|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-568 |
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: 570.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 2 IDKRLFKL-PGLTLTLIWVTILTGIQGIAIICQAHFLTRALVNSW-QMKPLATLTTAIILFGGAFLLRHVCVWLKNIILD 79
Cdd:COG4988 4 LDKRLKRLaRGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 80 HYADHTSNLLRDRLLDQVYVTGANQIAQTGTGKLVTVALDGINNVYNYFNLIFAKIFDMMIIPFLVIIYIYWQSVRSGII 159
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 160 LTIVFPVVILFMIILGFAAQDKADRQYAGFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAIL 239
Cdd:COG4988 164 LLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 240 STFALDWFTTLSIALLALFLGLALINGSMPLFPALVSLILAPEFFLPIRDFGNDYHATLDGKNALGDILDILDQPtIQNR 319
Cdd:COG4988 244 SSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAP-EPAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 320 ELVSDSFHWDANSTLTANHFNLQYNPDNAyqiDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDN 399
Cdd:COG4988 323 PAGTAPLPAAGPPSIELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP------YSGS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 400 FTLNGQALPHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRG 479
Cdd:COG4988 394 ILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 480 ISGGQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQ 559
Cdd:COG4988 474 LSGGQAQRLALARALL-RDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
....*....
gi 2159754173 560 GPVAELAQQ 568
Cdd:COG4988 553 GTHEELLAK 561
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-551 |
6.30e-156 |
|
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: 457.52 E-value: 6.30e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 14 LTLIWVTILTGIQGIAIICQAHFLTRALVNSW-QMKPLATLTTAIILFGGAFLLRHVCVWLKNIILDHYADHTSNLLRDR 92
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLIsAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 93 LLDQVYVTGANQIAQTGTGKLVTVALDGINNVYNYFNLIFAKIFDMMIIPFLVIIYIYWQSVRSGIILTIVFPVVILFMI 172
Cdd:TIGR02857 83 LLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 173 ILGFAAQDKADRQYAGFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAILSTFALDWFTTLSI 252
Cdd:TIGR02857 163 LIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 253 ALLALFLGLALINGSMPLFPALVSLILAPEFFLPIRDFGNDYHATLDGKNALGDILDILD---QPTIQNRELVSDSFhwd 329
Cdd:TIGR02857 243 ALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDaapRPLAGKAPVTAAPA--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 330 anSTLTANHFNLQY-NPDNAyqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQALP 408
Cdd:TIGR02857 320 --SSLEFSGVSVAYpGRRPA----LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP---TEGSI---AVNGVPLA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 409 HLSQANWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRI 488
Cdd:TIGR02857 388 DADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 489 ALARAFLDqDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVM 551
Cdd:TIGR02857 468 ALARAFLR-DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-579 |
8.25e-106 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 330.27 E-value: 8.25e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 20 TILTG-IQGIAIICQAHFLTRAL-----VNSwqmkPLATLTTAIILFGGAFLLRHVCVWLKNIILDHYADHTSNLLRDRL 93
Cdd:PRK11174 27 SILLGfLSGLLLIAQAWLLATILqaliiENI----PREALLPPFILLILLFVLRALLAWLRERVGFKAGQHIRQQIRQQV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 94 LDQVYVTGANQIAQTGTGKLVTVALDGINNVYNYFNLIFAKIFDMMIIPFLVIIYIYWQSVRSGIILTIVFPVVILFMII 173
Cdd:PRK11174 103 LDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTAPLIPLFMAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 174 LGFAAQDKADRQYAGFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAILSTFALDWFTTLSIA 253
Cdd:PRK11174 183 VGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASISIA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 254 LLALFLGLALI--------NGSMPLFPALVSLILAPEFFLPIRDFGNDYHATLDGKNALGDILDILDQPTIQNRElVSDS 325
Cdd:PRK11174 263 LVAVYFGFSYLgelnfghyGTGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQ-GEKE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 326 FHWDANSTLTANHFNLqYNPDNayQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLtpmlktqSQTDNFTLNGQ 405
Cdd:PRK11174 342 LASNDPVTIEAEDLEI-LSPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-------PYQGSLKINGI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 406 ALPHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQA 485
Cdd:PRK11174 412 ELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQA 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 486 QRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAEL 565
Cdd:PRK11174 492 QRLALARALL-QPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
570
....*....|....
gi 2159754173 566 AQQPnGEFKALTEH 579
Cdd:PRK11174 571 SQAG-GLFATLLAH 583
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-576 |
1.09e-91 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 293.22 E-value: 1.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 4 KRLFKL-----PGLTLTLIWVTILTGIQGIAIICQAHFLTRALVNswqmKPLATLTTAIILFGGAFLLRHVCVWLKNIIL 78
Cdd:COG1132 10 RRLLRYlrpyrGLLILALLLLLLSALLELLLPLLLGRIIDALLAG----GDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 79 DHYADHTSNLLRDRLLDQVYVTGANQIAQTGTGKLVTVALDGINNVYNYFNLIFAKIFDMMIIPFLVIIYIYWQSVRSGI 158
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 159 ILTIVFPVVILFMIILGFAAQDKADRQYAGFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAI 238
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 239 LSTFALDWFTTLSIALLALFLGLALINGSMPLfPALVSLI-LAPEFFLPIRDFGNDYHATLDGKNALGDILDILDQP-TI 316
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTV-GDLVAFIlYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPpEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 317 QNRELVSDSFhwDANSTLTANHFNLQYNPDnayQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQ 396
Cdd:COG1132 325 PDPPGAVPLP--PVRGEIEFENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP------T 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 397 TDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVgeg 476
Cdd:COG1132 394 SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVger 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 477 grgisggQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQI 556
Cdd:COG1132 474 gvnlsggQRQRIAIARALL-KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
570 580
....*....|....*....|
gi 2159754173 557 VQQGPVAELAQQpNGEFKAL 576
Cdd:COG1132 553 VEQGTHEELLAR-GGLYARL 571
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
19-307 |
2.34e-90 |
|
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: 280.45 E-value: 2.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 19 VTILTGIQGIAIICQAHFLTRALVNSW-QMKPLATLTTAIILFGGAFLLRHVCVWLKNIILDHYADHTSNLLRDRLLDQV 97
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFlEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 98 YVTGANQIAQTGTGKLVTVALDGINNVYNYFNLIFAKIFDMMIIPFLVIIYIYWQSVRSGIILTIVFPVVILFMIILGFA 177
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 178 AQDKADRQYAGFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAILSTFALDWFTTLSIALLAL 257
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2159754173 258 FLGLALINGSMPLFPALVSLILAPEFFLPIRDFGNDYHATLDGKNALGDI 307
Cdd:cd18584 241 YIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
144-579 |
2.02e-73 |
|
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: 245.06 E-value: 2.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 144 LVIIYIYWQSVRSGIILTIVFPVVILFMIILGFAAQDKADRQYA-GFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEV 222
Cdd:COG4987 145 AAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAaARAALRARLTDLLQGAAELAAYGALDRALARLDAA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 223 SEDYRRSTMDTLRIAILSTFALDWFTTLSIALLALFLGLALINGSMPlFPALVSLILAP----EFFLPIRDFGNDYHATL 298
Cdd:COG4987 225 EARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAAlalfEALAPLPAAAQHLGRVR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 299 DgknALGDILDILDQPTiqNRELVSDSFHWDANSTLTANHFNLQYnpDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKST 378
Cdd:COG4987 304 A---AARRLNELLDAPP--AVTEPAEPAPAPGGPSLELEDVSFRY--PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKST 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 379 LLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGL 458
Cdd:COG4987 377 LLALLLRFLDP------QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGL 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 459 ADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHR 538
Cdd:COG4987 451 GDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALL-RDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR 529
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2159754173 539 LHWLKEMDYVIVMKDGQIVQQGPVAELAQQpNGEFKALTEH 579
Cdd:COG4987 530 LAGLERMDRILVLEDGRIVEQGTHEELLAQ-NGRYRQLYQR 569
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-576 |
1.57e-71 |
|
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: 243.20 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 4 KRLFKLPGLTLTLIWVTILTGIQGIAIIcqahFLTRALVNS-WQMKPLATLTTAIILFGGAFLLRHVCVWLKNIILDH-- 80
Cdd:COG2274 149 RLLRRYRRLLLQVLLASLLINLLALATP----LFTQVVIDRvLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRlg 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 81 ----------YADHtsnLLRDRL--LDQVYV-------TGANQIAQTGTGKLVTVALDGInnvynyfnlifakifdMMII 141
Cdd:COG2274 225 qridlrlssrFFRH---LLRLPLsfFESRSVgdlasrfRDVESIREFLTGSLLTALLDLL----------------FVLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 142 pFLVIIYIYwqsvrsGIILTIVFPVVILFMIILGFAAQDK-ADRQYAGFI---KLSNHFVDSLRGLATLKFLGLSKRYET 217
Cdd:COG2274 286 -FLIVLFFY------SPPLALVVLLLIPLYVLLGLLFQPRlRRLSREESEasaKRQSLLVETLRGIETIKALGAESRFRR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 218 NVYEVSEDYRRSTMDTLRIAILSTFALDWFTTLSIALLALFLGLALINGSMPL-----FPALVSLILAPefFLPIRDFGN 292
Cdd:COG2274 359 RWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLgqliaFNILSGRFLAP--VAQLIGLLQ 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 293 DYHATLDGKNALGDILDILDQPTIQNRELVSDSFHwdanSTLTANHFNLQYNPDNAYQidLKDISFTLHGYQKVAIIGMS 372
Cdd:COG2274 437 RFQDAKIALERLDDILDLPPEREEGRSKLSLPRLK----GDIELENVSFRYPGDSPPV--LDNISLTIKPGERVAIVGRS 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 373 GSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAA 452
Cdd:COG2274 511 GSGKSTLLKLLLGLYEP------TSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEA 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 453 VVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLV 532
Cdd:COG2274 585 ARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALL-RNPRILILDEATSALDAETEAIILENLRRLLKGRTV 663
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2159754173 533 LFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQpNGEFKAL 576
Cdd:COG2274 664 IIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAEL 706
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
334-555 |
7.51e-50 |
|
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: 169.87 E-value: 7.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAYQidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQA 413
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP------TSGEILIDGVDLRDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 414 NWQKQFSFIPQFPYLFADTIAANIkfyrpeateaevqaavvkagladfvasLKDGlatkvgeggrgisggQAQRIALARA 493
Cdd:cd03228 73 SLRKNIAYVPQDPFLFSGTIRENI---------------------------LSGG---------------QRQRIAIARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 494 FLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQ 555
Cdd:cd03228 111 LL-RDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
337-576 |
1.30e-48 |
|
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: 168.95 E-value: 1.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 337 NHFNLQYNPDNayQIdLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQ 416
Cdd:cd03253 4 ENVTFAYDPGR--PV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDV------SSGSILIDGQDIREVTLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 417 KQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLd 496
Cdd:cd03253 75 RAIGVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAIL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 497 QDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAqQPNGEFKAL 576
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEM 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
340-568 |
7.97e-48 |
|
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: 166.63 E-value: 7.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNayqIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQF 419
Cdd:cd03254 9 NFSYDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDP------QKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 SFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDR 499
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAML-RDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 500 RILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-539 |
5.11e-46 |
|
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: 169.85 E-value: 5.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 4 KRLFKLPGLTLTL-IWVTILTGIQGIAII-CQAHFLTRAlvnsWQMKPLATLTTAIILFGGAFLLRHVCVWLKNIILDHY 81
Cdd:TIGR02868 5 LPLLKPRRRRLALaVLLGALALGSAVALLgVSAWLISRA----AEMPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGHDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 82 ADHTSNLLRDRLLDQVYVTGANQIAQTGTGKLVTVALDGINNVYNyfnLIFAKIFDMmIIPFLVII----YIYWQSVRSG 157
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQD---LYVRVIVPA-GVALVVGAaavaAIAVLSVPAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 158 IILTIVFPVVILFM-IILGFAAQDKADRQYAGFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRI 236
Cdd:TIGR02868 157 LILAAGLLLAGFVApLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 237 AILSTFALDWFTTLSIALLALFLGLALINGSMP--LFPALVSLILAP-EFFLPIRDFGNDYHAtldGKNALGDILDILDQ 313
Cdd:TIGR02868 237 TALGAALTLLAAGLAVLGALWAGGPAVADGRLApvTLAVLVLLPLAAfEAFAALPAAAQQLTR---VRAAAERIVEVLDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 314 PtiqnRELVSDSFHWDANS-----TLTANHFNLQYNPDnayQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLT 388
Cdd:TIGR02868 314 A----GPVAEGSAPAAGAVglgkpTLELRDLSAGYPGA---PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 389 PmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDG 468
Cdd:TIGR02868 387 P------LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDG 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 469 LATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRL 539
Cdd:TIGR02868 461 LDTVLGEGGARLSGGERQRLALARALL-ADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
353-576 |
1.36e-44 |
|
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: 158.16 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADT 432
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV------DSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLD 512
Cdd:cd03251 92 VAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALL-KDPPILILDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 513 IETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQpNGEFKAL 576
Cdd:cd03251 171 TESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
337-561 |
5.33e-42 |
|
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: 150.72 E-value: 5.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 337 NHFNLQYNPDNAYQidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLggF-LTPMLKTQsqtdnFTLNGQALPHLSQANW 415
Cdd:cd03244 6 KNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLAL--FrLVELSSGS-----ILIDGVDISKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 416 QKQFSFIPQFPYLFADTIAANIKFYRpEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFL 495
Cdd:cd03244 77 RSRISIIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 496 dQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGP 561
Cdd:cd03244 156 -RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
346-560 |
2.33e-41 |
|
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: 148.89 E-value: 2.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 346 DNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQALPHLSQANWQKQFSFIPQF 425
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKP---TSGSV---LLDGTDIRQLDPADLRRNIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFD 505
Cdd:cd03245 87 VTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL-NDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2159754173 506 EPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQG 560
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
353-578 |
3.17e-41 |
|
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: 149.23 E-value: 3.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADT 432
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP------TSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLD 512
Cdd:cd03249 93 IAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL-RNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 513 IETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQpNGEFKALTE 578
Cdd:cd03249 172 AESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVK 236
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
340-568 |
1.61e-39 |
|
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: 153.87 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLSQANWQKQF 419
Cdd:TIGR03375 468 NVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQP---TEGS---VLLDGVDIRQIDPADLRRNI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 SFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDR 499
Cdd:TIGR03375 542 GYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALL-RDP 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 500 RILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:TIGR03375 621 PILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
27-296 |
2.82e-39 |
|
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: 145.50 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 27 GIAIICQAHFLTRALVNSWQMKPLATLTTAIILFGGAFLLRHVCVWLKNIILDHYADHTSNLLRDRLLDQVYVTGANQIA 106
Cdd:cd18561 9 TALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 107 QTGTGKLVTVALDGINNVYNYFNLIFAKIFDMMIIPFLVIIYIYWQSVRSGIILTIVFPVVILFMIILGFAAQDKADRQY 186
Cdd:cd18561 89 GERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 187 AGFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAILSTFALDWFTTLSIALLALFLGLALING 266
Cdd:cd18561 169 AAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGG 248
|
250 260 270
....*....|....*....|....*....|
gi 2159754173 267 SMPLFPALVSLILAPEFFLPIRDFGNDYHA 296
Cdd:cd18561 249 QLTLSSLLLILFLSREFFRPLRDLGAYWHA 278
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
301-576 |
7.66e-38 |
|
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: 148.04 E-value: 7.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 301 KNALGDI---LDILDQ-PTIQNR----ELVSDsfhwdaNSTLTANHFNLQYNPDNayQIdLKDISFTLHGYQKVAIIGMS 372
Cdd:COG5265 323 RQALADMermFDLLDQpPEVADApdapPLVVG------GGEVRFENVSFGYDPER--PI-LKGVSFEVPAGKTVAIVGPS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 373 GSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAA 452
Cdd:COG5265 394 GAGKSTLARLLFRFYDV------TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 453 VVKAGLADFVASLKDGLATKVgeggrgisggqaQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLV 532
Cdd:COG5265 468 ARAAQIHDFIESLPDGYDTRVgerglklsggekQRVAIARTLL-KNPPILIFDEATSALDSRTERAIQAALREVARGRTT 546
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2159754173 533 LFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQpNGEFKAL 576
Cdd:COG5265 547 LVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQM 589
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
338-568 |
1.47e-36 |
|
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: 143.69 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 338 HFNLQYNPDnayQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQK 417
Cdd:TIGR02204 344 NFAYPARPD---QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDP------QSGRILLDGVDLRQLDPAELRA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 418 QFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQ 497
Cdd:TIGR02204 415 RMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAIL-K 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:TIGR02204 494 DAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
104-568 |
8.72e-35 |
|
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: 139.88 E-value: 8.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 104 QIAQTGTGKLVTVALDginnvynyfnLIFAKIFdmmiipflVIIYIYWQSVRSGIILtIVFPVVILFMIILGFAAQDKAD 183
Cdd:TIGR01846 247 QIRNFLTGSALTVVLD----------LLFVVVF--------LAVMFFYSPTLTGVVI-GSLVCYALLSVFVGPILRKRVE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 184 RQYAGFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAILSTFALDWFTTLSIALLALFLGLAL 263
Cdd:TIGR01846 308 DKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLV 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 264 INGSMPL-----FPALVSLILAPefFLPIRDFGNDYHATLDGKNALGDILDILDQPTIQNRELVSDsfhwdANSTLTANH 338
Cdd:TIGR01846 388 IGGALSPgqlvaFNMLAGRVTQP--VLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAALPE-----LRGAITFEN 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 339 FNLQYNPDNAYQIDlkDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQ 418
Cdd:TIGR01846 461 IRFRYAPDSPEVLS--NLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTP------QHGQVLVDGVDLAIADPAWLRRQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 419 FSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLDqD 498
Cdd:TIGR01846 533 MGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVG-N 611
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 499 RRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL 681
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
334-560 |
4.18e-34 |
|
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: 127.43 E-value: 4.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYnPDNAYQIdLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGqALPHLSQA 413
Cdd:cd03247 1 LSINNVSFSY-PEQEQQV-LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP------QQGEITLDG-VPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 414 NWQKQFSFIPQFPYLFADTIAANIKfyrpeateaevqaavvkagladfvASLKDGlatkvgeggrgisggQAQRIALARA 493
Cdd:cd03247 72 ALSSLISVLNQRPYLFDTTLRNNLG------------------------RRFSGG---------------ERQRLALARI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 494 FLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQG 560
Cdd:cd03247 113 LL-QDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
334-565 |
1.33e-32 |
|
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: 125.29 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAYQidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQALPHLSQA 413
Cdd:cd03252 1 ITFEHVRFRYKPDGPVI--LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP---ENGRV---LVDGHDLALADPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 414 NWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARA 493
Cdd:cd03252 73 WLRRQVGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 494 fLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAEL 565
Cdd:cd03252 153 -LIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
307-579 |
1.47e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 132.26 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 307 ILDILDQ-PTIQnrelvsdsfhWDANSTLTANHFNLQYN------PDNAyQIDLKDISFTLHGYQKVAIIGMSGSGKSTL 379
Cdd:PRK11160 314 INEITEQkPEVT----------FPTTSTAAADQVSLTLNnvsftyPDQP-QPVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 380 LNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLA 459
Cdd:PRK11160 383 LQLLTRAWDP------QQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 460 DFVASlKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRL 539
Cdd:PRK11160 457 KLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALL-HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRL 534
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2159754173 540 HWLKEMDYVIVMKDGQIVQQGPVAELAQQpNGEFKALTEH 579
Cdd:PRK11160 535 TGLEQFDRICVMDNGQIIEQGTHQELLAQ-QGRYYQLKQR 573
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
353-576 |
4.06e-32 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 130.91 E-value: 4.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLtpmlktQSQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADT 432
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY------DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRPEA-TEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHL 511
Cdd:PRK11176 433 IANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL-RDSPILILDEATSAL 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159754173 512 DIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQpNGEFKAL 576
Cdd:PRK11176 512 DTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ-NGVYAQL 575
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
353-569 |
9.56e-31 |
|
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: 126.40 E-value: 9.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADT 432
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP------TAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANI-KFyrPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLDqDRRILMFDEPTAHL 511
Cdd:COG4618 422 IAENIaRF--GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG-DPRLVVLDEPNSNL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 512 DIETEYALKETMKPLfKDH--LVLFATHRLHWLKEMDYVIVMKDGQIVQQGP----VAELAQQP 569
Cdd:COG4618 499 DDEGEAALAAAIRAL-KARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPrdevLARLARPA 561
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
338-576 |
1.46e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 127.15 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 338 HFNLQYNPDNayQIdLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLSQANWQK 417
Cdd:TIGR00958 485 SFSYPNRPDV--PV-LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP---TGGQ---VLLDGVPLVQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 418 QFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAfLDQ 497
Cdd:TIGR00958 556 QVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARA-LVR 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKplFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQPnGEFKAL 576
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHL 710
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
353-569 |
2.08e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 125.60 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLggfltpmlktQSQTD----NFTLNGQALPHLSQANWQKQFSFIPQFPYL 428
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLI----------QRHFDvsegDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 FADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPT 508
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALL-LNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 509 AHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
353-576 |
5.48e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 124.69 E-value: 5.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADT 432
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDP------QSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLD 512
Cdd:PRK13657 425 IEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALL-KDPPILILDEATSALD 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 513 IETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQpNGEFKAL 576
Cdd:PRK13657 504 VETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR-GGRFAAL 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
353-556 |
6.86e-30 |
|
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: 117.19 E-value: 6.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADT 432
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQP------QGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLD 512
Cdd:cd03248 104 LQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI-RNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2159754173 513 IETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQI 556
Cdd:cd03248 183 AESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
331-579 |
3.33e-29 |
|
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: 122.93 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 331 NSTLTANHFNLQYN-PDNAyqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLtpmlktQSQTDNFTLNGQALPH 409
Cdd:TIGR01193 471 NGDIVINDVSYSYGyGSNI----LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF------QARSGEILLNGFSLKD 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 410 LSQANWQKQFSFIPQFPYLFADTIAANIKF-YRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRI 488
Cdd:TIGR01193 541 IDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRI 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 489 ALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLfKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:TIGR01193 621 ALARALL-TDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
250
....*....|.
gi 2159754173 569 pNGEFKALTEH 579
Cdd:TIGR01193 699 -NGFYASLIHN 708
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
340-568 |
1.30e-28 |
|
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: 120.15 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMlktqsqTDNFTLNGQALPHLSQANWQKQF 419
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPT------SGSVRLDGADLKQWDRETFGKHI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 SFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDR 499
Cdd:TIGR01842 395 GYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALY-GDP 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 500 RILMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKALKARGItVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
334-565 |
2.13e-28 |
|
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: 113.99 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAyqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQA 413
Cdd:COG1120 2 LEAENLSVGYGGRPV----LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP------SSGEVLLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 414 NWQKQFSFIPQ-----FPYLFADTIA----ANIKFYRPEATE--AEVQAAVVKAGLADF----VASLKDGlatkvgeggr 478
Cdd:COG1120 72 ELARRIAYVPQeppapFGLTVRELVAlgryPHLGLFGRPSAEdrEAVEEALERTGLEHLadrpVDELSGG---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 479 gisggQAQRIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRL-HWLKEMDYVIVMKDGQ 555
Cdd:COG1120 142 -----ERQRVLIARA-LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLnLAARYADRLVLLKDGR 215
|
250
....*....|
gi 2159754173 556 IVQQGPVAEL 565
Cdd:COG1120 216 IVAQGPPEEV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-555 |
3.60e-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: 112.18 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 337 NHFNLQYNPDNAYQidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQ 416
Cdd:cd03225 3 KNLSFSYPDGARPA--LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP------TSGEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 417 KQFSFIPQFP--YLFADTIAANIKF------YRPEATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQ 484
Cdd:cd03225 75 RKVGLVFQNPddQFFGPTVEEEVAFglenlgLPEEEIEERVEEALELVGLEGLrdrsPFTLSGG---------------Q 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 485 AQRIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHWLKE-MDYVIVMKDGQ 555
Cdd:cd03225 140 KQRVAIAGV-LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
353-560 |
1.18e-27 |
|
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: 109.45 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQfpylfadt 432
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP------SSGEILLDGKDLASLSPKELARKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 iaanikfyrpeateaevqaAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAFLdQDRRILMFDEPT 508
Cdd:cd03214 81 -------------------ALELLGLAHLadrpFNELSGG---------------ERQRVLLARALA-QEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2159754173 509 AHLDIETEYALKETMKPLFKDH--LVLFATHRL-HWLKEMDYVIVMKDGQIVQQG 560
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERgkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
340-556 |
1.48e-27 |
|
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: 109.23 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQF 419
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP------TSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 SFIPQFPYLFADTIAANIkfyrpeateaevqaavvkagladfvasLKDGlatkvgeggrgisggQAQRIALARAFLdQDR 499
Cdd:cd03246 79 GYLPQDDELFSGSIAENI---------------------------LSGG---------------QRQRLGLARALY-GNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 500 RILMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHWLKEMDYVIVMKDGQI 556
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGAtRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
353-584 |
4.59e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 117.19 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLntlggfLTPMLKTQSQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADT 432
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLL------LTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRpEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLDQDRRILMFDEPTAHLD 512
Cdd:PTZ00243 1400 VRQNVDPFL-EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILMDEATANID 1478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 513 IETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQPNGEFKALTEHMRKRV 584
Cdd:PTZ00243 1479 PALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEALGRSE 1550
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
353-565 |
6.65e-27 |
|
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: 108.96 E-value: 6.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFP--YLFA 430
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP------TSGEVLVDGKDITKKNLRELRRKVGLVFQNPddQLFA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 431 DTIAANIKF------YRPEATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAfLDQDRR 500
Cdd:COG1122 91 PTVEEDVAFgpenlgLPREEIRERVEEALELVGLEHLadrpPHELSGG---------------QKQRVAIAGV-LAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 501 ILMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAEL 565
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREV 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
328-568 |
7.22e-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: 116.58 E-value: 7.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 328 WDANSTLTANHFNLQYNPDnaYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLlnTLGGFLTpmlkTQSQTDNFTLNGQAL 407
Cdd:TIGR00957 1279 WPPRGRVEFRNYCLRYRED--LDLVLRHINVTIHGGEKVGIVGRTGAGKSSL--TLGLFRI----NESAEGEIIIDGLNI 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 408 PHLSQANWQKQFSFIPQFPYLFADTIAANIKFYrPEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQR 487
Cdd:TIGR00957 1351 AKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPF-SQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQL 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 488 IALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLkeMDY--VIVMKDGQIVQQGPVAEL 565
Cdd:TIGR00957 1430 VCLARALL-RKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI--MDYtrVIVLDKGEVAEFGAPSNL 1506
|
...
gi 2159754173 566 AQQ 568
Cdd:TIGR00957 1507 LQQ 1509
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
334-556 |
1.77e-26 |
|
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: 107.58 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNP-DNAYQIdLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLSQ 412
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQA-LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRP---TSGE---VRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 413 ANW----QKQFSFIPQFPYLFAD-TIAANIK----FYRPEATEAEVQAAVV--KAGLAD----FVASLKDGlatkvgegg 477
Cdd:cd03255 74 KELaafrRRHIGFVFQSFNLLPDlTALENVElpllLAGVPKKERRERAEELleRVGLGDrlnhYPSELSGG--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 478 rgisggQAQRIALARAfLDQDRRILMFDEPTAHLDIETEyalKETMKPLFK-----DHLVLFATHRLHWLKEMDYVIVMK 552
Cdd:cd03255 145 ------QQQRVAIARA-LANDPKIILADEPTGNLDSETG---KEVMELLRElnkeaGTTIVVVTHDPELAEYADRIIELR 214
|
....
gi 2159754173 553 DGQI 556
Cdd:cd03255 215 DGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
340-556 |
2.67e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.44 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNayQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQF 419
Cdd:COG4619 5 GLSFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP------TSGEIYLDGKPLSAMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 SFIPQFPYLFADTIAANIKF---YRPEA-TEAEVQAAVVKAGLADF-----VASLKDGlatkvgeggrgisggQAQRIAL 490
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFpfqLRERKfDRERALELLERLGLPPDildkpVERLSGG---------------ERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 491 ARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQI 556
Cdd:COG4619 142 IRALL-LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
353-569 |
4.02e-26 |
|
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: 112.30 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGfLTPmlKTQSQTDNFTLNGQALPHLSQANWQKQFSFIPQFPY--LFA 430
Cdd:COG1123 22 VDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLP--HGGRISGEVLLDGRDLLELSEALRGRRIGMVFQDPMtqLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 431 DTIAANIKF------YRPEATEAEVQAAVVKAGLADFVASLKDGLATkvgeggrgisgGQAQRIALARAfLDQDRRILMF 504
Cdd:COG1123 99 VTVGDQIAEalenlgLSRAEARARVLELLEAVGLERRLDRYPHQLSG-----------GQRQRVAIAMA-LALDPDLLIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 505 DEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:COG1123 167 DEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
353-559 |
1.49e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 105.13 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLSQANW----QKQFSFIPQFPYL 428
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRP---TSGE---VLIDGQDISSLSERELarlrRRHIGFVFQFFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 FAD-TIAANIKF------YRPEATEAEVQAAVVKAGLAD----FVASLKDGlatkvgeggrgisggQAQRIALARAFLdQ 497
Cdd:COG1136 98 LPElTALENVALplllagVSRKERRERARELLERVGLGDrldhRPSQLSGG---------------QQQRVAIARALV-N 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEMDYVIVMKDGQIVQQ 559
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
353-572 |
1.92e-25 |
|
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: 105.32 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQAnWQKQFSFIPQFPYLFAD- 431
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKP------DSGSILIDGEDVRKEPRE-ARRQIGVLPDERGLYDRl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKFYRP------EATEAEVQAAVVKAGLADFVASLKDGLATkvgeggrgisgGQAQRIALARAFLdQDRRILMFD 505
Cdd:COG4555 90 TVRENIRYFAElyglfdEELKKRIEELIELLGLEEFLDRRVGELST-----------GMKKKVALARALV-HDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 506 EPTAHLDIETEYALKETMKPLFK-DHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPNGE 572
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
353-569 |
8.19e-25 |
|
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: 108.07 E-value: 8.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLSQANWQ---KQFSFIPQFPY-- 427
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP---TSGS---ILFDGKDLTKLSRRSLRelrRRVQMVFQDPYss 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LF-----ADTIAANIKFYRpEATEAEVQAAVvkAGLADFV---ASLKD--------GlatkvgeggrgisggQAQRIALA 491
Cdd:COG1123 355 LNprmtvGDIIAEPLRLHG-LLSRAERRERV--AELLERVglpPDLADryphelsgG---------------QRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 492 RAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:COG1123 417 RA-LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFAN 495
|
.
gi 2159754173 569 P 569
Cdd:COG1123 496 P 496
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
334-560 |
1.37e-24 |
|
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: 102.20 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLS-- 411
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP------TSGSIIFDGKDLLKLSrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 412 -QANWQKQFSFIPQFPY-----------LFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVAS-----LKDGlatkvg 474
Cdd:cd03257 76 lRKIRRKEIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGG------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 475 eggrgisggQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVM 551
Cdd:cd03257 150 ---------QRQRVAIARALA-LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIaDRVAVM 219
|
....*....
gi 2159754173 552 KDGQIVQQG 560
Cdd:cd03257 220 YAGKIVEEG 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
348-568 |
1.76e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 107.88 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 348 AYQID---LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQ 424
Cdd:PRK10790 349 AYRDDnlvLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL------TEGEIRLDGRPLSSLSHSVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 425 FPYLFADTIAANIKFYRpEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAfLDQDRRILMF 504
Cdd:PRK10790 423 DPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV-LVQTPQILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 505 DEPTAHLDIETEYALKETMKpLFKDH--LVLFAtHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:PRK10790 501 DEATANIDSGTEQAIQQALA-AVREHttLVVIA-HRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
339-565 |
1.80e-24 |
|
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: 101.87 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 339 FNLQYNPDNAyqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGF--LTPMLKTQSQTDnftLNGQALPHLSQA--N 414
Cdd:cd03260 6 LNVYYGDKHA----LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndLIPGAPDEGEVL---LDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 415 WQKQFSFIPQFPYLFADTIAANIKF------YRP-EATEAEVQAAVVKAGLADFVASLKDGLATKVGeggrgisggQAQR 487
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYglrlhgIKLkEELDERVEEALRKAALWDEVKDRLHALGLSGG---------QQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 488 IALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAEL 565
Cdd:cd03260 150 LCLARA-LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
353-509 |
2.43e-24 |
|
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: 99.26 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLF--- 429
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP------TEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFprl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 430 --ADTIAANIKFYRPEATEAEVQAAVVKAGLadfvaSLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEP 507
Cdd:pfam00005 75 tvRENLRLGLLLKGLSKREKDARAEEALEKL-----GLGDLADRPVGERPGTLSGGQRQRVAIARALL-TKPKLLLLDEP 148
|
..
gi 2159754173 508 TA 509
Cdd:pfam00005 149 TA 150
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
340-576 |
3.70e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.98 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYnpdnAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQAnwQKQF 419
Cdd:COG3840 6 DLTY----RYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPP------DSGRILWNGQDLTALPPA--ERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 SFIPQ----FPYLfadTIAANIKF-YRP-----EATEAEVQAAVVKAGLADFV----ASLKDGlatkvgeggrgisggQA 485
Cdd:COG3840 74 SMLFQennlFPHL---TVAQNIGLgLRPglkltAEQRAQVEQALERVGLAGLLdrlpGQLSGG---------------QR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 486 QRIALARAFLdQDRRILMFDEPTAHLDIeteyALKETMKPLFKD------HLVLFATH------RLhwlkeMDYVIVMKD 553
Cdd:COG3840 136 QRVALARCLV-RKRPILLLDEPFSALDP----ALRQEMLDLVDElcrergLTVLMVTHdpedaaRI-----ADRVLLVAD 205
|
250 260
....*....|....*....|....
gi 2159754173 554 GQIVQQGPVAEL-AQQPNGEFKAL 576
Cdd:COG3840 206 GRIAADGPTAALlDGEPPPALAAY 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
328-560 |
5.35e-24 |
|
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: 100.18 E-value: 5.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 328 WDANSTLTANHFNLQYNPDNAyQIdLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQAL 407
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLP-PV-LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA------EEGKIEIDGIDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 408 PHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRpEATEAEVQAAV-VKAGLADFVASlkdglatkvgeggrgisggQAQ 486
Cdd:cd03369 73 STIPLEDLRSSLTIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALrVSEGGLNLSQG-------------------QRQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 487 RIALARAFLDQdRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQG 560
Cdd:cd03369 133 LLCLARALLKR-PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
135-565 |
1.08e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 103.45 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 135 IFDMMIIPFLVIIYIYWQSVRSGIILTIVFPVVILFMIILGF---AAQDKADRQYAGFIKLSNHFVDSLRGLATLKFLGl 211
Cdd:TIGR01271 1003 LFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYflrTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFG- 1081
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 212 skryetnvyevsedyRRSTMDTLRIAILSTFALDWFTTLS-----------IALLALFLGLALINGSMPLFPALVSLILA 280
Cdd:TIGR01271 1082 ---------------RQSYFETLFHKALNLHTANWFLYLStlrwfqmridiIFVFFFIAVTFIAIGTNQDGEGEVGIILT 1146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 281 PEF-FLPIRDFGNDYHATLDG-KNALGDILDILDQPTIQNR------------ELVSDSFH----WDANSTLTANHFNLQ 342
Cdd:TIGR01271 1147 LAMnILSTLQWAVNSSIDVDGlMRSVSRVFKFIDLPQEEPRpsggggkyqlstVLVIENPHaqkcWPSGGQMDVQGLTAK 1226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 343 YNPDNayQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLggfltpmLKTQSQTDNFTLNGQALPHLSQANWQKQFSFI 422
Cdd:TIGR01271 1227 YTEAG--RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL-------LRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVI 1297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 423 PQFPYLFADTIAANIKFYRpEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLDQdRRIL 502
Cdd:TIGR01271 1298 PQKVFIFSGTFRKNLDPYE-QWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSK-AKIL 1375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 503 MFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAEL 565
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
353-555 |
1.21e-22 |
|
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: 94.62 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQfpylfadt 432
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP------TSGEILIDGKDIAKLPLEELRRRIGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 iaanikfyrpeateaevqaavvkagladfvasLKDGlatkvgeggrgisggQAQRIALARAFLdQDRRILMFDEPTAHLD 512
Cdd:cd00267 81 --------------------------------LSGG---------------QRQRVALARALL-LNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2159754173 513 IETEYALKETMKPLFKDHL-VLFATHRLHWLKE-MDYVIVMKDGQ 555
Cdd:cd00267 113 PASRERLLELLRELAEEGRtVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
334-569 |
1.25e-22 |
|
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: 97.18 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQA 413
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP------WSGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 414 NWQKQFSFIPQFPYL-------FADTIAANIKFYRPEATEAEVQAAVVKAGLAD-----FVASLKDGlatkvgeggrgis 481
Cdd:COG1124 76 AFRRRVQMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGLPPsfldrYPHQLSGG------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 482 ggQAQRIALARAFLdQDRRILMFDEPTAHLDIETEyalKETMKpLFKDhL-------VLFATHRLHWLKEM-DYVIVMKD 553
Cdd:COG1124 143 --QRQRVAIARALI-LEPELLLLDEPTSALDVSVQ---AEILN-LLKD-LreergltYLFVSHDLAVVAHLcDRVAVMQN 214
|
250
....*....|....*.
gi 2159754173 554 GQIVQQGPVAELAQQP 569
Cdd:COG1124 215 GRIVEELTVADLLAGP 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
353-573 |
1.72e-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: 99.02 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqTD-NFTLNGQALPHLsqANWQKQFSFIPQ----FPY 427
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETP-------DSgRILLDGRDVTGL--PPEKRNVGMVFQdyalFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LfadTIAANIKF------YRPEATEAEVQAA--VVK-AGLAD-FVASLKDGlatkvgeggrgisggQAQRIALARAfLDQ 497
Cdd:COG3842 92 L---TVAENVAFglrmrgVPKAEIRARVAELleLVGlEGLADrYPHQLSGG---------------QQQRVALARA-LAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 498 DRRILMFDEPTAHLDieteYALKETMKPLFKDHL------VLFATHRLHwlkE---M-DYVIVMKDGQIVQQGPVAELAQ 567
Cdd:COG3842 153 EPRVLLLDEPLSALD----AKLREEMREELRRLQrelgitFIYVTHDQE---EalaLaDRIAVMNDGRIEQVGTPEEIYE 225
|
....*.
gi 2159754173 568 QPNGEF 573
Cdd:COG3842 226 RPATRF 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
325-555 |
2.71e-22 |
|
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: 94.84 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 325 SFHWDANSTLTANHfnlqynpdnayqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMlktqsqtdnftlNG 404
Cdd:cd03250 7 SFTWDSGEQETSFT--------------LKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKL------------SG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 405 QAlphlsqaNWQKQFSFIPQFPYLFADTIAANIKFYRPEatEAEVQAAVVKA-GLADFVASLKDGLATKVGEGGRGISGG 483
Cdd:cd03250 61 SV-------SVPGSIAYVSQEPWIQNGTIRENILFGKPF--DEERYEKVIKAcALEPDLEILPDGDLTEIGEKGINLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 484 QAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKET--MKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQ 555
Cdd:cd03250 132 QKQRISLARAVY-SDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
353-565 |
4.28e-22 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 96.46 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLggfltpmLKTQSQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADT 432
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAF-------LRLLNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRPEATEaEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLDQdRRILMFDEPTAHLD 512
Cdd:cd03289 93 FRKNLDPYGKWSDE-EIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK-AKILLLDEPSAHLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 513 IETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAEL 565
Cdd:cd03289 171 PITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
353-570 |
6.04e-22 |
|
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: 94.88 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQ---KQFSFIPQFPYLF 429
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP------DSGEVLIDGEDISGLSEAELYrlrRRMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 430 AD-TIAANIKFYRPEAT---EAEVQAAVVK----AGLADFV----ASLKDGlatkvgeggrgisggQAQRIALARAfLDQ 497
Cdd:cd03261 90 DSlTVFENVAFPLREHTrlsEEEIREIVLEkleaVGLRGAEdlypAELSGG---------------MKKRVALARA-LAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKPLfKDHL---VLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPN 570
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSL-KKELgltSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
353-560 |
9.51e-21 |
|
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: 90.66 E-value: 9.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLsqANWQKQFSFIPQFPYLFAD- 431
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP---DSGE---ILIDGRDVTGV--PPERRNIGMVFQDYALFPHl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKF-----YRPEATEAE-VQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAfLDQDRRI 501
Cdd:cd03259 88 TVAENIAFglklrGVPKAEIRArVRELLELVGLEGLlnryPHELSGG---------------QQQRVALARA-LAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 502 LMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQIVQQG 560
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
297-573 |
1.61e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 96.58 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 297 TLDGKNALGDILDILDQPT--IQNRELVSDsfhWDANSTLTANHFNLQYNPDnaYQIDLKDISFTLHGYQKVAIIGMSGS 374
Cdd:PLN03232 1199 SLNSVERVGNYIDLPSEATaiIENNRPVSG---WPSRGSIKFEDVHLRYRPG--LPPVLHGLSFFVSPSEKVGVVGRTGA 1273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 375 GKSTLLNTLGGFLtpmlktQSQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRpEATEAEVQAAVV 454
Cdd:PLN03232 1274 GKSSMLNALFRIV------ELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALE 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 455 KAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLDQDRrILMFDEPTAHLDIETEYALKETMKPLFKDHLVLF 534
Cdd:PLN03232 1347 RAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK-ILVLDEATASVDVRTDSLIQRTIREEFKSCTMLV 1425
|
250 260 270
....*....|....*....|....*....|....*....
gi 2159754173 535 ATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQPNGEF 573
Cdd:PLN03232 1426 IAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-570 |
2.72e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 90.15 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAyqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPH---- 409
Cdd:COG1121 7 IELENLTVSYGGRPV----LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP------TSGTVRLFGKPPRRarrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 410 ---LSQanwqkQFSFIPQFPYLFADTIAAN-------IKFYRPEATEAeVQAAVVKAGLADF----VASLKDGlatkvge 475
Cdd:COG1121 77 igyVPQ-----RAEVDWDFPITVRDVVLMGrygrrglFRRPSRADREA-VDEALERVGLEDLadrpIGELSGG------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 476 ggrgisggQAQRIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLfKDH--LVLFATHRLHWLKEM-DYVIVMk 552
Cdd:COG1121 144 --------QQQRVLLARA-LAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREgkTILVVTHDLGAVREYfDRVLLL- 212
|
250
....*....|....*...
gi 2159754173 553 DGQIVQQGPVAELAQQPN 570
Cdd:COG1121 213 NRGLVAHGPPEEVLTPEN 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
353-570 |
3.60e-20 |
|
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: 90.04 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQ---KQFSFIPQFPYLF 429
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP------DSGEILVDGQDITGLSEKELYelrRRIGMLFQGGALF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 430 AD-TIAANIKF---YRPEATEAEVQAAVVKA----GLADFV----ASLKDGlatkvgeggrgisggQAQRIALARAfLDQ 497
Cdd:COG1127 95 DSlTVFENVAFplrEHTDLSEAEIRELVLEKlelvGLPGAAdkmpSELSGG---------------MRKRVALARA-LAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKPLfKDHL---VLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPN 570
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIREL-RDELgltSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLASDD 234
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
18-303 |
3.73e-20 |
|
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: 91.06 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 18 WVTILTGIQGIAIICQahFLTRALVNSWqmkPLATLTTAIILFGGAFLLRHVCVWLKNIILDHYADHTSNLLRDRLLDQV 97
Cdd:cd18781 6 WISLLANIAFVFSIAN--LLQKLLEGKL---TTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 98 YVTGANQIAQTGTGKLVTVALDGINNVYNYFNLIFAKIFDMMIIPFLVIIYIYWQSVRSGIILTIVFPVVILFMIILGFA 177
Cdd:cd18781 81 LRLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 178 AQDKADRQYAGFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAILSTFALDWF----TTLSIA 253
Cdd:cd18781 161 AKKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVayggAALGII 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2159754173 254 LLALFLglalINGSMPLFPALVSLILAPEFFLPIRDFGNDYHATLDGKNA 303
Cdd:cd18781 241 LALLQF----ANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAA 286
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
351-560 |
4.74e-20 |
|
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: 88.70 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 351 IDLKDISFTLH-----------GYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQAnwQKQF 419
Cdd:cd03298 1 VRLDKIRFSYGeqpmhfdltfaQGEITAIVGPSGSGKSTLLNLIAGFETP------QSGRVLINGVDVTAAPPA--DRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 SFIPQFPYLFAD-TIAANIKF-------YRPEATEAeVQAAVVKAGLADFVASLKDGLATKvgeggrgisggQAQRIALA 491
Cdd:cd03298 73 SMLFQENNLFAHlTVEQNVGLglspglkLTAEDRQA-IEVALARVGLAGLEKRLPGELSGG-----------ERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 492 RAFLdQDRRILMFDEPTAHLDIeteyALKETMKPLFKD------HLVLFATHRLHWLKEM-DYVIVMKDGQIVQQG 560
Cdd:cd03298 141 RVLV-RDKPVLLLDEPFAALDP----ALRAEMLDLVLDlhaetkMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
353-556 |
7.30e-20 |
|
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: 87.07 E-value: 7.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQAlPHLSQANWQKQFSFIPQFPYLFAD- 431
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKP------DSGEIKVLGKD-IKKEPEEVKRRIGYLPEEPSLYENl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKFyrpeateaevqaavvkagladfvaSLkdGlatkvgeggrgisggQAQRIALARAFLdQDRRILMFDEPTAHL 511
Cdd:cd03230 89 TVRENLKL------------------------SG--G---------------MKQRLALAQALL-HDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2159754173 512 DIETEYALKETMKPL-FKDHLVLFATHRLHWLKEM-DYVIVMKDGQI 556
Cdd:cd03230 127 DPESRREFWELLRELkKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
353-569 |
9.50e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 88.51 E-value: 9.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALpHLSQANWQK---QFSFIPQ----F 425
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEP------DSGTITVDGEDL-TDSKKDINKlrrKVGMVFQqfnlF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLfadTIAANI--------KFYRPEAtEAEVQAAVVKAGLADFV----ASLKDGlatkvgeggrgisggQAQRIALARA 493
Cdd:COG1126 90 PHL---TVLENVtlapikvkKMSKAEA-EERAMELLERVGLADKAdaypAQLSGG---------------QQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 494 fLDQDRRILMFDEPTAHLDIETEyalKE---TMKPLFKDHL-VLFATHrlhwlkEM-------DYVIVMKDGQIVQQGPV 562
Cdd:COG1126 151 -LAMEPKVMLFDEPTSALDPELV---GEvldVMRDLAKEGMtMVVVTH------EMgfarevaDRVVFMDGGRIVEEGPP 220
|
....*..
gi 2159754173 563 AELAQQP 569
Cdd:COG1126 221 EEFFENP 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
353-573 |
1.32e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 90.59 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALP-HLS-QanwQKQFSFIPQ----FP 426
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETP---DSGR---IVLNGRDLFtNLPpR---ERRVGFVFQhyalFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 427 YLfadTIAANIKF---YRPeATEAEVQAAVVK-------AGLAD-FVASLKDGlatkvgeggrgisggQAQRIALARAfL 495
Cdd:COG1118 89 HM---TVAENIAFglrVRP-PSKAEIRARVEEllelvqlEGLADrYPSQLSGG---------------QRQRVALARA-L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 496 DQDRRILMFDEPTAHLDIETEYALKETMKPLFKD-HL-VLFATH------RLhwlkeMDYVIVMKDGQIVQQGPVAELAQ 567
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGtTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYD 223
|
....*.
gi 2159754173 568 QPNGEF 573
Cdd:COG1118 224 RPATPF 229
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
340-576 |
1.74e-19 |
|
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: 88.43 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLlnTLGGFltpmlktqSQTDNF----TLNGQALPHLSQANW 415
Cdd:cd03288 24 DLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFF--------RMVDIFdgkiVIDGIDISKLPLHTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 416 QKQFSFIPQFPYLFADTIAANIKfyrPE--ATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARA 493
Cdd:cd03288 94 RSRLSIILQDPILFSGSIRFNLD---PEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 494 FLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQPNGEF 573
Cdd:cd03288 171 FV-RKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
...
gi 2159754173 574 KAL 576
Cdd:cd03288 250 ASL 252
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
353-537 |
1.95e-19 |
|
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: 86.76 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALpHLSQANWQKQFSFIPQFPYLFAD- 431
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP------SAGEVLWNGEPI-RDAREDYRRRLAYLGHADGLKPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKFYR----PEATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAFLdQDRRILM 503
Cdd:COG4133 91 TVRENLRFWAalygLRADREAIDEALEAVGLAGLadlpVRQLSAG---------------QKRRVALARLLL-SPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2159754173 504 FDEPTAHLDIETEYALKEtmkpLFKDHL-----VLFATH 537
Cdd:COG4133 155 LDEPFTALDAAGVALLAE----LIAAHLarggaVLLTTH 189
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
353-573 |
3.06e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 92.49 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADT 432
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL------ERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRpEATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdqdRR--ILMFDEPTAH 510
Cdd:PLN03130 1329 VRFNLDPFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL---RRskILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 511 LDIETEYALKETMKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQPNGEF 573
Cdd:PLN03130 1405 VDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
334-540 |
5.92e-19 |
|
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: 85.99 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSqa 413
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERP------TSGEVLVDGEPVTGPG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 414 nwqKQFSFIPQFPYLFA-DTIAANIKF-------YRPEAtEAEVQAAVVKAGLADFV----ASLKDGlatkvgeggrgis 481
Cdd:cd03293 73 ---PDRGYVFQQDALLPwLTVLDNVALglelqgvPKAEA-RERAEELLELVGLSGFEnaypHQLSGG------------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 482 ggQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHL--VLFATHRLH 540
Cdd:cd03293 136 --MRQRVALARALA-VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGktVLLVTHDID 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
353-559 |
7.90e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.02 E-value: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQAN----WQKQFSFIPQFPYL 428
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP------TSGDVIFNGQPMSKLSSAAkaelRNQKLGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 FAD-TIAANI-------KFYRPEATEA--EVQAAVvkagladfvaslkdGLATKVGEGGRGISGGQAQRIALARAFLDQD 498
Cdd:PRK11629 99 LPDfTALENVamplligKKKPAEINSRalEMLAAV--------------GLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 499 RRILMfDEPTAHLDIETEYALKETMKPLFKDHLVLF--ATHRLHWLKEMDYVIVMKDGQIVQQ 559
Cdd:PRK11629 165 RLVLA-DEPTGNLDARNADSIFQLLGELNRLQGTAFlvVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
353-569 |
8.18e-19 |
|
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: 85.71 E-value: 8.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQ-----TDNFTLNGQALPHLsqanwQKQFSFIPQ-FP 426
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERP---TSGSvlvdgTDLTLLSGKELRKA-----RRRIGMIFQhFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 427 YLFADTIAANIKFyrP----EATEAEVQAAVVKagLADFVaslkdGLATKVGEGGRGISGGQAQRIALARAfLDQDRRIL 502
Cdd:cd03258 93 LLSSRTVFENVAL--PleiaGVPKAEIEERVLE--LLELV-----GLEDKADAYPAQLSGGQKQRVGIARA-LANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 503 MFDEPTAHLDIETEYA----LKETMKPLfkDHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:cd03258 163 LCDEATSALDPETTQSilalLRDINREL--GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
353-565 |
1.00e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqtD--NFTLNGQALPHLS-QANWQKQFSFIPQ----F 425
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQP--------DsgEILLDGEPVRFRSpRDAQAAGIAIIHQelnlV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLfadTIAANI---------KFYRPEATEAEVQAAVVKAGLaDF-----VASLkdGLAtkvgeggrgisggQAQRIALA 491
Cdd:COG1129 92 PNL---SVAENIflgreprrgGLIDWRAMRRRARELLARLGL-DIdpdtpVGDL--SVA-------------QQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 492 RAfLDQDRRILMFDEPTAHL-DIETEyALKETMKPLfKDH--LVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAEL 565
Cdd:COG1129 153 RA-LSRDARVLILDEPTASLtEREVE-RLFRIIRRL-KAQgvAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
353-575 |
1.24e-18 |
|
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: 85.47 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANwqKQFSFIPQFPYLFAD- 431
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKP------DSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKF------YRPEATEAEVQ--AAVVKAG--LADFVASLKDGlatkvgeggrgisggQAQRIALARAfLDQDRRI 501
Cdd:cd03299 87 TVYKNIAYglkkrkVDKKEIERKVLeiAEMLGIDhlLNRKPETLSGG---------------EQQRVAIARA-LVVNPKI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 502 LMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPNGEFKA 575
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
353-570 |
2.36e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.17 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSqaNWQ--KQFSFIPQ-----F 425
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTP------SSGEVRLNGRPLAAWS--PWElaRRRAVLPQhsslaF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLFADTIA--ANIKFYRPEATEAEVQAAVVKAGLADFVA----SLKDGlatkvgeggrgisggQAQRIALARAFL---- 495
Cdd:COG4559 89 PFTVEEVVAlgRAPHGSSAAQDRQIVREALALVGLAHLAGrsyqTLSGG---------------EQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 496 --DQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHwLKEM--DYVIVMKDGQIVQQGPVAELAQQPN 570
Cdd:COG4559 154 pvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGgVVAVLHDLN-LAAQyaDRILLLHQGRLVAQGTPEEVLTDEL 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
334-560 |
3.77e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.67 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAYQID-LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTD-----NFTLNGQAL 407
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELVaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 408 PHLSQ-----ANWQKQFSFIPQFP--YLFADTIAANIKFyRPEA-----TEAEVQAA--VVKAGL-ADFVASLKDGLATK 472
Cdd:PRK13631 102 NPYSKkiknfKELRRRVSMVFQFPeyQLFKDTIEKDIMF-GPVAlgvkkSEAKKLAKfyLNKMGLdDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 473 vgeggrgisggQAQRIALArAFLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFA-THRL-HWLKEMDYVIV 550
Cdd:PRK13631 181 -----------QKRRVAIA-GILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFViTHTMeHVLEVADEVIV 248
|
250
....*....|
gi 2159754173 551 MKDGQIVQQG 560
Cdd:PRK13631 249 MDKGKILKTG 258
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
353-565 |
4.98e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQK-QFSFIPQFPYLFAD 431
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPP------DSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 -TIAANIKF--YRPEATEAEVQAAV----------VKAGLADfVAslkdglatkvgeggrgisggQAQRIALARAFLdQD 498
Cdd:PRK15439 101 lSVKENILFglPKRQASMQKMKQLLaalgcqldldSSAGSLE-VA--------------------DRQIVEILRGLM-RD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 499 RRILMFDEPTAHLD-IETEYALKETMKPLFKDHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAEL 565
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
329-565 |
8.79e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.91 E-value: 8.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 329 DANSTLTANHFNLQYnpDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQAlp 408
Cdd:PRK13635 1 MKEEIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLP------EAGTITVGGMV-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 409 hLSQAN-WQ--KQFSFIPQFP------YLFADTIA---ANIKFYRPEATEaEVQAAVVKAGLADFV----ASLKDGlatk 472
Cdd:PRK13635 71 -LSEETvWDvrRQVGMVFQNPdnqfvgATVQDDVAfglENIGVPREEMVE-RVDQALRQVGMEDFLnrepHRLSGG---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 473 vgeggrgisggQAQRIALArAFLDQDRRILMFDEPTAHLDIETEYALKETMKPLfKDHL---VLFATHRLHWLKEMDYVI 549
Cdd:PRK13635 145 -----------QKQRVAIA-GVLALQPDIIILDEATSMLDPRGRREVLETVRQL-KEQKgitVLSITHDLDEAAQADRVI 211
|
250
....*....|....*.
gi 2159754173 550 VMKDGQIVQQGPVAEL 565
Cdd:PRK13635 212 VMNKGEILEEGTPEEI 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
354-574 |
1.09e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.39 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 354 KDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLT---------------------------------------PMLKTQ 394
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefSLTKEG 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 395 SQTDNFT---------LNGQALPHLSQANWQKQFSFIPQFPYLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVASL 465
Cdd:PTZ00265 1265 GSGEDSTvfknsgkilLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 466 KDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFK--DHLVLFATHRLHWLK 543
Cdd:PTZ00265 1345 PNKYDTNVGPYGKSLSGGQKQRIAIARALL-REPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIK 1423
|
250 260 270
....*....|....*....|....*....|....*.
gi 2159754173 544 EMDYVIVM----KDGQIVQ-QGPVAELAQQPNGEFK 574
Cdd:PTZ00265 1424 RSDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVYK 1459
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
332-584 |
2.47e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 332 STLTANHFNLQYNPDNAyqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLS 411
Cdd:PRK11231 1 MTLRTENLTVGYGTKRI----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP------QSGTVFLGDKPISMLS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 412 QANWQKQFSFIPQFPyLFADTIAAN--IKFYRP----------EATEAEVQAAVVKAGLADF----VASLKDGlatkvge 475
Cdd:PRK11231 71 SRQLARRLALLPQHH-LTPEGITVRelVAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLadrrLTDLSGG------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 476 ggrgisggQAQRIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFAThrLHWLKEM----DYVIVM 551
Cdd:PRK11231 143 --------QRQRAFLAMV-LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTV--LHDLNQAsrycDHLVVL 211
|
250 260 270
....*....|....*....|....*....|...
gi 2159754173 552 KDGQIVQQGPVAELaqqpngefkaLTEHMRKRV 584
Cdd:PRK11231 212 ANGHVMAQGTPEEV----------MTPGLLRTV 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
353-556 |
3.31e-17 |
|
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: 80.65 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQA--NWQKQFSFIPQFPYLFA 430
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEP------DSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 431 D-TIAANIKF------YRPEAtEAEVQA--AVVKAGLADFV----ASLKDGlatkvgeggrgisggQAQRIALARAfLDQ 497
Cdd:cd03262 90 HlTVLENITLapikvkGMSKA-EAEERAleLLEKVGLADKAdaypAQLSGG---------------QQQRVAIARA-LAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHWLKEM-DYVIVMKDGQI 556
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-569 |
4.13e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 84.35 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLggfltpmLKTQSQTDNFTLNGQALPHLSQANWQK-----QFSFipQFPY 427
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLAL-------LRLIPSEGEIRFDGQDLDGLSRRALRPlrrrmQVVF--QDPF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 -------LFADTIAANIKFYRPEATEAEVQAAVVKA----GLAdfvASLKD--------GlatkvgeggrgisggQAQRI 488
Cdd:COG4172 373 gslsprmTVGQIIAEGLRVHGPGLSAAERRARVAEAleevGLD---PAARHryphefsgG---------------QRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 489 ALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLV--LFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAEL 565
Cdd:COG4172 435 AIARA-LILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLayLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQV 513
|
....
gi 2159754173 566 AQQP 569
Cdd:COG4172 514 FDAP 517
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
353-537 |
4.51e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 81.29 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqTD-NFTLNGQALPHLSQanwqkQFSFIPQ----FPY 427
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKP-------TSgEVLVDGKPVTGPGP-----DRGVVFQepalLPW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LfadTIAANIKF------YRPEATEAEVQAAVVKAGLADFVAS----LKDGlatkvgeggrgisggQAQRIALARAFLdQ 497
Cdd:COG1116 95 L---TVLDNVALglelrgVPKAERRERARELLELVGLAGFEDAyphqLSGG---------------MRQRVAIARALA-N 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATH 537
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTH 197
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
353-557 |
6.01e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.10 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLSQAnwqkqfsfipQFPYL---- 428
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERP---TSGQ---VLVNGQDLSRLKRR----------EIPYLrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 ---FAD-------TIAANIKF------YRPEATEAEVQAAVVKAGLAD----FVASLKDGlatkvgeggrgisggQAQRI 488
Cdd:COG2884 82 gvvFQDfrllpdrTVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDkakaLPHELSGG---------------EQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 489 ALARAFLDQDrRILMFDEPTAHLDIETEYalkETMKpLFKDhL------VLFATHRLHWLKEMDY-VIVMKDGQIV 557
Cdd:COG2884 147 AIARALVNRP-ELLLADEPTGNLDPETSW---EIME-LLEE-InrrgttVLIATHDLELVDRMPKrVLELEDGRLV 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
353-560 |
7.58e-17 |
|
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: 79.50 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQalphlSQANWQKQFSFIPQ-------F 425
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP------TSGSIRVFGK-----PLEKERKRIGYVPQrrsidrdF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLFADTIA----ANIKFYRP--EATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAfL 495
Cdd:cd03235 84 PISVRDVVLmglyGHKGLFRRlsKADKAKVDEALERVGLSELadrqIGELSGG---------------QQQRVLLARA-L 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 496 DQDRRILMFDEPTAHLDIETEYALKETMKPL-FKDHLVLFATHRLHWLKE-MDYVIVMkDGQIVQQG 560
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
353-584 |
9.63e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.20 E-value: 9.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQ-----FPY 427
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSP------DSGEVRLNGRPLADWSPAELARRRAVLPQhsslsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LFADTIA------ANikfyRPEATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAFL-- 495
Cdd:PRK13548 92 TVEEVVAmgraphGL----SRAEDDALVAAALAQVDLAHLagrdYPQLSGG---------------EQQRVQLARVLAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 496 ---DQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH-----LVLfatHRL----HWlkeMDYVIVMKDGQIVQQGPVA 563
Cdd:PRK13548 153 wepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglaviVVL---HDLnlaaRY---ADRIVLLHQGRLVADGTPA 226
|
250 260
....*....|....*....|.
gi 2159754173 564 ElaqqpngefkALTEHMRKRV 584
Cdd:PRK13548 227 E----------VLTPETLRRV 237
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
353-565 |
1.75e-16 |
|
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: 79.15 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQ-----TDNFTLNGQALPHLSQAN---WQkQFSFIPQ 424
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP---TSGSvlidgTDINKLKGKALRQLRRQIgmiFQ-QFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 425 FpylfadTIAANI--------KFYRPEA---TEAEVQAAVvkagladfvASLKD-GLATKVGEGGRGISGGQAQRIALAR 492
Cdd:cd03256 93 L------SVLENVlsgrlgrrSTWRSLFglfPKEEKQRAL---------AALERvGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 493 AfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKE-MDYVIVMKDGQIVQQGPVAEL 565
Cdd:cd03256 158 A-LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
353-573 |
1.92e-16 |
|
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: 78.92 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQAnwQKQFSFIPQFPYLFAD- 431
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP------DSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRHm 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKF---YRPEAT---EAEVQAAVVK-------AGLAD-FVASLKDGlatkvgeggrgisggQAQRIALARAfLDQ 497
Cdd:cd03296 90 TVFDNVAFglrVKPRSErppEAEIRAKVHEllklvqlDWLADrYPAQLSGG---------------QRQRVALARA-LAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKPLFKD--HLVLFATH-RLHWLKEMDYVIVMKDGQIVQQGPVAELAQQPNGEF 573
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDElhVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
367-578 |
2.47e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.80 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 367 AIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTDNFtLNGQALPHLSQANWQKQFSFIPQFP------YLFaDTIAANIKFY 440
Cdd:PRK14247 33 ALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVY-LDGQDIFKMDVIELRRRVQMVFQIPnpipnlSIF-ENVALGLKLN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 441 RPEATEAEVQA----AVVKAGLADFVASLKDGLATKVGEGgrgisggQAQRIALARAfLDQDRRILMFDEPTAHLDIETE 516
Cdd:PRK14247 111 RLVKSKKELQErvrwALEKAQLWDEVKDRLDAPAGKLSGG-------QQQRLCIARA-LAFQPEVLLADEPTANLDPENT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 517 YALKETMKPLFKDHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPNGEfkaLTE 578
Cdd:PRK14247 183 AKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREVFTNPRHE---LTE 242
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
355-569 |
7.01e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 79.37 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 355 DISFTLHGyQKV-AIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQAL----------PHlsqanwQKQFSFIP 423
Cdd:COG4148 17 DVDFTLPG-RGVtALFGPSGSGKTTLLRAIAGLERP------DSGRIRLGGEVLqdsargiflpPH------RRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 424 Q----FPYLfadTIAANIKF-YR--PEATEAEVQAAVVKA-GLAD----FVASLKDGlatkvgeggrgisggQAQRIALA 491
Cdd:COG4148 84 QearlFPHL---SVRGNLLYgRKraPRAERRISFDEVVELlGIGHlldrRPATLSGG---------------ERQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 492 RAFLDQDRRILMfDEPTAHLDieteYALKETMKPLFK---DHL---VLFATHRLHwlkEM----DYVIVMKDGQIVQQGP 561
Cdd:COG4148 146 RALLSSPRLLLM-DEPLAALD----LARKAEILPYLErlrDELdipILYVSHSLD---EVarlaDHVVLLEQGRVVASGP 217
|
....*...
gi 2159754173 562 VAELAQQP 569
Cdd:COG4148 218 LAEVLSRP 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
353-571 |
9.41e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.54 E-value: 9.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQ--SQTDNFTLNGQALPHLSqanwQKQFSFIPQFPYLFA 430
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrvAGQDVATLDADALAQLR----REHFGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 431 DTIAANikfyrpeateaEVQAAVVKAGLA---------DFVASLkdGLATKVGEGGRGISGGQAQRIALARAFLDQDRRI 501
Cdd:PRK10535 100 HLTAAQ-----------NVEVPAVYAGLErkqrllraqELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 502 LMfDEPTAHLDIETEYALKETMKPLF-KDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPvAELAQQPNG 571
Cdd:PRK10535 167 LA-DEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPP-AQEKVNVAG 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
353-555 |
1.41e-15 |
|
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: 74.92 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQalphlsqaNWQKQFSFIPQFP----YL 428
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP---DSGS---ILIDGE--------DLTDLEDELPPLRrrigMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 FAD-------TIAANIKFyrpeateaevqaavvkagladfvaSLKDGlatkvgeggrgisggQAQRIALARAfLDQDRRI 501
Cdd:cd03229 82 FQDfalfphlTVLENIAL------------------------GLSGG---------------QQQRVALARA-LAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 502 LMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQ 555
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
353-560 |
1.84e-15 |
|
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: 75.31 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTL----HGyqkvaIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQK------QFSFI 422
Cdd:cd03264 16 LDGVSLTLgpgmYG-----LLGPNGAGKTTLMRILATLTPP------SSGTIRIDGQDVLKQPQKLRRRigylpqEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 423 PQFP-YLFADTIAAnIKFYRPEATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAFLdQ 497
Cdd:cd03264 85 PNFTvREFLDYIAW-LKGIPSKEVKARVDEVLELVNLGDRakkkIGSLSGG---------------MRRRVGIAQALV-G 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQG 560
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
353-569 |
2.24e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.82 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGfltpmlktqsqtdNFTLNgqalphlSQANW-QKQFSFIPQFPYLFAD 431
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-------------QFEIS-------EGRVWaERSIAYVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKFYRPEaTEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHL 511
Cdd:PTZ00243 736 TVRGNILFFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVY-ANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 512 DietEYALKETMKPLFKDHL-----VLfATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:PTZ00243 814 D---AHVGERVVEECFLGALagktrVL-ATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
332-537 |
5.54e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 75.28 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 332 STLTANHFNLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLS 411
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAP------SSGEITLDGVPVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 412 qAN----WQKQfsfiPQFPYLFA-DTIAANIKFYRPEATEAEVQAA--VVKAGLADF----VASLKDGlatkvgeggrgi 480
Cdd:COG4525 76 -ADrgvvFQKD----ALLPWLNVlDNVAFGLRLRGVPKAERRARAEelLALVGLADFarrrIWQLSGG------------ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 481 sggQAQRIALARAfLDQDRRILMFDEPTAHLDIETeyalKETMKPLFKD------HLVLFATH 537
Cdd:COG4525 139 ---MRQRVGIARA-LAADPRFLLMDEPFGALDALT----REQMQELLLDvwqrtgKGVFLITH 193
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
353-557 |
6.22e-15 |
|
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: 72.46 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQalphlsqanwqkqfsfipqfPYLFADT 432
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKP---DSGE---ILVDGK--------------------EVSFASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANikfyrpeateaevqaavvKAGLAdFVASLkdGLATKvgeggrgisggqaQRIALARAfLDQDRRILMFDEPTAHLD 512
Cdd:cd03216 70 RDAR------------------RAGIA-MVYQL--SVGER-------------QMVEIARA-LARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2159754173 513 I-ETEyALKETMKPLFKDHL-VLFATHRLHWLKEM-DYVIVMKDGQIV 557
Cdd:cd03216 115 PaEVE-RLFKVIRRLRAQGVaVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
355-569 |
8.71e-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: 75.47 E-value: 8.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 355 DISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTqsqTDNFTLNGQALPHLSQANWQ----KQFSFIPQFPY--- 427
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT---SGEILFDGEDLLKLSEKELRkirgREIQMIFQDPMtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 --LF--ADTIAANIKFYRPeATEAEVQAAVVKA----GLADFVASLKD-------GlatkvgeggrgisggQAQRIALAR 492
Cdd:COG0444 100 npVMtvGDQIAEPLRIHGG-LSKAEARERAIELlervGLPDPERRLDRyphelsgG---------------MRQRVMIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 493 AfLDQDRRILMFDEPTAHLDIETEyalKETMKpLFKDhL-------VLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAE 564
Cdd:COG0444 164 A-LALEPKLLIADEPTTALDVTIQ---AQILN-LLKD-LqrelglaILFITHDLGVVAEIaDRVAVMYAGRIVEEGPVEE 237
|
....*
gi 2159754173 565 LAQQP 569
Cdd:COG0444 238 LFENP 242
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
358-565 |
9.87e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.85 E-value: 9.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 358 FTLHGYQ--KVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQalPHLSQANWQKQFSFIPQ----FPYLfad 431
Cdd:PRK10771 18 FDLTVERgeRVAILGPSGAGKSTLLNLIAGFLTP------ASGSLTLNGQ--DHTTTPPSRRPVSMLFQennlFSHL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKF-YRP-----EATEAEVQAAVVKAGLADFVASLKDGLATKvgeggrgisggQAQRIALARAFLDQdRRILMFD 505
Cdd:PRK10771 87 TVAQNIGLgLNPglklnAAQREKLHAIARQMGIEDLLARLPGQLSGG-----------QRQRVALARCLVRE-QPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 506 EPTAHLDIeteyALKETMKPLFKD-----HL-VLFATHRLH-WLKEMDYVIVMKDGQIVQQGPVAEL 565
Cdd:PRK10771 155 EPFSALDP----ALRQEMLTLVSQvcqerQLtLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
353-575 |
1.04e-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: 73.81 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLSQAnwQKQFSFIPQ----FPYL 428
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETP---TSGE---ILLDGKDITNLPPH--KRPVNTVFQnyalFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 fadTIAANIKF--YRPEATEAEVQAAVVKA-------GLAD-FVASLKDGlatkvgeggrgisggQAQRIALARAFLDQD 498
Cdd:cd03300 88 ---TVFENIAFglRLKKLPKAEIKERVAEAldlvqleGYANrKPSQLSGG---------------QQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 499 RRILMfDEPTAHLDIETEYALKETMKPLFKD--HLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPNGEFKA 575
Cdd:cd03300 150 KVLLL-DEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEIYEEPANRFVA 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
313-582 |
1.16e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.71 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 313 QPTIQNRELVSDSFHWDANSTltanhfnlqyNPDnayqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMlk 392
Cdd:PLN03232 609 QPGAPAISIKNGYFSWDSKTS----------KPT------LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA-- 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 393 tqsQTDNFTLNGQAlphlsqanwqkqfSFIPQFPYLFADTIAANIKF---YRPEATEAEVQAAVVKAGLADFVAslKDgl 469
Cdd:PLN03232 671 ---ETSSVVIRGSV-------------AYVPQVSWIFNATVRENILFgsdFESERYWRAIDVTALQHDLDLLPG--RD-- 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 470 ATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKET-MKPLFKDHLVLFATHRLHWLKEMDYV 548
Cdd:PLN03232 731 LTEIGERGVNISGGQKQRVSMARAVY-SNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRI 809
|
250 260 270
....*....|....*....|....*....|....*
gi 2159754173 549 IVMKDGQIVQQGPVAELAQqpNGE-FKALTEHMRK 582
Cdd:PLN03232 810 ILVSEGMIKEEGTFAELSK--SGSlFKKLMENAGK 842
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
341-560 |
3.02e-14 |
|
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: 72.30 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 341 LQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFL--TPMLKTQsqtdnFTLNGQAlphLSQANWQKQ 418
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVegGGTTSGQ-----ILFNGQP---RKPDQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 419 FSFIPQF----PYLfadTIAANIKFYRPEATEAEVQAAVVKAGLADFvaSLKDgLATKVGEGGRGISGG--QAQRIALAR 492
Cdd:cd03234 83 VAYVRQDdillPGL---TVRETLTYTAILRLPRKSSDAIRKKRVEDV--LLRD-LALTRIGGNLVKGISggERRRVSIAV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 493 AFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFK-DHLVLFATH--RLHWLKEMDYVIVMKDGQIVQQG 560
Cdd:cd03234 157 QLL-WDPKVLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
340-560 |
5.10e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.33 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmLKTQSQTDNFTLNGQALPHLsqanwQKQF 419
Cdd:PRK13632 12 NVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKP-QSGEIKIDGITISKENLKEI-----RKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 SFIPQFP--YLFADTIAANIKF------YRPEATEAEVQAAVVKAGLADFV----ASLKDGlatkvgeggrgisggQAQR 487
Cdd:PRK13632 86 GIIFQNPdnQFIGATVEDDIAFglenkkVPPKKMKDIIDDLAKKVGMEDYLdkepQNLSGG---------------QKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159754173 488 IALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFK--DHLVLFATHRLHWLKEMDYVIVMKDGQIVQQG 560
Cdd:PRK13632 151 VAIASV-LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
353-570 |
7.90e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.14 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFP--YLFA 430
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKP------TSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 431 DTIAANIKF------YRPEATEAEVQAAVVKAGLADFVASLKDGLATKvgeggrgisggQAQRIALArAFLDQDRRILMF 504
Cdd:PRK13652 94 PTVEQDIAFgpinlgLDEETVAHRVSSALHMLGLEELRDRVPHHLSGG-----------EKKRVAIA-GVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 505 DEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPN 570
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
367-565 |
1.02e-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: 71.38 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 367 AIIGMSGSGKSTLLNTLGGFLTPMLKTqsqtdnFTLNGQALPHLSQANWQKQFSFIPQ-----FPYLFADTIA-ANIKFY 440
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGT------VDLAGVDLHGLSRRARARRVALVEQdsdtaVPLTVRDVVAlGRIPHR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 441 RPEATEAEVQAAVVKAGLADFVASlkdGLATKvgeGGRGISGGQAQRIALARAfLDQDRRILMFDEPTAHLDIETEYALK 520
Cdd:TIGR03873 105 SLWAGDSPHDAAVVDRALARTELS---HLADR---DMSTLSGGERQRVHVARA-LAQEPKLLLLDEPTNHLDVRAQLETL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2159754173 521 ETMKPLFKDHL-VLFATHRL-HWLKEMDYVIVMKDGQIVQQGPVAEL 565
Cdd:TIGR03873 178 ALVRELAATGVtVVAALHDLnLAASYCDHVVVLDGGRVVAAGPPREV 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
350-572 |
1.30e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.93 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 350 QIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMlKTQSQTDNFTLNGQAlpHLSQA-----NWQKQFSFIPQ 424
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPE-AGTIRVGDITIDTAR--SLSQQkglirQLRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 425 FPYLFAD-TIAANIkFYRPEATEAEVQAAVVKAG---LAdfvaslKDGLATKVGEGGRGISGGQAQRIALARAFLDQDRR 500
Cdd:PRK11264 93 NFNLFPHrTVLENI-IEGPVIVKGEPKEEATARArelLA------KVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 501 ILmFDEPTAHLDIETEYALKETMKPLFKD-HLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPNGE 572
Cdd:PRK11264 166 IL-FDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFADPQQP 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
329-564 |
1.49e-13 |
|
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: 70.54 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 329 DANSTLTANHFNLQYnPDNAYQID-LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQAL 407
Cdd:COG4181 4 SSAPIIELRGLTKTV-GTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRP------TSGTVRLAGQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 408 PHLSQ---ANWQKQ-----F-SF--IP--------QFPYLFADtiaanikfyRPEAtEAEVQAAVVKAGLAD----FVAS 464
Cdd:COG4181 77 FALDEdarARLRARhvgfvFqSFqlLPtltalenvMLPLELAG---------RRDA-RARARALLERVGLGHrldhYPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 465 LKDGlatkvgeggrgisggQAQRIALARAFLDQDrRILMFDEPTAHLDIETEYALKETMKPLFKDH---LVLfATHRLHW 541
Cdd:COG4181 147 LSGG---------------EQQRVALARAFATEP-AILFADEPTGNLDAATGEQIIDLLFELNRERgttLVL-VTHDPAL 209
|
250 260
....*....|....*....|...
gi 2159754173 542 LKEMDYVIVMKDGQIVQQGPVAE 564
Cdd:COG4181 210 AARCDRVLRLRAGRLVEDTAATA 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
353-573 |
2.06e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 71.64 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqTD-NFTLNGQALPHLSQAnwQKQFSFIPQ----FPY 427
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDP-------TSgEILIGGRDVTDLPPK--DRNIAMVFQsyalYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LfadTIAANIKFY-----RPEAteaEVQAAVVKA----GLADF----VASLKDGlatkvgeggrgisggQAQRIALARAf 494
Cdd:COG3839 90 M---TVYENIAFPlklrkVPKA---EIDRRVREAaellGLEDLldrkPKQLSGG---------------QRQRVALGRA- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 495 LDQDRRILMFDEPTAHLDieteYALKETM----KPLFKD--HLVLFATHRLHwlkE-M---DYVIVMKDGQIVQQGPVAE 564
Cdd:COG3839 148 LVREPKVFLLDEPLSNLD----AKLRVEMraeiKRLHRRlgTTTIYVTHDQV---EaMtlaDRIAVMNDGRIQQVGTPEE 220
|
....*....
gi 2159754173 565 LAQQPNGEF 573
Cdd:COG3839 221 LYDRPANLF 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
353-573 |
2.13e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 71.65 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGfltpmLKTQSqTDNFTLNGQALPHLSQANwqKQFSFIPQFPYLFAD- 431
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-----LEHQT-SGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHm 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKF--------YRPEAteAEVQAAVVK-------AGLAD-FVASLKDGlatkvgeggrgisggQAQRIALARAfL 495
Cdd:PRK10851 90 TVFDNIAFgltvlprrERPNA--AAIKAKVTQllemvqlAHLADrYPAQLSGG---------------QKQRVALARA-L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 496 DQDRRILMFDEPTAHLDIETEYALKETMKPL---FKDHLVlFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPNG 571
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLheeLKFTSV-FVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQVWREPAT 230
|
..
gi 2159754173 572 EF 573
Cdd:PRK10851 231 RF 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
348-573 |
2.14e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 348 AYQIDLKDISFTLHGYQKVAIIGMSGSGKStllnTLGGFLTPMLKTQSQtdnFTLNGQALPHLSQanwQKQFSFIPQFPY 427
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKS----TTGLALLRLINSQGE---IWFDGQPLHNLNR---RQLLPVRHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LFAD-------------TIAANIKFYRPEATEAEVQAAVVKA----GLAD-----FVASLKDGlatkvgeggrgisggQA 485
Cdd:PRK15134 367 VFQDpnsslnprlnvlqIIEEGLRVHQPTLSAAQREQQVIAVmeevGLDPetrhrYPAEFSGG---------------QR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 486 QRIALARAFLDQDrRILMFDEPTAHLDIETEYALKETMKPLFKDHLV--LFATHRLHWLKEMDY-VIVMKDGQIVQQGPV 562
Cdd:PRK15134 432 QRIAIARALILKP-SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHqVIVLRQGEVVEQGDC 510
|
250
....*....|.
gi 2159754173 563 AELAQQPNGEF 573
Cdd:PRK15134 511 ERVFAAPQQEY 521
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
340-565 |
3.18e-13 |
|
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: 70.15 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYN-PDNAYQIdLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktQSQTdnFTLNGqaLPHLSQAN-WQ- 416
Cdd:TIGR04520 5 NVSFSyPESEKPA-LKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLP----TSGK--VTVDG--LDTLDEENlWEi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 417 -KQFSFIPQFPylfaDT--IAA-----------NIKFYRPEaTEAEVQAAVVKAGLADFV----ASLKDGlatkvgeggr 478
Cdd:TIGR04520 76 rKKVGMVFQNP----DNqfVGAtveddvafgleNLGVPREE-MRKRVDEALKLVGMEDFRdrepHLLSGG---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 479 gisggQAQRIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEMDYVIVMKDGQI 556
Cdd:TIGR04520 141 -----QKQRVAIAGV-LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKI 214
|
....*....
gi 2159754173 557 VQQGPVAEL 565
Cdd:TIGR04520 215 VAEGTPREI 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
343-558 |
3.19e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 343 YNPDNAYQ-IDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKT--------QSQTDNftlngQALPHLsqa 413
Cdd:PRK13641 12 YSPGTPMEkKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTitiagyhiTPETGN-----KNLKKL--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 414 nwQKQFSFIPQFP--YLFADTIAANIKF----YRPEATEAEVQAA--VVKAGLADFVAS-----LKDGlatkvgeggrgi 480
Cdd:PRK13641 84 --RKKVSLVFQFPeaQLFENTVLKDVEFgpknFGFSEDEAKEKALkwLKKVGLSEDLISkspfeLSGG------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 481 sggQAQRIALARAFLDQDrRILMFDEPTAHLDIETEyalKETMKpLFKD-----HLVLFATHRLHWLKE-MDYVIVMKDG 554
Cdd:PRK13641 150 ---QMRRVAIAGVMAYEP-EILCLDEPAAGLDPEGR---KEMMQ-LFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHG 221
|
....
gi 2159754173 555 QIVQ 558
Cdd:PRK13641 222 KLIK 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
293-574 |
3.38e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 293 DYHATLDGKNALGDIldildqptIQNRELVSDSFHWDANSTLTANHF-NLQYNPDNAYQIDL-KDISFTLHGYQKVAIIG 370
Cdd:PTZ00265 347 EYMKSLEATNSLYEI--------INRKPLVENNDDGKKLKDIKKIQFkNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 371 MSGSGKSTLLNTLGGFLTPmlktqSQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADTIAANIKF----------- 439
Cdd:PTZ00265 419 ESGCGKSTILKLIERLYDP-----TEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdleal 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 440 --YRPEAT--------------------------------------------EAEVQAAVVKAGLADFVASLKDGLATKV 473
Cdd:PTZ00265 494 snYYNEDGndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVSALPDKYETLV 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 474 GEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPL--FKDHLVLFATHRLHWLKEMDYVIVM 551
Cdd:PTZ00265 574 GSNASKLSGGQKQRISIARAII-RNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRYANTIFVL 652
|
330 340
....*....|....*....|...
gi 2159754173 552 KDGQIVQQGPVAELAQQPNGEFK 574
Cdd:PTZ00265 653 SNRERGSTVDVDIIGEDPTKDNK 675
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
351-575 |
4.67e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.52 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 351 IDlkDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLS-QanwQKQFSFIPQ----F 425
Cdd:PRK11432 22 ID--NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKP---TEGQ---IFIDGEDVTHRSiQ---QRDICMVFQsyalF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYL-FADTIAANIKFYRPEATE-----AEVQAAVVKAGLAD-FVASLKDGlatkvgeggrgisggQAQRIALARAfLDQD 498
Cdd:PRK11432 91 PHMsLGENVGYGLKMLGVPKEErkqrvKEALELVDLAGFEDrYVDQISGG---------------QQQRVALARA-LILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 499 RRILMFDEPTAHLDIETEYALKETMKPLFK--DHLVLFATH-RLHWLKEMDYVIVMKDGQIVQQGPVAELAQQPNGEFKA 575
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMA 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
353-565 |
6.34e-13 |
|
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: 68.96 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnFTLNGQALPHLSQANWQKQFSFI-PQFPYLF-- 429
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPP---TYGND--VRLFGERRGGEDVWELRKRIGLVsPALQLRFpr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 430 ----ADTIA----ANIKFYRpEATEAEVQAAvvKAGLADF-VASLKD--------GlatkvgeggrgisggQAQRIALAR 492
Cdd:COG1119 94 detvLDVVLsgffDSIGLYR-EPTDEQRERA--RELLELLgLAHLADrpfgtlsqG---------------EQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 493 AFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHL--VLFATHRLH-WLKEMDYVIVMKDGQIVQQGPVAEL 565
Cdd:COG1119 156 ALV-KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAptLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
353-573 |
7.69e-13 |
|
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: 71.90 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLggfLTPMLKTQSQTdnfTLNGQAlphlsqanwqkqfSFIPQFPYLFADT 432
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHV---HMKGSV-------------AYVPQQAWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRPeATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLD 512
Cdd:TIGR00957 715 LRENILFGKA-LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVY-SNADIYLFDDPLSAVD 792
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 513 IET-EYALKETMKP--LFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQQpNGEF 573
Cdd:TIGR00957 793 AHVgKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR-DGAF 855
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
343-564 |
8.62e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.92 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 343 YNPDNAYQ-IDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQAL--PHLSQANWQKQF 419
Cdd:PRK13637 12 YMEGTPFEkKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP------TSGKIIIDGVDItdKKVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 SFIPQFP--YLFADTIAANIKF--YRPEATEAEVQAAVVKAglADFVASLKDGLATKvgeGGRGISGGQAQRIALArAFL 495
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAFgpINLGLSEEEIENRVKRA--MNIVGLDYEDYKDK---SPFELSGGQKRRVAIA-GVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 496 DQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWL-KEMDYVIVMKDGQIVQQGPVAE 564
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
353-554 |
9.60e-13 |
|
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: 67.74 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLL-NTLGGFLTPMLKTQSQTDNFTLNGQALphlSQANWQKQFSFIPQFPYLFAD 431
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEA---TRSRNRYSVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKFYRPeATEAEVQAAVVKAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAfLDQDRRILMFDEPTAHL 511
Cdd:cd03290 94 TVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA-LYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2159754173 512 DIE-TEYALKETMKPLFKD--HLVLFATHRLHWLKEMDYVIVMKDG 554
Cdd:cd03290 172 DIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
334-560 |
9.83e-13 |
|
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: 67.78 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHlSQA 413
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEP------DAGFATVDGFDVVK-EPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 414 NWQKQFSFIPQFPYLFAD-TIAANIKFY------RPEATEAEVQAAVVKAGLADFVASLKDGLATKvgeggrgisggQAQ 486
Cdd:cd03266 75 EARRRLGFVSDSTGLYDRlTARENLEYFaglyglKGDELTARLEELADRLGMEELLDRRVGGFSTG-----------MRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 487 RIALARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLfKD--HLVLFATHRLHWLKEM-DYVIVMKDGQIVQQG 560
Cdd:cd03266 144 KVAIARALV-HDPPVLLLDEPTTGLDVMATRALREFIRQL-RAlgKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
353-569 |
1.16e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.34 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFT-----LHGyqkvaIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQALPHLSQA---NWQKQFSFIPQ 424
Cdd:COG1135 21 LDDVSLTiekgeIFG-----IIGYSGAGKSTLIRCINLLERP---TSGSV---LVDGVDLTALSERelrAARRKIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 425 FPYLFAD-TIAANIKF------YRPEATEAEVQA--AVVkaGLAD----FVASLKDGlatkvgeggrgisggQAQRIALA 491
Cdd:COG1135 90 HFNLLSSrTVAENVALpleiagVPKAEIRKRVAEllELV--GLSDkadaYPSQLSGG---------------QKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 492 RAfLDQDRRILMFDEPTAHLDIETEYA----LKE-------TmkplfkdhlVLFATHrlhwlkEM-------DYVIVMKD 553
Cdd:COG1135 153 RA-LANNPKVLLCDEATSALDPETTRSildlLKDinrelglT---------IVLITH------EMdvvrricDRVAVLEN 216
|
250
....*....|....*.
gi 2159754173 554 GQIVQQGPVAELAQQP 569
Cdd:COG1135 217 GRIVEQGPVLDVFANP 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
356-537 |
1.41e-12 |
|
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: 66.75 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 356 ISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALpHLSQANWQKQFSFIPQFPYLFAD-TIA 434
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP------LAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTlSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 435 ANIKFYRPEATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAFLDQdRRILMFDEPTAH 510
Cdd:cd03231 92 ENLRFWHADHSDEQVEEALARVGLNGFedrpVAQLSAG---------------QQRRVALARLLLSG-RPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|..
gi 2159754173 511 LDIETEYALKEtmkpLFKDHL-----VLFATH 537
Cdd:cd03231 156 LDKAGVARFAE----AMAGHCarggmVVLTTH 183
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
349-551 |
1.47e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.43 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 349 YQID----LKDISFTL-HGYQKVaIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIP 423
Cdd:PRK10247 15 YLAGdakiLNNISFSLrAGEFKL-ITGPSGCGKSTLLKIVASLISP------TSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 424 QFPYLFADTIAANIKFyrP-EATEAEVQAAVVKAGLADFvaSLKDGLATKvgeGGRGISGGQAQRIALAR--AFLDqdrR 500
Cdd:PRK10247 88 QTPTLFGDTVYDNLIF--PwQIRNQQPDPAIFLDDLERF--ALPDTILTK---NIAELSGGEKQRISLIRnlQFMP---K 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 501 ILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEMDYVIVM 551
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
353-565 |
1.74e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.49 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYL-FAD 431
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP------TAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKFYRP----------EATEAEVQAAVVKAGLADFVA----SLKDGlatkvgeggrgisggQAQRIALARAfLDQ 497
Cdd:PRK09536 93 DVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFADrpvtSLSGG---------------ERQRVLLARA-LAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKPLFKD-HLVLFATHRLHW-LKEMDYVIVMKDGQIVQQGPVAEL 565
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLaARYCDELVLLADGRVRAAGPPADV 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
355-560 |
1.78e-12 |
|
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: 66.93 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 355 DISFTLHGyQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTDNFTLNGQALPHLSQAnwQKQFSFIPQ----FPYLfa 430
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQ--QRKIGLVFQqyalFPHL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 431 dTIAANI----KFYRPEATEAEVQAAVVKAGLADFVASLKDGLATKvgeggrgisggQAQRIALARAFLDQDRRILMfDE 506
Cdd:cd03297 91 -NVRENLafglKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGG-----------EKQRVALARALAAQPELLLL-DE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 507 PTAHLDIETEYALKETMKPLFKD-HL-VLFATHRLHWLKEM-DYVIVMKDGQIVQQG 560
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNlNIpVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
334-560 |
1.91e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.64 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAyqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPM-------LKTQSQTDNFTLNGQA 406
Cdd:PRK11701 7 LSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDagevhyrMRDGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 407 LPHLSQANWqkqfSFIPQFPylfAD------TIAANI---------KFY---RPEATE--AEVQAAVvkAGLADFVASLK 466
Cdd:PRK11701 83 RRRLLRTEW----GFVHQHP---RDglrmqvSAGGNIgerlmavgaRHYgdiRATAGDwlERVEIDA--ARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 467 DGLatkvgeggrgisggqAQRIALARAFLDQDRRILMfDEPTAHLDIETEYALKETMKPLFKD-HL-VLFATH-----RL 539
Cdd:PRK11701 154 GGM---------------QQRLQIARNLVTHPRLVFM-DEPTGGLDVSVQARLLDLLRGLVRElGLaVVIVTHdlavaRL 217
|
250 260
....*....|....*....|.
gi 2159754173 540 hwLKemDYVIVMKDGQIVQQG 560
Cdd:PRK11701 218 --LA--HRLLVMKQGRVVESG 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
353-556 |
1.94e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.40 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqTDNFTLNGQALphLSQANWQKQFSFipQFPYLFA-- 430
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETP-------SAGELLAGTAP--LAEAREDTRLMF--QDARLLPwk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 431 ---DTIAANIK-FYRPEATEAevQAAVvkaGLAD----FVASLKDGlatkvgeggrgisggQAQRIALARAFLDQDrRIL 502
Cdd:PRK11247 97 kviDNVGLGLKgQWRDAALQA--LAAV---GLADraneWPAALSGG---------------QKQRVALARALIHRP-GLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 503 MFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQI 556
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
16-252 |
3.32e-12 |
|
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: 67.28 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 16 LIWVTILTGIQGIAIICQAHFLTRAL--VNSWQMKPLATLTTAIILFGGAFLLRHVCVWLKNIILDHYADHTSNLLRDRL 93
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILdvLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 94 LDQVYVTGANQIAQTGTGKLVTVALDGINNVYNYFNLIFAKIFDMMIIPFLVIIYIYWQSVRSGIILTIVFPVVILFMII 173
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 174 LGFAAQDKADRQYAGFIKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAILSTFALDWFTTLSI 252
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
343-570 |
3.46e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.35 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 343 YNPDNAYQ-IDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTDNFTLNGQALPHLSQAnwQKQFSF 421
Cdd:PRK13634 12 YQYKTPFErRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPL--RKKVGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 422 IPQFP--YLFADTIAANI-----KFYRPEAtEAEVQA-AVVK-AGLADFVAS-----LKDGlatkvgeggrgisggQAQR 487
Cdd:PRK13634 90 VFQFPehQLFEETVEKDIcfgpmNFGVSEE-DAKQKArEMIElVGLPEELLArspfeLSGG---------------QMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 488 IALArAFLDQDRRILMFDEPTAHLDIETEyalKETMKPLFKDH-----LVLFATHRLH-WLKEMDYVIVMKDGQIVQQGP 561
Cdd:PRK13634 154 VAIA-GVLAMEPEVLVLDEPTAGLDPKGR---KEMMEMFYKLHkekglTTVLVTHSMEdAARYADQIVVMHKGTVFLQGT 229
|
....*....
gi 2159754173 562 VAELAQQPN 570
Cdd:PRK13634 230 PREIFADPD 238
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
353-569 |
5.53e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.88 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLL---NTL----GGFLTpmlktqsqTDNFTLNGqalPHLSQANWQKQFSFIPQF 425
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLeeitSGDLI--------VDGLKVND---PKVDERLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLFADTIA-ANIKF-------YRPEATEAEVQAAVVKAGLAD----FVASLKDGlatkvgeggrgisggQAQRIALARA 493
Cdd:PRK09493 86 FYLFPHLTAlENVMFgplrvrgASKEEAEKQARELLAKVGLAErahhYPSELSGG---------------QQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 494 fLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVL-FATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:PRK09493 151 -LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMvIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
353-569 |
6.59e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALP-----HLSQA------------NW 415
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP------TSGELLIDDHPLHfgdysYRSQRirmifqdpstslNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 416 QKQFSFIPQFPYLFADTIAanikfyrPEATEAEVQAAVVKAGL-ADFVASLKDGLATKvgeggrgisggQAQRIALARAF 494
Cdd:PRK15112 103 RQRISQILDFPLRLNTDLE-------PEQREKQIIETLRQVGLlPDHASYYPHMLAPG-----------QKQRLGLARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 495 LDQDRRILMfDEPTAHLDIETEYALKETMKPLFKDHLV--LFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:PRK15112 165 ILRPKVIIA-DEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVLASP 241
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
353-573 |
6.74e-12 |
|
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: 66.13 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQALPHLSQANWQ----KQFSFIPQ---- 424
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEP---TSGKV---LIDGQDIAAMSRKELRelrrKKISMVFQsfal 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 425 FPYLfadTIAANIKF-----YRPEATEAEVQAAVVKA-GLADFVASLKDGLATKvgeggrgisggQAQRIALARAfLDQD 498
Cdd:cd03294 114 LPHR---TVLENVAFglevqGVPRAEREERAAEALELvGLEGWEHKYPDELSGG-----------MQQRVGLARA-LAVD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 499 RRILMFDEPTAHLD--IETEyaLKETMKPLFKDH--LVLFATHRL-HWLKEMDYVIVMKDGQIVQQGPVAELAQQPNGEF 573
Cdd:cd03294 179 PDILLMDEAFSALDplIRRE--MQDELLRLQAELqkTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
353-566 |
7.79e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.91 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFP--YLFA 430
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLP------QRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 431 DTIAANIKF------YRPEATEAEVQAAVVKAGLADFVASLKDGLAtkvgeggrgisGGQAQRIALArAFLDQDRRILMF 504
Cdd:PRK13647 95 STVWDDVAFgpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPYHLS-----------YGQKKRVAIA-GVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 505 DEPTAHLDIETEYALKETMKPLFKD-HLVLFATHRLHWLKE-MDYVIVMKDGQIVQQGPVAELA 566
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
356-537 |
7.80e-12 |
|
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: 64.69 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 356 ISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSqtdnftLNGQALPHLsQANWQKQFSFIPQFPYLFAD-TIA 434
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVR------WNGTPLAEQ-RDEPHENILYLGHLPGLKPElSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 435 ANIKFYRP--EATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAFLDQdRRILMFDEPT 508
Cdd:TIGR01189 92 ENLHFWAAihGGAQRTIEDALAAVGLTGFedlpAAQLSAG---------------QQRRLALARLWLSR-RPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|....
gi 2159754173 509 AHLDIETEYALKEtmkpLFKDHL-----VLFATH 537
Cdd:TIGR01189 156 TALDKAGVALLAG----LLRAHLarggiVLLTTH 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
353-570 |
1.12e-11 |
|
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: 68.01 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqtdnftlNGQALPHlsqanwQKQFSFIPQFPYLFADT 432
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEP-------------SEGKIKH------SGRISFSPQTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKF------YRpeateaevQAAVVKA-GLADFVASLKDGLATKVGEGGRGISGGQAQRIALARAfLDQDRRILMFD 505
Cdd:TIGR01271 503 IKDNIIFglsydeYR--------YTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARA-VYKDADLYLLD 573
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 506 EPTAHLDIETEYALKET-MKPLFKDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGPVAEL-AQQPN 570
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELqAKRPD 640
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-569 |
1.35e-11 |
|
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: 67.02 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKS-TLLNTLGgfLTPmlKTQSQTD-NFTLNGQALPHLSQANWQK----QFSFIPQFP 426
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSvTALSILR--LLP--DPAAHPSgSILFDGQDLLGLSERELRRirgnRIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 427 Y-----LFadTIAANI-------KFYRPEATEAEVQAAVVKAGLADFVASLKD-------GlatkvgeggrgisggQAQR 487
Cdd:COG4172 102 MtslnpLH--TIGKQIaevlrlhRGLSGAAARARALELLERVGIPDPERRLDAyphqlsgG---------------QRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 488 IALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAE 564
Cdd:COG4172 165 VMIAMA-LANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFaDRVAVMRQGEIVEQGPTAE 243
|
....*
gi 2159754173 565 LAQQP 569
Cdd:COG4172 244 LFAAP 248
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
322-570 |
1.83e-11 |
|
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: 64.88 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 322 VSDSFHWDANSTLTANHFNLQYNPDnayqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqtdnft 401
Cdd:cd03291 28 NNDRKHSSDDNNLFFSNLCLVGAPV------LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEP------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 402 lNGQALPHlsqanwQKQFSFIPQFPYLFADTIAANIKF------YRpeateaevQAAVVKA-GLADFVASLKDGLATKVG 474
Cdd:cd03291 90 -SEGKIKH------SGRISFSSQFSWIMPGTIKENIIFgvsydeYR--------YKSVVKAcQLEEDITKFPEKDNTVLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 475 EGGRGISGGQAQRIALARAFLdQDRRILMFDEPTAHLDIETEYALKET-MKPLFKDHLVLFATHRLHWLKEMDYVIVMKD 553
Cdd:cd03291 155 EGGITLSGGQRARISLARAVY-KDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHE 233
|
250
....*....|....*...
gi 2159754173 554 GQIVQQGPVAEL-AQQPN 570
Cdd:cd03291 234 GSSYFYGTFSELqSLRPD 251
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
334-569 |
2.04e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAyqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLG--GFLTPMLKTqsqTDNFTLNGQAL--PH 409
Cdd:PRK14239 6 LQVSDLSVYYNKKKA----LNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTI---TGSIVYNGHNIysPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 410 LSQANWQKQFSFIPQFPYLFADTIAANI-----------KFYRPEATEAEVQAAV----VKAGLADFVASLKDGlatkvg 474
Cdd:PRK14239 79 TDTVDLRKEIGMVFQQPNPFPMSIYENVvyglrlkgikdKQVLDEAVEKSLKGASiwdeVKDRLHDSALGLSGG------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 475 eggrgisggQAQRIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEM-DYVIVMKD 553
Cdd:PRK14239 153 ---------QQQRVCIARV-LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLD 222
|
250
....*....|....*.
gi 2159754173 554 GQIVQQGPVAELAQQP 569
Cdd:PRK14239 223 GDLIEYNDTKQMFMNP 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
340-575 |
2.08e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.01 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAYQIDlkDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLsqANWQKQF 419
Cdd:PRK11607 24 NLTKSFDGQHAVD--DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---TAGQ---IMLDGVDLSHV--PPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 SFIPQ----FPYLfadTIAANIKF--YRPEATEAEVQAAVVK----AGLADFVASLKDGLATKvgeggrgisggQAQRIA 489
Cdd:PRK11607 94 NMMFQsyalFPHM---TVEQNIAFglKQDKLPKAEIASRVNEmlglVHMQEFAKRKPHQLSGG-----------QRQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 490 LARAfLDQDRRILMFDEPTAHLDIEteyaLKETMKPLFKDHL------VLFATHRLHWLKEMDYVI-VMKDGQIVQQGPV 562
Cdd:PRK11607 160 LARS-LAKRPKLLLLDEPMGALDKK----LRDRMQLEVVDILervgvtCVMVTHDQEEAMTMAGRIaIMNRGKFVQIGEP 234
|
250
....*....|...
gi 2159754173 563 AELAQQPNGEFKA 575
Cdd:PRK11607 235 EEIYEHPTTRYSA 247
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
353-561 |
2.14e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.52 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLtpmlktQSQTDNFTLNGQAlphLSQANWQKQFSFIPQ-------F 425
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV------RLASGKISILGQP---TRQALQKNLVAYVPQseevdwsF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLFADTIA----ANIKFYR-PEATEAE-VQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAfL 495
Cdd:PRK15056 94 PVLVEDVVMmgryGHMGWLRrAKKRDRQiVTAALARVDMVEFrhrqIGELSGG---------------QKKRVFLARA-I 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 496 DQDRRILMFDEPTAHLDIETEYALKETMKPLFKD-HLVLFATHRLHWLKEM-DYVIVMKdGQIVQQGP 561
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFcDYTVMVK-GTVLASGP 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
353-575 |
3.74e-11 |
|
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: 63.47 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLSQANWQKQFSFIPQ----FPYL 428
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP---TSGE---IFIDGEDIREQDPVELRRKIGYVIQqiglFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 fadTIAANIKF------YRPEATEAEVQAAVVKAGL--ADFVASLKDGLATKvgeggrgisggQAQRIALARAfLDQDRR 500
Cdd:cd03295 91 ---TVEENIALvpkllkWPKEKIRERADELLALVGLdpAEFADRYPHELSGG-----------QQQRVGVARA-LAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 501 ILMFDEPTAHLDIETEYALKETMKPLFKD--HLVLFATHRL-HWLKEMDYVIVMKDGQIVQQGPVAELAQQPNGEFKA 575
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
353-537 |
3.85e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPM---LKTQSQTDNFTLNGQALPHLSQANWQKqfsfipqfPYLf 429
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAagtIKLDGGDIDDPDVAEACHYLGHRNAMK--------PAL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 430 adTIAANIKFYRP--EATEAEVQAAVVKAGLADfVASLKDG-LATKvgeggrgisggQAQRIALARaFLDQDRRILMFDE 506
Cdd:PRK13539 89 --TVAENLEFWAAflGGEELDIAAALEAVGLAP-LAHLPFGyLSAG-----------QKRRVALAR-LLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 2159754173 507 PTAHLDIETEYALKEtmkpLFKDHL-----VLFATH 537
Cdd:PRK13539 154 PTAALDAAAVALFAE----LIRAHLaqggiVIAATH 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
329-519 |
5.30e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 329 DANSTLTANHFNLQyNPDnaYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGfLTPmlktqsqtdnftlNGQ--- 405
Cdd:COG4178 358 SEDGALALEDLTLR-TPD--GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWP-------------YGSgri 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 406 ALPHLSQAnwqkqfSFIPQFPYLFADTIAANIkfYRPEA----TEAEVQAAVVKAGLADFVASLKD----------Glat 471
Cdd:COG4178 421 ARPAGARV------LFLPQRPYLPLGTLREAL--LYPATaeafSDAELREALEAVGLGHLAERLDEeadwdqvlslG--- 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2159754173 472 kvgeggrgisggQAQRIALARAFLDQdRRILMFDEPTAHLDIETEYAL 519
Cdd:COG4178 490 ------------EQQRLAFARLLLHK-PDWLFLDEATSALDEENEAAL 524
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
334-565 |
7.27e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.33 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYnPDNAYQidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMlktqsqTDNFTLNGQALPHLSQA 413
Cdd:PRK13636 6 LKVEELNYNY-SDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS------SGRILFDGKPIDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 414 --NWQKQFSFIPQFP--YLFADTIAANIKF--YRPEATEAEVQAAVVKAGLADFVASLKDglatkvgEGGRGISGGQAQR 487
Cdd:PRK13636 77 lmKLRESVGMVFQDPdnQLFSASVYQDVSFgaVNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 488 IALArAFLDQDRRILMFDEPTAHLD----IETEYALKETMKPLfkDHLVLFATHRLHWLK-EMDYVIVMKDGQIVQQGPV 562
Cdd:PRK13636 150 VAIA-GVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNP 226
|
...
gi 2159754173 563 AEL 565
Cdd:PRK13636 227 KEV 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
353-580 |
8.12e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.66 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP----MLktqsqtdnftLNGQALPHLS-------------Qanw 415
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPdsgeIL----------IDGKPVRIRSprdaialgigmvhQ--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 416 qkQFSFIPQFpylfadTIAANI---------KFYRPEATEAEVQAAVVKAGLA----DFVASLKDGlatkvgeggrgisg 482
Cdd:COG3845 88 --HFMLVPNL------TVAENIvlgleptkgGRLDRKAARARIRELSERYGLDvdpdAKVEDLSVG-------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 483 gQAQRIALARAfLDQDRRILMFDEPTAHL-DIETEyALKETMKPLFKDHL-VLFATHRLHWLKEM-DYVIVMKDGQIVQQ 559
Cdd:COG3845 146 -EQQRVEILKA-LYRGARILILDEPTAVLtPQEAD-ELFEILRRLAAEGKsIIFITHKLREVMAIaDRVTVLRRGKVVGT 222
|
250 260
....*....|....*....|.
gi 2159754173 560 GPVAELAQQpngefkALTEHM 580
Cdd:COG3845 223 VDTAETSEE------ELAELM 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
329-569 |
9.37e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 62.36 E-value: 9.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 329 DANSTLTANHFNLQYNPDNAyqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGF--LTPMLKTQSQtdnFTLNGQA 406
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQA----LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGARVEGE---ILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 407 L--PHLSQANWQKQFSFIPQFPYLFADTIAANIKF------YRPEATEAE-VQAAVVKAGLADFVaslKDGL---ATKVG 474
Cdd:COG1117 80 IydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYglrlhgIKSKSELDEiVEESLRKAALWDEV---KDRLkksALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 475 EGgrgisggQAQRIALARAfLDQDRRILMFDEPTAHLD-IETEyALKETMKPLFKDHLVLFATHRlhwlkeM-------D 546
Cdd:COG1117 157 GG-------QQQRLCIARA-LAVEPEVLLMDEPTSALDpISTA-KIEELILELKKDYTIVIVTHN------MqqaarvsD 221
|
250 260
....*....|....*....|...
gi 2159754173 547 YVIVMKDGQIVQQGPVAELAQQP 569
Cdd:COG1117 222 YTAFFYLGELVEFGPTEQIFTNP 244
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
353-565 |
1.36e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.40 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQALPHLSQANWqKQFSFIPQFpyLFADT 432
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESP---SQGNV---SWRGEPLAKLNRAQR-KAFRRDIQM--VFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAA-NIKF---------------YRPEATEAEVQAAVVKAGLADFVAS-----LKDGlatkvgeggrgisggQAQRIALA 491
Cdd:PRK10419 99 ISAvNPRKtvreiireplrhllsLDKAERLARASEMLRAVDLDDSVLDkrppqLSGG---------------QLQRVCLA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 492 RAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFK--DHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAEL 565
Cdd:PRK10419 164 RA-LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFcQRVMVMDNGQIVETQPVGDK 239
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
353-569 |
1.41e-10 |
|
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: 61.68 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQtdnFTLNGQALPHLS-QANWQKQF--SFipQFPYLF 429
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRP---TSGS---VLFDGEDITGLPpHEIARLGIgrTF--QIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 430 AD-TIAANI------------KFYRPEATEAEVQAAVvkAGLADFVaslkdGLATKVGEGGRGISGGQAQRIALARAfLD 496
Cdd:cd03219 88 PElTVLENVmvaaqartgsglLLARARREEREARERA--EELLERV-----GLADLADRPAGELSYGQQRRLEIARA-LA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159754173 497 QDRRILMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
353-570 |
1.74e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANW----QKQFSFIPQFP-- 426
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP------TTGTVTVDDITITHKTKDKYirpvRKRIGMVFQFPes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 427 YLFADTIAANIKFyRPEATEAEVQAavVKAGLADFVASLkdGLATKVGEGGRGISGG-QAQRIALArAFLDQDRRILMFD 505
Cdd:PRK13646 97 QLFEDTVEREIIF-GPKNFKMNLDE--VKNYAHRLLMDL--GFSRDVMSQSPFQMSGgQMRKIAIV-SILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 506 EPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWL-KEMDYVIVMKDGQIVQQGPVAELAQQPN 570
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDEnkTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
353-575 |
1.78e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.04 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQAnwQKQFSFIPQ----FPYL 428
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETP------DSGRIMLDGQDITHVPAE--NRHVNTVFQsyalFPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 fadTIAANIKF-YRPEAT-EAEVQAAVVKA----GLADF----VASLKDGlatkvgeggrgisggQAQRIALARAFLDQD 498
Cdd:PRK09452 102 ---TVFENVAFgLRMQKTpAAEITPRVMEAlrmvQLEEFaqrkPHQLSGG---------------QQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 499 rRILMFDEPTAHLDieteYALKETMKPLFKdHL-------VLFATH-RLHWLKEMDYVIVMKDGQIVQQGPVAELAQQPN 570
Cdd:PRK09452 164 -KVLLLDESLSALD----YKLRKQMQNELK-ALqrklgitFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
....*
gi 2159754173 571 GEFKA 575
Cdd:PRK09452 238 NLFVA 242
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
353-570 |
1.93e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.39 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLtpmlktqSQTDNFTLNGQALPHLSQAN------W----QKQFSFI 422
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-------PGQGEILLNGRPLSDWSAAElarhraYlsqqQSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 423 PQFPYLfadtiaaniKFYRPeateAEVQAAVVKAGLADFVASLkdGLATKVGEGGRGISGGQAQRIALARAFL------D 496
Cdd:COG4138 85 PVFQYL---------ALHQP----AGASSEAVEQLLAQLAEAL--GLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptiN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 497 QDRRILMFDEPTAHLDIETEYALketmkplfkDHL----------VLFATHRL-HWLKEMDYVIVMKDGQIVQQGPVAEL 565
Cdd:COG4138 150 PEGQLLLLDEPMNSLDVAQQAAL---------DRLlrelcqqgitVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEV 220
|
....*
gi 2159754173 566 AQQPN 570
Cdd:COG4138 221 MTPEN 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
353-567 |
2.02e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQ--TDNFTLNGQALPHLSQANWQKQFSFIPQ-----F 425
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGArvTGDVTLNGEPLAAIDAPRLARLRAVLPQaaqpaF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYlFADTIAANIKFyrPEATEAEvQAAVVKAGLADFVASLKDGlATKVGEGGRGISGGQAQRIALARAFLD--------Q 497
Cdd:PRK13547 97 AF-SAREIVLLGRY--PHARRAG-ALTHRDGEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLAQlwpphdaaQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 498 DRRILMFDEPTAHLDIETEYALKETMKPLFKD-HL-VLFATHRLHW-LKEMDYVIVMKDGQIVQQGPVAELAQ 567
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLgVLAIVHDPNLaARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
340-556 |
2.04e-10 |
|
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: 60.88 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAyqiDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKT--QSQTDNFTLNGQALPHLSQanwqk 417
Cdd:cd03292 7 TKTYPNGTA---ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTirVNGQDVSDLRGRAIPYLRR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 418 QFSFIPQ-FPYLFADTIAANIKF------YRPEATEAEVQAAVVKAGLADFVASLKDGLAtkvgeggrgisGGQAQRIAL 490
Cdd:cd03292 79 KIGVVFQdFRLLPDRNVYENVAFalevtgVPPREIRKRVPAALELVGLSHKHRALPAELS-----------GGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 491 ARAFLDqDRRILMFDEPTAHLDIETEYALKETMKPLFK-DHLVLFATHRLHWLKEMDY-VIVMKDGQI 556
Cdd:cd03292 148 ARAIVN-SPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
367-578 |
2.21e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 367 AIIGMSGSGKSTLLNTLGGF--LTPMLKTQSQTDNFTLNGQAlPHLSQANWQKQFSFIPQFPYLFA-----DTIAANIKF 439
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLleLNEEARVEGEVRLFGRNIYS-PDVDPIEVRREVGMVFQYPNPFPhltiyDNVAIGVKL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 440 YRPEATEAE----VQAAVVKAGLADFVaslKDGLATKvgegGRGISGGQAQRIALARAfLDQDRRILMFDEPTAHLDIET 515
Cdd:PRK14267 113 NGLVKSKKElderVEWALKKAALWDEV---KDRLNDY----PSNLSGGQRQRLVIARA-LAMKPKILLMDEPTANIDPVG 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 516 EYALKETMKPLFKDHLVLFATHR-LHWLKEMDYVIVMKDGQIVQQGPVAELAQQPNGEfkaLTE 578
Cdd:PRK14267 185 TAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE---LTE 245
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
10-557 |
2.32e-10 |
|
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: 63.28 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 10 PGLTLTLIWVTILTGIQGIAIIcqahfltrALVNSWQMKPLATLTTAIILFGGAFLLRHVCVWLKNIILDHYADHTSNLL 89
Cdd:COG4615 12 RWLLLLALLLGLLSGLANAGLI--------ALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 90 RDRLLDQVYVTGANQIAQTGTGKLVTVALDGINNVYNYFNLIFAKIFDMMIIpFLVIIYIYWQSVRsgiiltiVFPVVIL 169
Cdd:COG4615 84 RLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALV-LGCLAYLAWLSPP-------LFLLTLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 170 FMIILGFAAQDKADRQYAGFIK-------LSNHFVDSLRGLATLKfLGLSKR---YETNVYEVSEDYRRstmdtLRIAIL 239
Cdd:COG4615 156 LLGLGVAGYRLLVRRARRHLRRareaedrLFKHFRALLEGFKELK-LNRRRRrafFDEDLQPTAERYRD-----LRIRAD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 240 STFALdwfttlsiallalflglaLINGSMPLFPALVSLILapeFFLPIrdFGNDYHATLDG--------KNALGDILDIL 311
Cdd:COG4615 230 TIFAL------------------ANNWGNLLFFALIGLIL---FLLPA--LGWADPAVLSGfvlvllflRGPLSQLVGAL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 312 dqPTIqNRELVS--------------DSFHWDANSTLTANHFN-LQ--------YNPDNAYQIDLKDISFTLHGYQKVAI 368
Cdd:COG4615 287 --PTL-SRANVAlrkieelelalaaaEPAAADAAAPPAPADFQtLElrgvtyryPGEDGDEGFTLGPIDLTIRRGELVFI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 369 IGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADTIAAnikfyRPEATEAE 448
Cdd:COG4615 364 VGGNGSGKSTLAKLLTGLYRP------ESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRLLGL-----DGEADPAR 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 449 VQAAVVKAGLADFVaSLKDG------LATkvgeggrgisgGQAQRIALARAFLDqDRRILMFDEPTAHLDieteyalket 522
Cdd:COG4615 433 ARELLERLELDHKV-SVEDGrfsttdLSQ-----------GQRKRLALLVALLE-DRPILVFDEWAADQD---------- 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 523 mkPLFKDhlvLFATHRLHWLKEM-----------------DYVIVMKDGQIV 557
Cdd:COG4615 490 --PEFRR---VFYTELLPELKARgktviaishddryfdlaDRVLKMDYGKLV 536
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
340-568 |
2.55e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAYQID-LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTDNFTLNGQALPHLSQAnwQKQ 418
Cdd:PRK13643 8 NYTYQPNSPFASRaLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPV--RKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 419 FSFIPQFP--YLFADTIAANIKFYRPEATEAEVQAAVVKAGLADFVaslkdGLATKV-GEGGRGISGGQAQRIALArAFL 495
Cdd:PRK13643 86 VGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFwEKSPFELSGGQMRRVAIA-GIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159754173 496 DQDRRILMFDEPTAHLDIETEYALKETMKPLFKD-HLVLFATHRLHWLKE-MDYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
353-551 |
2.85e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.94 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTDNFTLngqalphlsqanwqkqfSFIPQ-------F 425
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV-----------------AYVPQrsevpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLFADTIA----ANIKFYRP--EATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAFL 495
Cdd:NF040873 71 PLTVRDLVAmgrwARRGLWRRltRDDRAAVDDALERVGLADLagrqLGELSGG---------------QRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 496 dQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHWLKEMDYVIVM 551
Cdd:NF040873 136 -QEADLLLLDEPTTGLDAESRERIIALLAEEHARGAtVVVVTHDLELVRRADPCVLL 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
353-560 |
3.36e-10 |
|
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: 59.87 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSqtdnFTLNGQAlphLSQANWQKQFSFIPQFPYLFadt 432
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGE----VLINGRP---LDKRSFRKIIGYVPQDDILH--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 iaanikfyrPEATeaeVQAAVvkaglaDFVASLKdGLATkvgeggrgisgGQAQRIALARAFLdQDRRILMFDEPTAHLD 512
Cdd:cd03213 95 ---------PTLT---VRETL------MFAAKLR-GLSG-----------GERKRVSIALELV-SNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 513 IETEYALKETMKPLFKDH-LVLFATHRLHWL--KEMDYVIVMKDGQIVQQG 560
Cdd:cd03213 144 SSSALQVMSLLRRLADTGrTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
353-578 |
3.41e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.22 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTqsqtdNFTLNGQAlphlsqanwqkqfSFIPQFPYLFADT 432
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA-----SVVIRGTV-------------AYVPQVSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRPEATEAEVQAAVVkAGLADFVASLKDGLATKVGEGGRGISGGQAQRIALARA-FLDQDrrILMFDEPTAHL 511
Cdd:PLN03130 695 VRDNILFGSPFDPERYERAIDV-TALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAvYSNSD--VYIFDDPLSAL 771
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 512 DietEYALKETMKPLFKDHL-----VLfATHRLHWLKEMDYVIVMKDGQIVQQGPVAELAQqpNGE-FKALTE 578
Cdd:PLN03130 772 D---AHVGRQVFDKCIKDELrgktrVL-VTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN--NGPlFQKLME 838
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
353-565 |
3.75e-10 |
|
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: 60.21 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQAL-PHLSQAnwQKQFSFIPQFPYLFAD 431
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRP------TSGTAYINGYSIrTDRKAA--RQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 -TIAANIKFY-----RPEATEAEVQAAVVKA-GLADF----VASLKDGlatkvgeggrgisggQAQRIALARAFLDqDRR 500
Cdd:cd03263 90 lTVREHLRFYarlkgLPKSEIKEEVELLLRVlGLTDKankrARTLSGG---------------MKRKLSLAIALIG-GPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 501 ILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHwlkEM----DYVIVMKDGQIVQQGPVAEL 565
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMD---EAealcDRIAIMSDGKLRCIGSPQEL 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
353-569 |
5.80e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.97 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQALPHLSQANWQK---QFSFIPQ-FPYL 428
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERP---TSGRV---LVDGQDLTALSEKELRKarrQIGMIFQhFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 FADTIAANIKFyrP-EA---TEAEVQAAVvkAGLADFVaslkdGLATKVGEGGRGISGGQAQRIALARAfLDQDRRILMF 504
Cdd:PRK11153 95 SSRTVFDNVAL--PlELagtPKAEIKARV--TELLELV-----GLSDKADRYPAQLSGGQKQRVAIARA-LASNPKVLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 505 DEPTAHLDIETEYA----LKETMKPLfkdHL-VLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:PRK11153 165 DEATSALDPATTRSilelLKDINREL---GLtIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-578 |
6.27e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.06 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGfLTPMLKTQSQTDNFTLN-GQALPHLSQANWQKQFSFIPQ----FPY 427
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNR-LIEIYDSKIKVDGKVLYfGKDIFQIDAIKLRKEVGMVFQqpnpFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 L-FADTIAANIKFY---RPEATEAEVQAAVVKAGLADFVASLKDGLATKVgeggrgiSGGQAQRIALARAfLDQDRRILM 503
Cdd:PRK14246 105 LsIYDNIAYPLKSHgikEKREIKKIVEECLRKVGLWKEVYDRLNSPASQL-------SGGQQQRLTIARA-LALKPKVLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 504 FDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPNGEfkaLTE 578
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTSPKNE---LTE 249
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
353-539 |
1.01e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.41 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLL---NTLGGfLTPMLKTQSQTdnfTLNGQAL--PHLSQANWQKQFSFIPQFPY 427
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLND-LIPGFRVEGKV---TFHGKNLyaPDVDPVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LFADTIAANIKF------YRPEATEAeVQAAVVKAGLADFVaslKDglatKVGEGGRGISGGQAQRIALARAFLDQDRRI 501
Cdd:PRK14243 102 PFPKSIYDNIAYgaringYKGDMDEL-VERSLRQAALWDEV---KD----KLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2159754173 502 LMfDEPTAHLDIETEYALKETMKPLFKDHLVLFATHRL 539
Cdd:PRK14243 174 LM-DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
353-585 |
1.11e-09 |
|
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: 59.43 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALphlSQANWQKQFSFIPQFPYLFADT 432
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKP------AQGTVSFRGQDL---YQLDRKQRRAFRRDVQLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAAnikfYRPEAT----------------EAEVQAAVvkAGLADFVaSLKDGLATKvgeGGRGISGGQAQRIALARAfLD 496
Cdd:TIGR02769 98 PSA----VNPRMTvrqiigeplrhltsldESEQKARI--AELLDMV-GLRSEDADK---LPRQLSGGQLQRINIARA-LA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 497 QDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLV--LFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAEL--AQQPNG 571
Cdd:TIGR02769 167 VKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLlsFKHPAG 246
|
250
....*....|....*..
gi 2159754173 572 EF---KALTEHMRKRVT 585
Cdd:TIGR02769 247 RNlqsAVLPEHPVRRSI 263
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
340-577 |
1.19e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.62 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYN-PDNAYQidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP-----MLKTQSQTDNFTLNG-QALPHLSQ 412
Cdd:PRK13644 6 NVSYSyPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPqkgkvLVSGIDTGDFSKLQGiRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 413 ANWQKQFsfipqfpylFADTIAANIKF------YRPEATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisg 482
Cdd:PRK13644 84 QNPETQF---------VGRTVEEDLAFgpenlcLPPIEIRKRVDRALAEIGLEKYrhrsPKTLSGG-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 483 gQAQRIALArAFLDQDRRILMFDEPTAHLDIETEYALKETMKPLF-KDHLVLFATHRLHWLKEMDYVIVMKDGQIVQQGP 561
Cdd:PRK13644 141 -QGQCVALA-GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
250
....*....|....*.
gi 2159754173 562 VAELAQQPNGEFKALT 577
Cdd:PRK13644 219 PENVLSDVSLQTLGLT 234
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
16-304 |
1.32e-09 |
|
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: 59.49 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 16 LIWVTILTGIQGIAIICQAHFLTRALVNSWQMKPLATLTTAIILFGGAFLLRHVCVWLKNIILDHYADHTSNLLRDRLLD 95
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 96 QVYVTGANQIAQTGTGKLVTVALDGINNVYNYFNLIFAKIFDMMIIPFLVIIYIYWQSVRSGIILTIVFPVVILFMIILG 175
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 176 ---FAAQDKADRQYAgfiKLSNHFVDSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAILSTFALDWFTTLSI 252
Cdd:cd07346 161 rriRKASREVRESLA---ELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 253 ALLALFLGLALINGSMPLFPALVSLILAPEFFLPIRDFGNDYHATLDGKNAL 304
Cdd:cd07346 238 ALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
353-515 |
1.33e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP--------------MLKtqsQTDNFTLNG-------QALPHLS 411
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdsgevsipkglrigYLP---QEPPLDDDLtvldtvlDGDAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 412 QAnwQKQFSFI---PQFPYLFADTIA-ANIKFYRPEATEAEVQAAVVKAGL----ADF---VASLKDGlatkvgeggrgi 480
Cdd:COG0488 91 AL--EAELEELeakLAEPDEDLERLAeLQEEFEALGGWEAEARAEEILSGLgfpeEDLdrpVSELSGG------------ 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 2159754173 481 sggQAQRIALARAFLDQ-DrrILMFDEPTAHLDIET 515
Cdd:COG0488 157 ---WRRRVALARALLSEpD--LLLLDEPTNHLDLES 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
353-560 |
1.42e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.26 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTD----NFTLNGQALPHLSQANWQ-----KQFSFIP 423
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIEllgrTVQREGRLARDIRKSRANtgyifQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 424 QFPYLFADTIAA---------NIKFYRPEATEAEVQAaVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIAL 490
Cdd:PRK09984 100 RLSVLENVLIGAlgstpfwrtCFSWFTREQKQRALQA-LTRVGMVHFahqrVSTLSGG---------------QQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 491 ARAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHW-LKEMDYVIVMKDGQIVQQG 560
Cdd:PRK09984 164 ARALM-QQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYaLRYCERIVALRQGHVFYDG 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
340-569 |
1.68e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.03 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAYQidLKDISFTLHGYQ------------KV-AIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQA 406
Cdd:PRK10575 3 EYTNHSDTTFA--LRNVSFRVPGRTllhplsltfpagKVtGLIGHNGSGKSTLLKMLGRHQPP------SEGEILLDAQP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 407 LPHLSQANWQKQFSFIPQ-FPYLFADTIAANIKFYR-P---------EATEAEVQAAVVKAGLADFVASLKDGLATKvge 475
Cdd:PRK10575 75 LESWSSKAFARKVAYLPQqLPAAEGMTVRELVAIGRyPwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGG--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 476 ggrgisggQAQRIALArAFLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH-LVLFAThrLHWL----KEMDYVIV 550
Cdd:PRK10575 152 --------ERQRAWIA-MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERgLTVIAV--LHDInmaaRYCDYLVA 220
|
250
....*....|....*....
gi 2159754173 551 MKDGQIVQQGPVAELAQQP 569
Cdd:PRK10575 221 LRGGEMIAQGTPAELMRGE 239
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
353-569 |
1.81e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 58.70 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPylfADT 432
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEP------TSGEILINGHKLEYGDYKYRCKHIRMIFQDP---NTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYR-------------PEATEAEVQAAVVKAGL----ADFVAS-LKDGlatkvgeggrgisggQAQRIALARAF 494
Cdd:COG4167 100 LNPRLNIGQileeplrlntdltAEEREERIFATLRLVGLlpehANFYPHmLSSG---------------QKQRVALARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 495 LDQDrRILMFDEPTAHLDIETEYALKETMKPLFKDHLV--LFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:COG4167 165 ILQP-KIIIADEALAALDMSVRSQIINLMLELQEKLGIsyIYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVFANP 241
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
353-565 |
2.08e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.87 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTpmlktqSQTDNFTLNGQALP-HLSQ----ANWQKQFSFIPQFP- 426
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLII------SETGQTIVGDYAIPaNLKKikevKRLRKEIGLVFQFPe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 427 -YLFADTIAANIKFyRPEATEAEVQAAVVKA-GLADFVASLKDglatKVGEGGRGISGGQAQRIALArAFLDQDRRILMF 504
Cdd:PRK13645 101 yQLFQETIEKDIAF-GPVNLGENKQEAYKKVpELLKLVQLPED----YVKRSPFELSGGQKRRVALA-GIIAMDGNTLVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 505 DEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRL-HWLKEMDYVIVMKDGQIVQQGPVAEL 565
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLNKEYkkRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
353-567 |
2.45e-09 |
|
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: 57.83 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMlktqsqTDNFTLNGQALPHL-SQANWQKQFSFIPQ----FPY 427
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR------SGSIRFDGRDITGLpPHERARAGIGYVPEgrriFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LfadTIAANIK---FYRPEATEAEVQAAVV------------KAGladfvaSLKDGlatkvgeggrgisggQAQRIALAR 492
Cdd:cd03224 90 L---TVEENLLlgaYARRRAKRKARLERVYelfprlkerrkqLAG------TLSGG---------------EQQMLAIAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 493 AFLdQDRRILMFDEPTAHL------DIETeyALKEtmkplFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVA 563
Cdd:cd03224 146 ALM-SRPKLLLLDEPSEGLapkiveEIFE--AIRE-----LRDEgvTILLVEQNARFALEIaDRAYVLERGRVVLEGTAA 217
|
....
gi 2159754173 564 ELAQ 567
Cdd:cd03224 218 ELLA 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
353-557 |
2.86e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.69 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPM---------LK----TQSQtDNFTLNgqalphlsqanwqkqf 419
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDsgtvklgetVKigyfDQHQ-EELDPD---------------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 420 sfipqfpylfaDTIAANIKFYRPEATEAEVQAAvvkagLADF----------VASLKDGlatkvgeggrgisggQAQRIA 489
Cdd:COG0488 394 -----------KTVLDELRDGAPGGTEQEVRGY-----LGRFlfsgddafkpVGVLSGG---------------EKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 490 LARAFLdQDRRILMFDEPTAHLDIET----EYALKE---TmkplfkdhlVLFATHRLHWLKEM-DYVIVMKDGQIV 557
Cdd:COG0488 443 LAKLLL-SPPNVLLLDEPTNHLDIETlealEEALDDfpgT---------VLLVSHDRYFLDRVaTRILEFEDGGVR 508
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
356-570 |
3.42e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 356 ISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLtpmlktqSQTDNFTLNGQALPHLSQANWQKQFSFIPQ----------F 425
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-------PGSGSIQFAGQPLEAWSAAELARHRAYLSQqqtppfampvF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLfadtiaaniKFYRPeateAEVQAAVVKAGLADFVASLKdgLATKVGEGGRGISGGQAQRIALARAFLDQDRRI---- 501
Cdd:PRK03695 88 QYL---------TLHQP----DKTRTEAVASALNEVAEALG--LDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpag 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 502 --LMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRL-HWLKEMDYVIVMKDGQIVQQGPVAELAQQPN 570
Cdd:PRK03695 153 qlLLLDEPMNSLDVAQQAALDRLLSELCQQGIaVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
331-560 |
4.84e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.89 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 331 NSTLTANHFNLQYnPDNAYQIdLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQtdnFTLNGQALPHL 410
Cdd:PRK13640 3 DNIVEFKHVSFTY-PDSKKPA-LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSK---ITVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 411 SQANWQKQFSFIPQFP--YLFADTIAANIKF-------YRPEATEAeVQAAVVKAGLADFVASLKDGLATKvgeggrgis 481
Cdd:PRK13640 78 TVWDIREKVGIVFQNPdnQFVGATVGDDVAFglenravPRPEMIKI-VRDVLADVGMLDYIDSEPANLSGG--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 482 ggQAQRIALArAFLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKD-HLVLFA-THRLHWLKEMDYVIVMKDGQIVQQ 559
Cdd:PRK13640 148 --QKQRVAIA-GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISiTHDIDEANMADQVLVLDDGKLLAQ 224
|
.
gi 2159754173 560 G 560
Cdd:PRK13640 225 G 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
353-579 |
4.89e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTDN-FTLNGQALPHLSQANWQK------QFSFIPQF 425
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqFDFSQKPSEKAIRLLRQKvgmvfqQYNLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLfADTIAANIKFYRPEATEAEVQAAVVKA--GLADFVAS----LKDGlatkvgeggrgisggQAQRIALARAfLDQDR 499
Cdd:COG4161 98 TVM-ENLIEAPCKVLGLSKEQAREKAMKLLArlRLTDKADRfplhLSGG---------------QQQRVAIARA-LMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 500 RILMFDEPTAHLDIETEYALKETMKPLFK--------DHLVLFAThrlhwlKEMDYVIVMKDGQIVQQGPVAELAQQPNG 571
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQtgitqvivTHEVEFAR------KVASQVVYMEKGRIIEQGDASHFTQPQTE 234
|
....*...
gi 2159754173 572 EFKALTEH 579
Cdd:COG4161 235 AFAHYLSH 242
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
367-565 |
6.54e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.30 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 367 AIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYLFADT----IAANIKF--- 439
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTP------AHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDItvqeLVARGRYphq 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 440 -----YRPEATEAeVQAAVVKAGLADFVASLKDGLATKvgeggrgisggQAQRIALARAfLDQDRRILMFDEPTAHLDIE 514
Cdd:PRK10253 111 plftrWRKEDEEA-VTKAMQATGITHLADQSVDTLSGG-----------QRQRAWIAMV-LAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2159754173 515 TEYALKETMKPLFKDHLVLFAThRLHWLKE----MDYVIVMKDGQIVQQGPVAEL 565
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAA-VLHDLNQacryASHLIALREGKIVAQGAPKEI 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
343-560 |
7.35e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.40 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 343 YNPDNAYQID-LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP------------MLKTQSQT-----DNFTLNG 404
Cdd:PRK13651 12 FNKKLPTELKaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPdtgtiewifkdeKNKKKTKEkekvlEKLVIQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 405 QALPHLSQAN-WQKQFSFIPQFP-Y-LFADTIAANIKF----YRPEATEAEVQAA--VVKAGL-ADFVA----SLKDGla 470
Cdd:PRK13651 92 TRFKKIKKIKeIRRRVGVVFQFAeYqLFEQTIEKDIIFgpvsMGVSKEEAKKRAAkyIELVGLdESYLQrspfELSGG-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 471 tkvgeggrgisggQAQRIALArAFLDQDRRILMFDEPTAHLDIEteyALKETMKPLFKDHL----VLFATHRL-HWLKEM 545
Cdd:PRK13651 170 -------------QKRRVALA-GILAMEPDFLVFDEPTAGLDPQ---GVKEILEIFDNLNKqgktIILVTHDLdNVLEWT 232
|
250
....*....|....*
gi 2159754173 546 DYVIVMKDGQIVQQG 560
Cdd:PRK13651 233 KRTIFFKDGKIIKDG 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
334-537 |
1.20e-08 |
|
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: 53.99 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPdnayQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqtdnftlngqalphlsqa 413
Cdd:cd03221 1 IELENLSKTYGG----KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEP------------------------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 414 nwqkqfsfipqfpylfadtiaanikfyrpeaTEAEVQ-AAVVKAGladFVASLKDGlatkvgeggrgisggQAQRIALAR 492
Cdd:cd03221 53 -------------------------------DEGIVTwGSTVKIG---YFEQLSGG---------------EKMRLALAK 83
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2159754173 493 AFLDQDRrILMFDEPTAHLDIETEYALKETMKPLfkDHLVLFATH 537
Cdd:cd03221 84 LLLENPN-LLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
340-556 |
1.60e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPD-NAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQ 418
Cdd:PRK13650 9 NLTFKYKeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEA------ESGQIIIDGDLLTEENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 419 FSFIPQFP--YLFADTIAANIKF------YRPEATEAEVQAAVVKAGLADFV----ASLKDGlatkvgeggrgisggQAQ 486
Cdd:PRK13650 83 IGMVFQNPdnQFVGATVEDDVAFglenkgIPHEEMKERVNEALELVGMQDFKerepARLSGG---------------QKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 487 RIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEMDYVIVMKDGQI 556
Cdd:PRK13650 148 RVAIAGA-VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
351-568 |
1.66e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.91 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 351 IDLKDISFTlhgyqkvAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQALPHLSQ----ANWQKQFSFIPQFP 426
Cdd:PRK13649 28 LTIEDGSYT-------AFIGHTGSGKSTIMQLLNGLHVP---TQGSV---RVDDTLITSTSKnkdiKQIRKKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 427 --YLFADTIAANIKF----YRPEATEAEvQAAVVKAGLADFVASLKDglatkvgEGGRGISGGQAQRIALArAFLDQDRR 500
Cdd:PRK13649 95 esQLFEETVLKDVAFgpqnFGVSQEEAE-ALAREKLALVGISESLFE-------KNPFELSGGQMRRVAIA-GILAMEPK 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 501 ILMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMtIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
353-558 |
2.29e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQalphlsqanwqkqfsfipqfPYLFADT 432
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQP------DAGSILIDGQ--------------------EMRFAST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 ---IAANIKF------YRPEATEAE--------VQAAVVKAGLADFVASLK-DGLATKVGEGGRGISGGQAQR--IALAR 492
Cdd:PRK11288 74 taaLAAGVAIiyqelhLVPEMTVAEnlylgqlpHKGGIVNRRLLNYEAREQlEHLGVDIDPDTPLKYLSIGQRqmVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 493 AfLDQDRRILMFDEPTAHLDI-ETEyALKETMKPLFKD-HLVLFATHRLHWLKEM-DYVIVMKDGQIVQ 558
Cdd:PRK11288 154 A-LARNARVIAFDEPTSSLSArEIE-QLFRVIRELRAEgRVILYVSHRMEEIFALcDAITVFKDGRYVA 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
334-537 |
2.41e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.09 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPDNAyqidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQAL--PHLS 411
Cdd:PRK11248 2 LQISHLYADYGGKPA----LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPY------QHGSITLDGKPVegPGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 412 QANWQKQFSFIPQfpylfaDTIAANIKF------YRPEATEAEVQAAVVKAGLAD----FVASLKDGlatkvgeggrgis 481
Cdd:PRK11248 72 RGVVFQNEGLLPW------RNVQDNVAFglqlagVEKMQRLEIAHQMLKKVGLEGaekrYIWQLSGG------------- 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 482 ggQAQRIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKD--HLVLFATH 537
Cdd:PRK11248 133 --QRQRVGIARA-LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
354-576 |
2.91e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.87 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 354 KDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLtpmlktQSQTDNFTLNGQALPHLSQANW---QKQFSFIPQFP---- 426
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV------KATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDPlasl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 427 ---YLFADTIAANIKFYRPEATEAE----VQAAVVKAGLadfvaslkdgLATKVGEGGRGISGGQAQRIALARAFLDQDR 499
Cdd:PRK15079 112 nprMTIGEIIAEPLRTYHPKLSRQEvkdrVKAMMLKVGL----------LPNLINRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 500 RILMfDEPTAHLDIETEYALKETMKPLFKDH-LVL-FATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPNGEF-KA 575
Cdd:PRK15079 182 LIIC-DEPVSALDVSIQAQVVNLLQQLQREMgLSLiFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYHNPLHPYtKA 260
|
.
gi 2159754173 576 L 576
Cdd:PRK15079 261 L 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
329-569 |
3.63e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 329 DANSTLTANHFNLQYNPDNAYQIDLKDISFTLHGYQKVAIIGMSGSGKST-------LLNTLGGFLT--PMLKTQSQTDN 399
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQcdKMLLRRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 400 FTLNGQA---LPHLSQANWQKQF-----SFIPQFPylFADTIAANIKFY----RPEA-TEA-----EVQAAVVKAGLADF 461
Cdd:PRK10261 88 IELSEQSaaqMRHVRGADMAMIFqepmtSLNPVFT--VGEQIAESIRLHqgasREEAmVEAkrmldQVRIPEAQTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 462 VASLKDGLAtkvgeggrgisggqaQRIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHL--VLFATHRL 539
Cdd:PRK10261 166 PHQLSGGMR---------------QRVMIAMA-LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDM 229
|
250 260 270
....*....|....*....|....*....|.
gi 2159754173 540 HWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:PRK10261 230 GVVAEIaDRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
353-569 |
3.99e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.36 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLlntlGGFLTpMLKTQSQTDnFTLNGQAL---PHLSQANWQKQFSFIPQFPY-- 427
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL----ARLLT-MIETPTGGE-LYYQGQDLlkaDPEAQKLLRQKIQIVFQNPYgs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 ---------LFADTIAANIKFYRPEATEaEVQAAVVKAGL----ADFVASLKDGlatkvgeggrgisgGQAQRIALARAf 494
Cdd:PRK11308 105 lnprkkvgqILEEPLLINTSLSAAERRE-KALAMMAKVGLrpehYDRYPHMFSG--------------GQRQRIAIARA- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 495 LDQDRRILMFDEPTAHLDIETEYALKETMKPLFKD-HLV-LFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSyVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
353-560 |
4.99e-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: 53.88 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQaLPhlsqanWQKQFSFIPQFPYLF--- 429
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQP---TSGEV---RVAGL-VP------WKRRKKFLRRIGVVFgqk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 430 ---------ADTIAANIKFYRPEATEAevqaavvKAGLADFVASLKdgLATKVGEGGRGISGGQAQRIALARAFLdQDRR 500
Cdd:cd03267 104 tqlwwdlpvIDSFYLLAAIYDLPPARF-------KKRLDELSELLD--LEELLDTPVRQLSLGQRMRAEIAAALL-HEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754173 501 ILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQIVQQG 560
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-569 |
5.12e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.72 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGfLTPMLKTQSQTDNFTLNGQALPHLSQA-NWQKQFSFIPQ----FPY 427
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNR-MNDKVSGYRYSGDVLLGGRSIFNYRDVlEFRRRVGMLFQrpnpFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LFADTIAANIKFYR---PEATEAEVQAAVVKAGLADfvaSLKDGLATKvgegGRGISGGQAQRIALARAfLDQDRRILMF 504
Cdd:PRK14271 116 SIMDNVLAGVRAHKlvpRKEFRGVAQARLTEVGLWD---AVKDRLSDS----PFRLSGGQQQLLCLART-LAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 505 DEPTAHLDIETEYALKETMKPLFKDHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
355-569 |
5.15e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 355 DISFTLHGYQKVAIIGMSGSGKS-TLLNTLGgfLTPMLKTQSQTDNFTLNGQALPHLSQANWQK----QFSFIPQFPYLF 429
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILR--LLPSPPVVYPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 430 AD---TIAANI-------KFYRPEATEAEVQAAVVKAG-------LADFVASLKDGlatkvgeggrgisggQAQRIALAR 492
Cdd:PRK15134 105 LNplhTLEKQLyevlslhRGMRREAARGEILNCLDRVGirqaakrLTDYPHQLSGG---------------ERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 493 AFLDQDrRILMFDEPTAHLDIETEYALKETMKPLfKDHL---VLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:PRK15134 170 ALLTRP-ELLIADEPTTALDVSVQAQILQLLREL-QQELnmgLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATLFSA 247
|
.
gi 2159754173 569 P 569
Cdd:PRK15134 248 P 248
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
351-573 |
5.32e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.42 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 351 IDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMlKTQSQTDNFTLNGQALPHLSQANWQK------QFSFIPQ 424
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT-RGQVLIDGVDIAKISDAELREVRRKKiamvfqSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 425 FPYLfaDTIAANIKFYRPEATEAEVQA--AVVKAGLADFVASLKDGLATKVGeggrgisggqaQRIALARAfLDQDRRIL 502
Cdd:PRK10070 121 MTVL--DNTAFGMELAGINAEERREKAldALRQVGLENYAHSYPDELSGGMR-----------QRVGLARA-LAINPDIL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 503 MFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRL-HWLKEMDYVIVMKDGQIVQQGPVAELAQQPNGEF 573
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-569 |
6.18e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 334 LTANHFNLQYNPdnayQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGF--LTPMLKTQSQTDNFtlnGQAL--PH 409
Cdd:PRK14258 8 IKVNNLSFYYDT----QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMneLESEVRVEGRVEFF---NQNIyeRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 410 LSQANWQKQFSFIPQFPYLFA----DTIAANIKF--YRPEATEAEVQAAVVKAgladfvASLKDGLATKVGEGGRGISGG 483
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFPmsvyDNVAYGVKIvgWRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 484 QAQRIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMK--PLFKDHLVLFATHRLHWLKEM-DYVIVMKD-----GQ 555
Cdd:PRK14258 155 QQQRLCIARA-LAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLsDFTAFFKGnenriGQ 233
|
250
....*....|....
gi 2159754173 556 IVQQGPVAELAQQP 569
Cdd:PRK14258 234 LVEFGLTKKIFNSP 247
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
353-389 |
6.96e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.55 E-value: 6.96e-08
10 20 30
....*....|....*....|....*....|....*..
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP 389
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEP 78
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
364-556 |
1.07e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.86 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 364 QKVAIIGMSGSGKSTLLNTLGGfltpmLKTQSQTDNFTLnGQALPHLSQ----ANWQKQFSFIPQfPYLFADTIAA--NI 437
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAG-----LDDGSSGEVSLV-GQPLHQMDEearaKLRAKHVGFVFQ-SFMLIPTLNAleNV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 438 KFYRPEATEAEVQAavvKAGLADFVASLkdGLATKVGEGGRGISGGQAQRIALARAFLDQDrRILMFDEPTAHLDIETEY 517
Cdd:PRK10584 110 ELPALLRGESSRQS---RNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRP-DVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2159754173 518 ALKETMKPLFKDH---LVLfATHRLHWLKEMDYVIVMKDGQI 556
Cdd:PRK10584 184 KIADLLFSLNREHgttLIL-VTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
353-560 |
1.12e-07 |
|
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: 52.64 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP-----------MLKTQSQTDNFTLNGQ--AL-PHLSqanwqkq 418
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtsgriyiggrdVTDLPPKDRDIAMVFQnyALyPHMT------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 419 fsfipqfpylFADTIAANIKF--YRPEATEAEVQ--AAVVKAG--LADFVASLKDGlatkvgeggrgisggQAQRIALAR 492
Cdd:cd03301 89 ----------VYDNIAFGLKLrkVPKDEIDERVRevAELLQIEhlLDRKPKQLSGG---------------QRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 493 AfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATH-RLHWLKEMDYVIVMKDGQIVQQG 560
Cdd:cd03301 144 A-IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLgtTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
353-568 |
1.46e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTqsqtdnFTLNGQALPHLSQA-NWQKQFSFIPQFPYLFAD 431
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGT------ITINNINYNKLDHKlAAQLGIGIIYQELSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 -TIAANIKFYR-----------PEATEAEVQAAV------VKAGLADFVASLKdglatkvgeggrgisGGQAQRIALARA 493
Cdd:PRK09700 95 lTVLENLYIGRhltkkvcgvniIDWREMRVRAAMmllrvgLKVDLDEKVANLS---------------ISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159754173 494 fLDQDRRILMFDEPTAHL-DIETEYaLKETMKPLFKD-HLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:PRK09700 160 -LMLDAKVIIMDEPTSSLtNKEVDY-LFLIMNQLRKEgTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
353-556 |
1.81e-07 |
|
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: 51.28 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQ-FSFIPQ------- 424
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP------ASGEITLDGKPVTRRSPRDAIRAgIAYVPEdrkregl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 425 FPYLfadTIAANIkfyrpeateaevqaavvkaGLADFvasLKDGlatkvgeggrgisggQAQRIALARAFLdQDRRILMF 504
Cdd:cd03215 90 VLDL---SVAENI-------------------ALSSL---LSGG---------------NQQKVVLARWLA-RDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 505 DEPTAHLDIETEYALKETMKPLFKD-HLVLFATHRLHWLKEM-DYVIVMKDGQI 556
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
348-579 |
2.02e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.32 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 348 AYQIdLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTDN-FTLNGQALPHLSQANWQK------QFS 420
Cdd:PRK11124 14 AHQA-LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhFDFSKTPSDKAIRELRRNvgmvfqQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 421 FIPQFPYLfADTIAANIKFYRPEATEAEVQAA--VVKAGLADFVAS----LKDGlatkvgeggrgisggQAQRIALARAF 494
Cdd:PRK11124 93 LWPHLTVQ-QNLIEAPCRVLGLSKDQALARAEklLERLRLKPYADRfplhLSGG---------------QQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 495 LDQDrRILMFDEPTAHLDIETEYALKETMKPLFKDHLV-LFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQPNGE 572
Cdd:PRK11124 157 MMEP-QVLLFDEPTAALDPEITAQIVSIIRELAETGITqVIVTHEVEVARKTaSRVVYMENGHIVEQGDASCFTQPQTEA 235
|
....*..
gi 2159754173 573 FKALTEH 579
Cdd:PRK11124 236 FKNYLSH 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
353-569 |
3.21e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.89 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQFPYL---- 428
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKP------SEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLrtrl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 ---------------FADTIAANIKFYRPEATEAEVQAA--VVKAGLAD-----FVASLKDGlatkvgeggrgisggQAQ 486
Cdd:PRK10619 95 tmvfqhfnlwshmtvLENVMEAPIQVLGLSKQEARERAVkyLAKVGIDEraqgkYPVHLSGG---------------QQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 487 RIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKD-HLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAE 564
Cdd:PRK10619 160 RVSIARA-LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQ 238
|
....*
gi 2159754173 565 LAQQP 569
Cdd:PRK10619 239 LFGNP 243
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
355-570 |
3.66e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.69 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 355 DISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQA---NWQKQFSFIPQFPYLFAD 431
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP------DHGEILFDGENIPAMSRSrlyTVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 -TIAANIKFYRPEAT---EAEVQA-------AVVKAGLADFVAS-LKDGLatkvgeggrgisggqAQRIALARAF-LDQD 498
Cdd:PRK11831 99 mNVFDNVAYPLREHTqlpAPLLHStvmmkleAVGLRGAAKLMPSeLSGGM---------------ARRAALARAIaLEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 499 rrILMFDEPTAHLDieteyalKETMKPLFKdhLVLFATHRL--------HWLKEM----DYVIVMKDGQIVQQGPVAELA 566
Cdd:PRK11831 164 --LIMFDEPFVGQD-------PITMGVLVK--LISELNSALgvtcvvvsHDVPEVlsiaDHAYIVADKKIVAHGSAQALQ 232
|
....
gi 2159754173 567 QQPN 570
Cdd:PRK11831 233 ANPD 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
353-567 |
4.29e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.74 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSqtdNFTLNGQALP----HLSQANWQKQFSFIPQFPYL 428
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSG---SVLLNGMPIDakemRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 FADTIAANIKFYRPEATEAEVQAavVKAGLADFvaSLKDGLATKVGEGGRGISGG--QAQRIALARAFLdQDRRILMFDE 506
Cdd:TIGR00955 118 EHLMFQAHLRMPRRVTKKEKRER--VDEVLQAL--GLRKCANTRIGVPGRVKGLSggERKRLAFASELL-TDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 507 PTAHLDIETEYALKETMKPLF-KDHLVLFATH----RLHWLkeMDYVIVMKDGQIVQQGPVAELAQ 567
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAqKGKTIICTIHqpssELFEL--FDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
329-560 |
5.97e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.29 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 329 DANSTLTANHFNLQYNPDNAYQidLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFltpmlkTQSQTDNFTLNGQALP 408
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI------EKVKSGEIFYNNQAIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 409 HLSQANWQKQFSFIPQFP--YLFADTIAANIKF------YRPEATEAEVQAAVVKAGLADFVASLKDGLATKvgeggrgi 480
Cdd:PRK13648 75 DDNFEKLRKHIGIVFQNPdnQFVGSIVKYDVAFglenhaVPYDEMHRRVSEALKQVDMLERADYEPNALSGG-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 481 sggQAQRIALArAFLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHLV--LFATHRLHWLKEMDYVIVMKDGQIVQ 558
Cdd:PRK13648 147 ---QKQRVAIA-GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItiISITHDLSEAMEADHVIVMNKGTVYK 222
|
..
gi 2159754173 559 QG 560
Cdd:PRK13648 223 EG 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
353-389 |
6.10e-07 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 50.61 E-value: 6.10e-07
10 20 30
....*....|....*....|....*....|....*..
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP 389
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPP 74
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
353-560 |
7.38e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMlKTQSQTDNF-TLNGQALphlsqanW--QKQFSFIPQFP--Y 427
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPS-EGKVYVDGLdTSDEENL-------WdiRNKAGMVFQNPdnQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LFADTIAANIKF------YRPEATEAEVQAAVVKAGLADF---VASLKDGlatkvgeggrgisgGQAQRIALArAFLDQD 498
Cdd:PRK13633 98 IVATIVEEDVAFgpenlgIPPEEIRERVDESLKKVGMYEYrrhAPHLLSG--------------GQKQRVAIA-GILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 499 RRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEMDYVIVMKDGQIVQQG 560
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
355-569 |
7.80e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 51.27 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 355 DISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQALPHLSQANWQK-----QFSFipQFPY-- 427
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEP---TSGEI---LFDGQDITGLSGRELRPlrrrmQMVF--QDPYas 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 L-----FADTIAANIKFYR---PEATEAEVQAAVVKAGLADFVAS-----LKDGlatkvgeggrgisggQAQRIALARAf 494
Cdd:COG4608 108 LnprmtVGDIIAEPLRIHGlasKAERRERVAELLELVGLRPEHADrypheFSGG---------------QRQRIGIARA- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 495 LDQDRRILMFDEPTAHLD-------------IETEYALkeTMkplfkdhlvLFATHRLHWLKEM-DYVIVMKDGQIVQQG 560
Cdd:COG4608 172 LALNPKLIVCDEPVSALDvsiqaqvlnlledLQDELGL--TY---------LFISHDLSVVRHIsDRVAVMYLGKIVEIA 240
|
....*....
gi 2159754173 561 PVAELAQQP 569
Cdd:COG4608 241 PRDELYARP 249
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
340-570 |
1.01e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.46 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAYQIdLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQA--NWQK 417
Cdd:PRK13639 6 DLKYSYPDGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKP------TSGEVLIKGEPIKYDKKSllEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 418 QFSFIPQFP--YLFADTIAANIKF------YRPEATEAEVQAAVVKAGLADFVASLKDGLATKvgeggrgisggQAQRIA 489
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFgplnlgLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGG-----------QKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 490 LArAFLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHWL-KEMDYVIVMKDGQIVQQGPVAELAQ 567
Cdd:PRK13639 148 IA-GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGItIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
...
gi 2159754173 568 QPN 570
Cdd:PRK13639 227 DIE 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
367-564 |
2.42e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 367 AIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANW----QKQFSFIPQ----FPYLfadTIAANIK 438
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRP------QKGRIVLNGRVLFDAEKGIClppeKRRIGYVFQdarlFPHY---KVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 439 F----YRPEATEAEVQAAVVKAGLADFVASLKDGlatkvgeggrgisggQAQRIALARAFLDQDRRILMfDEPTAHLDIE 514
Cdd:PRK11144 99 YgmakSMVAQFDKIVALLGIEPLLDRYPGSLSGG---------------EKQRVAIGRALLTAPELLLM-DEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 515 TEyalKETMKPLFK-----DHLVLFATHRL-HWLKEMDYVIVMKDGQIVQQGPVAE 564
Cdd:PRK11144 163 RK---RELLPYLERlareiNIPILYVSHSLdEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
353-568 |
2.43e-06 |
|
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: 48.29 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqSQTD-NFTLNGQALPHLSqanwqkqfsfipqfPY---- 427
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKY-----EVTEgEILFKGEDITDLP--------------PEerar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 --LFadtiaanIKFYRPEATEAevqaavVKagLADFVASLKDGLATKvgeggrgisggQAQRIALARAFLdQDRRILMFD 505
Cdd:cd03217 77 lgIF-------LAFQYPPEIPG------VK--NADFLRYVNEGFSGG-----------EKKRNEILQLLL-LEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 506 EPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLHWLKEM--DYVIVMKDGQIVQQGPVaELAQQ 568
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEGKsVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDK-ELALE 194
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
355-565 |
3.26e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.42 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 355 DISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTqsqtdnFTLNGQALP-HLSQAnwQKQFSFIPQFPYLFAD-T 432
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGS------ISLCGEPVPsRARHA--RQRVGVVPQFDNLDPDfT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFYRPEATEAEVQAAVVKAGLADFVAslkdgLATKVGEGGRGISGGQAQRIALARAFLDqDRRILMFDEPTAHLD 512
Cdd:PRK13537 97 VRENLLVFGRYFGLSAAAARALVPPLLEFAK-----LENKADAKVGELSGGMKRRLTLARALVN-DPDVLVLDEPTTGLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2159754173 513 IETEYALKETMKPLF-KDHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAEL 565
Cdd:PRK13537 171 PQARHLMWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
353-557 |
4.26e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.95 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQ--SQTDNFTLNGQALPHLsqanwQKQFSFIPQFPYLFA 430
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfSGHDITRLKNREVPFL-----RRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 431 D-TIAANIKF------YRPEATEAEVQAAVVKAGLAD----FVASLKDGlatkvgeggrgisggQAQRIALARAFLDQDr 499
Cdd:PRK10908 93 DrTVYDNVAIpliiagASGDDIRRRVSAALDKVGLLDkaknFPIQLSGG---------------EQQRVGIARAVVNKP- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 500 RILMFDEPTAHLDieteYALKETMKPLFKDH-----LVLFATHRLHWLKEMDY-VIVMKDGQIV 557
Cdd:PRK10908 157 AVLLADEPTGNLD----DALSEGILRLFEEFnrvgvTVLMATHDIGLISRRSYrMLTLSDGHLH 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
353-569 |
6.22e-06 |
|
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: 48.11 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQAnwqkQF-------SFipQF 425
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRP------TSGRILFDGRDITGLPPH----RIarlgiarTF--QN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 426 PYLFAD------------------TIAANIKFYRPEATEAEVQAAVVKA----GLADFVASLKDGLAtkvgeggrgisGG 483
Cdd:COG0411 88 PRLFPEltvlenvlvaaharlgrgLLAALLRLPRARREEREARERAEELlervGLADRADEPAGNLS-----------YG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 484 QAQRIALARAfLDQDRRILMFDEPTAHLDI-ETEyALKETMKPLfKDHL---VLFATHRLHWLKEM-DYVIVMKDGQIVQ 558
Cdd:COG0411 157 QQRRLEIARA-LATEPKLLLLDEPAAGLNPeETE-ELAELIRRL-RDERgitILLIEHDMDLVMGLaDRIVVLDFGRVIA 233
|
250
....*....|.
gi 2159754173 559 QGPVAELAQQP 569
Cdd:COG0411 234 EGTPAEVRADP 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
340-538 |
6.84e-06 |
|
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: 46.38 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 340 NLQYNPDNAyQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGfltpmlktqsqtdnftlngqaLPHLSQANWQK-- 417
Cdd:cd03223 5 NLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG---------------------LWPWGSGRIGMpe 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 418 --QFSFIPQFPYLfadtiaanikfyrPEATeaevqaavvkagLADFVA-----SLKDGlatkvgeggrgisggQAQRIAL 490
Cdd:cd03223 63 geDLLFLPQRPYL-------------PLGT------------LREQLIypwddVLSGG---------------EQQRLAF 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2159754173 491 ARAFLDQDRRILMfDEPTAHLDIETEYALKEtmkpLFKDHL--VLFATHR 538
Cdd:cd03223 103 ARLLLHKPKFVFL-DEATSALDEESEDRLYQ----LLKELGitVISVGHR 147
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
353-569 |
7.77e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLggfltpMLKTQSQTDNFTLNGQALPHLSQANWQ---KQFSFIPQFPYLF 429
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRAL------LRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIFQDPYAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 430 AD---TIAANI-------KFYRPEATEAEVQAAVVKAGLadfvaslkdgLATKVGEGGRGISGGQAQRIALARAfLDQDR 499
Cdd:PRK10261 414 LDprqTVGDSImeplrvhGLLPGKAAAARVAWLLERVGL----------LPEHAWRYPHEFSGGQRQRICIARA-LALNP 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 500 RILMFDEPTAHLDIETEYALKETMKPLFKDHLV--LFATHRLHWLKEMDY-VIVMKDGQIVQQGP---VAELAQQP 569
Cdd:PRK10261 483 KVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHrVAVMYLGQIVEIGPrraVFENPQHP 558
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
356-582 |
8.93e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 47.69 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 356 ISFTLHGYqkVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQA--NWQKQFSFIPQFP--YLFAD 431
Cdd:PRK13638 22 LDFSLSPV--TGLVGANGCGKSTLFMNLSGLLRP------QKGAVLWQGKPLDYSKRGllALRQQVATVFQDPeqQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 432 TIAANIKFYRPE--ATEAEVQAAVvkaglaDFVASLKDGLATKvGEGGRGISGGQAQRIALARAFLDQDRRILMfDEPTA 509
Cdd:PRK13638 94 DIDSDIAFSLRNlgVPEAEITRRV------DEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLL-DEPTA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159754173 510 HLDIETEYALKETMKPLF-KDHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQGpvaelaqQPnGEFKALTEHMRK 582
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHG-------AP-GEVFACTEAMEQ 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
353-569 |
9.70e-06 |
|
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: 47.28 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMlktqsqTDNFTLNGQALPHLS-QANWQKQFSFIPQ----FPY 427
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR------SGSIRFDGEDITGLPpHRIARLGIGYVPEgrriFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LfadTIAANIK----FYRPEATEAEVQAAV------------VKAGladfvaSLKDGlatkvgeggrgisggQAQRIALA 491
Cdd:COG0410 93 L---TVEENLLlgayARRDRAEVRADLERVyelfprlkerrrQRAG------TLSGG---------------EQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 492 RAfLDQDRRILMFDEPTAHL------DIETeyALKEtmkpLFKDHL-VLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVA 563
Cdd:COG0410 149 RA-LMSRPKLLLLDEPSLGLapliveEIFE--IIRR----LNREGVtILLVEQNARFALEIaDRAYVLERGRIVLEGTAA 221
|
....*.
gi 2159754173 564 ELAQQP 569
Cdd:COG0410 222 ELLADP 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
484-568 |
1.18e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.41 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 484 QAQRIALARAFLdQDRRILMFDEPTAHLD-IETEyALKETMKPLF-KDHLVLFATHRLHWLKEM-DYVIVMKDGQIVQQG 560
Cdd:COG4152 134 NQQKVQLIAALL-HDPELLILDEPFSGLDpVNVE-LLKDVIRELAaKGTTVIFSSHQMELVEELcDRIVIINKGRKVLSG 211
|
....*...
gi 2159754173 561 PVAELAQQ 568
Cdd:COG4152 212 SVDEIRRQ 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
354-569 |
1.47e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.00 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 354 KDISFTLHGYQKVAIIGMSGSGKS-TLLNTLGgfLTPMLKTQSQtDNFTLNGQalPHLSQANWQKQFSFIPQFP------ 426
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALG--ILPAGVRQTA-GRVLLDGK--PVAPCALRGRKIATIMQNPrsafnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 427 -YLFAD----TIAANIKfyrpEATEAEVQAAVVKAGLADFVASLK-------DGLAtkvgeggrgisggqaQRIALARAF 494
Cdd:PRK10418 95 lHTMHThareTCLALGK----PADDATLTAALEAVGLENAARVLKlypfemsGGML---------------QRMMIALAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 495 LdQDRRILMFDEPTAHLDIETEYALKETMKPLFKDHL--VLFATH------RLhwlkeMDYVIVMKDGQIVQQGPVAELA 566
Cdd:PRK10418 156 L-CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHdmgvvaRL-----ADDVAVMSHGRIVEQGDVETLF 229
|
...
gi 2159754173 567 QQP 569
Cdd:PRK10418 230 NAP 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
355-568 |
2.08e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 46.75 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 355 DISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANwQKQFSFIPQFPYLFAD-TI 433
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSP------DAGKITVLGVPVPARARLA-RARIGVVPQFDNLDLEfTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 434 AANI----KFYRPEATEAEvqaAVVKAgLADFVAslkdgLATKVGEGGRGISGGQAQRIALARAFLDqDRRILMFDEPTA 509
Cdd:PRK13536 132 RENLlvfgRYFGMSTREIE---AVIPS-LLEFAR-----LESKADARVSDLSGGMKRRLTLARALIN-DPQLLILDEPTT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 510 HLDIETEYALKETMKPLF-KDHLVLFATHRLHWLKEM-DYVIVMKDG-QIVQQGPVAELAQQ 568
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVLEAGrKIAEGRPHALIDEH 263
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
353-560 |
3.19e-05 |
|
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: 46.72 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGfltpmlktqsqTDNF-TLNGQALPHLS---QANWQKQFSFIPQ---- 424
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG-----------MDQYePTSGRIIYHVAlceKCGYVERPSKVGEpcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 425 ------------------------------FPYLFA----DTIAANIKFYRPEAtEAEVQAAVVKAglADFVASLKdgLA 470
Cdd:TIGR03269 85 cggtlepeevdfwnlsdklrrrirkriaimLQRTFAlygdDTVLDNVLEALEEI-GYEGKEAVGRA--VDLIEMVQ--LS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 471 TKVGEGGRGISGGQAQRIALARAfLDQDRRILMFDEPTAHLDIETEYALKETMKPLFKDH---LVLFAthrlHWLKEM-- 545
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQ-LAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgisMVLTS----HWPEVIed 234
|
250
....*....|....*..
gi 2159754173 546 --DYVIVMKDGQIVQQG 560
Cdd:TIGR03269 235 lsDKAIWLENGEIKEEG 251
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
356-569 |
5.22e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.98 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 356 ISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTqsqtdnFTLNGQALPHLSQAN---------WQ-----KQFSF 421
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGT------ILLRGQHIEGLPGHQiarmgvvrtFQhvrlfREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 422 I-----PQFPYLFADTIAANIK---FYRPEAtEAEVQAAV--VKAGLADFVASLKDGLAtkvgeggrgisGGQAQRIALA 491
Cdd:PRK11300 98 IenllvAQHQQLKTGLFSGLLKtpaFRRAES-EALDRAATwlERVGLLEHANRQAGNLA-----------YGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 492 RAFLDQDrRILMFDEPTAHLDIETEYALKETMKPLFKDH--LVLFATHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:PRK11300 166 RCMVTQP-EILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGIsDRIYVVNQGTPLANGTPEEIRNN 244
|
.
gi 2159754173 569 P 569
Cdd:PRK11300 245 P 245
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
353-540 |
6.18e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 44.72 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTDnftlngqalphlsqanwQKQFSFIPQFPYLFAdT 432
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------------KLRIGYVPQKLYLDT-T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 433 IAANIKFY---RPEATEAEVQAAV--VKAG-LADF-VASLKDGlatkvgeggrgisggQAQRIALARAFLDQDrRILMFD 505
Cdd:PRK09544 82 LPLTVNRFlrlRPGTKKEDILPALkrVQAGhLIDApMQKLSGG---------------ETQRVLLARALLNRP-QLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 2159754173 506 EPTAHLDIETEYALKETMKPLFK--DHLVLFATHRLH 540
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLH 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
331-565 |
6.51e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.08 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 331 NSTLTANHFNLQYNPDNAYQiDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLtpmlktQSQTDNFTLNGQALPHL 410
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVN-QLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF------EEFEGKVKIDGELLTAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 411 SQANWQKQFSFIPQFP--YLFADTIAANIKFYRP------EATEAEVQAAVVKAGLADFV----ASLKDGlatkvgeggr 478
Cdd:PRK13642 75 NVWNLRRKIGMVFQNPdnQFVGATVEDDVAFGMEnqgiprEEMIKRVDEALLAVNMLDFKtrepARLSGG---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 479 gisggQAQRIALArAFLDQDRRILMFDEPTAHLDIETEYALKETMKPLfKD--HL-VLFATHRLHWLKEMDYVIVMKDGQ 555
Cdd:PRK13642 145 -----QKQRVAVA-GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI-KEkyQLtVLSITHDLDEAASSDRILVMKAGE 217
|
250
....*....|
gi 2159754173 556 IVQQGPVAEL 565
Cdd:PRK13642 218 IIKEAAPSEL 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-389 |
7.32e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 44.69 E-value: 7.32e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP 389
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPP 58
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
353-521 |
1.33e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.93 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqtdnftLNGQALPhlsqanwQKQFS--FIPQFPYL-- 428
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------------FNGEARP-------QPGIKvgYLPQEPQLdp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 -----------FADTIAA-------NIKFYRPEA-------TEAEVQAAVVKAGLADF-------------------VAS 464
Cdd:TIGR03719 82 tktvrenveegVAEIKDAldrfneiSAKYAEPDAdfdklaaEQAELQEIIDAADAWDLdsqleiamdalrcppwdadVTK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 465 LKDGlatkvgeggrgisggQAQRIALARAFLDQ-DrrILMFDEPTAHLDIET----EYALKE 521
Cdd:TIGR03719 162 LSGG---------------ERRRVALCRLLLSKpD--MLLLDEPTNHLDAESvawlERHLQE 206
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
353-561 |
1.45e-04 |
|
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: 43.76 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLN-TLGGFLTPML-KTQSQTDNFTLNGQA-----LPHLSQ-----------AN 414
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLYPALARRLhLKKEQPGNHDRIEGLehidkVIVIDQspigrtprsnpAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 415 WQKQFSFIPQfpyLFADTIAAniKFYRPEATE--------AEVQAAVVKAGLADF--VASLKDGLATKVGEGGRGISGGQ 484
Cdd:cd03271 91 YTGVFDEIRE---LFCEVCKG--KRYNRETLEvrykgksiADVLDMTVEEALEFFenIPKIARKLQTLCDVGLGYIKLGQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 485 ---------AQRIALARAFLDQD--RRILMFDEPTAHLDIETEYALKETMKPLF-KDHLVLFATHRLHWLKEMDYVIVM- 551
Cdd:cd03271 166 pattlsggeAQRIKLAKELSKRStgKTLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWIIDLg 245
|
250
....*....|....*
gi 2159754173 552 -----KDGQIVQQGP 561
Cdd:cd03271 246 peggdGGGQVVASGT 260
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
353-389 |
2.01e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 2.01e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP 389
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEP 371
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
356-569 |
2.67e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 356 ISFTLHGYQKVAIIGMSGSGKS-TLLNTLGGFLTPmlkTQSQTDNFTLNGQALPHLSQANWQK----QFSFIPQFP---- 426
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP---GRVMAEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPmtsl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 427 ---YLFADTIAANIKFYRPEATEAEVQAAV---VKAGLAD-------FVASLKDGLATKVGeggrgisggqaqrIALARA 493
Cdd:PRK11022 103 npcYTVGFQIMEAIKVHQGGNKKTRRQRAIdllNQVGIPDpasrldvYPHQLSGGMSQRVM-------------IAMAIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 494 FldqDRRILMFDEPTAHLDIETEYALKETMKPLFKDH---LVLFaTHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:PRK11022 170 C---RPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmaLVLI-THDLALVAEAaHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
355-537 |
2.84e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.48 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 355 DISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPM--------LKTQSQTDNFtlnGQALPHLSQANWQKqfsfipqfP 426
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDagevlwqgEPIRRQRDEY---HQDLLYLGHQPGIK--------T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 427 YLFADTiaaNIKFYRP---EATEAEVQAAVVKAGLADF----VASLKDGlatkvgeggrgisggQAQRIALARAFLDqDR 499
Cdd:PRK13538 88 ELTALE---NLRFYQRlhgPGDDEALWEALAQVGLAGFedvpVRQLSAG---------------QQRRVALARLWLT-RA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2159754173 500 RILMFDEP-TAhLDIETEYALKEtmkpLFKDHL-----VLFATH 537
Cdd:PRK13538 149 PLWILDEPfTA-IDKQGVARLEA----LLAQHAeqggmVILTTH 187
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
487-557 |
3.66e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 3.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754173 487 RIALARAfLDQDRRILMFDEPTAHLDIET----EYALKEtmkplFKDHLVlFATHRLHWLKEMDYVIVMKD-GQIV 557
Cdd:PRK11147 164 KAALGRA-LVSNPDVLLLDEPTNHLDIETiewlEGFLKT-----FQGSII-FISHDRSFIRNMATRIVDLDrGKLV 232
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
353-389 |
4.43e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 4.43e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP 389
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSP 76
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
343-560 |
4.57e-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: 43.46 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 343 YNPDNAYQIDLKDISFtlHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqTDNFTLNGQALPHLSQANWQKQFSFI 422
Cdd:TIGR01257 938 FEPSGRPAVDRLNITF--YENQITAFLGHNGAGKTTTLSILTGLLPP-------TSGTVLVGGKDIETNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 423 PQFPYLFAD-TIAANIKFYrpeateAEVQAAVVKAGLADFVASLKD-GLATKVGEGGRGISGGQAQRIALARAFLDqDRR 500
Cdd:TIGR01257 1009 PQHNILFHHlTVAEHILFY------AQLKGRSWEEAQLEMEAMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVG-DAK 1081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 501 ILMFDEPTAHLDIETEYALKETMKPLFKDHLVLFATHrlhwlkEMDYVIVMKDG-QIVQQG 560
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTH------HMDEADLLGDRiAIISQG 1136
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
353-512 |
5.06e-04 |
|
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: 42.04 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTL-GGFLTpmlktQSQTDNFTLNGQALPhLSQAN-------------WQKQ 418
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIyGNYLP-----DSGSILVRHDGGWVD-LAQASpreilalrrrtigYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 419 F-SFIPQFPYLfaDTIAanikfyRP------EATEAEVQAavvKAGLADFvaSLKDGL-----AT-----Kvgeggrgis 481
Cdd:COG4778 101 FlRVIPRVSAL--DVVA------EPllergvDREEARARA---RELLARL--NLPERLwdlppATfsggeQ--------- 158
|
170 180 190
....*....|....*....|....*....|.
gi 2159754173 482 ggqaQRIALARAFLdQDRRILMFDEPTAHLD 512
Cdd:COG4778 159 ----QRVNIARGFI-ADPPLLLLDEPTASLD 184
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
353-513 |
5.59e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.71 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLS-QANWQKQFSFIPQFPY---L 428
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP------ASGSIRLDGEDITGLSpRERRRLGVAYIPEDRLgrgL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 429 FAD-TIAANI---KFYRPE----------ATEAEVQAAV----VKA-GLADFVASLKDGlatkvgeggrgisggQAQRIA 489
Cdd:COG3845 348 VPDmSVAENLilgRYRRPPfsrggfldrkAIRAFAEELIeefdVRTpGPDTPARSLSGG---------------NQQKVI 412
|
170 180
....*....|....*....|....
gi 2159754173 490 LARAfLDQDRRILMFDEPTAHLDI 513
Cdd:COG3845 413 LARE-LSRDPKLLIAAQPTRGLDV 435
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
12-294 |
6.39e-04 |
|
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: 41.99 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 12 LTLTLIWVTILTGIQGIAIICQAHFLTRALVNSWqmKPLATLTTAIILFGGAFLLRHVCVWLKNIILDHYADHTSNLLRD 91
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQ--GDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 92 RLLDQVYVTGANQIAQTGTGKLVT-VALDgINNVYNYFNLIFAKIF-DMMIIpFLVIIYIYWQSVRSGIILTIVFPVVIL 169
Cdd:cd18544 79 DLFSHIQRLPLSFFDRTPVGRLVTrVTND-TEALNELFTSGLVTLIgDLLLL-IGILIAMFLLNWRLALISLLVLPLLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 170 FMIILgfaaQDKADRQYAGF-IKLS--NHFV-DSLRGLATLKFLGLSKRYETNVYEVSEDYRRSTMDTLRIAILSTFALD 245
Cdd:cd18544 157 ATYLF----RKKSRKAYREVrEKLSrlNAFLqESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVE 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2159754173 246 WFTTLSIALLALFLGLALINGSMPL--FPALVSLILapEFFLPIRDFGNDY 294
Cdd:cd18544 233 LLSSLALALVLWYGGGQVLSGAVTLgvLYAFIQYIQ--RFFRPIRDLAEKF 281
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
345-556 |
6.45e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.65 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 345 PDNAYqiDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsQTDNFTLNGQALPHLSQANWQKQFSFIPQ 424
Cdd:PRK10522 333 QDNGF--SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP------QSGEILLDGKPVTAEQPEDYRKLFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 425 FPYLFADTIAanikfyrPEATEAE---VQAAVVKAGLADFVaSLKDG--LATKVgeggrgiSGGQAQRIALARAFLDQdR 499
Cdd:PRK10522 405 DFHLFDQLLG-------PEGKPANpalVEKWLERLKMAHKL-ELEDGriSNLKL-------SKGQKKRLALLLALAEE-R 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 500 RILMFDEPTAHLDIETEYALKETMKPLFKD--HLVLFATHRLHWLKEMDYVIVMKDGQI 556
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
353-526 |
9.03e-04 |
|
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: 40.69 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISftlhGYQK----VAIIGMSGSGKSTLLNTLGGfltpmLKTQSQ-TDNFTLNGQALPhlsqANWQKQFSFIPQFPY 427
Cdd:cd03232 23 LNNIS----GYVKpgtlTALMGESGAGKTTLLDVLAG-----RKTAGViTGEILINGRPLD----KNFQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 428 LFadtiaanikfyrPEATeaevqaavVKAGLaDFVASLKdGLATKvgeggrgisggQAQRIALARAfLDQDRRILMFDEP 507
Cdd:cd03232 90 HS------------PNLT--------VREAL-RFSALLR-GLSVE-----------QRKRLTIGVE-LAAKPSILFLDEP 135
|
170
....*....|....*....
gi 2159754173 508 TAHLDIETEYALKETMKPL 526
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKL 154
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
357-551 |
1.02e-03 |
|
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: 41.20 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 357 SFTLHGY------QKVAIIGMSGSGKSTLLNTLGGFLTPMLKTQSQTDNFTlngQALPHLSQANWQKQFSFI-------- 422
Cdd:cd03236 14 SFKLHRLpvpregQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWD---EILDEFRGSELQNYFTKLlegdvkvi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 423 --PQF----PYLFADTIAANIKfyrpEATEAEVQAAVVKA----GLAD-FVASLKDGlatkvgeggrgisggQAQRIALA 491
Cdd:cd03236 91 vkPQYvdliPKAVKGKVGELLK----KKDERGKLDELVDQlelrHVLDrNIDQLSGG---------------ELQRVAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 492 RAFLdQDRRILMFDEPTAHLDIETEYALKETMKPLFKD-HLVLFATHRLHWLKEM-DYVIVM 551
Cdd:cd03236 152 AALA-RDADFYFFDEPSSYLDIKQRLNAARLIRELAEDdNYVLVVEHDLAVLDYLsDYIHCL 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
484-565 |
1.24e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 484 QAQRIALARAfLDQDRRILMFDEPTAHL-DIETEyALKETMKPLfKDHLV--LFATHRLHWLKEM-DYVIVMKDGQIVQQ 559
Cdd:PRK13549 148 QQQLVEIAKA-LNKQARLLILDEPTASLtESETA-VLLDIIRDL-KAHGIacIYISHKLNEVKAIsDTICVIRDGRHIGT 224
|
....*.
gi 2159754173 560 GPVAEL 565
Cdd:PRK13549 225 RPAAGM 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
367-565 |
1.56e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 367 AIIGMSGSGKSTLLNTLGGFLTP---MLKTQSQTDNFtlNGqalPHLSQanwQKQFSFIPQ----FPYLfadTIAANIkF 439
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRdagSILYLGKEVTF--NG---PKSSQ---EAGIGIIHQelnlIPQL---TIAENI-F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 440 YRPEATE-----------AEVQAAVVKAGLA----DFVASLKDGlatkvgeggrgisggQAQRIALARAFLDQDRRILMf 504
Cdd:PRK10762 102 LGREFVNrfgridwkkmyAEADKLLARLNLRfssdKLVGELSIG---------------EQQMVEIAKVLSFESKVIIM- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754173 505 DEPTAHL-DIETEyALKETMKPL-FKDHLVLFATHRlhwLKEM----DYVIVMKDGQIVQQGPVAEL 565
Cdd:PRK10762 166 DEPTDALtDTETE-SLFRVIRELkSQGRGIVYISHR---LKEIfeicDDVTVFRDGQFIAEREVADL 228
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
370-514 |
1.57e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.22 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 370 GMSGSGKSTLLNTLGGFLtpmlktQSQTDNFTLNGQalpHLSQANWQKQFSFIPQFPYLFADTIA-ANIKF------YRP 442
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLL------HVESGQIQIDGK---TATRGDRSRFMAYLGHLPGLKADLSTlENLHFlcglhgRRA 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159754173 443 EATEAEVQAAVvkaGLADFVASLKDGLATKvgeggrgisggQAQRIALARAFLDQdRRILMFDEPTAHLDIE 514
Cdd:PRK13543 115 KQMPGSALAIV---GLAGYEDTLVRQLSAG-----------QKKRLALARLWLSP-APLWLLDEPYANLDLE 171
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
346-389 |
1.65e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 1.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2159754173 346 DNAYQIDLKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP 389
Cdd:PRK13545 33 DGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMP 76
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
365-384 |
2.78e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 38.93 E-value: 2.78e-03
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
356-568 |
3.19e-03 |
|
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: 40.17 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 356 ISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP---------------MLKTqsqtdNFTLNGQALPHLSQANwqKQFS 420
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPtsgevnvrvgdewvdMTKP-----GPDGRGRAKRYIGILH--QEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 421 FIPQFPYLFADTIAANIKFyrPEateaevQAAVVKAGLADFVASLKDGLATKVGEGGRGISGG-QAQRIALARAfLDQDR 499
Cdd:TIGR03269 376 LYPHRTVLDNLTEAIGLEL--PD------ELARMKAVITLKMVGFDEEKAEEILDKYPDELSEgERHRVALAQV-LIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754173 500 RILMFDEPTAHLDIETEYALKETM----KPLFKDHLVLfaTHRLHWLKEM-DYVIVMKDGQIVQQGPVAELAQQ 568
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIV--SHDMDFVLDVcDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
364-554 |
5.08e-03 |
|
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: 37.74 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 364 QKVAIIGMSGSGKSTLLNTLGGFLTPmlktqsqtdnftlngqalphlsqanwqKQFSFIpqfpYLFADTIAANIKFYRPE 443
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGP---------------------------PGGGVI----YIDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 444 ATEAEVQAAVVKAgladfvaslkdglatkvgeggrgisggQAQRIALARAfLDQDRRILMFDEPTAHLDIETEYAL---- 519
Cdd:smart00382 52 IIVGGKKASGSGE---------------------------LRLRLALALA-RKLKPDVLILDEITSLLDAEQEALLllle 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2159754173 520 ---KETMKPLFKDHLVLFATHRLHWLKEM------DYVIVMKDG 554
Cdd:smart00382 104 elrLLLLLKSEKNLTVILTTNDEKDLGPAllrrrfDRRIVLLLI 147
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
365-383 |
5.84e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.83 E-value: 5.84e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
484-566 |
6.19e-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: 39.61 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 484 QAQRIALARAFLDQD--RRILMFDEPTAHLDIETEYALKETMKPLF-KDHLVLFATHRLHWLKEMDYVIVM------KDG 554
Cdd:TIGR00630 834 EAQRIKLAKELSKRStgRTLYILDEPTTGLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGG 913
|
90
....*....|..
gi 2159754173 555 QIVQQGPVAELA 566
Cdd:TIGR00630 914 TVVASGTPEEVA 925
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
126-284 |
6.82e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 38.62 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 126 NYFNLIFAKIFDMMIIPFLVIIYIYWQSVRSGIILTIVFPVVILFMIILGFAAQDKADRQYAGFI-KLSNHFVDSLRGLA 204
Cdd:cd18585 107 NLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLGKKIGQQLVQLRaELRTELVDGLQGMA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 205 TLKFLGLSKRYETNVYEVSEDY-----RRSTMDTLRIAiLSTFALDWFTTLSIALLALFLGLALING---------SMPL 270
Cdd:cd18585 187 ELLIFGALERQRQQLEQLSDALikeqrRLARLSGLSQA-LMILLSGLTVWLVLWLGAPLVQNGALDGallamlvfaVLAS 265
|
170
....*....|....
gi 2159754173 271 FPALVSLILAPEFF 284
Cdd:cd18585 266 FEAVAPLPLAFQYL 279
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
48-252 |
7.02e-03 |
|
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: 38.56 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 48 KPLATLTTAIILFGGAFLLRHVCVWLKNIILDHYADHTSNLLRDRLLDQVYVTGANQIAQTGTGKLVTVALDGINNVYNY 127
Cdd:cd18552 33 KDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 128 FNLIFAKIF-DMMIIPFLvIIYIYWQSVRSGIILTIVFPVVILFMIILGFAAQDKADRQYAGFIKLSNHFVDSLRGLATL 206
Cdd:cd18552 113 LTSALTVLVrDPLTVIGL-LGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVV 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2159754173 207 KFLGLSKRYETNVYEVSEDYRRSTMDTLRIAILSTFALDWFTTLSI 252
Cdd:cd18552 192 KAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAI 237
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-389 |
7.32e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 38.91 E-value: 7.32e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTP 389
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVP 74
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
353-569 |
7.66e-03 |
|
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: 38.29 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 353 LKDISFTLHGYQKVAIIGMSGSGKSTLLNTLGGFLTPmlkTQSQTdnfTLNGQALPHL---SQAnwQKQFSFIPQFPYLF 429
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKP---DSGKI---LLDGQDITKLpmhKRA--RLGIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754173 430 AD-TIAANIK-----FYRPEATEAEVqaavVKAGLADF-VASLKDGLAtkvgeggRGISGGQAQRIALARAfLDQDRRIL 502
Cdd:cd03218 88 RKlTVEENILavleiRGLSKKEREEK----LEELLEEFhITHLRKSKA-------SSLSGGERRRVEIARA-LATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 503 MFDEPTAHLDIETEYALKETMKPLFKDHL-VLFATHRLH-WLKEMDYVIVMKDGQIVQQGPVAELAQQP 569
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
486-555 |
7.94e-03 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 38.54 E-value: 7.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159754173 486 QRIALArAFLDQDRRILMFDEPTAHLDIET---------EYALKETMKPLFKDHLVLFATHRlhwlkeMDYVIVMkDGQ 555
Cdd:cd03237 122 QRVAIA-ACLSKDADIYLLDEPSAYLDVEQrlmaskvirRFAENNEKTAFVVEHDIIMIDYL------ADRLIVF-EGE 192
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
360-394 |
7.96e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 7.96e-03
10 20 30
....*....|....*....|....*....|....*
gi 2159754173 360 LHGYQKVAIIGMSGSGKSTLLNTLGGflTPMLKTQ 394
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLG--EEVQKTG 224
|
|
| |
