGNTSLLLLlvlgLAGAYVLSALLGILRGRLLARLGERITADLRRDLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 110 TKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILV 189
Cdd:cd18563 84 EHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 190 GSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVAL 269
Cdd:cd18563 164 WKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLI 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 658756163 270 VAVIIGFRLFFGTLDFAT--GFVVLLLapEFYLPLRQLG 306
Cdd:cd18563 244 VWYFGGRQVLSGTMTLGTlvAFLSYLG--MFYGPLQWLS 280
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
362-565 |
2.41e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 362 EGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFY---QSI 438
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLnprQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 439 SDNIKIAKPAATQLELE-------QAAHQAGAL-DFINTLENGfdtligeqgegLSGGQKQRIALARAFLKQAPILVLDE 510
Cdd:PRK15112 107 SQILDFPLRLNTDLEPEqrekqiiETLRQVGLLpDHASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 511 PTAHLD-SQTEQLIQQAINKYAKNHLVLV-IAHRLNTVKNASN-ILVMQNGEIAQQGT 565
Cdd:PRK15112 176 ALASLDmSMRSQLINLMLELQEKQGISYIyVTQHLGMMKHISDqVLVMHQGEVVERGS 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
348-562 |
2.76e-15 |
|
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: 75.55 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPnSNEG----IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvIEQ-----ISINNKPLDAtsMS 418
Cdd:COG4181 9 IELRGLTKTVG-TGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-----LDRptsgtVRLAGQDLFA--LD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 419 TLQNA------IAWIPQT----PTLfyqSISDNIkiakpaATQLEL---EQAAHQAGALdfintLEN-GFDTLIGEQGEG 484
Cdd:COG4181 81 EDARArlrarhVGFVFQSfqllPTL---TALENV------MLPLELagrRDARARARAL-----LERvGLGHRLDHYPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 LSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQ---AINKYAKNHLVLV-----IAHRlntvknASNILVMQ 556
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDllfELNRERGTTLVLVthdpaLAAR------CDRVLRLR 220
|
....*.
gi 658756163 557 NGEIAQ 562
Cdd:COG4181 221 AGRLVE 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
366-559 |
3.24e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.43 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 366 NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQ--VIEQISINNKPLDATSMS-TLQNAIAWIPQTPTLFYQ-SISDN 441
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEELQASNIRdTERAGIAIIHQELALVKElSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 442 I---------KIAKPAATQLELEQAAHQAGaLDfINTlengfDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPT 512
Cdd:PRK13549 103 IflgneitpgGIMDYDAMYLRAQKLLAQLK-LD-INP-----ATPVGN----LGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658756163 513 AHL-DSQTEQLIqqAINKYAKNHLV--LVIAHRLNTVKNAS-NILVMQNGE 559
Cdd:PRK13549 172 ASLtESETAVLL--DIIRDLKAHGIacIYISHKLNEVKAISdTICVIRDGR 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
366-556 |
3.32e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.14 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 366 NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIKIa 445
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIF- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 446 kPAATQLELEQAAHQAGALDFINTLENGFDTLIGEqgegLSGGQKQRIALAR--AFLKQapILVLDEPTAHLDSQTEQLI 523
Cdd:PRK10247 104 -PWQIRNQQPDPAIFLDDLERFALPDTILTKNIAE----LSGGEKQRISLIRnlQFMPK--VLLLDEITSALDESNKHNV 176
|
170 180 190
....*....|....*....|....*....|....*
gi 658756163 524 QQAINKYAKNH--LVLVIAHRLNTVKNASNILVMQ 556
Cdd:PRK10247 177 NEIIHRYVREQniAVLWVTHDKDEINHADKVITLQ 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
364-569 |
3.99e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPL-DATSMSTLQNAIAWIPQTPTLF-YQSISDN 441
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPAKAHQLGIYLVPQEPLLFpNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 442 I--KIAKPAATQLELEQA----------AHQAGALDfintlengfdtlIGEQgeglsggqkQRIALARAFLKQAPILVLD 509
Cdd:PRK15439 107 IlfGLPKRQASMQKMKQLlaalgcqldlDSSAGSLE------------VADR---------QIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 510 EPTAHLD-SQTEQLIQQAINKYAKNHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQL 569
Cdd:PRK15439 166 EPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
348-565 |
4.48e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.79 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGF-HPQVIEQISinnKPLDATSMSTLQNA--- 423
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLlRPQKGKVLV---SGIDTGDFSKLQGIrkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 IAWIPQTP-TLFY-QSISDNIKIAKP--AATQLELEQAAHQAGAldfintlENGFDTLIGEQGEGLSGGQKQRIALARAF 499
Cdd:PRK13644 79 VGIVFQNPeTQFVgRTVEEDLAFGPEnlCLPPIEIRKRVDRALA-------EIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 500 LKQAPILVLDEPTAHLDSQTEQLIQQAINK-YAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
350-570 |
5.12e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTyPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfHP--QVIE-QISINNKplDATSMSTLQNAIAW 426
Cdd:COG0396 3 IKNLHVS-VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPkyEVTSgSILLDGE--DILELSPDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IpqtptlFY--Q--------SISDNIKIAKPAATQLELeqaahqaGALDFINTLENGFDTL-IGEQ------GEGLSGGQ 489
Cdd:COG0396 79 I------FLafQypveipgvSVSNFLRTALNARRGEEL-------SAREFLKLLKEKMKELgLDEDfldryvNEGFSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 490 KQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAH--R-LNTVKnASNILVMQNGEIAQQGT 565
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRgILIITHyqRiLDYIK-PDFVHVLVDGRIVKSGG 224
|
....*...
gi 658756163 566 YS---QLE 570
Cdd:COG0396 225 KElalELE 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-569 |
5.74e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.08 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 349 NINNLnFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPL---------DATSmst 419
Cdd:PRK14246 12 NISRL-YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqiDAIK--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 420 LQNAIAWIPQTPTLF-YQSISDNIKIA-KPAATQLELEQAAHQAGALDFINTLENGFDTLiGEQGEGLSGGQKQRIALAR 497
Cdd:PRK14246 88 LRKEVGMVFQQPNPFpHLSIYDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 498 AFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASN-ILVMQNGEIAQQGTYSQL 569
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADyVAFLYNGELVEWGSSNEI 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
350-569 |
6.04e-15 |
|
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: 75.86 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPNSNEGIK---NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIE---QISINNKPLDATSMSTLQ-- 421
Cdd:COG0444 4 VRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGItsgEILFDGEDLLKLSEKELRki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 422 --NAIAWIPQTP--------TLFYQsISDNIKIAKP---------AATQLEL------EQAA----HQagaldfintlen 472
Cdd:COG0444 84 rgREIQMIFQDPmtslnpvmTVGDQ-IAEPLRIHGGlskaearerAIELLERvglpdpERRLdrypHE------------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 473 gfdtligeqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLD----SQTEQLIQQaINKyaKNHL-VLVIAHRLNTVK 547
Cdd:COG0444 151 ------------LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKD-LQR--ELGLaILFITHDLGVVA 215
|
250 260
....*....|....*....|...
gi 658756163 548 N-ASNILVMQNGEIAQQGTYSQL 569
Cdd:COG0444 216 EiADRVAVMYAGRIVEEGPVEEL 238
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
364-568 |
6.58e-15 |
|
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: 74.69 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDA---------------------TSMSTLQN 422
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphriarlgiartfqnprlfPELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 423 -AIAWIPQTPTLFYQSIsdnIKIAKPAATQLELEQAAHQAgaLDFIntlenGFDTLIGEQGEGLSGGQKQRIALARAFLK 501
Cdd:COG0411 100 vLVAAHARLGRGLLAAL---LRLPRARREEREARERAEEL--LERV-----GLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 502 QAPILVLDEPTAHLDSQ-TEQLIQ--QAINKyAKNHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQ 568
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEeTEELAEliRRLRD-ERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
348-565 |
6.92e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.44 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTY----PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS----MST 419
Cdd:PRK13634 3 ITFQKVEHRYqyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkkLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 420 LQNAIAWIPQTP--TLFYQSISDNIKIAkP---AATQLELEQAAHQAGALdfintleNGFDTLIGEQGE-GLSGGQKQRI 493
Cdd:PRK13634 83 LRKKVGIVFQFPehQLFEETVEKDICFG-PmnfGVSEEDAKQKAREMIEL-------VGLPEELLARSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 494 ALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH---LVLViAHRLNTVKN-ASNILVMQNGEIAQQGT 565
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKgltTVLV-THSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
364-564 |
7.10e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 74.04 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS---MSTLQNaIAWIPqtptlfYQSISD 440
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGpdrMVVFQN-YSLLP------WLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 441 NIKIA----KPAATQLELEQAAHQAgaLDFINtLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLD 516
Cdd:TIGR01184 74 NIALAvdrvLPDLSKSERRAIVEEH--IALVG-LTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658756163 517 SQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKNASNILVM-QNGEIAQQG 564
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVVMlTNGPAANIG 197
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
366-527 |
7.30e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.55 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 366 NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdATSMSTLQNAIAWIpqtptlfyqSISDNIKIA 445
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYL---------GHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 446 KPAATQLELEQAAHQAGALDFINTLE----NGFDTLIGEQgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQ 521
Cdd:TIGR01189 88 LSALENLHFWAAIHGGAQRTIEDALAavglTGFEDLPAAQ---LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
....*.
gi 658756163 522 LIQQAI 527
Cdd:TIGR01189 165 LLAGLL 170
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
357-523 |
7.66e-15 |
|
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: 73.23 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 357 YPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLG-FHPQViEQISINNKPLDAT--SMSTLQNAIAWIPQTP-- 431
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQS-GAVLIDGEPLDYSrkGLLERRQRVGLVFQDPdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 432 TLFYQSISDNIKIA------KPAATQLELEQAAHQAGALDFINTLENGfdtligeqgegLSGGQKQRIALARAFLKQAPI 505
Cdd:TIGR01166 80 QLFAADVDQDVAFGplnlglSEAEVERRVREALTAVGASGLRERPTHC-----------LSGGEKKRVAIAGAVAMRPDV 148
|
170
....*....|....*....
gi 658756163 506 LVLDEPTAHLDSQ-TEQLI 523
Cdd:TIGR01166 149 LLLDEPTAGLDPAgREQML 167
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
350-569 |
1.24e-14 |
|
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: 73.48 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPNSnEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdaTSMSTLQNA---IAW 426
Cdd:COG0410 6 VENLHAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI--TGLPPHRIArlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQT----PTLfyqSISDNIKIAKPAATQleleqAAHQAGALDFINTLengFDTL---IGEQGEGLSGGQKQRIALARAF 499
Cdd:COG0410 83 VPEGrrifPSL---TVEENLLLGAYARRD-----RAEVRADLERVYEL---FPRLkerRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 500 LKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKN-----------HLVLVIAHRlntvknasnILVMQNGEIAQQGTYSQ 568
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgvtillveqnaRFALEIADR---------AYVLERGRIVLEGTAAE 222
|
.
gi 658756163 569 L 569
Cdd:COG0410 223 L 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
348-564 |
1.30e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.64 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNkpLDATSMSTLQNAIAWI 427
Cdd:PRK11607 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLSHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLF-YQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLEngfdtLIGEQGEGLSGGQKQRIALARAFLKQAPIL 506
Cdd:PRK11607 97 FQSYALFpHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE-----FAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 507 VLDEPTAHLDSQTEQLIQQA---INKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQG 564
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEvvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
350-560 |
1.34e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.07 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPNSNEGI---KNINLTLPAKGLVAVVGASGSGKSTLFDcLLGfhpqVIEQISINNKPLDATSMSTLQN-AIA 425
Cdd:PRK10535 7 LKDIRRSYPSGEEQVevlKGISLDIYAGEMVAIVGASGSGKSTLMN-ILG----CLDKPTSGTYRVAGQDVATLDAdALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 --------WIPQTPTLF-YQSISDNIKIAkpaATQLELEQAAHQAGALDFINTLenGFDTLIGEQGEGLSGGQKQRIALA 496
Cdd:PRK10535 82 qlrrehfgFIFQRYHLLsHLTAAQNVEVP---AVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 497 RAFLKQAPILVLDEPTAHLDSQT--------EQLIQQAinkyaknHLVLVIAHRLNTVKNASNILVMQNGEI 560
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSgeevmailHQLRDRG-------HTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
367-516 |
1.37e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 367 INLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTL-FYQSISDNIKIA 445
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 446 K-PAATQLE---------LEQAAHQAGALDFIntlENGFDTLigeqgeglSGGQKQRIALARAFLKQAPILVLDEPTAHL 515
Cdd:PRK09536 102 RtPHRSRFDtwtetdraaVERAMERTGVAQFA---DRPVTSL--------SGGERQRVLLARALAQATPVLLLDEPTASL 170
|
.
gi 658756163 516 D 516
Cdd:PRK09536 171 D 171
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-551 |
1.53e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.92 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 345 ISSININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCL---------------LGFHPQVIEQISINn 409
Cdd:PRK14258 5 IPAIKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelesevrvegrVEFFNQNIYERRVN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 410 kpldatsMSTLQNAIAWIPQTPTLFYQSISDNIKIA------KPaatQLELEQAAHQA-GALDFINTLENGfdtlIGEQG 482
Cdd:PRK14258 83 -------LNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRP---KLEIDDIVESAlKDADLWDEIKHK----IHKSA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658756163 483 EGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS----QTEQLIQqaiNKYAKNHLVLVI-AHRLNTVKNASN 551
Cdd:PRK14258 149 LDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPiasmKVESLIQ---SLRLRSELTMVIvSHNLHQVSRLSD 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
347-572 |
1.70e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLNFTY----PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS----MS 418
Cdd:PRK13649 2 GINLQNVSYTYqagtPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 419 TLQNAIAWIPQTP--TLFYQSISDNIKIAKP--AATQLELEQAAHQAGALDFINtlENGFDTLIGEqgegLSGGQKQRIA 494
Cdd:PRK13649 82 QIRKKVGLVFQFPesQLFEETVLKDVAFGPQnfGVSQEEAEALAREKLALVGIS--ESLFEKNPFE----LSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 495 LARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLV-IAHRLNTVKN-ASNILVMQNGEIAQQGTYSQLEQQ 572
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
363-526 |
2.23e-14 |
|
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: 72.85 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 363 GIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLG-FHPQvieQISI----NNKPLDATSMSTLQ------NAIAW----- 426
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPD---SGSIlvrhDGGWVDLAQASPREilalrrRTIGYvsqfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 --IPQTPTLfyqsisdNIkIAKPA-ATQLELEQAAHQAGA-LDFINTLENGFD----TLigeqgeglSGGQKQRIALARA 498
Cdd:COG4778 103 rvIPRVSAL-------DV-VAEPLlERGVDREEARARARElLARLNLPERLWDlppaTF--------SGGEQQRVNIARG 166
|
170 180 190
....*....|....*....|....*....|..
gi 658756163 499 FLKQAPILVLDEPTAHLDSQTEQ----LIQQA 526
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAvvveLIEEA 198
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
348-565 |
2.58e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 72.72 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPqvIE--QISINNKPLDA--TSMSTLQNA 423
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE--PDsgTITVDGEDLTDskKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 IAWIPQTPTLF-YQSISDNI--------KIAKPAATQL---ELEQA--AHQAGALDfintlengfdtligEQgegLSGGQ 489
Cdd:COG1126 79 VGMVFQQFNLFpHLTVLENVtlapikvkKMSKAEAEERameLLERVglADKADAYP--------------AQ---LSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 490 KQRIALARAfLKQAP-ILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIA-HRLNTVKNASN-ILVMQNGEIAQQGT 565
Cdd:COG1126 142 QQRVAIARA-LAMEPkVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVtHEMGFAREVADrVVFMDGGRIVEEGP 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
348-564 |
3.00e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 71.93 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSmstlQNAIAWI 427
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLFY-QSISDNIK-IAKPAAtqLELEQAAHQAgaLDFINTLEngfdtlIGEQG----EGLSGGQKQRIALARAFLK 501
Cdd:cd03269 76 PEERGLYPkMKVIDQLVyLAQLKG--LKKEEARRRI--DEWLERLE------LSEYAnkrvEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 502 QAPILVLDEPTAHLDSQTEQLIQQAINKYA-KNHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQG 564
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
348-564 |
5.65e-14 |
|
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: 72.04 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVI-EQISINNKPLDATSMSTLQNAIAW 426
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYgNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IpqTPTL---FYQSIS----------DNIKI-AKPAATQLEL-EQAAHQAGALDFINTLengFDTLigeqgeglSGGQKQ 491
Cdd:COG1119 83 V--SPALqlrFPRDETvldvvlsgffDSIGLyREPTDEQRERaRELLELLGLAHLADRP---FGTL--------SQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 492 RIALARAFLKQAPILVLDEPTAHLD-SQTEQLIqQAINKYAKN---HLVLViAHRLNTVKNA-SNILVMQNGEIAQQG 564
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDlGARELLL-ALLDKLAAEgapTLVLV-THHVEEIPPGiTHVLLLKDGRVVAAG 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
364-559 |
5.87e-14 |
|
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: 74.48 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVI--EQISINNKPLDATSMS-TLQNAIAWIPQTPTLFYQ-SIS 439
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 440 DNI----KIAKPAAtQLELEQAAHQAGALDFINTLENGFDTL-IGEQGeglsGGQKQRIALARAFLKQAPILVLDEPTAH 514
Cdd:TIGR02633 97 ENIflgnEITLPGG-RMAYNAMYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658756163 515 L-DSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASN-ILVMQNGE 559
Cdd:TIGR02633 172 LtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDtICVIRDGQ 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
366-565 |
6.18e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.94 E-value: 6.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 366 NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS---------MSTLQNAiawipqtpTLFYQ 436
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqiarmgvVRTFQHV--------RLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 437 -SISDNIKIAK---------------PAATQLE---LEQAAHQagaLDFINTLEngfdtLIGEQGEGLSGGQKQRIALAR 497
Cdd:PRK11300 95 mTVIENLLVAQhqqlktglfsgllktPAFRRAEseaLDRAATW---LERVGLLE-----HANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 498 AFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKNASN-ILVMQNGEIAQQGT 565
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDrIYVVNQGTPLANGT 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
364-565 |
8.48e-14 |
|
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: 71.11 E-value: 8.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdaTSMSTLQNAIAWIPQTPTLF-YQSISDNI 442
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 443 ----KIAKPAATqlELEQAAHQAgaLDFINtLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQ 518
Cdd:cd03300 94 afglRLKKLPKA--EIKERVAEA--LDLVQ-LEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658756163 519 TEQLIQQAINKYAKN---HLVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:cd03300 165 LRKDMQLELKRLQKElgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
364-564 |
1.25e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.89 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLlgfhpQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFYQSISdnik 443
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-----NKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQFY---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 444 iAKPAATQLE-------------LEQAAHQAGALDFINTLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDE 510
Cdd:PRK09493 88 -LFPHLTALEnvmfgplrvrgasKEEAEKQARELLAKVGLAERAHHYPSE----LSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 511 PTAHLDSQTEQLIQQAINKYAKNHLVLVI-AHRLNTV-KNASNILVMQNGEIAQQG 564
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIvTHEIGFAeKVASRLIFIDKGRIAEDG 218
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
32-306 |
1.34e-13 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 71.69 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 32 LSIALGTFNAILMIAGAYLLAQTIHNVMFEGAslsqvTHFLWPLAGII----LLRALFLAISERLSAYAALKIKSAMRQT 107
Cdd:cd18542 3 LAILALLLATALNLLIPLLIRRIIDSVIGGGL-----RELLWLLALLIlgvaLLRGVFRYLQGYLAEKASQKVAYDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 108 LLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMI 187
Cdd:cd18542 78 LYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 188 LVGSKAEALNQKRWQQLAVL---------GNyffdRVqgltqLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFA 258
Cdd:cd18542 158 VFFKKVRPAFEEIREQEGELntvlqenltGV----RV-----VKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 658756163 259 LEFLATISVALVAVIIGF-----RLFFGTLDFATGFVVLLLapefyLPLRQLG 306
Cdd:cd18542 229 MDFLSGLQIVLVLWVGGYlvingEITLGELVAFISYLWMLI-----WPVRQLG 276
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
364-565 |
1.35e-13 |
|
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: 71.00 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQviEQISINNKPLDATSMSTLQNA--IAWIPQ-TPTLFYQSISD 440
Cdd:TIGR03873 17 VDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRP--DAGTVDLAGVDLHGLSRRARArrVALVEQdSDTAVPLTVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 441 NIKIAKPAATQLELEQAAHQAGALDFINTlENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTE 520
Cdd:TIGR03873 95 VVALGRIPHRSLWAGDSPHDAAVVDRALA-RTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658756163 521 QLIQQAINKYAKNHLVLVIA-HRLN-TVKNASNILVMQNGEIAQQGT 565
Cdd:TIGR03873 174 LETLALVRELAATGVTVVAAlHDLNlAASYCDHVVVLDGGRVVAAGP 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
348-570 |
1.48e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEG-----IKNINLTLPAKGLVAVVGASGSGKSTL---FDCLLgfHPQVIEQISINNKPLDATSMST 419
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklaLDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL--IPSEGKVYVDGLDTSDEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 420 LQNAIAWIPQTP------TLFYQSIS---DNIKIaKPAATQLELEQAAHQAGALDFINtlengfdtligEQGEGLSGGQK 490
Cdd:PRK13633 83 IRNKAGMVFQNPdnqivaTIVEEDVAfgpENLGI-PPEEIRERVDESLKKVGMYEYRR-----------HAPHLLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 491 QRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKNASNILVMQNGEIAQQGT--- 565
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTpke 230
|
....*.
gi 658756163 566 -YSQLE 570
Cdd:PRK13633 231 iFKEVE 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
379-565 |
1.55e-13 |
|
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: 71.76 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 379 VVGASGSGKSTLFDCLLGFhpqviEQISINNKPLDATSMSTL---QNAIAWIPQTPTLF-YQSISDNI----KIAK-PAA 449
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF-----EQPDSGSIMLDGEDVTNVpphLRHINMVFQSYALFpHMTVEENVafglKMRKvPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 450 tqlelEQAAHQAGALDFINtLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQ---A 526
Cdd:TIGR01187 76 -----EIKPRVLEALRLVQ-LEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLelkT 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 658756163 527 INKYAKNHLVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
348-562 |
1.59e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.08 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWI 427
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLFYQSISDNIKIAKPAATQLELE--QAAHQAgaldfinTLENGFDTLIgeqgeGLSGGQKQRIALARAFLKQAPI 505
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKPANPALVEKWLErlKMAHKL-------ELEDGRISNL-----KLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 506 LVLDEPTAHLDSQTEQLIQQAINKY--AKNHLVLVIAHRLNTVKNASNILVMQNGEIAQ 562
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLlqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
347-573 |
2.19e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 347 SININNLnftypnSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMST-LQNAIA 425
Cdd:PRK10762 257 RLKVDNL------SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPT----LFYQSISDNIKIAkpAATQL-----ELEQAAHQAGALDFI---NTLENGFDTLIGEqgegLSGGQKQRI 493
Cdd:PRK10762 331 YISEDRKrdglVLGMSVKENMSLT--ALRYFsraggSLKHADEQQAVSDFIrlfNIKTPSMEQAIGL----LSGGNQQKV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 494 ALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHRLNTVKNASN-ILVMQNGEIAQQGTYSQLEQ 571
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLsIILVSSEMPEVLGMSDrILVMHEGRISGEFTREQATQ 484
|
..
gi 658756163 572 QQ 573
Cdd:PRK10762 485 EK 486
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
348-565 |
2.23e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.81 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTY----PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDA-----TSMS 418
Cdd:PRK13645 7 IILDNVSYTYakktPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 419 TLQNAIAWIPQTP--TLFYQSISDNIKIAkPAATQLELEQAAHQAGALDFINTLENGFdtlIGEQGEGLSGGQKQRIALA 496
Cdd:PRK13645 87 RLRKEIGLVFQFPeyQLFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 497 RAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTV-KNASNILVMQNGEIAQQGT 565
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYkkRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
348-542 |
2.58e-13 |
|
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: 67.95 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISinnKPLDATSMstlqnaiaWI 427
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---MPEGEDLL--------FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLfyqsisdnikiakPAATqleLEQAahqagaldfintlengfdtLIGEQGEGLSGGQKQRIALARAFLKQAPILV 507
Cdd:cd03223 70 PQRPYL-------------PLGT---LREQ-------------------LIYPWDDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*..
gi 658756163 508 LDEPTAHLDSQTEQLIQQAINKyaknHLVLVI--AHR 542
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKE----LGITVIsvGHR 147
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
348-573 |
2.80e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWI 427
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTP--TLFYQSISDNIKIAkPAATQLELEQAAHQAG-ALDFINTLEngfdtLIGEQGEGLSGGQKQRIALARAFLKQAP 504
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFG-PVNMGLDKDEVERRVEeALKAVRMWD-----FRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 505 ILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIA-HRLNTVKN-ASNILVMQNGEIAQQGTYSQLEQQQ 573
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
332-571 |
3.47e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.82 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 332 EQSQQHETKFEehissinINNLNFTYPNSNEgIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKP 411
Cdd:PRK10575 3 EYTNHSDTTFA-------LRNVSFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 412 LDATSMSTLQNAIAWIPQT-PTLFYQSISDNIKIAK----------PAATQLELEQAAHQAGALDFINTLEngfdtlige 480
Cdd:PRK10575 75 LESWSSKAFARKVAYLPQQlPAAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLV--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 481 qgEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIA--HRLNTVKNASNILV-MQN 557
Cdd:PRK10575 146 --DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINMAARYCDYLVaLRG 223
|
250
....*....|....
gi 658756163 558 GEIAQQGTYSQLEQ 571
Cdd:PRK10575 224 GEMIAQGTPAELMR 237
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
364-576 |
3.70e-13 |
|
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: 68.96 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdatSMSTLQNAIAWIPQTPTLFYQSISDNIK 443
Cdd:TIGR03740 16 VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW---TRKDLHKIGSLIESPPLYENLTARENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 444 IAkpaATQLELEQAAHQAgALDFINtLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLI 523
Cdd:TIGR03740 93 VH---TTLLGLPDSRIDE-VLNIVD-LTNTGKKKAKQ----FSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQEL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 524 QQAINKYAKNHLVLVI-AHRLNTVKN-ASNILVMQNGEIAQQGTYSQLEQQQGAF 576
Cdd:TIGR03740 164 RELIRSFPEQGITVILsSHILSEVQQlADHIGIISEGVLGYQGKINKSENLEKLF 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
348-565 |
3.84e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.99 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGI---KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNA- 423
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 --IAWIPQ------TPTLFyqsisDNI------------KIAKPAATQLELEQAAHQAgaldfintlengfDTLIGEqge 483
Cdd:PRK11153 82 rqIGMIFQhfnllsSRTVF-----DNValplelagtpkaEIKARVTELLELVGLSDKA-------------DRYPAQ--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 484 gLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQ---AINKyaKNHL-VLVIAHRLNTVKN-ASNILVMQNG 558
Cdd:PRK11153 141 -LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILEllkDINR--ELGLtIVLITHEMDVVKRiCDRVAVIDAG 217
|
....*..
gi 658756163 559 EIAQQGT 565
Cdd:PRK11153 218 RLVEQGT 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
345-569 |
4.00e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.39 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 345 ISSININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCL-LGFHPQV----IEQISIN-NKPLDATS-- 416
Cdd:PRK11264 1 MSAIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPEAgtirVGDITIDtARSLSQQKgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 417 MSTLQNAIAWIPQTPTLF-YQSISDNIkIAKPAATQLELEQAAHQAG----ALDFINTLENGFDtligeqgEGLSGGQKQ 491
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFpHRTVLENI-IEGPVIVKGEPKEEATARArellAKVGLAGKETSYP-------RRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 492 RIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVI-AHRLNTVKNASN-ILVMQNGEIAQQGTYSQL 569
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARDVADrAIFMDQGRIVEQGPAKAL 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
365-565 |
4.78e-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: 71.64 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 365 KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQviE-QISINNKPLDATS---MSTLQNAIAWIPQTPtlfY----- 435
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS--EgEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP---Fgslsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 436 -----QSISDNIKIAKPAATQLELEQAAhqAGALDFINTLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDE 510
Cdd:COG4172 378 rmtvgQIIAEGLRVHGPGLSAAERRARV--AEALEEVGLDPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 511 PTAHLD----SQTEQLIQQAINKYaknHLV-LVIAHRLNTVKN-ASNILVMQNGEIAQQGT 565
Cdd:COG4172 452 PTSALDvsvqAQILDLLRDLQREH---GLAyLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
329-586 |
5.49e-13 |
|
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: 72.35 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 329 PLPEQSQQ-------HETKFE-EH---ISSININNLNFTY-PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLG 396
Cdd:TIGR01257 899 PLTEEMEDpehpegiNDSFFErELpglVPGVCVKNLVKIFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTG 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 397 FHPQVIEQISINNKPLDaTSMSTLQNAIAWIPQTPTLFYqsisdNIKIAKPAATQLELEQAAHQAGALDFINTLEN-GFD 475
Cdd:TIGR01257 979 LLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFH-----HLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDtGLH 1052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 476 TLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASN-ILV 554
Cdd:TIGR01257 1053 HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDrIAI 1132
|
250 260 270
....*....|....*....|....*....|....*...
gi 658756163 555 MQNGEIAQQGTYSQLEQQQGA------FKSLLNLQAQG 586
Cdd:TIGR01257 1133 ISQGRLYCSGTPLFLKNCFGTgfyltlVRKMKNIQSQR 1170
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
366-569 |
6.11e-13 |
|
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: 69.06 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 366 NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKP---LDATSMSTLQNAIAWIPQ-TPTLFYQSISDN 441
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDlyqLDRKQRRAFRRDVQLVFQdSPSAVNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 442 IKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEgLSGGQKQRIALARAFLKQAPILVLDEPTAHLD----- 516
Cdd:TIGR02769 109 QIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ-LSGGQLQRINIARALAVKPKLIVLDEAVSNLDmvlqa 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 517 ---SQTEQLIQQAINKYaknhlvLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQL 569
Cdd:TIGR02769 188 vilELLRKLQQAFGTAY------LFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQL 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
359-561 |
6.62e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 359 NSNEGIKNINLTLpAKG-LVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS-MSTLQNAIAWIP---QTPTL 433
Cdd:COG1129 263 SVGGVVRDVSFSV-RAGeILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPedrKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 434 F-YQSISDNIKIAKPAA--------TQLELEQAAHQAGALDfINTleNGFDTLIGEqgegLSGGQKQRIALARAFLKQAP 504
Cdd:COG1129 342 VlDLSIRENITLASLDRlsrgglldRRRERALAEEYIKRLR-IKT--PSPEQPVGN----LSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 505 ILVLDEPTAHLD--SQTEqlIQQAINKYAKNHL-VLVI----------AHRlntvknasnILVMQNGEIA 561
Cdd:COG1129 415 VLILDEPTRGIDvgAKAE--IYRLIRELAAEGKaVIVIsselpellglSDR---------ILVMREGRIV 473
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
348-569 |
6.78e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.84 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINN-------------KPLDA 414
Cdd:PRK10619 6 LNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 415 TSMSTLQNAIAWIPQTPTLF-YQSISDNIKIAkPAATqLELEQAAHQAGALDFINTLEngfdtlIGEQGEG-----LSGG 488
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWsHMTVLENVMEA-PIQV-LGLSKQEARERAVKYLAKVG------IDERAQGkypvhLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 489 QKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKN-HLVLVIAHRLNTVKNASN-ILVMQNGEIAQQGTY 566
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAP 236
|
...
gi 658756163 567 SQL 569
Cdd:PRK10619 237 EQL 239
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
364-541 |
8.50e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINnkpldatsmstlqnaiawIPQTPtlFYQ--SISDN 441
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQ--FGReaSLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 442 IKIAKPAATQLELeqaAHQAGALDFINTLENgFDTLigeqgeglSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQ 521
Cdd:COG2401 106 IGRKGDFKDAVEL---LNAVGLSDAVLWLRR-FKEL--------STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180
....*....|....*....|...
gi 658756163 522 LIQQAINKYAKNH---LVLVIAH 541
Cdd:COG2401 174 RVARNLQKLARRAgitLVVATHH 196
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
348-541 |
1.32e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.19 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSnEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMS---TLQNAi 424
Cdd:PRK11248 2 LQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvVFQNE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 425 AWIPqtptlfYQSISDNIKIAKPAA--TQLELEQAAHQAGALDFINTLENGFdtlIGEqgegLSGGQKQRIALARAFLKQ 502
Cdd:PRK11248 80 GLLP------WRNVQDNVAFGLQLAgvEKMQRLEIAHQMLKKVGLEGAEKRY---IWQ----LSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 658756163 503 APILVLDEPTAHLDS----QTEQLIQQAINKYAKNhlVLVIAH 541
Cdd:PRK11248 147 PQLLLLDEPFGALDAftreQMQTLLLKLWQETGKQ--VLLITH 187
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
359-564 |
1.50e-12 |
|
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: 66.78 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 359 NSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIpqtpTLFYQSi 438
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDLPPEERARLGI----FLAFQY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 439 sdniKIAKPAATQLELeqaahqagaLDFINtlengfdtligeqgEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQ 518
Cdd:cd03217 86 ----PPEIPGVKNADF---------LRYVN--------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658756163 519 TEQLIQQAINKYA-KNHLVLVIAHR---LNTVKnASNILVMQNGEIAQQG 564
Cdd:cd03217 139 ALRLVAEVINKLReEGKSVLIITHYqrlLDYIK-PDRVHVLYDGRIVKSG 187
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
365-527 |
1.71e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 365 KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTL------QNAIawipqTPTLfyqSI 438
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNAM-----KPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 439 SDNIKIAKPAATQLELEQAAhqagALDFIntlenGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQ 518
Cdd:PRK13539 91 AENLEFWAAFLGGEELDIAA----ALEAV-----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
....*....
gi 658756163 519 TEQLIQQAI 527
Cdd:PRK13539 162 AVALFAELI 170
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
346-569 |
2.27e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.83 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYPNSNEG--IKNINLTLPAKGLVAVVGASGSGKST---LFDCLLgfhpqVIE--QISINNKPLDATSMS 418
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEKytLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL-----EAEsgQIIIDGDLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 419 TLQNAIAWIPQTP--TLFYQSISDNIkiakpaATQLELEQAAHQA------GALDFINTLEngFDTligEQGEGLSGGQK 490
Cdd:PRK13650 78 DIRHKIGMVFQNPdnQFVGATVEDDV------AFGLENKGIPHEEmkervnEALELVGMQD--FKE---REPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 491 QRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKNASNILVMQNGEIAQQGTYSQ 568
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
.
gi 658756163 569 L 569
Cdd:PRK13650 227 L 227
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
345-565 |
2.96e-12 |
|
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: 67.25 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 345 ISSININNLnftypnsnegiKNINLTLPAKGLVAVVGASGSGKSTLFDCLLgfHPqVIEQISINNK--PLDATSMSTLQN 422
Cdd:cd03271 3 LKGARENNL-----------KNIDVDIPLGVLTCVTGVSGSGKSSLINDTL--YP-ALARRLHLKKeqPGNHDRIEGLEH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 423 aIAW---IPQTPT--------LFYQSISDNIKI---------------------AKPAATQLEL--EQA----AHQAGAL 464
Cdd:cd03271 69 -IDKvivIDQSPIgrtprsnpATYTGVFDEIRElfcevckgkrynretlevrykGKSIADVLDMtvEEAleffENIPKIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 465 DFINTLEN-GFDTL-IGEQGEGLSGGQKQRIALARAFLKQAP---ILVLDEPTAHLDSQTEQLIQQAINKY-AKNHLVLV 538
Cdd:cd03271 148 RKLQTLCDvGLGYIkLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVV 227
|
250 260 270
....*....|....*....|....*....|...
gi 658756163 539 IAHRLNTVKNASNILVM------QNGEIAQQGT 565
Cdd:cd03271 228 IEHNLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
376-565 |
3.76e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.66 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 376 LVAVVGASGSGKSTLFDCLLG-FHPQV----IEQISINNKP--LDATSMSTLQNAIAWIPQTptlFYQSISDNIKIAKPa 448
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGvLKPDEgdieIELDTVSYKPqyIKADYEGTVRDLLSSITKD---FYTHPYFKTEIAKP- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 449 atqLELEQaahqagaldfintlengfdtLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAIN 528
Cdd:cd03237 103 ---LQIEQ--------------------ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 658756163 529 KYAKNH--LVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:cd03237 160 RFAENNekTAFVVEHDIIMIDYLADRLIVFEGEPSVNGV 198
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
348-573 |
4.57e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.57 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGF-----HPQVIEQISINNKPLDATSMSTLQN 422
Cdd:PRK09984 5 IRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdkSAGSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 423 AIAwipQTPTLFYQ-------SISDNIKIAKPAATQL--------ELEQAAHQAGALDFIntlenGFDTLIGEQGEGLSG 487
Cdd:PRK09984 84 SRA---NTGYIFQQfnlvnrlSVLENVLIGALGSTPFwrtcfswfTREQKQRALQALTRV-----GMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 488 GQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLN-TVKNASNILVMQNGEIAQQG 564
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
|
....*....
gi 658756163 565 TYSQLEQQQ 573
Cdd:PRK09984 236 SSQQFDNER 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
360-565 |
4.94e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.99 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 360 SNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLD---ATSMSTLQN-AIAWIPQtptlFY 435
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklsSAAKAELRNqKLGFIYQ----FH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 436 QSISDNIKIAKPAATQL--ELEQAAHQAGALDFINTLenGFDTLIGEQGEGLSGGQKQRIALARAfLKQAPILVL-DEPT 512
Cdd:PRK11629 97 HLLPDFTALENVAMPLLigKKKPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARA-LVNNPRLVLaDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 513 AHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
376-569 |
5.22e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 376 LVAVVGASGSGKSTLFDCLLGFHP---QVIEQISINNKPLDATSMST----LQNAIAWIPQTPTLFYQSISDNIKIAKPA 448
Cdd:TIGR00955 53 LLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKEMRAisayVQQDDLFIPTLTVREHLMFQAHLRMPRRV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 449 AT---QLELEQAAHQAGaldfintLENGFDTLIGEQG--EGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLI 523
Cdd:TIGR00955 133 TKkekRERVDEVLQALG-------LRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658756163 524 QQAINKYA-KNHLVLVIAHRLNT--VKNASNILVMQNGEIAQQGTYSQL 569
Cdd:TIGR00955 206 VQVLKGLAqKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
364-565 |
6.36e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.69 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQ-----VIEQISINNKPLDATSmstlQNAIAWIPQTPTLFYQ-S 437
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRdagniIIDDEDISLLPLHARA----RRGIGYLPQEASIFRRlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 438 ISDNIKIAKPAATQLELEQAAHQAGAL--DF-INTLENGFdtligeqGEGLSGGQKQRIALARAFLKQAPILVLDEPTAH 514
Cdd:PRK10895 95 VYDNLMAVLQIRDDLSAEQREDRANELmeEFhIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658756163 515 LDSQTEQLIQQAINKYAKNHL-VLVIAHRL-NTVKNASNILVMQNGEIAQQGT 565
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLgVLITDHNVrETLAVCERAYIVSQGHLIAHGT 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
362-565 |
6.59e-12 |
|
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: 67.91 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 362 EGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLG---FHP---QVIEQISINNK------------------------- 410
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPtsgRIIYHVALCEKcgyverpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 411 ----PLDATSMSTLQNAIAWIPQTPTLFY--QSISDNIKIAkpaatqleLEQAAHQAG-----ALDFINTLEngFDTLIG 479
Cdd:TIGR03269 94 vdfwNLSDKLRRRIRKRIAIMLQRTFALYgdDTVLDNVLEA--------LEEIGYEGKeavgrAVDLIEMVQ--LSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 480 EQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH-LVLVIAHRLNTV--KNASNILVMQ 556
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHWPEVieDLSDKAIWLE 243
|
....*....
gi 658756163 557 NGEIAQQGT 565
Cdd:TIGR03269 244 NGEIKEEGT 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
348-564 |
6.82e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYP----------NSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEqISINNKPLDATS- 416
Cdd:PRK15134 276 LDVEQLQVAFPirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGE-IWFDGQPLHNLNr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 417 --MSTLQNAIAWIPQTPTL-------FYQSISDNIKIAKPAATQLELEQAAHQAGAldfintlENGFDTLIGEQGEG-LS 486
Cdd:PRK15134 355 rqLLPVRHRIQVVFQDPNSslnprlnVLQIIEEGLRVHQPTLSAAQREQQVIAVME-------EVGLDPETRHRYPAeFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 487 GGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLV--LVIAHRLNTVKN-ASNILVMQNGEIAQQ 563
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQ 507
|
.
gi 658756163 564 G 564
Cdd:PRK15134 508 G 508
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
270-533 |
9.22e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 270 VAVIIGFRLFFgtldfatgFVVLLLAPEFYLPLRQLGS---------HYHARLQGISAA------ADMVTILNAPLPEQS 334
Cdd:TIGR00956 672 FGIIIGFTVFF--------FFVYILLTEFNKGAKQKGEilvfrrgslKRAKKAGETSASnkndieAGEVLGSTDLTDESD 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 335 QQHETKFEEHISSINI---NNLNFTYPNSNEG---IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLG-FHPQVIEQ--I 405
Cdd:TIGR00956 744 DVNDEKDMEKESGEDIfhwRNLTYEVKIKKEKrviLNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErVTTGVITGgdR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 406 SINNKPLDatsmSTLQNAIAWIPQTPTLFYQSisdNIKIAKPAATQLELEQAAHQAGALDFINT------LENGFDTLIG 479
Cdd:TIGR00956 824 LVNGRPLD----SSFQRSIGYVQQQDLHLPTS---TVRESLRFSAYLRQPKSVSKSEKMEYVEEviklleMESYADAVVG 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 480 EQGEGLSGGQKQRIALARAFL-KQAPILVLDEPTAHLDSQTEQLIQQAINKYAKN 533
Cdd:TIGR00956 897 VPGEGLNVEQRKRLTIGVELVaKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADH 951
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
351-573 |
1.17e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 351 NNLNFTYPNSNEGIKNINLT-LP-AKglVAVVGASGSGKSTLFDCLLGfhpqvIEQISINnkplDATSMSTLQnaIAWIP 428
Cdd:PRK11819 10 NRVSKVVPPKKQILKDISLSfFPgAK--IGVLGLNGAGKSTLLRIMAG-----VDKEFEG----EARPAPGIK--VGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 429 QTPTLfyqsisdnikiaKPAATQLE-LEQA-AHQAGALDFINTL-------ENGFDTLIGEQGE---------------- 483
Cdd:PRK11819 77 QEPQL------------DPEKTVREnVEEGvAEVKAALDRFNEIyaayaepDADFDALAAEQGElqeiidaadawdldsq 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 484 ------------------GLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNhlVLVIAH-R-- 542
Cdd:PRK11819 145 leiamdalrcppwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGT--VVAVTHdRyf 222
|
250 260 270
....*....|....*....|....*....|...
gi 658756163 543 LNTVknASNILVMQNGE-IAQQGTYSQ-LEQQQ 573
Cdd:PRK11819 223 LDNV--AGWILELDRGRgIPWEGNYSSwLEQKA 253
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
348-578 |
1.25e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.53 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTY-PNS---NEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATS----MST 419
Cdd:PRK13643 2 IKFEKVNYTYqPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 420 LQNAIAWIPQTP--TLFYQSI-------SDNIKIAKPAATQLELEQAAHQAGALDFINtlENGFDtligeqgegLSGGQK 490
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVlkdvafgPQNFGIPKEKAEKIAAEKLEMVGLADEFWE--KSPFE---------LSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 491 QRIALARAFLKQAPILVLDEPTAHLDSQTE-QLIQQAINKYAKNHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQ 568
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
250
....*....|
gi 658756163 569 LEQQQGAFKS 578
Cdd:PRK13643 231 VFQEVDFLKA 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
365-559 |
1.33e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.97 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 365 KNINLTLpAKGLV-AVVGASGSGKSTLFDCLLGFHP----QVI---EQISINNkPLDAtsmstLQNAIAWIPQTPTLF-Y 435
Cdd:COG3845 22 DDVSLTV-RPGEIhALLGENGAGKSTLMKILYGLYQpdsgEILidgKPVRIRS-PRDA-----IALGIGMVHQHFMLVpN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 436 QSISDNIKIA--KPAATQLELEQAAHQAGAL--DFintlenGF----DTLIGEqgegLSGGQKQRIALARAFLKQAPILV 507
Cdd:COG3845 95 LTVAENIVLGlePTKGGRLDRKAARARIRELseRY------GLdvdpDAKVED----LSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 508 LDEPTAHLDSQ-TEQLIqQAINKYAKNHL-VLVIAHRLNTVKNASN-ILVMQNGE 559
Cdd:COG3845 165 LDEPTAVLTPQeADELF-EILRRLAAEGKsIIFITHKLREVMAIADrVTVLRRGK 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
365-564 |
1.35e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.21 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 365 KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvIEQISINNKPLDATSMSTLQNA---IAWIPQTPTLF-YQSISD 440
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-----LEDITSGDLFIGEKRMNDVPPAergVGMVFQSYALYpHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 441 N----IKIAKpaATQLELEQAAHQAGAldfinTLEngFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLD 516
Cdd:PRK11000 95 NmsfgLKLAG--AKKEEINQRVNQVAE-----VLQ--LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658756163 517 SQTEQLIQQAINKYAKN---HLVLVIAHRLNTVKNASNILVMQNGEIAQQG 564
Cdd:PRK11000 166 AALRVQMRIEISRLHKRlgrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
363-569 |
1.41e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.60 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 363 GIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINN----KPLDATSMSTLQNAIAWIPQTPTLF-YQS 437
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiaKISDAELREVRRKKIAMVFQSFALMpHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 438 ISDNIKIAKPAATqleLEQAAHQAGALDFINTLenGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS 517
Cdd:PRK10070 123 VLDNTAFGMELAG---INAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 518 QTEQLIQQAINKYAKNH--LVLVIAHRLN-TVKNASNILVMQNGEIAQQGTYSQL 569
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHqrTIVFISHDLDeAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
355-569 |
3.10e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.11 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 355 FTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQ-----NAIAWIPQ 429
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK--DLLGMKDDEwravrSDIQMIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 430 TP-------TLFYQSISDNIKIAKPAATQLELEQAAHQAgaLDFINTLENgfdtLIGEQGEGLSGGQKQRIALARAFLKQ 502
Cdd:PRK15079 106 DPlaslnprMTIGEIIAEPLRTYHPKLSRQEVKDRVKAM--MLKVGLLPN----LINRYPHEFSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 503 APILVLDEPTAHLD----SQTEQLIQQaINKYAKNHLVLvIAHRLNTVKNASN-ILVMQNGEIAQQGTYSQL 569
Cdd:PRK15079 180 PKLIICDEPVSALDvsiqAQVVNLLQQ-LQREMGLSLIF-IAHDLAVVKHISDrVLVMYLGHAVELGTYDEV 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
354-573 |
4.40e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 354 NFT-YPNSNEGIK---NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIE-QISINNKPLD-ATSMSTLQNAIAWI 427
Cdd:PRK13549 264 NLTaWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEgEIFIDGKPVKiRNPQQAIAQGIAMV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQ-------TPTLfyqSISDNIKIA--KPAATQLELEQAAHQAGALDFINTLEngFDTLIGEQGEG-LSGGQKQRIALAR 497
Cdd:PRK13549 344 PEdrkrdgiVPVM---GVGKNITLAalDRFTGGSRIDDAAELKTILESIQRLK--VKTASPELAIArLSGGNQQKAVLAK 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 498 AFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHRLNTVKNASN-ILVMQNGEIAQQGTYSQLEQQQ 573
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVaIIVISSELPEVLGLSDrVLVMHEGKLKGDLINHNLTQEQ 496
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
364-573 |
6.10e-11 |
|
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: 64.85 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIE-QISINNKPLDA-TSMSTLQNAIAWIPQ-------TPTLf 434
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEgNVFINGKPVDIrNPAQAIRAGIAMVPEdrkrhgiVPIL- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 435 yqSISDNIKIA--KPAATQLELEQAAHQAGALDFINTLE---NGFDTLIGeqgeGLSGGQKQRIALARAFLKQAPILVLD 509
Cdd:TIGR02633 355 --GVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKvktASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 510 EPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHRLNTVKNASN-ILVMQNGEIAQQGTYSQLEQQQ 573
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVaIIVVSSELAEVLGLSDrVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
364-569 |
6.47e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAW------IPQTPTLFYQS 437
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFrrrvgmLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 438 ISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS 517
Cdd:PRK14271 117 IMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658756163 518 QTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASN-ILVMQNGEIAQQGTYSQL 569
Cdd:PRK14271 197 TTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDrAALFFDGRLVEEGPTEQL 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
377-519 |
7.22e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.49 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdaTSMSTLQNA------IAWIPQT----PTLfyqSISDNIKIak 446
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL--HQMDEEARAklrakhVGFVFQSfmliPTL---NALENVEL-- 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 447 PAATQLELEQAAHQaGALDFINTLenGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQT 519
Cdd:PRK10584 112 PALLRGESSRQSRN-GAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
350-586 |
8.34e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.73 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYPNSNEG---IKNINLTLPAKGLVAVVGASGSGKS-TLFDC--LLGFHPQVIEQ--ISINNKPLDATSMSTLQ 421
Cdd:PRK15134 8 IENLSVAFRQQQTVrtvVNDVSLQIEAGETLALVGESGSGKSvTALSIlrLLPSPPVVYPSgdIRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 422 ----NAIAWIPQTPTLfyqSISDNIKIAKPAATQLELEQAA-HQAGALDFINTLENgfdtlIG-EQGEG--------LSG 487
Cdd:PRK15134 88 gvrgNKIAMIFQEPMV---SLNPLHTLEKQLYEVLSLHRGMrREAARGEILNCLDR-----VGiRQAAKrltdyphqLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 488 GQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAIN--KYAKNHLVLVIAHRLNTVKN-ASNILVMQNGEIAQQG 564
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQN 239
|
250 260
....*....|....*....|....
gi 658756163 565 TYSQL--EQQQGAFKSLLNLQAQG 586
Cdd:PRK15134 240 RAATLfsAPTHPYTQKLLNSEPSG 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
364-560 |
8.48e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKP---LDATSMSTLQNAIAWIPQ-TPTLFYQSIS 439
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlakLNRAQRKAFRRDIQMVFQdSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 440 DNIKIAKPAATQLELEQAAHQAGALDFINTLENGfDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLD--- 516
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLARASEMLRAVDLD-DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvl 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658756163 517 -----SQTEQLIQQAINKYaknhlvLVIAHRLNTVKN-ASNILVMQNGEI 560
Cdd:PRK10419 187 qagviRLLKKLQQQFGTAC------LFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
32-283 |
1.16e-10 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 62.81 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 32 LSIALGTFNAILMIAGAYLLAQTIHNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTK 111
Cdd:cd18541 3 LGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 112 LTHLGPSYIEQHGQG-----ATlntvHDgVEALHDYYAkylPGVAYSA---LIPLAILVVIFPTDYKAGLIFLLTAPLIP 183
Cdd:cd18541 83 LLTLSPSFYQKNRTGdlmarAT----ND-LNAVRMALG---PGILYLVdalFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 184 FFMILVGSKAEALNQKRWQQLAVLgnyfFDRVQ----GLTQLKLFNATQQELKQIAKISDDFRHATLGVLKI-AFLSSFa 258
Cdd:cd18541 155 LLVYRLGKKIHKRFRKVQEAFSDL----SDRVQesfsGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVdALFFPL- 229
|
250 260
....*....|....*....|....*
gi 658756163 259 LEFLATISVALVAVIIGFRLFFGTL 283
Cdd:cd18541 230 IGLLIGLSFLIVLWYGGRLVIRGTI 254
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
373-565 |
1.26e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 373 AKGLVAVVGASGSGKSTLFDCLLGFHPQVIEqISINNKPLDATSMSTLQNAIAWIPQtptlfyqsiSDNIKIAKPAATQL 452
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAGLLPGSGS-IQFAGQPLEAWSAAELARHRAYLSQ---------QQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 453 ELEQAA--HQAGALDFINTLEN--GFDTLIGEQGEGLSGGQKQRIALARAFLKQAP-------ILVLDEPTAHLDSQTEQ 521
Cdd:PRK03695 91 TLHQPDktRTEAVASALNEVAEalGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDVAQQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 658756163 522 LIQQAINKYAKNHL-VLVIAHRLN-TVKNASNILVMQNGEIAQQGT 565
Cdd:PRK03695 171 ALDRLLSELCQQGIaVVMSSHDLNhTLRHADRVWLLKQGKLLASGR 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
352-569 |
1.46e-10 |
|
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: 61.40 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 352 NLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNkpLDATSMSTLQNA---IAWIP 428
Cdd:cd03218 5 NLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG--QDITKLPMHKRArlgIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 429 QTPTLFYQ-SISDNIKIAKPAATQLELEQAAHQAGALDfintlENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILV 507
Cdd:cd03218 82 QEASIFRKlTVEENILAVLEIRGLSKKEREEKLEELLE-----EFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 508 LDEPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHrlntvkNASNIL-------VMQNGEIAQQGTYSQL 569
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDH------NVRETLsitdrayIIYEGKVLAEGTPEEI 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
348-569 |
1.57e-10 |
|
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: 61.23 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNkpLDATSMST-LQNAIAW 426
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPReVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFYQ-SISDNIKI-AK----PAAtqlELEQAAHQAgaLDFINTLENGfDTLIGEqgegLSGGQKQRIALARAFL 500
Cdd:cd03265 78 VFQDLSVDDElTGWENLYIhARlygvPGA---ERRERIDEL--LDFVGLLEAA-DRLVKT----YSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 501 KQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTV-KNASNILVMQNGEIAQQGTYSQL 569
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
348-565 |
1.73e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.04 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMSTLQNAIAWI 427
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PQTPTLF-YQSISDNI----KIAK-PAAtqlelEQAAHQAGALDFINtLENgfdtLIGEQGEGLSGGQKQRIALARAFLK 501
Cdd:PRK09452 92 FQSYALFpHMTVFENVafglRMQKtPAA-----EITPRVMEALRMVQ-LEE----FAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 502 QAPILVLDEPTAHLDSQTEQLIQQAInKYAKNHL----VLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNEL-KALQRKLgitfVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
366-564 |
2.00e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 366 NINLTLPAKGLVAVVGASGSGKSTLFDCLLGF-HPQVIEqISINNKPL-DA---TSMSTLQNAIAWIPQTPTLF-YQSIS 439
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLtRPQKGR-IVLNGRVLfDAekgICLPPEKRRIGYVFQDARLFpHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 440 DNIK--IAKPAATQLEleqaahqagalDFINTLenGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS 517
Cdd:PRK11144 95 GNLRygMAKSMVAQFD-----------KIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658756163 518 QTEQLIQQAINKYAK--NHLVLVIAHRLNTV-KNASNILVMQNGEIAQQG 564
Cdd:PRK11144 162 PRKRELLPYLERLAReiNIPILYVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
50-321 |
2.54e-10 |
|
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: 61.68 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 50 LLAQTIHNVMFEGASLSQVthfLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATL 129
Cdd:cd18551 20 LLVKNLIDALSAGGSSGGL---LALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 130 NTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGN 209
Cdd:cd18551 97 SRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 210 YFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKI-AFLSSFAlefLATISVALVAVII--GFRLFFGTLDFA 286
Cdd:cd18551 177 ALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIeALIGPLM---GLAVQLALLVVLGvgGARVASGALTVG 253
|
250 260 270
....*....|....*....|....*....|....*....
gi 658756163 287 T--GFVVLLlapeFYL--PLRQLGSHYhARLQGISAAAD 321
Cdd:cd18551 254 TlvAFLLYL----FQLitPLSQLSSFF-TQLQKALGALE 287
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
50-323 |
2.55e-10 |
|
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: 61.73 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 50 LLAQTIHNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATL 129
Cdd:cd18576 17 LLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 130 NTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGN 209
Cdd:cd18576 97 SRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 210 YFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKI-AFLSSFaLEFLATISVALVaVIIGFRLFF-GTLDFAT 287
Cdd:cd18576 177 IVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIrALFSSF-IIFLLFGAIVAV-LWYGGRLVLaGELTAGD 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 658756163 288 GFVVLLLAPEFYLPLRQLGSHYhARLQGISAAADMV 323
Cdd:cd18576 255 LVAFLLYTLFIAGSIGSLADLY-GQLQKALGASERV 289
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
473-564 |
2.98e-10 |
|
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: 60.46 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 473 GFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKY-AKNHLVLVIAHRLNTVKN-AS 550
Cdd:cd03266 125 GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERlCD 204
|
90
....*....|....
gi 658756163 551 NILVMQNGEIAQQG 564
Cdd:cd03266 205 RVVVLHRGRVVYEG 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
348-542 |
3.20e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLG-FHPQVIEqISINNKPLDaTSMSTLQNAIAW 426
Cdd:PRK13540 2 LDVIELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPEKGE-ILFERQSIK-KDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTptlfyQSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPIL 506
Cdd:PRK13540 79 VGHR-----SGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----LSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAINKY-AKNHLVLVIAHR 542
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHrAKGGAVLLTSHQ 186
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
350-565 |
3.70e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 350 INNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfHP--QVIE------QISINNkpLDATSMSTLQ 421
Cdd:CHL00131 10 IKNLHASV-NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPayKILEgdilfkGESILD--LEPEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 422 NAIAWipQTPtlfyqsisdnIKIakPAATQLELEQAA----HQAGALDFINTLEngFDTLIGEQ---------------G 482
Cdd:CHL00131 86 IFLAF--QYP----------IEI--PGVSNADFLRLAynskRKFQGLPELDPLE--FLEIINEKlklvgmdpsflsrnvN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 483 EGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYA-KNHLVLVIAH--RLNTVKNASNILVMQNGE 559
Cdd:CHL00131 150 EGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGK 229
|
....*.
gi 658756163 560 IAQQGT 565
Cdd:CHL00131 230 IIKTGD 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
331-564 |
4.31e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.13 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 331 PEQSQQHETKFEEHIssININNLNFTYPNSNEG----IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqVIEQIS 406
Cdd:TIGR03269 265 SEVEKECEVEVGEPI--IKVRNVSKRYISVDRGvvkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG----VLEPTS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 407 ------INNKPLDATSMSTLQNA-----IAWIPQTPTLF-YQSISDNIKiakpAATQLEL--EQAAHQAgaldfINTLEN 472
Cdd:TIGR03269 339 gevnvrVGDEWVDMTKPGPDGRGrakryIGILHQEYDLYpHRTVLDNLT----EAIGLELpdELARMKA-----VITLKM 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 473 -GFD-----TLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAK--NHLVLVIAHRLN 544
Cdd:TIGR03269 410 vGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMD 489
|
250 260
....*....|....*....|.
gi 658756163 545 TVKNASN-ILVMQNGEIAQQG 564
Cdd:TIGR03269 490 FVLDVCDrAALMRDGKIVKIG 510
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
352-558 |
4.41e-10 |
|
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: 59.18 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 352 NLNFTYPNSNEG---IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGF-HPQVIE-QISINNKPLDAtsmsTLQNAIAW 426
Cdd:cd03232 8 NLNYTVPVKGGKrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRkTAGVITgEILINGRPLDK----NFQRSTGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQTPTLFyqsisdnikiakPAATQLEleqaahqagALDFINTLengfdtligeqgEGLSGGQKQRIALARAFLKQAPIL 506
Cdd:cd03232 84 VEQQDVHS------------PNLTVRE---------ALRFSALL------------RGLSVEQRKRLTIGVELAAKPSIL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 507 VLDEPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHRLNTV--KNASNILVMQNG 558
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFLKKLADSGQaILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
378-565 |
4.60e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.13 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 378 AVVGASGSGKSTLFDCLlgfhpQVIE-----QISINNKPL---DATSMSTLQNAIAWIPQTPtlfYQSISDNIKI----A 445
Cdd:PRK11308 45 AVVGESGCGKSTLARLL-----TMIEtptggELYYQGQDLlkaDPEAQKLLRQKIQIVFQNP---YGSLNPRKKVgqilE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 446 KPAATQLELEQAAHQAGALDFINTLengfdtligeqgeGL------------SGGQKQRIALARAFLKQAPILVLDEPTA 513
Cdd:PRK11308 117 EPLLINTSLSAAERREKALAMMAKV-------------GLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 514 HLD----SQTEQL---IQQAIN-KYaknhlvLVIAHRLNTVKN-ASNILVMQNGEIAQQGT 565
Cdd:PRK11308 184 ALDvsvqAQVLNLmmdLQQELGlSY------VFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
364-558 |
5.02e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDA-TSMSTLQNAIAWIPQTPTLFYQ-SISDN 441
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKlDHKLAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 442 IKIAKPAATQ------LELEQAAHQAGALDFINTLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHL 515
Cdd:PRK09700 101 LYIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658756163 516 -DSQTEQL--IQQAINKYAKNhlVLVIAHRLNTVKNASN-ILVMQNG 558
Cdd:PRK09700 177 tNKEVDYLflIMNQLRKEGTA--IVYISHKLAEIRRICDrYTVMKDG 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
377-541 |
5.69e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.11 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLFDCLLG-FHP---QVIEQISINNKP------LDATSMSTLQNAIAwiPQTPTLFYQSisdniKIAK 446
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGvLKPdegEVDEDLKISYKPqyispdYDGTVEEFLRSANT--DDFGSSYYKT-----EIIK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 447 PAAtqleleqaahqagaldfintLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQA 526
Cdd:COG1245 442 PLG--------------------LEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
|
170
....*....|....*..
gi 658756163 527 INKYAKNH--LVLVIAH 541
Cdd:COG1245 498 IRRFAENRgkTAMVVDH 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
377-541 |
6.04e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLFDCLLGfhpqVIeqisinnKPLDATSMSTLQnaIAWIPQtptlfYqsisdnIKIAKPAATQLELEQ 456
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAG----VL-------KPDEGEVDPELK--ISYKPQ-----Y------IKPDYDGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 457 AAHQAGAlDFINT-------LENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSqtEQLIQ--QAI 527
Cdd:PRK13409 424 ITDDLGS-SYYKSeiikplqLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAvaKAI 496
|
170
....*....|....*.
gi 658756163 528 NKYAKNH--LVLVIAH 541
Cdd:PRK13409 497 RRIAEEReaTALVVDH 512
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
365-564 |
7.07e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.00 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 365 KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNAIAWIPQTPTL-----FYQSIS 439
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgditVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 440 DNIKIAKPAATQLELEQAAHQAGALDfintlENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLD-SQ 518
Cdd:PRK10253 104 RGRYPHQPLFTRWRKEDEEAVTKAMQ-----ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658756163 519 TEQLIQ--QAINKyAKNHLVLVIAHRLN-TVKNASNILVMQNGEIAQQG 564
Cdd:PRK10253 179 QIDLLEllSELNR-EKGYTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
68-306 |
1.07e-09 |
|
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: 59.89 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 68 VTHFLWPLAGIILLRALFLAISERLSAYA----ALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYY 143
Cdd:cd18565 49 PRGQLWLLGGLTVAAFLLESLFQYLSGVLwrrfAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 144 AKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKL 223
Cdd:cd18565 129 DDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 224 FNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATG-----FVV-LLLAPE 297
Cdd:cd18565 209 FTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTltvgtLVTfLFYTQR 288
|
....*....
gi 658756163 298 FYLPLRQLG 306
Cdd:cd18565 289 LLWPLTRLG 297
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
364-541 |
1.19e-09 |
|
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: 61.10 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvieqisiNNKPlDATSMS---TLQnaIAWIPQT------PTLF 434
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG-----------QEQP-DSGTIEigeTVK--LAYVDQSrdaldpNKTV 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 435 YQSIS---DNIKIAKpaatqLELEQAAHqAGALDFintleNGFDT--LIGEqgegLSGGQKQRIALARAFLKQAPILVLD 509
Cdd:TIGR03719 404 WEEISgglDIIKLGK-----REIPSRAY-VGRFNF-----KGSDQqkKVGQ----LSGGERNRVHLAKTLKSGGNVLLLD 468
|
170 180 190
....*....|....*....|....*....|..
gi 658756163 510 EPTAHLDSQTEQLIQQAINKYAKNhlVLVIAH 541
Cdd:TIGR03719 469 EPTNDLDVETLRALEEALLNFAGC--AVVISH 498
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
364-564 |
1.27e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHP----QVIEQISINNKPLDATSMSTLQnaIAWIPQTP-------- 431
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAPCALRGRK--IATIMQNPrsafnplh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 432 TLFYQSISDNIKIAKPAATQLeLEQAAHQAGaldfintLENGfDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEP 511
Cdd:PRK10418 97 TMHTHARETCLALGKPADDAT-LTAALEAVG-------LENA-ARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 512 TAHLDSQTEQLIQQAINKYAKNHL--VLVIAHRLNTV-KNASNILVMQNGEIAQQG 564
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
334-569 |
1.84e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 334 SQQHETKFEEHISsinINNLNFTYPNSNE---GIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQIS---- 406
Cdd:PRK10261 2 PHSDELDARDVLA---VENLNIAFMQEQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 407 ---------INNKPLDATSMSTLQNA-IAWIPQTPTlfyQSISDNIKIAKPAATQLELEQAAHQAGA-------LDFINT 469
Cdd:PRK10261 79 llrrrsrqvIELSEQSAAQMRHVRGAdMAMIFQEPM---TSLNPVFTVGEQIAESIRLHQGASREEAmveakrmLDQVRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 470 LENgfDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHL--VLVIAHRLNTVK 547
Cdd:PRK10261 156 PEA--QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVA 233
|
250 260
....*....|....*....|...
gi 658756163 548 N-ASNILVMQNGEIAQQGTYSQL 569
Cdd:PRK10261 234 EiADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
348-570 |
1.96e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTY----PNSNEGIKNINLTLPAKGLVAVVGASGSGKSTL---FDCLLGFHPQVIEQISINNKPLDATSMSTL 420
Cdd:PRK13651 3 IKVKNIVKIFnkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 421 QNAIAWIPQTPT-----------------------LFYQSISDNIkIAKPAATQLELEQAAHQAgaLDFINTLenGFDTL 477
Cdd:PRK13651 83 VLEKLVIQKTRFkkikkikeirrrvgvvfqfaeyqLFEQTIEKDI-IFGPVSMGVSKEEAKKRA--AKYIELV--GLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 478 IGEQGE-GLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQ-TEQLIQQAINKYAKNHLVLVIAHRL-NTVKNASNILV 554
Cdd:PRK13651 158 YLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIF 237
|
250
....*....|....*..
gi 658756163 555 MQNGEIAQQG-TYSQLE 570
Cdd:PRK13651 238 FKDGKIIKDGdTYDILS 254
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
485-579 |
2.12e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 LSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNhlVLVIAHRLNTVKNAsnilVMQ------NG 558
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGT--VLLVSHDRQFVDNT----VTEcwifegNG 514
|
90 100
....*....|....*....|..
gi 658756163 559 EIAQQ-GTYSQLEQQQGAFKSL 579
Cdd:PRK11147 515 KIGRYvGGYHDARQQQAQYLAL 536
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
364-555 |
2.16e-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: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTL-FDCLlgfhpqvieqisinNKPLDATSMSTLQNAiawiPQTPTLFYQSISDNI 442
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLvNEGL--------------YASGKARLISFLPKF----SRNKLIFIDQLQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 443 KIAkpaATQLELEQAAhqagaldfiNTLengfdtligeqgeglSGGQKQRIALARaFLKQAP---ILVLDEPTAHLD-SQ 518
Cdd:cd03238 73 DVG---LGYLTLGQKL---------STL---------------SGGELQRVKLAS-ELFSEPpgtLFILDEPSTGLHqQD 124
|
170 180 190
....*....|....*....|....*....|....*..
gi 658756163 519 TEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVM 555
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
329-574 |
3.95e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.69 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 329 PLPEQSQQHETKFEE------HISSININNLNFTYPNSNEGIKN-INLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQV 401
Cdd:PRK13536 15 ELSPIERKHQGISEAkasipgSMSTVAIDLAGVSKSYGDKAVVNgLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 402 IEQISINNKPLDATSMSTlQNAIAWIPQTPTLFYQ-SISDNI----KIAKPAATQLEleqaAHQAGALDFINtLENGFDT 476
Cdd:PRK13536 95 AGKITVLGVPVPARARLA-RARIGVVPQFDNLDLEfTVRENLlvfgRYFGMSTREIE----AVIPSLLEFAR-LESKADA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 477 LIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINK-YAKNHLVLVIAHRLNTVKNASNIL-V 554
Cdd:PRK13536 169 RVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLcV 244
|
250 260
....*....|....*....|.
gi 658756163 555 MQNG-EIAQQGTYSQLEQQQG 574
Cdd:PRK13536 245 LEAGrKIAEGRPHALIDEHIG 265
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
364-565 |
4.80e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.53 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHP--------QVIEQISINNKPLDATSMSTLQNAIAWIPQTPTLFY 435
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 436 QSISDNI-------KIAKPAATQLELEQAAHQAGALdfintleNGFDTLIGEQGEGLSGGQKQRIALARAFLKQAP---- 504
Cdd:PRK13547 97 AFSAREIvllgrypHARRAGALTHRDGEIAWQALAL-------AGATALVGRDVTTLSGGELARVQFARVLAQLWPphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 505 -----ILVLDEPTAHLDSQTEQLIQQAINKYAKN-HL-VLVIAHRLN-TVKNASNILVMQNGEIAQQGT 565
Cdd:PRK13547 170 aqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
364-565 |
4.86e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFhpqvieqisinNKPLDATSMSTLQNAIAWIPQT----PTL-----F 434
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL-----------VAPDEGVIKRNGKLRIGYVPQKlyldTTLpltvnR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 435 YQSISDNIKIAK--PAatqLELEQAAHqagaldfintlengfdtLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPT 512
Cdd:PRK09544 89 FLRLRPGTKKEDilPA---LKRVQAGH-----------------LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 513 AHLDSQTEQLIQQAINKYAK--NHLVLVIAHRLNTVKNASNILVMQNGEIAQQGT 565
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGT 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
374-541 |
4.97e-09 |
|
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: 56.46 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 374 KGLVAVVGASGSGKSTLFDCLL----GFHPQvieqisiNNKPLDA-TSMSTLQNAIAWIPQTptlFYQSISDNIKIA-KP 447
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIIEALKyaltGELPP-------NSKGGAHdPKLIREGEVRAQVKLA---FENANGKKYTITrSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 448 AAtqleLEQAA--HQagaldfintleNGFDTLIGEQGEGLSGGQKQ------RIALARAFLKQAPILVLDEPTAHLDSQ- 518
Cdd:cd03240 92 AI----LENVIfcHQ-----------GESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEn 156
|
170 180
....*....|....*....|....*.
gi 658756163 519 -TEQLIqQAINKYA--KNHLVLVIAH 541
Cdd:cd03240 157 iEESLA-EIIEERKsqKNFQLIVITH 181
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
368-543 |
5.18e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 368 NLTLPAKGLV-AVVGASGSGKSTLFDCLLGfhpQVIEQISINNKP------LDATSMSTLQNaiawipqtptlFYQSISD 440
Cdd:PRK13409 92 GLPIPKEGKVtGILGPNGIGKTTAVKILSG---ELIPNLGDYEEEpswdevLKRFRGTELQN-----------YFKKLYN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 441 N-IKIA-KPAATQL----------ELEQAAHQAGALDFINT---LENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPI 505
Cdd:PRK13409 158 GeIKVVhKPQYVDLipkvfkgkvrELLKKVDERGKLDEVVErlgLENILDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 658756163 506 LVLDEPTAHLDsqteqlIQQ------AINKYAKNHLVLVIAHRL 543
Cdd:PRK13409 234 YFFDEPTSYLD------IRQrlnvarLIRELAEGKYVLVVEHDL 271
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
379-574 |
5.30e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.89 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 379 VVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNaIAWIPQTPTL---FyqSISDNIKI-----AKPAAT 450
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VGVVPQFDNLdpdF--TVRENLLVfgryfGLSAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 451 QLELEQaahqaGALDFINtLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINK- 529
Cdd:PRK13537 115 ARALVP-----PLLEFAK-LENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSl 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658756163 530 YAKNHLVLVIAHRLNTVKNASNIL-VMQNG-EIAQQGTYSQLEQQQG 574
Cdd:PRK13537 185 LARGKTILLTTHFMEEAERLCDRLcVIEEGrKIAEGAPHALIESEIG 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
366-564 |
6.00e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.82 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 366 NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKP---LDATSMSTLQNAIAWIPQTP--------TLf 434
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDPyaslnprmTV- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 435 YQSISDNIKIAKPAATQlELEQAAHQAGAL-----DFINTLENGFdtligeqgeglSGGQKQRIALARAFLKQAPILVLD 509
Cdd:COG4608 115 GDIIAEPLRIHGLASKA-ERRERVAELLELvglrpEHADRYPHEF-----------SGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 510 EPTAHLD-SqteqlIQ-QAIN-----------KYaknhlvLVIAHRLNTVKNASN-ILVMQNGEIAQQG 564
Cdd:COG4608 183 EPVSALDvS-----IQaQVLNlledlqdelglTY------LFISHDLSVVRHISDrVAVMYLGKIVEIA 240
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
363-559 |
6.26e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 363 GIK---NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLD-ATSMSTLQNAIAWIPQTPTLFYQ-S 437
Cdd:PRK10982 10 GVKaldNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQrS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 438 ISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTliGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS 517
Cdd:PRK10982 90 VMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDP--RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 658756163 518 QTEQLIQQAINKYAKNHLVLV-IAHRLNTVKNASN-ILVMQNGE 559
Cdd:PRK10982 168 KEVNHLFTIIRKLKERGCGIVyISHKMEEIFQLCDeITILRDGQ 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
365-569 |
7.32e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.54 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 365 KNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIE----QISINNKPLDATSMSTLQ----NAIAWIPQTPT---- 432
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAhpsgSILFDGQDLLGLSERELRrirgNRIAMIFQEPMtsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 433 -LFyqSISDNI--------KIAKPAATQ--LEL------EQAA-------HQagaldfintlengfdtligeqgegLSGG 488
Cdd:COG4172 107 pLH--TIGKQIaevlrlhrGLSGAAARAraLELlervgiPDPErrldaypHQ------------------------LSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 489 QKQRIALARAFLKQAPILVLDEPTAHLD----SQTEQLIQ--QAINKYAknhlVLVIAHRLNTVKN-ASNILVMQNGEIA 561
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKdlQRELGMA----LLLITHDLGVVRRfADRVAVMRQGEIV 236
|
....*...
gi 658756163 562 QQGTYSQL 569
Cdd:COG4172 237 EQGPTAEL 244
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
486-578 |
8.51e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 486 SGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNhlVLVIAHR---LNTVknASNILVMQNGEI-A 561
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKT--FIVVSHArefLNTV--VTDILHLHGQKLvT 421
|
90 100
....*....|....*....|....*
gi 658756163 562 QQGTY--------SQLEQQQGAFKS 578
Cdd:PLN03073 422 YKGDYdtfertreEQLKNQQKAFES 446
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
360-562 |
9.16e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 9.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 360 SNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKplDATSMST---LQNAIAWIP---QTPTL 433
Cdd:PRK15439 275 TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK--EINALSTaqrLARGLVYLPedrQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 434 FYQS-ISDNIK---------IAKPAATQLELEQaAHQAGALDFintleNGFDTLIGeqgeGLSGGQKQRIALARAfLKQA 503
Cdd:PRK15439 353 YLDApLAWNVCalthnrrgfWIKPARENAVLER-YRRALNIKF-----NHAEQAAR----TLSGGNQQKVLIAKC-LEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 504 P-ILVLDEPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHRLNTV-KNASNILVMQNGEIAQ 562
Cdd:PRK15439 422 PqLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIeQMADRVLVMHQGEISG 483
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
29-309 |
1.05e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 56.71 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 29 WLKLSIALGTFNAILMIAGAYLLAQTIHNVMFEGaSLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTL 108
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNG-DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 109 LTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMIL 188
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 189 VGSKAealnQKRWQQ----LAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLAT 264
Cdd:cd18545 160 LRRRA----RKAWQRvrkkISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 658756163 265 ISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHY 309
Cdd:cd18545 236 LGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFY 280
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
485-568 |
1.10e-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: 54.89 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 LSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHL--VLVIAHRLNTVKNASNILVMQNGEIAQ 562
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKktALVVEHDLAVLDYLSDRIHVFEGEPGV 151
|
....*.
gi 658756163 563 QGTYSQ 568
Cdd:cd03222 152 YGIASQ 157
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-323 |
1.24e-08 |
|
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: 56.75 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 19 LKRQSKPAGAWLKLSIALGTFNAILMIAGAYLlaqtihnvmfegaslsqvthflwplaGIILLRALFLAISERLSAYAAL 98
Cdd:cd18564 30 LGDKPLPGLLGLAPLLGPDPLALLLLAAAALV--------------------------GIALLRGLASYAGTYLTALVGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 99 KIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLT 178
Cdd:cd18564 84 RVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 179 APLIPFFMILVGSK-AEALNQKRWQQLAVLGnyffdRVQ-GLTQLKL---FNATQQELKQIAKISDDFRHATLGVLKIAF 253
Cdd:cd18564 164 APLLLLAARRFSRRiKEASREQRRREGALAS-----VAQeSLSAIRVvqaFGREEHEERRFARENRKSLRAGLRAARLQA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658756163 254 LSSFALEFLATISVALVaviigfrLFFGTLDFATG---------FVVLLLApeFYLPLRQLgSHYHARLQGISAAADMV 323
Cdd:cd18564 239 LLSPVVDVLVAVGTALV-------LWFGAWLVLAGrltpgdllvFLAYLKN--LYKPVRDL-AKLTGRIAKASASAERV 307
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
366-525 |
1.38e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 366 NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLDATSMSTLQNaIAWIPQTPTL-----------F 434
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD-LLYLGHQPGIkteltalenlrF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 435 YQSISDNIKiakpaatqlelEQAAHQAgaLDFINTLenGFDTLIGEQgegLSGGQKQRIALARAFLKQAPILVLDEP-TA 513
Cdd:PRK13538 98 YQRLHGPGD-----------DEALWEA--LAQVGLA--GFEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPfTA 159
|
170
....*....|...
gi 658756163 514 hLDSQ-TEQLIQQ 525
Cdd:PRK13538 160 -IDKQgVARLEAL 171
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
362-564 |
1.96e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 55.42 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 362 EGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLG-FHP-----QVIEQISINNKPLDATSMSTL---QNAIAWipqtpt 432
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPtsgevRVAGLVPWKRRKKFLRRIGVVfgqKTQLWW------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 433 lfyqsisdNIkiakPAATQLELEQAAHQAGALDFINTLENGFDTL-IGE----QGEGLSGGQKQRIALARAFLKQAPILV 507
Cdd:cd03267 109 --------DL----PVIDSFYLLAAIYDLPPARFKKRLDELSELLdLEElldtPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 508 LDEPTAHLDSQTEQLIQQAINKYAKNH--LVLVIAHRLNTV-KNASNILVMQNGEIAQQG 564
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
329-565 |
2.03e-08 |
|
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: 57.33 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 329 PLPEQSQQHETKFEEhISSININNLnftypnsnegiKNINLTLPAKGLVAVVGASGSGKSTLFDCLLgfHPQVIEQ---- 404
Cdd:TIGR00630 601 EVPAERRPGNGKFLT-LKGARENNL-----------KNITVSIPLGLFTCITGVSGSGKSTLINDTL--YPALANRlnga 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 405 -------------------ISINNKPLDATSMST----------LQNAIAWIPQTPTLFYQS--ISDNIKIAKPAATQ-- 451
Cdd:TIGR00630 667 ktvpgrytsieglehldkvIHIDQSPIGRTPRSNpatytgvfdeIRELFAETPEAKVRGYTPgrFSFNVKGGRCEACQgd 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 452 -----------------------------LE-----------LEQAAHQAgaLDF---INTLENGFDTL---------IG 479
Cdd:TIGR00630 747 gvikiemhflpdvyvpcevckgkrynretLEvkykgkniadvLDMTVEEA--YEFfeaVPSISRKLQTLcdvglgyirLG 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 480 EQGEGLSGGQKQRIALARAFLKQA---PILVLDEPTA--HLD--SQTEQLIQQAInkyAKNHLVLVIAHRLNTVKNASNI 552
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTglHFDdiKKLLEVLQRLV---DKGNTVVVIEHNLDVIKTADYI 901
|
330
....*....|....*....
gi 658756163 553 LVM------QNGEIAQQGT 565
Cdd:TIGR00630 902 IDLgpeggdGGGTVVASGT 920
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
346-542 |
4.10e-08 |
|
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: 56.30 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKpldatsmstlqNAIA 425
Cdd:TIGR00954 450 NGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 426 WIPQTPTLFYQSISDNI-------KIAKPAATQLELEQAAhQAGALDFINTLENGFDTlIGEQGEGLSGGQKQRIALARA 498
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIiypdsseDMKRRGLSDKDLEQIL-DNVQLTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 658756163 499 FLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNhlVLVIAHR 542
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYMYRLCREFGIT--LFSVSHR 638
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
346-516 |
5.34e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.23 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvIEQIS-----INNKPLDatsmsTL 420
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-----LERITsgeiwIGGRVVN-----EL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 421 QNA---IAWIPQTPTLF-YQSISDNI----KIAKPAATQLElEQAAHQAGALdfintlenGFDTLIGEQGEGLSGGQKQR 492
Cdd:PRK11650 72 EPAdrdIAMVFQNYALYpHMSVRENMayglKIRGMPKAEIE-ERVAEAARIL--------ELEPLLDRKPRELSGGQRQR 142
|
170 180
....*....|....*....|....
gi 658756163 493 IALARAFLKQAPILVLDEPTAHLD 516
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
364-577 |
7.53e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 54.34 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqVIE----QISINNKPLDATSmstlQNAIAWIPQTPTLfYQsis 439
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILG----ILApdsgEVLWDGEPLDPED----RRRIGYLPEERGL-YP--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 440 dNIKIAKpaatQLE-------LEQAAHQAGALDFINTLEngfdtlIGEQG----EGLSGGQKQRIALARAFLKQAPILVL 508
Cdd:COG4152 85 -KMKVGE----QLVylarlkgLSKAEAKRRADEWLERLG------LGDRAnkkvEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 509 DEPTAHLDSQTEQLIQQAINKYAKN-HLVLVIAHRLNTV-KNASNILVMQNGEIAQQGTYSQLEQQQGAFK 577
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGRNT 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
368-543 |
9.27e-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: 54.79 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 368 NLTLPAKGLV-AVVGASGSGKSTLFDCLLGfhpQVIEQISINNKP------LDATSMSTLQNaiawipqtptlFYQSISD 440
Cdd:COG1245 92 GLPVPKKGKVtGILGPNGIGKSTALKILSG---ELKPNLGDYDEEpswdevLKRFRGTELQD-----------YFKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 441 N-IKIA-KPAATQL----------ELEQAAHQAGALDFINT---LENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPI 505
Cdd:COG1245 158 GeIKVAhKPQYVDLipkvfkgtvrELLEKVDERGKLDELAEklgLENILDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 658756163 506 LVLDEPTAHLDsqteqlIQQ------AINKYAK-NHLVLVIAHRL 543
Cdd:COG1245 234 YFFDEPSSYLD------IYQrlnvarLIRELAEeGKYVLVVEHDL 272
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
369-543 |
9.55e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.52 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 369 LTLPAKGLV-AVVGASGSGKSTLFDCLLGfhpQVIEQISINNKP------LDATSMSTLQNaiawipqtptLFYQSISDN 441
Cdd:cd03236 20 LPVPREGQVlGLVGPNGIGKSTALKILAG---KLKPNLGKFDDPpdwdeiLDEFRGSELQN----------YFTKLLEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 442 IKIAK--------PAA---TQLELEQAAHQAGALD-FINTLEngFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLD 509
Cdd:cd03236 87 VKVIVkpqyvdliPKAvkgKVGELLKKKDERGKLDeLVDQLE--LRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....*
gi 658756163 510 EPTAHLDSQTEQLIQQAINKYAK-NHLVLVIAHRL 543
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDL 199
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
64-305 |
1.32e-07 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 53.58 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 64 SLSQVTHFLWPLAGIILLRALFLA-----ISERLSAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDGVEA 138
Cdd:cd18554 36 TLDEKVYKLFTIIGIMFFIFLILRppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 139 LHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLtapLIPFFMILVG---SKAEALNQKRWQQLAVLGNYFFDRV 215
Cdd:cd18554 116 TKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLV---IFPFYILAVKyffGRLRKLTKERSQALAEVQGFLHERI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 216 QGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLA 295
Cdd:cd18554 193 QGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYM 272
|
250
....*....|
gi 658756163 296 PEFYLPLRQL 305
Cdd:cd18554 273 ERMYSPLRRL 282
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
345-564 |
1.53e-07 |
|
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: 52.65 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 345 ISSININNLnftypnsnegiKNINLTLPAKGLVAVVGASGSGKSTL-FDCLLG------------FHPQVIEQISinnKP 411
Cdd:cd03270 3 VRGAREHNL-----------KNVDVDIPRNKLVVITGVSGSGKSSLaFDTIYAegqrryveslsaYARQFLGQMD---KP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 412 lDATSMSTLQNAIAwIPQtptlfyQSISDNikiakPAAT---------QLELEQAahQAG---ALDFINTLENGFDTLiG 479
Cdd:cd03270 69 -DVDSIEGLSPAIA-IDQ------KTTSRN-----PRSTvgtvteiydYLRLLFA--RVGireRLGFLVDVGLGYLTL-S 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 480 EQGEGLSGGQKQRIALARAFLKQ--APILVLDEPTAHL-DSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVM- 555
Cdd:cd03270 133 RSAPTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLhPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIg 212
|
250
....*....|....
gi 658756163 556 -----QNGEIAQQG 564
Cdd:cd03270 213 pgagvHGGEIVAQG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
364-562 |
1.69e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNK------PLDAtsmstLQNAIAWIPQT--PTLFY 435
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDA-----VKKGMAYITESrrDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 436 Q--SISDNIKIAKpaatQLELeqaAHQAGALDFIN------TLENGFDTL----------IGEqgegLSGGQKQRIALAR 497
Cdd:PRK09700 354 PnfSIAQNMAISR----SLKD---GGYKGAMGLFHevdeqrTAENQRELLalkchsvnqnITE----LSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 498 AFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKN-HLVLVIAHRLNTVKNASN-ILVMQNGEIAQ 562
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDrIAVFCEGRLTQ 489
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
364-519 |
1.73e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.88 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPqviEQISINNKpldaTSMSTLQNAIAWIPQTPTLFYQSISDnIK 443
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGD----IHYNGIPYKEFAEKYPGEIIYVSEED-VH 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658756163 444 IAkpaatQLELEQAahqagaLDFINTLeNGFDTLigeqgEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQT 519
Cdd:cd03233 95 FP-----TLTVRET------LDFALRC-KGNEFV-----RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
364-541 |
1.87e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvIEQisinnkpLDATSM---STLQnaIAWIPQT-------PTL 433
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG-----QEQ-------PDSGTIkigETVK--LAYVDQSrdaldpnKTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 434 FyQSIS---DNIKIAKpaatqLELEQAAHqAGALDFintleNGFD--TLIGEqgegLSGGQKQRIALARAfLKQ-APILV 507
Cdd:PRK11819 406 W-EEISgglDIIKVGN-----REIPSRAY-VGRFNF-----KGGDqqKKVGV----LSGGERNRLHLAKT-LKQgGNVLL 468
|
170 180 190
....*....|....*....|....*....|....
gi 658756163 508 LDEPTAHLDSQTEQLIQQAINKYAKNhlVLVIAH 541
Cdd:PRK11819 469 LDEPTNDLDVETLRALEEALLEFPGC--AVVISH 500
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
348-524 |
5.55e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLfdcllgfhpqvIEQISINNKPLDATSMSTLQNAIAwi 427
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTI-----------LKLISGELQPSSGTVFRSAKVRMA-- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 pqtptLFYQSISDNIKIAK----------PAATQLELEqaAHqAGALDFINTLENgfdtligEQGEGLSGGQKQRIALAR 497
Cdd:PLN03073 576 -----VFSQHHVDGLDLSSnpllymmrcfPGVPEQKLR--AH-LGSFGVTGNLAL-------QPMYTLSGGQKSRVAFAK 640
|
170 180
....*....|....*....|....*...
gi 658756163 498 AFLKQAPILVLDEPTAHLD-SQTEQLIQ 524
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDlDAVEALIQ 668
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
340-575 |
6.06e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 340 KFEE----HISSININNLNFTYPNsNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvieqisinNKPLDAT 415
Cdd:PRK15064 308 RFEQdkklHRNALEVENLTKGFDN-GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG------------ELEPDSG 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 416 SMSTLQNA-IAWIPQTP--------TLF-----YQSISDNikiakpaatqlelEQAAHQA-GALDFintleNGFDtlIGE 480
Cdd:PRK15064 375 TVKWSENAnIGYYAQDHaydfendlTLFdwmsqWRQEGDD-------------EQAVRGTlGRLLF-----SQDD--IKK 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 481 QGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYaKNHLVLViAHRLNTVKN-ASNIL-VMQNG 558
Cdd:PRK15064 435 SVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EGTLIFV-SHDREFVSSlATRIIeITPDG 512
|
250
....*....|....*..
gi 658756163 559 EIAQQGTYSQLEQQQGA 575
Cdd:PRK15064 513 VVDFSGTYEEYLRSQGI 529
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
369-555 |
6.34e-07 |
|
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: 49.67 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 369 LTLPAKGLVAVVGASGSGKSTLFDcllgfhpqvieqisinnkpldatsmstlqnAIAWIpqtptLFYQSisdnikiakPA 448
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILD------------------------------AIGLA-----LGGAQ---------SA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 449 ATQLELEQAAHQAGA--LDFINTLEngfdtligeqgeGLSGGQKQRIALARAF----LKQAPILVLDEPTAHLDSQTEQL 522
Cdd:cd03227 52 TRRRSGVKAGCIVAAvsAELIFTRL------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|....
gi 658756163 523 IQQAINKYAKNH-LVLVIAHRLNTVKNASNILVM 555
Cdd:cd03227 120 LAEAILEHLVKGaQVIVITHLPELAELADKLIHI 153
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
348-516 |
6.34e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.64 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqvIEQISINNKPLDATSMSTLQNA---- 423
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-----IERPSAGKIWFSGHDITRLKNRevpf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 ----IAWIPQTPTLFY-QSISDNIKIAKPAATQLELEQAAHQAGALDFINTLENGFDTLIGeqgegLSGGQKQRIALARA 498
Cdd:PRK10908 77 lrrqIGMIFQDHHLLMdRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGIARA 151
|
170
....*....|....*...
gi 658756163 499 FLKQAPILVLDEPTAHLD 516
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLD 169
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
485-553 |
7.49e-07 |
|
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: 52.28 E-value: 7.49e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 485 LSGGQKQRIALARAF----LKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNIL 553
Cdd:pfam02463 1078 LSGGEKTLVALALIFaiqkYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
32-318 |
8.67e-07 |
|
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: 50.95 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 32 LSIALGTFNAILMIAGAYLLAQTIHNvmfeGASLSQVTHFLWP---LAGIILLRALFLAISERLSAYAALKIKSAMRQTL 108
Cdd:cd18546 3 LALLLVVVDTAASLAGPLLVRYGIDS----GVRAGDLGVLLLAaaaYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 109 LTKLTHLGPSYIEQHGQGATLNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMIL 188
Cdd:cd18546 79 FAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 189 VGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVA 268
Cdd:cd18546 159 FRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 658756163 269 LVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISA 318
Cdd:cd18546 239 AVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAA 288
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
348-569 |
1.47e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYPNSN---EGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGF--HPQVI--EQISINNKPLDATSMSTL 420
Cdd:PRK11022 4 LNVDKLSVHFGDESapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRVmaEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 421 QN----AIAWIPQTP--------TLFYQsISDNIKIAKPAATQLELEQAAH---QAGALDFINTLENgfdtligeQGEGL 485
Cdd:PRK11022 84 RNlvgaEVAMIFQDPmtslnpcyTVGFQ-IMEAIKVHQGGNKKTRRQRAIDllnQVGIPDPASRLDV--------YPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 486 SGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTE-QLIQQAINKYAKNHLVLV-IAHRLNTVKNASN-ILVMQNGEIAQ 562
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQaQIIELLLELQQKENMALVlITHDLALVAEAAHkIIVMYAGQVVE 234
|
....*..
gi 658756163 563 QGTYSQL 569
Cdd:PRK11022 235 TGKAHDI 241
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
379-527 |
2.06e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 379 VVGASGSGKSTLFDCLLGFHPQVIEQISINNKPldaTSMSTLQNAIAWIPQTPTLfYQSIS--DNIKIAkpaaTQLELEQ 456
Cdd:PRK13543 42 VQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT---ATRGDRSRFMAYLGHLPGL-KADLStlENLHFL----CGLHGRR 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 457 AAHQAGALDFINTLENGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAI 527
Cdd:PRK13543 114 AKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
43-284 |
2.65e-06 |
|
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: 49.40 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 43 LMIAGAYLLAQTIhnvmFEGASLSQVTHFLwPLAGIILLrALFLAIS---ERL-SAYAALKIKSAMRQTLLTKLTHLGPS 118
Cdd:cd18585 11 LLALSGWFISAAA----LAGLAAPTFNYFT-PAAGVRGF-AITRTAGrygERLvSHDATFRLLSNLRVWFYRKLEPLAPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 119 YIEQHGQGATLNTVHDGVEALHDYYAK-YLPGVAysALIplAILVVIFPTDY-------KAGLIFLLTAPLIPFFMILVG 190
Cdd:cd18585 85 RLQKYRSGDLLNRIVADIDTLDNLYLRvLSPPVV--ALL--VILATILFLAFfspalalILLAGLLLAGVVIPLLFYRLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 191 SK-AEALNQKRwqqlAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVAL 269
Cdd:cd18585 161 KKiGQQLVQLR----AELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWL 236
|
250
....*....|....*
gi 658756163 270 VAVIIGFRLFFGTLD 284
Cdd:cd18585 237 VLWLGAPLVQNGALD 251
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
362-569 |
4.00e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.34 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 362 EGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfHPQVIEQiSINNKPLDATSMST---LQNAIAWIPQTPTLFYQ-S 437
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRATSG-RIVFDGKDITDWQTakiMREAVAIVPEGRRVFSRmT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 438 ISDNIKIAKPAATQLELEQAAHQAGALdFINTLENGFdtligEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS 517
Cdd:PRK11614 97 VEENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRI-----QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658756163 518 QTEQLIQQAINKYAKNHLV--LVIAHRLNTVKNASNILVMQNGEIAQQGTYSQL 569
Cdd:PRK11614 171 IIIQQIFDTIEQLREQGMTifLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
473-561 |
5.06e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 473 GFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYA-KNHLVLVIAHRLNTVKNASN 551
Cdd:PRK10982 384 GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGITD 459
|
90
....*....|.
gi 658756163 552 -ILVMQNGEIA 561
Cdd:PRK10982 460 rILVMSNGLVA 470
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
461-545 |
5.70e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 461 AGALDFINTLENGFDTLIGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAI-------NKYAKN 533
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLKSEKN 116
|
90
....*....|..
gi 658756163 534 HLVLVIAHRLNT 545
Cdd:smart00382 117 LTVILTTNDEKD 128
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
351-546 |
8.27e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 351 NNLNFTYPnsneGIK---NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLD-ATSMSTLQNAIAW 426
Cdd:PRK11288 8 DGIGKTFP----GVKaldDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQ----TPTLfyqSISDNIKIAK-PAATQLeLEQAAHQAGALDFINTLenGFDTLIGEQGEGLSGGQKQRIALARAFLK 501
Cdd:PRK11288 84 IYQelhlVPEM---TVAENLYLGQlPHKGGI-VNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 658756163 502 QAPILVLDEPTAHLDSQ-TEQLIQQAINKYAKNHLVLVIAHRLNTV 546
Cdd:PRK11288 158 NARVIAFDEPTSSLSAReIEQLFRVIRELRAEGRVILYVSHRMEEI 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
377-575 |
9.00e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 377 VAVVGASGSGKSTLFDCLLGfhpqvieQISInnkplDATSMSTLQN-AIAWIPQ-TPTLFYQSIsDNIKIAKPAATQLE- 453
Cdd:PRK10636 30 VGLVGKNGCGKSTLLALLKN-------EISA-----DGGSYTFPGNwQLAWVNQeTPALPQPAL-EYVIDGDREYRQLEa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 454 -LEQA---------AHQAGALDFIN--TLENGFDTLI---GEQGEGL-------SGGQKQRIALARAFLKQAPILVLDEP 511
Cdd:PRK10636 97 qLHDAnerndghaiATIHGKLDAIDawTIRSRAASLLhglGFSNEQLerpvsdfSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 512 TAHLDSQTEQLIQQAINKYAKNhLVLVIAHR--LNTVKNasNILVMQNGEIAQ-QGTYSQLEQQQGA 575
Cdd:PRK10636 177 TNHLDLDAVIWLEKWLKSYQGT-LILISHDRdfLDPIVD--KIIHIEQQSLFEyTGNYSSFEVQRAT 240
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
374-557 |
1.11e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 46.30 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 374 KGLVAVVGASGSGKSTLFDCL---LGfhpqviEQisiNNKPLDATSMSTLqnaiawipqtptLFYQSISdnikiaKPAAT 450
Cdd:cd03278 22 PGLTAIVGPNGSGKSNIIDAIrwvLG------EQ---SAKSLRGEKMSDV------------IFAGSET------RKPAN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 451 QLELEqaahqagaLDFINtlENGFDTLIGeQG----------------EGLSGGQKQRIALARAF----LKQAPILVLDE 510
Cdd:cd03278 75 FAEVT--------LTFDN--SDGRYSIIS-QGdvseiieapgkkvqrlSLLSGGEKALTALALLFaifrVRPSPFCVLDE 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658756163 511 PTAHLD-SQTEQLIqQAINKYAKNHLVLVIAHRLNTVKNASNIL--VMQN 557
Cdd:cd03278 144 VDAALDdANVERFA-RLLKEFSKETQFIVITHRKGTMEAADRLYgvTMQE 192
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
486-565 |
2.13e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.03 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 486 SGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAIN--KYAKNHLVLVIAHRLNTVKNASN-ILVMQNGEIAQ 562
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLGVVAGICDkVLVMYAGRTME 242
|
...
gi 658756163 563 QGT 565
Cdd:PRK09473 243 YGN 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
376-517 |
2.18e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.57 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 376 LVAVVGASGSGKSTLFDCLLG-FHPQVIE-QISINNKPLDATSMS----TLQNAIAWIPQT--PTLFYQSIsdnIKIAKP 447
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGrIQGNNFTgTILANNRKPTKQILKrtgfVTQDDILYPHLTvrETLVFCSL---LRLPKS 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 448 AATQLELEQAAHQAGALDfINTLENgfdTLIGEQG-EGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS 517
Cdd:PLN03211 173 LTKQEKILVAESVISELG-LTKCEN---TIIGNSFiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
364-519 |
2.27e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTLFDCLL----GFHPQVIEQISINNKPLDATsMSTLQNAIAWIPQTPTLF-YQSI 438
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFpHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 439 SDNIKIAKPAAT-QL------ELEQAAHQAGALDFINTLENGFDTLIG-EQGEGLSGGQKQRIALARAFLKQAPILVLDE 510
Cdd:TIGR00956 156 GETLDFAARCKTpQNrpdgvsREEYAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
....*....
gi 658756163 511 PTAHLDSQT 519
Cdd:TIGR00956 236 ATRGLDSAT 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
346-519 |
2.37e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 346 SSININN--LNFTYpnsNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGfhpqviEQisinnkPLDATSMSTLQNA 423
Cdd:PRK11147 2 SLISIHGawLSFSD---APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG------EV------LLDDGRIIYEQDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 424 I-AWIPQTP------TLF------YQSISDNIKIAKPAATQLE-------LEQAAHQAGALDFINTLEngFDTLIGEQGE 483
Cdd:PRK11147 67 IvARLQQDPprnvegTVYdfvaegIEEQAEYLKRYHDISHLVEtdpseknLNELAKLQEQLDHHNLWQ--LENRINEVLA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658756163 484 -----------GLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQT 519
Cdd:PRK11147 145 qlgldpdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
485-569 |
3.85e-05 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 45.56 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 LSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNH-LVLVIAHRLNTVKNASN-ILVMQNGEIAQ 562
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGrTMLVVTHEMGFARDVSShVVFLHQGRIEE 234
|
....*..
gi 658756163 563 QGTYSQL 569
Cdd:COG4598 235 QGPPAEV 241
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
344-529 |
4.24e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.00 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 344 HISSININNLNftypnSNEGIKNINLTlpaKGLVAVVGASGSGKSTLFD----CLLGFHPQVIEQIS--IN--------- 408
Cdd:COG0419 1 KLLRLRLENFR-----SYRDTETIDFD---DGLNLIVGPNGAGKSTILEairyALYGKARSRSKLRSdlINvgseeasve 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 409 -------------------NKPLDATSmSTLQNAIAWIPQTPTlfYQSISDNIKIAKPAATQlELEQAAHQAGALDFINT 469
Cdd:COG0419 73 lefehggkryrierrqgefAEFLEAKP-SERKEALKRLLGLEI--YEELKERLKELEEALES-ALEELAELQKLKQEILA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 470 LENGFDTLigeqgEGLSGGQKQRIALARAFLkqapiLVLDepTAHLDSQTEQLIQQAINK 529
Cdd:COG0419 149 QLSGLDPI-----ETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
375-561 |
7.08e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 375 GLVAVVGAsgsGKSTLFDCLLGFHPQVIEQISINNKPLDATS-MSTLQNAIAWIPQ-------TPTlfyQSISDNIKIA- 445
Cdd:PRK11288 283 GLFGLVGA---GRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAGIMLCPEdrkaegiIPV---HSVADNINISa 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 446 ----KPAATQL----ELEQAAHQAGALDfINTleNGFDTLIGEqgegLSGGQKQRIALARAFLKQAPILVLDEPTAHLDS 517
Cdd:PRK11288 357 rrhhLRAGCLInnrwEAENADRFIRSLN-IKT--PSREQLIMN----LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 658756163 518 QTEQLIQQAINKYAKNHL-VLVIAHRLNTVKNASN-ILVMQNGEIA 561
Cdd:PRK11288 430 GAKHEIYNVIYELAAQGVaVLFVSSDLPEVLGVADrIVVMREGRIA 475
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
349-390 |
8.96e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.45 E-value: 8.96e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 658756163 349 NINNLnftypnsnegiKNINLTLPAKGLVAVVGASGSGKSTL 390
Cdd:PRK00349 621 RENNL-----------KNVDVEIPLGKFTCVTGVSGSGKSTL 651
|
|
| 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 |
1.08e-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: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 75 LAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGATLNTVHDgVEALHDYYAkylpGVAYSA 154
Cdd:cd18566 48 VVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNS-LEQIREFLT----GQALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 155 LI--PLAI--LVVIFPTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQE 230
Cdd:cd18566 123 LLdlPFVLifLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQM 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 658756163 231 LKQIAKISddfRHATLGVLKIAFLSSFALEFLATISVALVAVIIGF 276
Cdd:cd18566 203 LRRYERLQ---ANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAF 245
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
326-553 |
1.22e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 326 LNAPLPEQSQQheTKFEEHISSININNLnftypnsnegiKNINLTLPAKGLVAVVGASGSGKSTLF-DCLLGFHPQVIEQ 404
Cdd:PRK00635 586 LTIPIPEKRTN--SLGTLTLSKATKHNL-----------KDLTISLPLGRLTVVTGVSGSGKSSLInDTLVPAVEEFIEQ 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 405 ----------------ISIN--------------------------------------------NKPLDAT-------SM 417
Cdd:PRK00635 653 gfcsnlsiqwgaisrlVHITrdlpgrsqrsipltyikafddlrelfaeqprskrlgltkshfsfNTPLGACaecqglgSI 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 418 STLQNAIA----------WIPQTPTLFYQ--SISDNIKIAKPAATQLELEQAA-HQAgaldfINTLEN-GFDTL-IGEQG 482
Cdd:PRK00635 733 TTTDNRTSipcpsclgkrFLPQVLEVRYKgkNIADILEMTAYEAEKFFLDEPSiHEK-----IHALCSlGLDYLpLGRPL 807
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658756163 483 EGLSGGQKQRIALARAFL---KQAPILVLDEPTAHLDSQ-TEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNIL 553
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHdIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
344-540 |
1.67e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.22 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 344 HISSININNlnFtypnsnEGIKNINLTLPaKGLVAVVGASGSGKSTLFDCL-LGFHPQVIEQISIN-------------- 408
Cdd:COG3593 2 KLEKIKIKN--F------RSIKDLSIELS-DDLTVLVGENNSGKSSILEALrLLLGPSSSRKFDEEdfylgddpdlpeie 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 409 -------------NKPLDATSMSTLQNAIAWIPQTPTLFYQSISDNIK-IAKPAATQLELEQAAHQAGALDFINTL---- 470
Cdd:COG3593 73 ieltfgsllsrllRLLLKEEDKEELEEALEELNEELKEALKALNELLSeYLKELLDGLDLELELSLDELEDLLKSLslri 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658756163 471 ENGFDTLIGEQGEGLsggqkQR---IALARAFL-----KQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIA 540
Cdd:COG3593 153 EDGKELPLDRLGSGF-----QRlilLALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIIT 225
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
351-390 |
1.73e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 1.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 658756163 351 NNLnftypnsnegiKNINLTLPAKGLVAVVGASGSGKSTL 390
Cdd:COG0178 619 NNL-----------KNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
365-392 |
2.05e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 2.05e-04
10 20
....*....|....*....|....*....
gi 658756163 365 KNINLTLPAKGLVAVVGASGSGKSTL-FD 392
Cdd:COG0178 17 KNIDVDIPRNKLVVITGLSGSGKSSLaFD 45
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
365-392 |
2.16e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 2.16e-04
10 20
....*....|....*....|....*....
gi 658756163 365 KNINLTLPAKGLVAVVGASGSGKSTL-FD 392
Cdd:PRK00349 17 KNIDLDIPRDKLVVFTGLSGSGKSSLaFD 45
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
327-527 |
2.53e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 327 NAPLPE-QSQQHETKFEEHISSININNLNFTYpNSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQV---- 401
Cdd:PRK10938 239 GVQLPEpDEPSARHALPANEPRIVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGysnd 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 402 --------------------IEQISiNNKPLDATSMSTLQNAIawipqTPTLF-----YQSISDnikiakpaatqleleq 456
Cdd:PRK10938 318 ltlfgrrrgsgetiwdikkhIGYVS-SSLHLDYRVSTSVRNVI-----LSGFFdsigiYQAVSD---------------- 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 457 aAHQAGALDFINTLenGFDTLIGEQG-EGLSGGQkQRIAL-ARAFLKQAPILVLDEPTAHLDSQTEQLIQQAI 527
Cdd:PRK10938 376 -RQQKLAQQWLDIL--GIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV 444
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
364-516 |
4.74e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 41.94 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNINLTLpAKG-LVAVVGASGSGKSTLFDCLLGFhpqvIE----QISINNKplDATSMSTLQNA---IAWIPQTPTLFY 435
Cdd:COG1137 19 VKDVSLEV-NQGeIVGLLGPNGAGKTTTFYMIVGL----VKpdsgRIFLDGE--DITHLPMHKRArlgIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 436 Q-SISDNIKIAkpaatqLEL-----EQAAHQAGAL--DFintlenGFDTLIGEQGEGLSGGQKQRIALARAfLKQAP--I 505
Cdd:COG1137 92 KlTVEDNILAV------LELrklskKEREERLEELleEF------GITHLRKSKAYSLSGGERRRVEIARA-LATNPkfI 158
|
170
....*....|.
gi 658756163 506 LvLDEPTAHLD 516
Cdd:COG1137 159 L-LDEPFAGVD 168
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
363-558 |
4.90e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 363 GIK---NINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHP------------QVIEQISINNKplDATSMSTLQNAIAWI 427
Cdd:NF040905 13 GVKaldDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsyegeilfdgEVCRFKDIRDS--EALGIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 428 PqtptlfYQSISDNIKIAKPAATQ--LELEQAAHQAGALDFINTLENGFDTLIGEQGEGlsggQKQRIALARAFLKQAPI 505
Cdd:NF040905 91 P------YLSIAENIFLGNERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVG----KQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 506 LVLDEPTAHL---DSQT-----EQLIQQAINKyaknhlvLVIAHRLNTV-KNASNILVMQNG 558
Cdd:NF040905 161 LILDEPTAALneeDSAAlldllLELKAQGITS-------IIISHKLNEIrRVADSITVLRDG 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
348-574 |
5.33e-04 |
|
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: 43.08 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 348 ININNLNFTYP-NSNEGIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLGFHPQVIEQISINNKPLdATSMSTLQNAIAW 426
Cdd:TIGR01257 1938 LRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 427 IPQtptlfYQSISDNIKIAK-----------PAAtqlELEQAAHQAgaldfINTLenGFDTLIGEQGEGLSGGQKQRIAL 495
Cdd:TIGR01257 2017 CPQ-----FDAIDDLLTGREhlylyarlrgvPAE---EIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLST 2081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 496 ARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKN-HLVLVIAHRLNTVKN-ASNILVMQNGEIAQQGTYSQLEQQQ 573
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
.
gi 658756163 574 G 574
Cdd:TIGR01257 2162 G 2162
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
469-550 |
6.08e-04 |
|
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: 41.14 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 469 TLENG-FDTLIGEQGEGLSGGQKQRIALARAF----LKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHL-VLVIAHR 542
Cdd:cd03239 78 TFDKSyFLVLQGKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSqFIVITLK 157
|
....*...
gi 658756163 543 LNTVKNAS 550
Cdd:cd03239 158 KEMFENAD 165
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
485-577 |
6.87e-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: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 LSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVI--AHRLNTVKN-ASNILVMQNGEIA 561
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILltSHDMDDIEAlCDRVIVIDHGRII 234
|
90
....*....|....*.
gi 658756163 562 QQGTYSQLEQQQGAFK 577
Cdd:COG4586 235 YDGSLEELKERFGPYK 250
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
364-394 |
8.02e-04 |
|
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: 42.69 E-value: 8.02e-04
10 20 30
....*....|....*....|....*....|..
gi 658756163 364 IKNINLTLPAKGLVAVVGASGSGKSTL-FDCL 394
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSLaFDTI 43
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
49-281 |
9.65e-04 |
|
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: 41.39 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 49 YLLAQTIhNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTKLTHLGPSYIEQHGQGAT 128
Cdd:cd18557 17 YLIGRLI-DTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 129 LNTVHDGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGSKAEALNQKRWQQLAVLG 208
Cdd:cd18557 96 TSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658756163 209 NYFFDRVQGLTQLKLFNatqQELKQIAKisddFRHATLGVLKIAFLSSFALEFLATISVALVAVIIGFRLFFG 281
Cdd:cd18557 176 QVAEESLSNIRTVRSFS---AEEKEIRR----YSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
32-285 |
1.01e-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: 41.23 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 32 LSIALGTFNAILMIAGAYLLAQTIhNVMFEGASLSQVTHFLWPLAGIILLRALFLAISERLSAYAALKIKSAMRQTLLTK 111
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADII-DEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 112 LTHLGPSYIEQHGQgATL--NTVHDgVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILV 189
Cdd:cd18548 82 IQSFSFAEIDKFGT-SSLitRLTND-VTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 190 GSKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATQQELKQIAKISDDFRHATLGVLKIAFLSSFALEFLATISVAL 269
Cdd:cd18548 160 MKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVA 239
|
250
....*....|....*.
gi 658756163 270 VAVIIGFRLFFGTLDF 285
Cdd:cd18548 240 ILWFGGHLINAGSLQV 255
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
488-546 |
1.31e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 1.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658756163 488 GQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYakNHLVLVIAH-R--LNTV 546
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNER--NSTMIIISHdRhfLNSV 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
363-569 |
1.94e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.29 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 363 GIKNINLTLPAKGLVAVVGASGSGKSTLFDCLLG-FHPQV--IEQISINNKPLDATSMSTlqnaiawiPQTPTLF----- 434
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDAgeVHYRMRDGQLRDLYALSE--------AERRRLLrtewg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 435 --YQSISDNIKIAKPA----ATQLELEQAAH----QAGALDFINTLENGFDTlIGEQGEGLSGGQKQRIALARAfLKQAP 504
Cdd:PRK11701 93 fvHQHPRDGLRMQVSAggniGERLMAVGARHygdiRATAGDWLERVEIDAAR-IDDLPTTFSGGMQQRLQIARN-LVTHP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 505 ILVL-DEPTAHLD-SQTEQLIQQAINKYAKNHL-VLVIAHRLNTVKN-ASNILVMQNGEIAQQG-----------TYSQL 569
Cdd:PRK11701 171 RLVFmDEPTGGLDvSVQARLLDLLRGLVRELGLaVVIVTHDLAVARLlAHRLLVMKQGRVVESGltdqvlddpqhPYTQL 250
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
485-572 |
2.32e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 LSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLV-IAHRLNTVKN-ASNILVMQNGEIAQ 562
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAE 215
|
90
....*....|
gi 658756163 563 QGTYSQLEQQ 572
Cdd:PRK10938 216 TGEREEILQQ 225
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
485-571 |
2.63e-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: 40.77 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 LSGGQKQRIALAraflKQ------APILVLDEPTAHLDSQ-TEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNILVM-- 555
Cdd:TIGR00630 489 LSGGEAQRIRLA----TQigsgltGVLYVLDEPSIGLHQRdNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIgp 564
|
90 100
....*....|....*....|
gi 658756163 556 ----QNGEIAQQGTYSQLEQ 571
Cdd:TIGR00630 565 gageHGGEVVASGTPEEILA 584
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
479-575 |
2.80e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 479 GEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKN-HLVLVIAHRLNTVKN-ASNILVMQ 556
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|....*....
gi 658756163 557 NGEIAQQGTYSQLEQQQGA 575
Cdd:NF000106 219 RGRVIADGKVDELKTKVGG 237
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
485-549 |
3.51e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 3.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658756163 485 LSGGQKQRIALARAFLKQAP---ILVLDEPTA--HLDsQTEQLIqQAINKY-AKNHLVLVIAHRLNTVKNA 549
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTglHFH-DIRKLL-EVLHRLvDKGNTVVVIEHNLDVIKTA 895
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
478-527 |
3.52e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 3.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 658756163 478 IGEQGEGLSGGQKQRIALARAFLKQAPILVLDEPTAHLDSQTEQLIQQAI 527
Cdd:PRK10636 424 VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
364-541 |
4.50e-03 |
|
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: 39.11 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 364 IKNI----NLTL-PAKGLVAVVGASGSGKSTLFDC---LLGFHPQ-----------VIEQI-SINNKPL----------- 412
Cdd:cd03241 6 IKNFalieELELdFEEGLTVLTGETGAGKSILLDAlslLLGGRASadlirsgaekaVVEGVfDISDEEEakalllelgie 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 413 --DATSMSTLQNA----IAWIPQTP---TLFYQSISDNIKIAKPAATQLELEQAAHQaGALDF-INTLENGFDTLIGEQG 482
Cdd:cd03241 86 ddDDLIIRREISRkgrsRYFINGQSvtlKLLRELGSLLVDIHGQHDHQNLLNPERQL-DLLDGgLDDVEFLFSTNPGEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658756163 483 ----EGLSGGQKQRIALA----RAFLKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAH 541
Cdd:cd03241 165 kplaKIASGGELSRLMLAlkaiLARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCITH 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
483-562 |
5.08e-03 |
|
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: 40.05 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 483 EGLSGGQKQRIALARAF----LKQAPILVLDEPTAHLDSQTEQLIQQAINKYAKNHLVLVIAHRLNTVKNASNIL--VMQ 556
Cdd:TIGR02169 1073 EAMSGGEKSLTALSFIFaiqrYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIgvTMR 1152
|
....*.
gi 658756163 557 NGEIAQ 562
Cdd:TIGR02169 1153 RNGESQ 1158
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
362-394 |
5.82e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.14 E-value: 5.82e-03
10 20 30
....*....|....*....|....*....|....
gi 658756163 362 EGIKNI-NLTLPAKGLVAVVGASGSGKSTLFDCL 394
Cdd:COG4637 8 KNFKSLrDLELPLGPLTVLIGANGSGKSNLLDAL 41
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
485-565 |
6.03e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658756163 485 LSGGQKQRIALARAFLKQA---PILVLDEPTA--HLDSqteqliqqaINKYAK--NHLV------LVIAHRLNTVKNASN 551
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTglHFED---------IRKLLEvlHRLVdkgntvVVIEHNLDVIKTADW 901
|
90 100
....*....|....*....|
gi 658756163 552 ILVM------QNGEIAQQGT 565
Cdd:PRK00349 902 IIDLgpeggdGGGEIVATGT 921
|
|
| |
