|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-556 |
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: 649.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 2 IDQHLFKLA-GAGSILKKLAVLEVLQAFLIIGQALSLSAVLTTLWQGKK---LNWQYLLIFIVCLTGRQLIDLLKDKMLE 77
Cdd:COG4988 4 LDKRLKRLArGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAplsALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 78 TYSSQEVEKLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYIKLIYTKVLAMMIIPILLFIAMLFINWQSALG 157
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 158 LLLMYPLIVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAML 237
Cdd:COG4988 164 LLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 238 STFALDFFTTLSIAVVAVYLGFGLLNGQLPLYPALSILILAPEYFLPIRNFASDYHATLNGKNAFKRINELISRPMQASA 317
Cdd:COG4988 244 SSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 318 DLAIE-PWNSKSELKLENLEFNYNNQTEI-GPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAAT 395
Cdd:COG4988 324 AGTAPlPAAGPPSIELEDVSFSYPGGRPAlDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 396 LNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIA 475
Cdd:COG4988 404 LDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 476 LARAFLdKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEA 555
Cdd:COG4988 484 LARALL-RDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
.
gi 543385153 556 G 556
Cdd:COG4988 563 G 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-537 |
0e+00 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 534.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 15 ILKKLAVLEVLQAFLIIGQALSLSAVLTTLWQGKK----LNWQYLLIFIVcLTGRQLIDLLKDKMLETYSSQEVEKLRQQ 90
Cdd:TIGR02857 4 ALALLALLGVLGALLIIAQAWLLARVVDGLISAGEplaeLLPALGALALV-LLLRALLGWLQERAAARAAAAVKSQLRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 91 LLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYIKLIYTKVLAMMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMI 170
Cdd:TIGR02857 83 LLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 171 ILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSI 250
Cdd:TIGR02857 163 LIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 251 AVVAVYLGFGLLNGQLPLYPALSILILAPEYFLPIRNFASDYHATLNGKNAFKRINELISRPMQASADLAIEPWNSKSEL 330
Cdd:TIGR02857 243 ALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 331 KLENLEFNYNNQTE-IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIP 409
Cdd:TIGR02857 323 EFSGVSVAYPGRRPaLRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVML 489
Cdd:TIGR02857 403 QHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFL-RDAPLLL 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 543385153 490 FDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVM 537
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-564 |
2.74e-128 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 388.05 E-value: 2.74e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 18 KLAVL-EVLQAFLIIGQAlslsAVLTTLWQG--------KKLNWQYLLIfIVCLTGRQLIDLLKD-------KMLETYss 81
Cdd:PRK11174 25 NLSILlGFLSGLLLIAQA----WLLATILQAliieniprEALLPPFILL-ILLFVLRALLAWLRErvgfkagQHIRQQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 82 qevekLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYikliYTKVLAMM----IIPILLFIAMLFINWQSALG 157
Cdd:PRK11174 98 -----IRQQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDF----YARYLPQMalavLVPLLILIAVFPINWAAGLI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 158 LLLMYPLIVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAML 237
Cdd:PRK11174 169 LLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 238 STFALDFFTTLSIAVVAVYLGFGLL--------NGQLPLYPALSILILAPEYFLPIRNFASDYHATLNGKNAFKRINELI 309
Cdd:PRK11174 249 SSAVLEFFASISIALVAVYFGFSYLgelnfghyGTGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 310 SRPMQASADLAIE-PWNSKSELKLENLE-FNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKsGKII 387
Cdd:PRK11174 329 ETPLAHPQQGEKElASNDPVTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLK 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 388 IDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLS 467
Cdd:PRK11174 408 INGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLS 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 468 GGQAQRIALARAFLDKTRkVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGT 547
Cdd:PRK11174 488 VGQAQRLALARALLQPCQ-LLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGD 566
|
570
....*....|....*..
gi 543385153 548 FDELTKEAGYFTKLTQE 564
Cdd:PRK11174 567 YAELSQAGGLFATLLAH 583
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-561 |
8.30e-118 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 360.63 E-value: 8.30e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 19 LAVLEVLQAFLIIGQALSLSAVLTTLWQGKKLN--WQYLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIF 96
Cdd:COG1132 26 ALLLLLLSALLELLLPLLLGRIIDALLAGGDLSalLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 97 KSGQSLVQSQGTGSLITMALYGIDEVRDYIKLIYTKVLAMMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYAA 176
Cdd:COG1132 106 RLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 177 KDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVY 256
Cdd:COG1132 186 RKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 257 LGFGLLNGQLPLYPALSILILAPEYFLPIRNFASDYHATLNGKNAFKRINELISRPMQ-ASADLAIEPWNSKSELKLENL 335
Cdd:COG1132 266 GGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEiPDPPGAVPLPPVRGEIEFENV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 336 EFNYNNQTEI--GpVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPY 413
Cdd:COG1132 346 SFSYPGDRPVlkD-ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTF 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 414 VFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVMLFDEP 493
Cdd:COG1132 425 LFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALL-KDPPILILDEA 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 494 TAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKL 561
Cdd:COG1132 504 TSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARL 571
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
19-305 |
1.48e-108 |
|
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: 326.67 E-value: 1.48e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 19 LAVLEVLQAFLIIGQALSLSAVLTTLWQGKKLN---WQYLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKI 95
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLaalLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 96 FKSGQSLVQSQGTGSLITMALYGIDEVRDYIKLIYTKVLAMMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYA 175
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 176 AKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAV 255
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 543385153 256 YLGFGLLNGQLPLYPALSILILAPEYFLPIRNFASDYHATLNGKNAFKRI 305
Cdd:cd18584 241 YIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
119-563 |
7.91e-93 |
|
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: 295.52 E-value: 7.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 119 IDEVRD-YIKLIYTKVLAMMIIpILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYAAKDRASKQFGD-FQKLSNNFID 196
Cdd:COG4987 122 VDALDNlYLRVLLPLLVALLVI-LAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAaRAALRARLTD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 197 SLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQLPLyPALSILI 276
Cdd:COG4987 201 LLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSG-PLLALLV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 277 LAP----EYFLPIRNFASDYHATLNgknAFKRINELISRPMQASADLAIEPWNSKSELKLENLEFNYNNQTE--IGPVSV 350
Cdd:COG4987 280 LAAlalfEALAPLPAAAQHLGRVRA---AARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRpvLDGLSL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 351 EIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEA 430
Cdd:COG4987 357 TLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDA 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 431 SDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLDIETEVDLKKQML 510
Cdd:COG4987 437 TDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALL-RDAPILLLDEPTEGLDAATEQALLADLL 515
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 543385153 511 PLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKLTQ 563
Cdd:COG4987 516 EALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
52-564 |
2.81e-92 |
|
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: 298.29 E-value: 2.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 52 WQYLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIFKSGQSLVQSQGTGSLITmALYGIDEVRDYIkliyT 131
Cdd:COG2274 196 WVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAS-RFRDVESIREFL----T 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 132 KVLAMMII--PILLF--IAMLFINWQSALGLLLMYPLIVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYL 207
Cdd:COG2274 271 GSLLTALLdlLFVLIflIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKAL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 208 GLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQLPL-----YPALSILILAPeyF 282
Cdd:COG2274 351 GAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLgqliaFNILSGRFLAP--V 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 283 LPIRNFASDYHATlngKNAFKRINELISRPM-QASADLAIEPWNSKSELKLENLEFNYNNQTE--IGPVSVEIKGYEKVG 359
Cdd:COG2274 429 AQLIGLLQRFQDA---KIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGDSPpvLDNISLTIKPGERVA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 360 IIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAI 439
Cdd:COG2274 506 IVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAA 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 440 HVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRkVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVI 519
Cdd:COG2274 586 RLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPR-ILILDEATSALDAETEAIILENLRRLLKGRTVI 664
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 543385153 520 FATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKLTQE 564
Cdd:COG2274 665 IIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
108-550 |
5.46e-65 |
|
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: 224.74 E-value: 5.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 108 TGSLITMaLYGIDEVRDYIKliYTKVLAMMIIP-ILLFIAMLFInwqsaLGLLLMYP--LIVLFMIILGYAAKDRASKQF 184
Cdd:TIGR03375 242 VGSFANQ-LREFESVRDFFT--SATLTALIDLPfALLFLLVIAI-----IGGPLVWVplVAIPLILLPGLLLQRPLSRLA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 185 GDFQKLSN----NFIDSLRGIDTLKYLGLS-------KRYSKSIFRVSEDFRHKTMAVLKVAMLSTFaldfFTTLSIAVV 253
Cdd:TIGR03375 314 EESMRESAqrnaVLVESLSGLETIKALNAEgrfqrrwEQTVAALARSGLKSRFLSNLATNFAQFIQQ----LVSVAIVVV 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 254 AVYLgfgLLNGQLPLYPALSILILAPEYFLPIRNFAS---DYHATlngKNAFKRINELISRPMQASADLA-IEPWNSKSE 329
Cdd:TIGR03375 390 GVYL---ISDGELTMGGLIACVMLSGRALAPLGQLAGlltRYQQA---KTALQSLDELMQLPVERPEGTRfLHRPRLQGE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLY 407
Cdd:TIGR03375 464 IEFRNVSFAYPGQETpaLDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRkV 487
Cdd:TIGR03375 544 VPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPP-I 622
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 488 MLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDE 550
Cdd:TIGR03375 623 LLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQ 685
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
328-556 |
7.84e-65 |
|
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: 211.32 E-value: 7.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 328 SELKLENLEFNYNNQTE-IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQML 406
Cdd:cd03254 1 GEIEFENVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 407 YIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRK 486
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAML-RDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 487 VMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAG 556
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
330-561 |
1.58e-60 |
|
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: 200.15 E-value: 1.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLY 407
Cdd:cd03251 1 VEFKNVTFRYPGDGPpvLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKV 487
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALL-KDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543385153 488 MLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKL 561
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
330-541 |
1.87e-59 |
|
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: 195.29 E-value: 1.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLY 407
Cdd:cd03228 1 IEFKNVSFSYPGRPKpvLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVFTASLRENIafytpeasdaeimkaihvvsldelvselpegldtiigqgkrvLSGGQAQRIALARAFLDKtRKV 487
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRD-PPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 543385153 488 MLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGK 541
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
332-563 |
4.26e-59 |
|
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: 196.61 E-value: 4.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 332 LENLEFNYNNQTEIG---PVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYI 408
Cdd:cd03249 3 FKNVSFRYPSRPDVPilkGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 409 PQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVM 488
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL-RNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 489 LFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKLTQ 563
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
85-525 |
9.49e-57 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 199.12 E-value: 9.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 85 EKLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYI-KLIYTKVLAMMIIPI-LLFIAMLFinWQSALGLLLMY 162
Cdd:TIGR02868 86 GALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYvRVIVPAGVALVVGAAaVAAIAVLS--VPAALILAAGL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 163 PLIVLFMIILGYaakdRASKQFGDFQK-----LSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAML 237
Cdd:TIGR02868 164 LLAGFVAPLVSL----RAARAAEQALArlrgeLAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATAL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 238 STFALDFFTTLSIAVVAVYLGFGLLNGQLPlYPALSILILAP----EYFLPIRNfASDYHATlnGKNAFKRINELI--SR 311
Cdd:TIGR02868 240 GAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPlaafEAFAALPA-AAQQLTR--VRAAAERIVEVLdaAG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 312 PMQASADLAIEPWNS-KSELKLENLEFNYNNQTEI-GPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIID 389
Cdd:TIGR02868 316 PVAEGSAPAAGAVGLgKPTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 390 GQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGG 469
Cdd:TIGR02868 396 GVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGG 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 470 QAQRIALARAFLDKTRkVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRL 525
Cdd:TIGR02868 476 ERQRLALARALLADAP-ILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
145-561 |
1.05e-56 |
|
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: 199.93 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 145 IAMLFI-NWQSALGLLLMYPLIVLFMIILGYAAKdRASKQFGDFQKLSNNFID-SLRGIDTLKYLGlSKRYSKSIF--RV 220
Cdd:TIGR02204 150 LIMMFItSPKLTSLVLLAVPLVLLPILLFGRRVR-KLSRESQDRIADAGSYAGeTLGAIRTVQAFG-HEDAERSRFggAV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 221 SEDFRHKTMAVLKVAMLSTFALdfftTLSIAVVAVYLGFGllnGQLPLYPALSILILAPEYFLPIrnFASDYHATLN--- 297
Cdd:TIGR02204 228 EKAYEAARQRIRTRALLTAIVI----VLVFGAIVGVLWVG---AHDVIAGKMSAGTLGQFVFYAV--MVAGSIGTLSevw 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 298 -----GKNAFKRINELisrpMQASADLAiEPWNSKS-------ELKLENLEFNYNNQTE---IGPVSVEIKGYEKVGIIG 362
Cdd:TIGR02204 299 gelqrAAGAAERLIEL----LQAEPDIK-APAHPKTlpvplrgEIEFEQVNFAYPARPDqpaLDGLNLTVRPGETVALVG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 363 MSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVV 442
Cdd:TIGR02204 374 PSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAA 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 443 SLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFAT 522
Cdd:TIGR02204 454 HAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAIL-KDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIA 532
|
410 420 430
....*....|....*....|....*....|....*....
gi 543385153 523 HRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKL 561
Cdd:TIGR02204 533 HRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
329-546 |
2.11e-56 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 188.95 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 329 ELKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQML 406
Cdd:cd03245 2 RIEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 407 YIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRk 486
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 487 VMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQG 546
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
332-564 |
1.18e-55 |
|
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: 187.44 E-value: 1.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 332 LENLEFNYN-NQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQ 410
Cdd:cd03253 3 FENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 411 NPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVMLF 490
Cdd:cd03253 83 DTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAIL-KNPPILLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543385153 491 DEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKLTQE 564
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
303-563 |
7.30e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 192.35 E-value: 7.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 303 KRINELISRPMQASADLAIEPWNSKSELKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLP 380
Cdd:PRK11160 312 RRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 381 PKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVsELPEGLDTIIG 460
Cdd:PRK11160 392 PQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 461 QGKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLDIETEvdlkKQMLPL----MENRLVIFATHRLHWLKEMDYILV 536
Cdd:PRK11160 471 EGGRQLSGGEQRRLGIARALL-HDAPLLLLDEPTEGLDAETE----RQILELlaehAQNKTVLMITHRLTGLEQFDRICV 545
|
250 260
....*....|....*....|....*..
gi 543385153 537 MHEGKLVQQGTFDELTKEAGYFTKLTQ 563
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
332-563 |
1.43e-53 |
|
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: 181.92 E-value: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 332 LENLEFNYNNQteiGP-----VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNiPAW-HQQM 405
Cdd:cd03252 3 FEHVRFRYKPD---GPvildnISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD-PAWlRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTR 485
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 486 kVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKLTQ 563
Cdd:cd03252 159 -ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
329-547 |
6.35e-53 |
|
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: 179.61 E-value: 6.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 329 ELKLENLEFNYNNQTEigPV----SVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQ 404
Cdd:cd03244 2 DIEFKNVSLRYRPNLP--PVlkniSFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 MLYIPQNPYVFTASLRENIAFYTpEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKT 484
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 485 rKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGT 547
Cdd:cd03244 159 -KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
134-567 |
1.05e-50 |
|
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: 185.72 E-value: 1.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 134 LAMMIIPILLFI---AMLFINWQSALGLLLMYPLIVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLS 210
Cdd:TIGR01846 257 LTVVLDLLFVVVflaVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 211 KRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVavyLGFG---LLNGQLPLYPALSILILAPEYFLPIRN 287
Cdd:TIGR01846 337 PQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAIL---LWFGahlVIGGALSPGQLVAFNMLAGRVTQPVLR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 288 FAS---DYHATLNgknAFKRINELISRPMQASADLAIEPWNSKSELKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIG 362
Cdd:TIGR01846 414 LAQlwqDFQQTGI---ALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRYAPDSPevLSNLNLDIKPGEFIGIVG 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 363 MSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNiPAW-HQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHV 441
Cdd:TIGR01846 491 PSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAD-PAWlRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 442 VSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRkVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFA 521
Cdd:TIGR01846 570 AGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPR-ILIFDEATSALDYESEALIMRNMREICRGRTVIII 648
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 543385153 522 THRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKLTQEMRG 567
Cdd:TIGR01846 649 AHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
134-561 |
2.62e-49 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 181.86 E-value: 2.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 134 LAMMIIPILLFIAMLFInwqsaLGLLLMYPLIVLFMIILG---------YAAKDRASKQFGDFQK----LSNNFIDSLRG 200
Cdd:TIGR01193 269 LASTILSLFLDMWILVI-----VGLFLVRQNMLLFLLSLLsipvyaviiILFKRTFNKLNHDAMQanavLNSSIIEDLNG 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 201 IDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTfALDFFTTLSIAVVAVYLG-FGLLNGQLPLYPALSILILAP 279
Cdd:TIGR01193 344 IETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQ-AIKAVTKLILNVVILWTGaYLVMRGKLTLGQLITFNALLS 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 280 EYFLPIRNFASDYHATLNGKNAFKRINELISRPMQASADLAI-EPWNSKSELKLENLEFNYN-NQTEIGPVSVEIKGYEK 357
Cdd:TIGR01193 423 YFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRtELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 358 VGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYT-PEASDAEIM 436
Cdd:TIGR01193 503 TTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIW 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 437 KAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMEnR 516
Cdd:TIGR01193 583 AACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS-KVLILDESTSNLDTITEKKIVNNLLNLQD-K 660
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 543385153 517 LVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKL 561
Cdd:TIGR01193 661 TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
19-305 |
4.90e-48 |
|
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: 169.00 E-value: 4.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 19 LAVLEVLQAFLIIGQALSLSAVLTTLWQGkkLNWQYLLIFIVCLTG----RQLIDLLKDKMLETYSSQEVEKLRQQLLNK 94
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAG--GPWEDIMPPLAGIAGvivlRAALLWLRERVAHRAAQRVKQHLRRRLFAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 95 IFKSGQSLVQSQGTGSLITMALYGIDEVRDYIKLIYTKVLAMMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMIILGY 174
Cdd:cd18561 79 LLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 175 AAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVA 254
Cdd:cd18561 159 LAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALAL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 543385153 255 VYLGFGLLNGQLPLYPALSILILAPEYFLPIRNFASDYHATLNGKNAFKRI 305
Cdd:cd18561 239 GVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
320-561 |
6.25e-48 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 175.92 E-value: 6.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 320 AIEPWNSKSELKLENLEFNYNNQTE-IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNI 398
Cdd:PRK13657 325 AIDLGRVKGAVEFDDVSFSYDNSRQgVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 399 PAWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALAR 478
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 479 AFLdKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYF 558
Cdd:PRK13657 485 ALL-KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRF 563
|
...
gi 543385153 559 TKL 561
Cdd:PRK13657 564 AAL 566
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
85-550 |
1.23e-47 |
|
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: 174.94 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 85 EKLRQQLLNKIFKsgQSLVQSQGTGSLitmALYGIDEVRDYIkliyTK--VLAMMIIP-ILLFIAMLFinwqsalgllLM 161
Cdd:COG4618 93 RRLGPRVFDAAFR--AALRGGGGAAAQ---ALRDLDTLRQFL----TGpgLFALFDLPwAPIFLAVLF----------LF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 162 YPLI-------VLFMIILGYAAkDRASK----QFGDFQKLSNNFIDS-LRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTM 229
Cdd:COG4618 154 HPLLgllalvgALVLVALALLN-ERLTRkplkEANEAAIRANAFAEAaLRNAEVIEAMGMLPALRRRWQRANARALALQA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 230 AVLKVA-MLSTFALDFFTTLSIAVVAV--YLgfgLLNGQLPlyP----ALSILI---LAPeyflpIRNFASDYHATLNGK 299
Cdd:COG4618 233 RASDRAgGFSALSKFLRLLLQSAVLGLgaYL---VIQGEIT--PgamiAASILMgraLAP-----IEQAIGGWKQFVSAR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 300 NAFKRINELISRPMQASADLAI-EPwnsKSELKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLS 376
Cdd:COG4618 303 QAYRRLNELLAAVPAEPERMPLpRP---KGRLSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 377 GFLPPKSGKIIIDGQkaatlNIPAWHQQML-----YIPQNPYVFTASLRENIA-FytPEASDAEIMKAIHVVSLDELVSE 450
Cdd:COG4618 380 GVWPPTAGSVRLDGA-----DLSQWDREELgrhigYLPQDVELFDGTIAENIArF--GDADPEKVVAAAKLAGVHEMILR 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 451 LPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRKVMLfDEPTAHLDIETEVDLKKQMLPL-MENRLVIFATHRLHWLK 529
Cdd:COG4618 453 LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVL-DEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLA 531
|
490 500
....*....|....*....|.
gi 543385153 530 EMDYILVMHEGKLVQQGTFDE 550
Cdd:COG4618 532 AVDKLLVLRDGRVQAFGPRDE 552
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
85-554 |
1.05e-45 |
|
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: 169.07 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 85 EKLRQQLLNKIFKSG--QSLVQSQGTGSLitmALYGIDEVRDYikLIYTKVLAMMIIPIL-LFIAMLFInWQSALGLLLM 161
Cdd:TIGR01842 75 EKLDGALNQPIFAASfsATLRRGSGDGLQ---ALRDLDQLRQF--LTGPGLFAFFDAPWMpIYLLVCFL-LHPWIGILAL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 162 YPLIVLFMI-ILGYAAKDRASKQFGDFQKLSNNFIDS-LRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVA-MLS 238
Cdd:TIGR01842 149 GGAVVLVGLaLLNNRATKKPLKEATEASIRANNLADSaLRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAgMLS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 239 TFALDFFTTLSIAVVAV--YLgfgLLNGQLP--LYPALSIL---ILAPeyflpIRNFASDYHATLNGKNAFKRINELISR 311
Cdd:TIGR01842 229 NLSKYFRIVLQSLVLGLgaYL---AIDGEITpgMMIAGSILvgrALAP-----IDGAIGGWKQFSGARQAYKRLNELLAN 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 312 PMQASADLAIEpwNSKSELKLENLEFNY--NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIID 389
Cdd:TIGR01842 301 YPSRDPAMPLP--EPEGHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 390 GqkaATLNipAWHQQML-----YIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKR 464
Cdd:TIGR01842 379 G---ADLK--QWDRETFgkhigYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 465 VLSGGQAQRIALARAFLDKTRKVMLfDEPTAHLDIETEVDLKKQMLPL-MENRLVIFATHRLHWLKEMDYILVMHEGKLV 543
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVL-DEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIA 532
|
490
....*....|.
gi 543385153 544 QQGTFDELTKE 554
Cdd:TIGR01842 533 RFGERDEVLAK 543
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
329-551 |
4.36e-43 |
|
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: 162.68 E-value: 4.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 329 ELKLENLEFNYNNQTEI-GPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaatlNIPAWHQQML- 406
Cdd:COG5265 357 EVRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ-----DIRDVTQASLr 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 407 ----YIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLd 482
Cdd:COG5265 432 aaigIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL- 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 483 KTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENR--LVIfaTHRLHWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRttLVI--AHRLSTIVDADEILVLEAGRIVERGTHAEL 579
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
143-561 |
2.62e-41 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 158.73 E-value: 2.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 143 LFIAMLFINWQSALGLLLMYPLIVLfmiilgyaakdrASKQFGDF-QKLSNNFIDS-----------LRGIDTLKYLGLS 210
Cdd:TIGR00958 292 LLGFMLWLSPRLTMVTLINLPLVFL------------AEKVFGKRyQLLSEELQEAvakanqvaeeaLSGMRTVRSFAAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 211 KRYSKSifrvsedFRHKTMAVLKVAMLSTFALDFFTTLS------IAVVAVYLGFGL-LNGQLPLYPALSILILAPEYFL 283
Cdd:TIGR00958 360 EGEASR-------FKEALEETLQLNKRKALAYAGYLWTTsvlgmlIQVLVLYYGGQLvLTGKVSSGNLVSFLLYQEQLGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 284 PIRNFASDYHATLNGKNAFKRINELISRPMQASADLAIEPWNSKSELKLENLEFNYNNQTEIgPV----SVEIKGYEKVG 359
Cdd:TIGR00958 433 AVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDV-PVlkglTFTLHPGEVVA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 360 IIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAI 439
Cdd:TIGR00958 512 LVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAA 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 440 HVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRkVMLFDEPTAHLDIETEVDLkkQMLPLMENRLVI 519
Cdd:TIGR00958 592 KAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR-VLILDEATSALDAECEQLL--QESRSRASRTVL 668
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 543385153 520 FATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKL 561
Cdd:TIGR00958 669 LIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
84-563 |
4.83e-41 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 156.80 E-value: 4.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 84 VEKLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRD-YIKLIYTKVLAMMIIPILLfIAMLFINWQSALGLLLMY 162
Cdd:PRK10790 97 VQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDlYVTVVATVLRSAALIGAML-VAMFSLDWRMALVAIMIF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 163 PLIVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKsifRVSEDFRHKTMAVLKVAMLSTFAL 242
Cdd:PRK10790 176 PAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGE---RMGEASRSHYMARMQTLRLDGFLL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 243 DffTTLSIAVVAVYLGFGLLNGQLP--------LYPALSILILAPEyflPIRNFASDYHATLNGKNAFKRINELISRPMQ 314
Cdd:PRK10790 253 R--PLLSLFSALILCGLLMLFGFSAsgtievgvLYAFISYLGRLNE---PLIELTTQQSMLQQAVVAGERVFELMDGPRQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 315 ASADlAIEPWNSKSeLKLENLEFNY-NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKA 393
Cdd:PRK10790 328 QYGN-DDRPLQSGR-IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 394 ATLNIPAWHQQMLYIPQNPYVFTASLRENIAFyTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQR 473
Cdd:PRK10790 406 SSLSHSVLRQGVAMVQQDPVVLADTFLANVTL-GRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 474 IALARAFLDkTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTK 553
Cdd:PRK10790 485 LALARVLVQ-TPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA 563
|
490
....*....|
gi 543385153 554 EAGYFTKLTQ 563
Cdd:PRK10790 564 AQGRYWQMYQ 573
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
80-558 |
1.04e-40 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 155.64 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 80 SSQEVEKLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEV-----RDYIKLIYTKVLAMMIipilLFIAMLFINWQs 154
Cdd:PRK10789 64 SYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaagEGVLTLVDSLVMGCAV----LIVMSTQISWQ- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 155 aLGLLLMYPLIVLFMIILGYAakDRASKQF----GDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMA 230
Cdd:PRK10789 139 -LTLLALLPMPVMAIMIKRYG--DQLHERFklaqAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 231 VLKVAMLstfaldFFTTLSIAV-VAVYLGFG-----LLNGQLPLYPALSILILAPEYFLPIRNFASDYHATLNGKNAFKR 304
Cdd:PRK10789 216 VARIDAR------FDPTIYIAIgMANLLAIGggswmVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 305 INELIS-RPMQASADLAIEPwnSKSELKLENLEFNY--NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPP 381
Cdd:PRK10789 290 IRAMLAeAPVVKDGSEPVPE--GRGELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 382 KSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQ 461
Cdd:PRK10789 368 SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 462 GKRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGK 541
Cdd:PRK10789 448 RGVMLSGGQKQRISIARALLLNA-EILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGH 526
|
490
....*....|....*..
gi 543385153 542 LVQQGTFDELTKEAGYF 558
Cdd:PRK10789 527 IAQRGNHDQLAQQSGWY 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
330-551 |
2.16e-40 |
|
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: 146.32 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEI-GPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYI 408
Cdd:COG1122 1 IELENLSFSYPGGTPAlDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 409 PQNP--YVFTASLRENIAF------YTPEASDAEIMKAIHVVSLDELvselpegLDTIIGQgkrvLSGGQAQRIALARAF 480
Cdd:COG1122 81 FQNPddQLFAPTVEEDVAFgpenlgLPREEIRERVEEALELVGLEHL-------ADRPPHE----LSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 481 LDKTrKVMLFDEPTAHLDIETEVDLKKQMLPL-MENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:COG1122 150 AMEP-EVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREV 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
330-556 |
3.84e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 146.16 E-value: 3.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNiPAWHQQMLYIP 409
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVF-TASLRENIAFYTP--EASDAEIMKAIhvvslDELVSELpeGLDTIIGQGKRVLSGGQAQRIALARAFLDKTrK 486
Cdd:COG4555 81 DERGLYdRLTVRENIRYFAElyGLFDEELKKRI-----EELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDP-K 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543385153 487 VMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDELTKEAG 556
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
330-541 |
1.84e-39 |
|
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: 142.99 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGP-----VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAatlnipawhqq 404
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIA----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 mlYIPQNPYVFTASLRENIAFYTPEasDAE-IMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDK 483
Cdd:cd03250 70 --YVSQEPWIQNGTIRENILFGKPF--DEErYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 484 TrKVMLFDEPTAHLDIETEVDLKKQML--PLMENRLVIFATHRLHWLKEMDYILVMHEGK 541
Cdd:cd03250 146 A-DIYLLDDPLSAVDAHVGRHIFENCIlgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
330-542 |
3.72e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 142.26 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIP 409
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVFTASLRENIAF---YTPEASDAEIMKAIhvvsLDELvsELPEG-LDTIIGQgkrvLSGGQAQRIALARAFLDKtR 485
Cdd:COG4619 81 QEPALWGGTVRDNLPFpfqLRERKFDRERALEL----LERL--GLPPDiLDKPVER----LSGGERQRLALIRALLLQ-P 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 486 KVMLFDEPTAHLDIETE-------VDLKKQmlplmENRLVIFATHRLHWLKEM-DYILVMHEGKL 542
Cdd:COG4619 150 DVLLLDEPTSALDPENTrrveellREYLAE-----EGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
330-564 |
8.43e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 142.12 E-value: 8.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATlNIPAWHQQMLYIP 409
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVFTA-SLRENIAFY------TPEASDAEIMKAIHVVSLDELvselpegLDTIIGQgkrvLSGGQAQRIALARAFLD 482
Cdd:COG1131 80 QEPALYPDlTVRENLRFFarlyglPRKEARERIDELLELFGLTDA-------ADRKVGT----LSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 483 KTrKVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDELTKEA--GYF 558
Cdd:COG1131 149 DP-ELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARLleDVF 227
|
....*.
gi 543385153 559 TKLTQE 564
Cdd:COG1131 228 LELTGE 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
323-542 |
8.84e-39 |
|
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: 141.84 E-value: 8.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 323 PWNSKSELKLENLEFNYNNQTE---IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIP 399
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 400 AWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARA 479
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 480 FLdKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKL 542
Cdd:cd03248 165 LI-RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
91-561 |
1.08e-37 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 147.09 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 91 LLNKI-FKSGQslVQSQGTGSLITMalygideVRD--YIkliytkvlammiipILLFIAMLFINWQSALGLLLMYPlIVL 167
Cdd:PRK11176 124 LLSRItYDSEQ--VASSSSGALITV-------VREgaSI--------------IGLFIMMFYYSWQLSLILIVIAP-IVS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 168 FMIILgyaakdrASKQFgdfQKLSNNFIDS-----------LRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAM 236
Cdd:PRK11176 180 IAIRV-------VSKRF---RNISKNMQNTmgqvttsaeqmLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 237 LSTFALDFFTTLSIAVVAVYLGFGLLNGQLPlypALSILILAPEYFLPIRNFASdyhatlngknaFKRINELISRPMQAS 316
Cdd:PRK11176 250 ISDPIIQLIASLALAFVLYAASFPSVMDTLT---AGTITVVFSSMIALMRPLKS-----------LTNVNAQFQRGMAAC 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 317 ADL-------------AIEPWNSKSELKLENLEFNY--NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPP 381
Cdd:PRK11176 316 QTLfaildleqekdegKRVIERAKGDIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 382 KSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEA-SDAEIMKAIHVVSLDELVSELPEGLDTIIG 460
Cdd:PRK11176 396 DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 461 QGKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEG 540
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIARALL-RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDG 554
|
490 500
....*....|....*....|.
gi 543385153 541 KLVQQGTFDELTKEAGYFTKL 561
Cdd:PRK11176 555 EIVERGTHAELLAQNGVYAQL 575
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
330-555 |
7.61e-37 |
|
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: 137.48 E-value: 7.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIP 409
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYV-FTASLRENIA---------FYTPEASDAEI-MKAIHVVSLDELvselpegLDTIIGQgkrvLSGGQAQRIALAR 478
Cdd:COG1120 82 QEPPApFGLTVRELVAlgryphlglFGRPSAEDREAvEEALERTGLEHL-------ADRPVDE----LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 479 AFLDKTRkVMLFDEPTAHLDI--ETEV-----DLKKQmlplmENRLVIFATHRL-HWLKEMDYILVMHEGKLVQQGTFDE 550
Cdd:COG1120 151 ALAQEPP-LLLLDEPTSHLDLahQLEVlellrRLARE-----RGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEE 224
|
....*.
gi 543385153 551 -LTKEA 555
Cdd:COG1120 225 vLTPEL 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
331-541 |
8.52e-37 |
|
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: 136.06 E-value: 8.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 331 KLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYI 408
Cdd:cd03225 1 ELKNLSFSYPDGARpaLDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 409 PQNP--YVFTASLRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPEgldtiigqgkrVLSGGQAQRIALARAF 480
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFglenlgLPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 481 LDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRL-VIFATHRLHWLKE-MDYILVMHEGK 541
Cdd:cd03225 150 AMDP-DILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
324-547 |
4.29e-36 |
|
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: 134.08 E-value: 4.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 324 WNSKSELKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAW 401
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPpvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 402 HQQMLYIPQNPYVFTASLRENIAFYTpEASDAEIMKAIHVvsldelvselpegldtiiGQGKRVLSGGQAQRIALARAFL 481
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 482 dKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGT 547
Cdd:cd03369 142 -KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
330-546 |
7.78e-36 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 132.05 E-value: 7.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNY--NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNiPAWHQQMLY 407
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVFTASLRENIafytpeasdaeimkaihvvsldelvselpegldtiigqGKRvLSGGQAQRIALARAFLDKTRKV 487
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRR-FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 488 MLfDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQG 546
Cdd:cd03247 121 LL-DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
331-546 |
1.29e-35 |
|
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: 131.79 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 331 KLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQ 410
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 411 npyvftaslreniafytpeasdaeimkAIHVVSLDELvseLPEGLDTiigqgkrvLSGGQAQRIALARAFLDKTrKVMLF 490
Cdd:cd03214 81 ---------------------------ALELLGLAHL---ADRPFNE--------LSGGERQRVLLARALAQEP-PILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 491 DEPTAHLDIETEVDLKKQM--LPLMENRLVIFATHRL-HWLKEMDYILVMHEGKLVQQG 546
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
31-305 |
5.71e-35 |
|
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: 133.43 E-value: 5.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 31 IGQALSLSAVLTTLWQGK---KLNWQYLLIFIVCLTGRQLIDLLKDKMLeTYSSQEV-EKLRQQLLNKIFKSGQSLVQSQ 106
Cdd:cd18781 13 IAFVFSIANLLQKLLEGKlttASLLIVLGILAIAIIVRFICTRLASRAS-YRASADVkKTLREKIYDKLLRLGPSYQEKV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 107 GTGSLITMALYGIDEVRDYI-----KLIYTkvlamMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYAAKDRAS 181
Cdd:cd18781 92 STAEVVQLSVEGVEQLEIYFgrylpQFFYS-----MLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKIAKKLLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 182 KQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFF----TTLSIAVVavyl 257
Cdd:cd18781 167 KYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVayggAALGIILA---- 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 543385153 258 GFGLLNGQLPLYPALSILILAPEYFLPIRNFASDYHATLNGKNAFKRI 305
Cdd:cd18781 243 LLQFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASDKI 290
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
330-542 |
6.02e-34 |
|
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: 126.95 E-value: 6.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNY--NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLY 407
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVFTASLRENIafytpeasdaeimkaihvvsldelvselpegldtiigqgkrvLSGGQAQRIALARAFLdKTRKV 487
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALY-GNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 488 MLFDEPTAHLDIETEVDLKKQMLPL-MENRLVIFATHRLHWLKEMDYILVMHEGKL 542
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
328-551 |
1.05e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 131.35 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 328 SELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLniPAWHQQMLY 407
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL--PPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVF-TASLRENIAFY-----TPEAS-DAEIMKAIHVVSLDELVSELPegldtiiGQgkrvLSGGQAQRIALARAf 480
Cdd:COG3839 80 VFQSYALYpHMTVYENIAFPlklrkVPKAEiDRRVREAAELLGLEDLLDRKP-------KQ----LSGGQRQRVALGRA- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 481 LDKTRKVMLFDEPTAHLD----IETEVDLKKqmlplMENRL---VIFATHRLHwlkE-M---DYILVMHEGKLVQQGTFD 549
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrVEMRAEIKR-----LHRRLgttTIYVTHDQV---EaMtlaDRIAVMNDGRIQQVGTPE 219
|
..
gi 543385153 550 EL 551
Cdd:COG3839 220 EL 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
331-541 |
2.30e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 124.66 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 331 KLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQ 410
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 411 npyvftaslreniafytpeasdaeimkaihvvsldelvselpegldtiigqgkrvLSGGQAQRIALARAFLdKTRKVMLF 490
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALL-LNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 543385153 491 DEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKE-MDYILVMHEGK 541
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
87-564 |
2.57e-33 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 136.23 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 87 LRQQLLNKIFKSGQSLVQSQGTGSLitmalygideVRDYIKLIYTkVLAMMIIPILLFIAMLFINWQSALGLLLMYPLIV 166
Cdd:TIGR00957 1040 LHQDLLHNKLRSPMSFFERTPSGNL----------VNRFSKELDT-VDSMIPPVIKMFMGSLFNVIGALIVILLATPIAA 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 167 LFMIILG---------YAAKDRASKQFGDFQK--LSNNFIDSLRGIDTLKYLGLSKRYS-KSIFRVSEDFRHKTMAVLKV 234
Cdd:TIGR00957 1109 VIIPPLGllyffvqrfYVASSRQLKRLESVSRspVYSHFNETLLGVSVIRAFEEQERFIhQSDLKVDENQKAYYPSIVAN 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 235 AMLSTfALDFF---TTLSIAVVAVYLGFGLLNGQLPLYPALSILILAPEYFLpIRnFASDYHATLNGKNAFKRINELISR 311
Cdd:TIGR00957 1189 RWLAV-RLECVgncIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWL-VR-MSSEMETNIVAVERLKEYSETEKE 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 312 -PMQASADLAIEPWNSKSELKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIII 388
Cdd:TIGR00957 1266 aPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDlvLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 389 DGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTpEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSG 468
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFS-QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSV 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 469 GQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLkeMDY--ILVMHEGKLVQQG 546
Cdd:TIGR00957 1425 GQRQLVCLARALLRKT-KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI--MDYtrVIVLDKGEVAEFG 1501
|
490
....*....|....*...
gi 543385153 547 TFDELTKEAGYFTKLTQE 564
Cdd:TIGR00957 1502 APSNLLQQRGIFYSMAKD 1519
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
302-551 |
4.40e-33 |
|
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: 132.72 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 302 FKRINELISRPMQASADLAIEPWNSKSE--LKLENLEFNYNNQTEIGP-----VSVEIKGYEKVGIIGMSGSGKSTLINL 374
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKGGVravddVSLTLRRGETLGLVGESGSGKSTLARL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 375 LSGFLPPKSGKIIIDGQKAATLN---IPAWHQQMLYIPQNPYvftASL------RENIAF-------YTPEASDAEIMKA 438
Cdd:COG1123 311 LLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPY---SSLnprmtvGDIIAEplrlhglLSRAERRERVAEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 439 IHVVSLDelvselPEGLDTIIGQgkrvLSGGQAQRIALARAFLdkTR-KVMLFDEPTAHLDieteVDLKKQMLPLME--- 514
Cdd:COG1123 388 LERVGLP------PDLADRYPHE----LSGGQRQRVAIARALA--LEpKLLILDEPTSALD----VSVQAQILNLLRdlq 451
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 543385153 515 ---NRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:COG1123 452 relGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
330-546 |
6.44e-33 |
|
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: 125.32 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLniPAWHQQMLYIP 409
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVF-TASLRENIAF-----YTPEAS-DAEIMKAIHVVSLDELVSELPEGldtiigqgkrvLSGGQAQRIALARAfLD 482
Cdd:cd03259 79 QDYALFpHLTVAENIAFglklrGVPKAEiRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARA-LA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 483 KTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENR--LVIFATHRLHWLKEM-DYILVMHEGKLVQQG 546
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
347-546 |
6.89e-33 |
|
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: 125.70 E-value: 6.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 347 PVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN---IPAWHQQMLYIPQNPY-----VFT-- 416
Cdd:cd03257 23 DVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPMsslnpRMTig 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 417 ASLRENIAFYTPEASDAEIMKAIHVvsLDELVSELPEGLDTIIGQgkrvLSGGQAQRIALARAFLDKTrKVMLFDEPTAH 496
Cdd:cd03257 103 EQIAEPLRIHGKLSKKEARKEAVLL--LLVGVGLPEEVLNRYPHE----LSGGQRQRVAIARALALNP-KLLIADEPTSA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 497 LDieteVDLKKQMLPLM-----ENRL-VIFATHRLHWLKEM-DYILVMHEGKLVQQG 546
Cdd:cd03257 176 LD----VSVQAQILDLLkklqeELGLtLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
329-563 |
1.09e-32 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 126.18 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 329 ELKLENLEFNYNNQteIGPVSVEIKGY----EKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQ 404
Cdd:cd03288 19 EIKIHDLCVRYENN--LKPVLKHVKAYikpgQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 MLYIPQNPYVFTASLRENIafyTPE--ASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLD 482
Cdd:cd03288 97 LSIILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 483 KTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDEL-TKEAGYFTKL 561
Cdd:cd03288 174 KS-SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLlAQEDGVFASL 252
|
..
gi 543385153 562 TQ 563
Cdd:cd03288 253 VR 254
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
54-563 |
1.46e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 133.95 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 54 YLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYIKliytkV 133
Cdd:PLN03232 952 YIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVA-----N 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 134 LAMMIIPIL--LFIAMLFINWQSALGLLLMYPLIVLFM-IILGYAAKDRASKQFGDFQK--LSNNFIDSLRGIDTLKYLG 208
Cdd:PLN03232 1027 LMNMFMNQLwqLLSTFALIGTVSTISLWAIMPLLILFYaAYLYYQSTSREVRRLDSVTRspIYAQFGEALNGLSSIRAYK 1106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 209 LSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVY--LGFGLLNGQLPLYPALSILIlapEYFLPIR 286
Cdd:PLN03232 1107 AYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFavLRNGNAENQAGFASTMGLLL---SYTLNIT 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 287 NFASDY----HATLNGKNAFKRINELISRPMQASA----DLAIEPWNSKSELKLENLEFNYnnQTEIGPV----SVEIKG 354
Cdd:PLN03232 1184 TLLSGVlrqaSKAENSLNSVERVGNYIDLPSEATAiienNRPVSGWPSRGSIKFEDVHLRY--RPGLPPVlhglSFFVSP 1261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 355 YEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTpEASDAE 434
Cdd:PLN03232 1262 SEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDAD 1340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 435 IMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLME 514
Cdd:PLN03232 1341 LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS-KILVLDEATASVDVRTDSLIQRTIREEFK 1419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 543385153 515 NRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDE-LTKEAGYFTKLTQ 563
Cdd:PLN03232 1420 SCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQElLSRDTSAFFRMVH 1469
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
330-552 |
2.45e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.10 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQT-EIgpvSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIpawHQQ---M 405
Cdd:COG3840 2 LRLDDLTYRYGDFPlRF---DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP---AERpvsM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LYIPQNpyVFTA-SLRENIAF-------YTPEASdAEIMKAIHVVSLDELVSELPegldtiiGQgkrvLSGGQAQRIALA 477
Cdd:COG3840 76 LFQENN--LFPHlTVAQNIGLglrpglkLTAEQR-AQVEQALERVGLAGLLDRLP-------GQ----LSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 478 RAFLDKtRKVMLFDEPTAHLDIEtevdLKKQMLPLME------NRLVIFATH------RLhwlkeMDYILVMHEGKLVQQ 545
Cdd:COG3840 142 RCLVRK-RPILLLDEPFSALDPA----LRQEMLDLVDelcrerGLTVLMVTHdpedaaRI-----ADRVLLVADGRIAAD 211
|
....*..
gi 543385153 546 GTFDELT 552
Cdd:COG3840 212 GPTAALL 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
86-563 |
2.62e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 133.18 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 86 KLRQQLLNKIFKSGQSLVQSQ----GTGSLITMalygIDEVRDYIKLIYTKVLAMMIIPILLFIAMLFINWQ----SALG 157
Cdd:PLN03232 371 RLRSTLVAAIFHKSLRLTHEArknfASGKVTNM----ITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQlgvaSLFG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 158 LLLMYPLIVLFMIILGYAAK------DRASKQFGdfqkLSNNFIDSLrgiDTLKYLGLSKRYSksiFRVsEDFRHKTMAV 231
Cdd:PLN03232 447 SLILFLLIPLQTLIVRKMRKltkeglQWTDKRVG----IINEILASM---DTVKCYAWEKSFE---SRI-QGIRNEELSW 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 232 LKVAMLsTFALDFFTTLSIAVVAVYLGFG---LLNGQLPLYPALSILILAPEYFLPIRNFASDYHATLNGKNAFKRINEL 308
Cdd:PLN03232 516 FRKAQL-LSAFNSFILNSIPVVVTLVSFGvfvLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEEL 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 309 -ISRPMQASADLAIEPwnSKSELKLENLEFNYNNQTE---IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPP-KS 383
Cdd:PLN03232 595 lLSEERILAQNPPLQP--GAPAISIKNGYFSWDSKTSkptLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaET 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 384 GKIIIDGQKAatlnipawhqqmlYIPQNPYVFTASLRENIAF---YTPEasdaEIMKAIHVVSLDELVSELPEGLDTIIG 460
Cdd:PLN03232 673 SSVVIRGSVA-------------YVPQVSWIFNATVRENILFgsdFESE----RYWRAIDVTALQHDLDLLPGRDLTEIG 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 461 QGKRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLD--IETEVdLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMH 538
Cdd:PLN03232 736 ERGVNISGGQKQRVSMARAVYSNS-DIYIFDDPLSALDahVAHQV-FDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVS 813
|
490 500
....*....|....*....|....*
gi 543385153 539 EGKLVQQGTFDELTKEAGYFTKLTQ 563
Cdd:PLN03232 814 EGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
326-547 |
4.76e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 126.75 E-value: 4.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 326 SKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLniPAWHQQM 405
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL--PPEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LYIPQNPYVF---TAslRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPegldtiiGQgkrvLSGGQAQRIAL 476
Cdd:COG3842 80 GMVFQDYALFphlTV--AENVAFglrmrgVPKAEIRARVAELLELVGLEGLADRYP-------HQ----LSGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 477 ARAfLDKTRKVMLFDEPTAHLDieteVDLKKQMlplmenRL------------VIFATHRLHwlkE---M-DYILVMHEG 540
Cdd:COG3842 147 ARA-LAPEPRVLLLDEPLSALD----AKLREEM------REelrrlqrelgitFIYVTHDQE---EalaLaDRIAVMNDG 212
|
....*..
gi 543385153 541 KLVQQGT 547
Cdd:COG3842 213 RIEQVGT 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
330-542 |
5.03e-32 |
|
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: 122.98 E-value: 5.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGP----VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAW---- 401
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalkgVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 402 HQQMLYIPQNPYV---FTAslRENIA---FYTPEASDAEIMKAIHVvsLDELvsELPEGLDTIIGQgkrvLSGGQAQRIA 475
Cdd:cd03255 81 RRHIGFVFQSFNLlpdLTA--LENVElplLLAGVPKKERRERAEEL--LERV--GLGDRLNHYPSE----LSGGQQQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543385153 476 LARAFLDKTrKVMLFDEPTAHLDIET--EV-----DLKKQMlplmeNRLVIFATHRLHWLKEMDYILVMHEGKL 542
Cdd:cd03255 151 IARALANDP-KIILADEPTGNLDSETgkEVmellrELNKEA-----GTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
140-561 |
5.43e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 132.17 E-value: 5.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 140 PILLFIAMLFINWQ-------SALGLLLMYPL---IVLFMIILGYAAKDRASKQFGdfqkLSNnfiDSLRGIDTLKYLGL 209
Cdd:PLN03130 425 PFRIIIAMVLLYQQlgvasliGSLMLVLMFPIqtfIISKMQKLTKEGLQRTDKRIG----LMN---EVLAAMDTVKCYAW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 210 SKRYSKSIFRVSED----FRhktmavlKVAMLStfALDFFTTLSIAVVAVYLGFG---LLNGQLPLYPALSILILAPEYF 282
Cdd:PLN03130 498 ENSFQSKVQTVRDDelswFR-------KAQLLS--AFNSFILNSIPVLVTVVSFGvftLLGGDLTPARAFTSLSLFAVLR 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 283 LPIRNFASDYHATLNGKNAFKRINELISRPMQASAD-LAIEP-------------WNSKSEL-KLENLEFnynnqtEIGP 347
Cdd:PLN03130 569 FPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPnPPLEPglpaisikngyfsWDSKAERpTLSNINL------DVPV 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVeikgyekVGIIGMSGSGKSTLINLLSGFLPPKS-GKIIIDGQKAatlnipawhqqmlYIPQNPYVFTASLRENIAFY 426
Cdd:PLN03130 643 GSL-------VAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVA-------------YVPQVSWIFNATVRDNILFG 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 427 TP-EASDAEimKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLD--IETEV 503
Cdd:PLN03130 703 SPfDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVY-SNSDVYIFDDPLSALDahVGRQV 779
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 504 dLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKL 561
Cdd:PLN03130 780 -FDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
347-495 |
6.67e-32 |
|
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: 120.45 E-value: 6.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 347 PVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVF-TASLRENIAF 425
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 426 ------YTPEASDAEIMKAIHVVSLDELvselpegLDTIIGQGKRVLSGGQAQRIALARAFLDKtRKVMLFDEPTA 495
Cdd:pfam00005 83 glllkgLSKREKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTK-PKLLLLDEPTA 150
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
85-558 |
2.34e-31 |
|
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: 130.03 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 85 EKLRQQLLNKIFKSGQSLVQSQGTGSLIT-----MALygIDE-----VRDYIKLIYTKVLAMMIIPIL---LFIAMLfin 151
Cdd:TIGR01271 958 KRLHEQMLHSVLQAPMAVLNTMKAGRILNrftkdMAI--IDDmlpltLFDFIQLTLIVLGAIFVVSVLqpyIFIAAI--- 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 152 wqsalglllmyPLIVLFMIILGYAAkdRASKQFGDFQK-----LSNNFIDSLRGIDTLKYLGlSKRYSKSIFRVSEDFrH 226
Cdd:TIGR01271 1033 -----------PVAVIFIMLRAYFL--RTSQQLKQLESearspIFSHLITSLKGLWTIRAFG-RQSYFETLFHKALNL-H 1097
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 227 KTMAVLKVAMLSTFALD---FFTTLSIAVVAVYLG-FGLLNGQLPLYPALSILILApeyflpIRNFASDYHATLNG-KNA 301
Cdd:TIGR01271 1098 TANWFLYLSTLRWFQMRidiIFVFFFIAVTFIAIGtNQDGEGEVGIILTLAMNILS------TLQWAVNSSIDVDGlMRS 1171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 302 FKRINELISRP------------MQASADLAIEP------WNSKSELKLENLEFNYnnqTEIG-----PVSVEIKGYEKV 358
Cdd:TIGR01271 1172 VSRVFKFIDLPqeeprpsggggkYQLSTVLVIENphaqkcWPSGGQMDVQGLTAKY---TEAGravlqDLSFSVEGGQRV 1248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 359 GIIGMSGSGKSTLinlLSGFLPPKS--GKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTpEASDAEIM 436
Cdd:TIGR01271 1249 GLLGRTGSGKSTL---LSALLRLLSteGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYE-QWSDEEIW 1324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 437 KAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENR 516
Cdd:TIGR01271 1325 KVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA-KILLLDEPSAHLDPVTLQIIRKTLKQSFSNC 1403
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 543385153 517 LVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYF 558
Cdd:TIGR01271 1404 TVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
330-542 |
3.69e-31 |
|
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: 119.04 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATlNIPAWHQQMLYIP 409
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVF-TASLRENIafytpeasdaeimkaihvvsldelvselpegldtiigqgkrVLSGGQAQRIALARAFLDKTrKVM 488
Cdd:cd03230 80 EEPSLYeNLTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDP-ELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 489 LFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEM-DYILVMHEGKL 542
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
325-554 |
1.83e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.10 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 325 NSKSELKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWH 402
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENnaLKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQNP--YVFTASLRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPEGldtiigqgkrvLSGGQAQRI 474
Cdd:PRK13632 83 KKIGIIFQNPdnQFIGATVEDDIAFglenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 475 ALARAF-LDKtrKVMLFDEPTAHLDIETEVDLKKQMLPLMENR--LVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:PRK13632 152 AIASVLaLNP--EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
...
gi 543385153 552 TKE 554
Cdd:PRK13632 230 LNN 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
297-563 |
2.34e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 127.16 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 297 NGKNAFKRINELISRPmqASADLAIEP------WNSKSELKLENLEFNYnnQTEIGPV----SVEIKGYEKVGIIGMSGS 366
Cdd:PLN03130 1201 NSLNAVERVGTYIDLP--SEAPLVIENnrpppgWPSSGSIKFEDVVLRY--RPELPPVlhglSFEISPSEKVGIVGRTGA 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 367 GKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTpEASDAEIMKAIHVVSLDE 446
Cdd:PLN03130 1277 GKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFN-EHNDADLWESLERAHLKD 1355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 447 LVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLH 526
Cdd:PLN03130 1356 VIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS-KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLN 1434
|
250 260 270
....*....|....*....|....*....|....*...
gi 543385153 527 WLKEMDYILVMHEGKLVQQGTFDEL-TKEAGYFTKLTQ 563
Cdd:PLN03130 1435 TIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQ 1472
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
330-545 |
3.47e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.22 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGP----VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN---IPAWH 402
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTalrgVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQML-YIPQNPY---VFTAslRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPegldtiiGQgkrvLSGGQAQ 472
Cdd:COG1136 85 RRHIgFVFQFFNllpELTA--LENVALplllagVSRKERRERARELLERVGLGDRLDHRP-------SQ----LSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 473 RIALARAFLdkTR-KVMLFDEPTAHLDIET--EV-----DLKKQmlplmENRLVIFATHRLHWLKEMDYILVMHEGKLVQ 544
Cdd:COG1136 152 RVAIARALV--NRpKLILADEPTGNLDSKTgeEVlellrELNRE-----LGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
.
gi 543385153 545 Q 545
Cdd:COG1136 225 D 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
348-551 |
4.45e-30 |
|
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: 118.37 E-value: 4.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPY-----VFT--ASLR 420
Cdd:COG1124 24 VSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYaslhpRHTvdRILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 421 ENIAFYTPEASDAEIMKAIHVVSLDelvselPEGLDTIIGQgkrvLSGGQAQRIALARAFLdkTR-KVMLFDEPTAHLD- 498
Cdd:COG1124 104 EPLRIHGLPDREERIAELLEQVGLP------PSFLDRYPHQ----LSGGQRQRVAIARALI--LEpELLLLDEPTSALDv 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 499 -IETEV-----DLKKQmlplmENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:COG1124 172 sVQAEIlnllkDLREE-----RGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
330-551 |
4.78e-30 |
|
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: 117.72 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKaaTLNIPAWHQQMLYIP 409
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD--ITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVFT-ASLRENIAF-----YTPEAS-DAEIMKAIHVVSLDELVSELPEGldtiigqgkrvLSGGQAQRIALARAFLD 482
Cdd:cd03300 79 QNYALFPhLTVFENIAFglrlkKLPKAEiKERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 483 KTrKVMLFDEPTAHLDieteVDLKKQM---LPLMENRL---VIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:cd03300 148 EP-KVLLLDEPLGALD----LKLRKDMqleLKRLQKELgitFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
330-551 |
8.62e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 123.09 E-value: 8.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPK---SGKIIIDGQKAATLNIPAWHQQ 404
Cdd:COG1123 5 LEVRDLSVRYPGGDVpaVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 MLYIPQNPYV--FTASLRENIAFyTPEA---SDAEIMKaiHVVSLDELVselpeGLDTIIGQGKRVLSGGQAQRIALARA 479
Cdd:COG1123 85 IGMVFQDPMTqlNPVTVGDQIAE-ALENlglSRAEARA--RVLELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 480 FLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENR--LVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:COG1123 157 LALDP-DLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEI 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
330-523 |
1.13e-29 |
|
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: 116.04 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkAATLNIPAWHQQMLYIP 409
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE-PIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVFTA-SLRENIAFYT----PEASDAEIMKAIHVVSLDELvselpegLDTIIGQgkrvLSGGQAQRIALARAFLDKt 484
Cdd:COG4133 82 HADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGL-------ADLPVRQ----LSAGQKRRVALARLLLSP- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 543385153 485 RKVMLFDEPTAHLDIETEVDLKKQML-PLMENRLVIFATH 523
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAaHLARGGAVLLTTH 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
330-551 |
1.25e-29 |
|
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: 116.51 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTL---INLLSGFLP--PKSGKIIIDGQKAATLNI-PAWH- 402
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLlrlLNRLNDLIPgaPDEGEVLLDGKDIYDLDVdVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 --QQMLYipQNPYVFTASLRENIAfYTP--------EASDAEIMKAIHVVSLDELVSELPEGLDtiigqgkrvLSGGQAQ 472
Cdd:cd03260 81 rrVGMVF--QKPNPFPGSIYDNVA-YGLrlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 473 RIALARAFLDKTRkVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:cd03260 149 RLCLARALANEPE-VLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
329-551 |
3.17e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.71 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 329 ELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATlNIPAWHQQMLYI 408
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-NLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 409 PQNPYVF---TAslRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPegldtiiGQgkrvLSGGQAQRIALARA 479
Cdd:COG1118 81 FQHYALFphmTV--AENIAFglrvrpPSKAEIRARVEELLELVQLEGLADRYP-------SQ----LSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 480 fLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLME--NRLVIFATH------RLhwlkeMDYILVMHEGKLVQQGTFDEL 551
Cdd:COG1118 148 -LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEV 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
330-555 |
4.01e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.57 E-value: 4.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATlnipAWHqQMLYIP 409
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----ARR-RIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYV---FTASLRENIA-----------FYTPEASDAeIMKAIHVVSLDELvselpegLDTIIGQgkrvLSGGQAQRIA 475
Cdd:COG1121 82 QRAEVdwdFPITVRDVVLmgrygrrglfrRPSRADREA-VDEALERVGLEDL-------ADRPIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 476 LARAFLDKtRKVMLFDEPTAHLDIETEVD-------LKKqmlplmENRLVIFATHRLHWLKEM-DYILVMhEGKLVQQGT 547
Cdd:COG1121 150 LARALAQD-PDLLLLDEPFAGVDAATEEAlyellreLRR------EGKTILVVTHDLGAVREYfDRVLLL-NRGLVAHGP 221
|
....*....
gi 543385153 548 FDE-LTKEA 555
Cdd:COG1121 222 PEEvLTPEN 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
329-558 |
5.25e-29 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 116.11 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 329 ELKLENLEFNYNN--QTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKsGKIIIDGQKAATLNIPAWHQQML 406
Cdd:cd03289 2 QMTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 407 YIPQNPYVFTASLRENIAFYTpEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTrK 486
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYG-KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA-K 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543385153 487 VMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYF 558
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
330-541 |
7.76e-29 |
|
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: 112.67 E-value: 7.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN--IPAWHQQMLY 407
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVFT-ASLRENIAFytpeasdaeimkaihvvsldelvselpegldtiigqgkrVLSGGQAQRIALARAfLDKTRK 486
Cdd:cd03229 81 VFQDFALFPhLTVLENIAL---------------------------------------GLSGGQQQRVALARA-LAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 487 VMLFDEPTAHLDIETEVDLKKQMLPLMEN--RLVIFATHRLHWLKEM-DYILVMHEGK 541
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
330-553 |
1.22e-28 |
|
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: 113.97 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNqTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGqkAATLNIPAWHQQMLYIP 409
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG--KDITNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVFT-ASLRENIAFytpeasdAEIMKAIHVVSLDELVSELPE--GLDTIIGQGKRVLSGGQAQRIALARAFLDKTrK 486
Cdd:cd03299 78 QNYALFPhMTVYKNIAY-------GLKKRKVDKKEIERKVLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNP-K 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 487 VMLFDEPTAHLDIETEVDLKKQMLPLMENR--LVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDELTK 553
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFK 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
330-553 |
1.33e-28 |
|
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: 113.92 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQ----- 404
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 MLYipQNPYVFTA-SLRENIAF----YTpEASDAEI----MKAIHVVSLDELVSELP-EgldtiigqgkrvLSGGQAQRI 474
Cdd:COG1127 86 MLF--QGGALFDSlTVFENVAFplreHT-DLSEAEIrelvLEKLELVGLPGAADKMPsE------------LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 475 ALARAF-LDKtrKVMLFDEPTAHLDIET--EVD-----LKKQMlplmeNRLVIFATHRLHWLKEM-DYILVMHEGKLVQQ 545
Cdd:COG1127 151 ALARALaLDP--EILLYDEPTAGLDPITsaVIDelireLRDEL-----GLTSVVVTHDLDSAFAIaDRVAVLADGKIIAE 223
|
....*...
gi 543385153 546 GTFDELTK 553
Cdd:COG1127 224 GTPEELLA 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
332-551 |
1.76e-28 |
|
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: 113.37 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 332 LENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNiPAWHQ----QMLY 407
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLS-EAELYrlrrRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVFTA-SLRENIAFYTPE---ASDAEI----MKAIHVVSLDELVSELPegldtiiGQgkrvLSGGQAQRIALARA 479
Cdd:cd03261 82 LFQSGALFDSlTVFENVAFPLREhtrLSEEEIreivLEKLEAVGLRGAEDLYP-------AE----LSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 480 F-LDKtrKVMLFDEPTAHLD-IETEV------DLKKQMlplmeNRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDE 550
Cdd:cd03261 151 LaLDP--ELLLYDEPTAGLDpIASGViddlirSLKKEL-----GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEE 223
|
.
gi 543385153 551 L 551
Cdd:cd03261 224 L 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
329-551 |
4.10e-28 |
|
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: 112.43 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 329 ELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAAtlNIPAWHQQMLYI 408
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 409 PQNPYVFT-ASLRENIAF------YTPEASDAEIMKAIH----VVSLDELVSELPEGldtiigqgkrvLSGGQAQRIALA 477
Cdd:cd03296 80 FQHYALFRhMTVFDNVAFglrvkpRSERPPEAEIRAKVHellkLVQLDWLADRYPAQ-----------LSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 478 RAfLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLV--IFATH-RLHWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:cd03296 149 RA-LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVttVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
330-551 |
6.40e-28 |
|
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: 111.90 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGP----VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN---IPAWH 402
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTalkdVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQNPYVFTA-SLRENIAFytP----EASDAEIMKAIHvvSLDELVSeLPEGLDTIIGQgkrvLSGGQAQRIALA 477
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVAL--PleiaGVPKAEIEERVL--ELLELVG-LEDKADAYPAQ----LSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 478 RAfLDKTRKVMLFDEPTAHLDIETevdlKKQMLPLMEN---RL---VIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDE 550
Cdd:cd03258 153 RA-LANNPKVLLCDEATSALDPET----TQSILALLRDinrELgltIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEE 227
|
.
gi 543385153 551 L 551
Cdd:cd03258 228 V 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
330-523 |
9.31e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 112.11 E-value: 9.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE----IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKaatlnIPAWHQQM 405
Cdd:COG1116 8 LELRGVSKRFPTGGGgvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LYIPQNPYVF---TAslRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPegldtiigqgkRVLSGGQAQRIAL 476
Cdd:COG1116 83 GVVFQEPALLpwlTV--LDNVALglelrgVPKAERRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 543385153 477 ARAFLDKtRKVMLFDEPTAHLDIETEVDLKKQMLPL-MENRL-VIFATH 523
Cdd:COG1116 150 ARALAND-PEVLLMDEPFGALDALTRERLQDELLRLwQETGKtVLFVTH 197
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
330-543 |
1.14e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.91 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEI-GPVSVEI-KGyEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN---IPAWHQQ 404
Cdd:COG2884 2 IRFENVSKRYPGGREAlSDVSLEIeKG-EFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 MLYIPQNpY-------VFtaslrENIAF------YTPEASDAEIMKAIHVVSLDELVSELPegldtiigqgkRVLSGGQA 471
Cdd:COG2884 81 IGVVFQD-FrllpdrtVY-----ENVALplrvtgKSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 472 QRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLkkqMLPLME-NRL---VIFATHRLHWLKEMDY-ILVMHEGKLV 543
Cdd:COG2884 144 QRVAIARALVNRP-ELLLADEPTGNLDPETSWEI---MELLEEiNRRgttVLIATHDLELVDRMPKrVLELEDGRLV 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
331-546 |
1.49e-27 |
|
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: 110.32 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 331 KLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNipawhQQMLYIPQ 410
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 411 NPYV---FTASLRENIA---------FYTPEASD-AEIMKAIHVVSLDELvselpegLDTIIGQgkrvLSGGQAQRIALA 477
Cdd:cd03235 76 RRSIdrdFPISVRDVVLmglyghkglFRRLSKADkAKVDEALERVGLSEL-------ADRQIGE----LSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 478 RAfLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPL-MENRLVIFATHRLHWLKE-MDYILVMhEGKLVQQG 546
Cdd:cd03235 145 RA-LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
330-551 |
1.84e-27 |
|
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: 111.37 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATL-NIPAWHQQML 406
Cdd:TIGR04520 1 IEVENVSFSYPESEKpaLKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 407 YIPQNP---YVfTASLRENIAFyTPE--ASDAEIMK-----AIHVVSLDELVSELPegldtiigqgkRVLSGGQAQRIAL 476
Cdd:TIGR04520 81 MVFQNPdnqFV-GATVEDDVAF-GLEnlGVPREEMRkrvdeALKLVGMEDFRDREP-----------HLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 477 ARAfLDKTRKVMLFDEPTAHLD-------IETEVDLKKQmlplmENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFD 549
Cdd:TIGR04520 148 AGV-LAMRPDIIILDEATSMLDpkgrkevLETIRKLNKE-----EGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
..
gi 543385153 550 EL 551
Cdd:TIGR04520 222 EI 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
330-526 |
3.19e-27 |
|
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: 109.48 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNY----NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKaatlnIPAWHQQM 405
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LYIPQNPYVF---TAslRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPegldtiigqgkRVLSGGQAQRIAL 476
Cdd:cd03293 76 GYVFQQDALLpwlTV--LDNVALglelqgVPKAEARERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVAL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 543385153 477 ARAFLDKtRKVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRL-VIFATHRLH 526
Cdd:cd03293 143 ARALAVD-PDVLLLDEPFSALDALTREQLQEELLDIWrETGKtVLLVTHDID 193
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
348-551 |
9.77e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 115.65 E-value: 9.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYT 427
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFL 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 428 pEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRKVMLFDEPTAHLDIETEVDLKK 507
Cdd:PTZ00243 1409 -EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILMDEATANIDPALDRQIQA 1487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 543385153 508 QMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:PTZ00243 1488 TVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
236-524 |
2.36e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 113.36 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 236 MLSTFALDFFTTlsiavvavylGFGLLNGQLPlypalsILILAPEYF------------------------LPIRNFAS- 290
Cdd:COG4178 262 IRRQRNLTFFTT----------GYGQLAVIFP------ILVAAPRYFageitlgglmqaasafgqvqgalsWFVDNYQSl 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 291 -DYHATLNGKNAFKR-INELISRPMQASADLAIEPwnskSELKLENLE-FNYNNQTEIGPVSVEIKGYEKVGIIGMSGSG 367
Cdd:COG4178 326 aEWRATVDRLAGFEEaLEAADALPEAASRIETSED----GALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 368 KSTLINLLSGFLPPKSGKIIIdgqkaatlniPAwHQQMLYIPQNPYVFTASLRENIAF-YTPEA-SDAEIMKAIHVVSLD 445
Cdd:COG4178 402 KSTLLRAIAGLWPYGSGRIAR----------PA-GARVLFLPQRPYLPLGTLREALLYpATAEAfSDAELREALEAVGLG 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 446 ELVSELPEGLDTIigqgkRVLSGGQAQRIALARAFLDKTRKVMLfDEPTAHLDIETEvdlkKQMLPLMENRL----VIFA 521
Cdd:COG4178 471 HLAERLDEEADWD-----QVLSLGEQQRLAFARLLLHKPDWLFL-DEATSALDEENE----AALYQLLREELpgttVISV 540
|
...
gi 543385153 522 THR 524
Cdd:COG4178 541 GHR 543
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
50-543 |
3.46e-26 |
|
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: 112.58 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 50 LNWQYLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIFKSGQSLVQSQGTGSL----------ITMALYGI 119
Cdd:COG4615 46 ALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLlaaltedvrtISQAFVRL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 120 DEvrdyikLIYTkvlAMMIIPILLFIAMLfiNWQSALGLLLMypliVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLR 199
Cdd:COG4615 126 PE------LLQS---VALVLGCLAYLAWL--SPPLFLLTLVL----LGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 200 GI-DTLKYLGLSKRYSKSIF-----RVSEDFRHKTMAVLkVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQLPLYPALS 273
Cdd:COG4615 191 ALlEGFKELKLNRRRRRAFFdedlqPTAERYRDLRIRAD-TIFALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 274 ILILapeyFL--PIRNFASDYHATLNGKNAFKRINEL---ISRPMQASADLAIEPWNSK-SELKLENLEFNYNNQTE--- 344
Cdd:COG4615 270 LVLL----FLrgPLSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGdeg 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 345 --IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFtaslrEN 422
Cdd:COG4615 346 ftLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 423 IAFYTPEASDAEIMKAIHVVSLDELVSelpegldtiIGQGK---RVLSGGQAQRIALARAFLDKtRKVMLFDEPTAHLDI 499
Cdd:COG4615 421 LLGLDGEADPARARELLERLELDHKVS---------VEDGRfstTDLSQGQRKRLALLVALLED-RPILVFDEWAADQDP 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 543385153 500 E------TEV--DLKKQmlplmeNRLVIFATHRLHWLKEMDYILVMHEGKLV 543
Cdd:COG4615 491 EfrrvfyTELlpELKAR------GKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
316-547 |
3.64e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.42 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 316 SADLAIEPWNSKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAAt 395
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 396 lNIPAWHQQMLYIPQNPYVFT-ASLRENIAF-----YTPEASDAE-IMKAIHVVSLDELVSELPegldtiigqgkRVLSG 468
Cdd:PRK09452 80 -HVPAENRHVNTVFQSYALFPhMTVFENVAFglrmqKTPAAEITPrVMEALRMVQLEEFAQRKP-----------HQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 469 GQAQRIALARAFLDKTrKVMLFDEPTAHLDIEtevdLKKQM---LPLMENRL---VIFATH-RLHWLKEMDYILVMHEGK 541
Cdd:PRK09452 148 GQQQRVAIARAVVNKP-KVLLLDESLSALDYK----LRKQMqneLKALQRKLgitFVFVTHdQEEALTMSDRIVVMRDGR 222
|
....*.
gi 543385153 542 LVQQGT 547
Cdd:PRK09452 223 IEQDGT 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
359-551 |
4.52e-26 |
|
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: 109.81 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 359 GIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ----KAATLNIPAWHQQMLYIPQNPYVF-TASLRENIAF---YTPEA 430
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFpHLSVRGNLLYgrkRAPRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 431 SDAeimkaihvVSLDELVSELpeGLDTIIGQGKRVLSGGQAQRIALARAFLdkTR-KVMLFDEPTAHLDieteVDLKKQM 509
Cdd:COG4148 109 ERR--------ISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALL--SSpRLLLMDEPLAALD----LARKAEI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 543385153 510 LPLMEnRL-------VIFATHRLHwlkEM----DYILVMHEGKLVQQGTFDEL 551
Cdd:COG4148 173 LPYLE-RLrdeldipILYVSHSLD---EVarlaDHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
330-551 |
5.78e-26 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 106.62 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNN-QTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYI 408
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 409 PQNPYVFT-ASLRENIAF------YTPEASDAEIMKAIHVVSLDelvselPEGLdtiIGQGKRVLSGGQAQRIALARAfL 481
Cdd:cd03295 81 IQQIGLFPhMTVEENIALvpkllkWPKEKIRERADELLALVGLD------PAEF---ADRYPHELSGGQQQRVGVARA-L 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 482 DKTRKVMLFDEPTAHLDIETEVDLKKQMLPLME--NRLVIFATHRL-HWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
348-546 |
1.75e-25 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 104.30 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGyEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ----KAATLNIPAWHQQMLYIPQNPYVFT-ASLREN 422
Cdd:cd03297 17 IDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFPhLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 423 IAFYTPEASDAEIMkaihvVSLDELVSELpeGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRkVMLFDEPTAHLDIEte 502
Cdd:cd03297 96 LAFGLKRKRNREDR-----ISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPE-LLLLDEPFSALDRA-- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 543385153 503 vdLKKQMLPLMENRL------VIFATHRLHWLKEM-DYILVMHEGKLVQQG 546
Cdd:cd03297 166 --LRLQLLPELKQIKknlnipVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
348-561 |
2.41e-25 |
|
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: 106.09 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaatlnipawhqqMLYIPQNPYVFTASLRENIAFYT 427
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 428 pEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLDIETEVDL-K 506
Cdd:cd03291 123 -SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVY-KDADLYLLDSPFGYLDVFTEKEIfE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 507 KQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKL 561
Cdd:cd03291 201 SCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSK 255
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
330-546 |
4.26e-25 |
|
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: 103.04 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEI-KGYekVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAatLNIPAWHQQML-Y 407
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLgPGM--YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--LKQPQKLRRRIgY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYV---FTAslRENIAFytpeasdAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRV--LSGGQAQRIALARAFLD 482
Cdd:cd03264 77 LPQEFGVypnFTV--REFLDY-------IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIgsLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 483 KTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQG 546
Cdd:cd03264 148 DP-SILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
330-555 |
5.57e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.13 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQT-----EIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAA--TLNIPAWH 402
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQNP--YVFTASLRENIAFyTPE---ASDAEI----MKAIHVVSLDelvselpegLDTIIGQGKRVLSGGQAQR 473
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAF-GPInlgLSEEEIenrvKRAMNIVGLD---------YEDYKDKSPFELSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 474 IALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLME--NRLVIFATHRLHWL-KEMDYILVMHEGKLVQQGTFDE 550
Cdd:PRK13637 153 VAIAGVVAMEP-KILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
....*
gi 543385153 551 LTKEA 555
Cdd:PRK13637 232 VFKEV 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
348-561 |
9.42e-25 |
|
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: 109.61 E-value: 9.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaatlnipawhqqMLYIPQNPYVFTASLRENIAFYT 427
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 428 pEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAfLDKTRKVMLFDEPTAHLDIETEVDLKK 507
Cdd:TIGR01271 512 -SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARA-VYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 508 QML-PLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYFTKL 561
Cdd:TIGR01271 590 SCLcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
297-551 |
7.86e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 106.65 E-value: 7.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 297 NGKNAFKRINELISRP--MQASADLAIEPWNS---KSELKLENLEFNYNNQTEIgPV----SVEIKGYEKVGIIGMSGSG 367
Cdd:PTZ00265 1128 NAKLSFEKYYPLIIRKsnIDVRDNGGIRIKNKndiKGKIEIMDVNFRYISRPNV-PIykdlTFSCDSKKTTAIVGETGSG 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 368 KSTLINLLSGFLPPK------------------------------------------------------SGKIIIDGQKA 393
Cdd:PTZ00265 1207 KSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDI 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 394 ATLNIPAWHQQMLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQR 473
Cdd:PTZ00265 1287 CDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQR 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 474 IALARAFLdKTRKVMLFDEPTAHLDIETEVDLKKQMLPLME--NRLVIFATHRLHWLKEMDYILVMHE----GKLVQ-QG 546
Cdd:PTZ00265 1367 IAIARALL-REPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHG 1445
|
....*
gi 543385153 547 TFDEL 551
Cdd:PTZ00265 1446 THEEL 1450
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
330-546 |
9.37e-24 |
|
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: 99.25 E-value: 9.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAAtlNIPAWHQQMLYIP 409
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QN----PYVftaSLRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPegldtiigqgkRVLSGGQAQRIALARA 479
Cdd:cd03301 79 QNyalyPHM---TVYDNIAFglklrkVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 480 fLDKTRKVMLFDEPTAHLDIETEVDLKKQmLPLMENRL---VIFATH-RLHWLKEMDYILVMHEGKLVQQG 546
Cdd:cd03301 145 -IVREPKVFLMDEPLSNLDAKLRVQMRAE-LKRLQQRLgttTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
330-555 |
1.26e-23 |
|
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: 99.95 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEI-GPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATL---NIPAWHQQM 405
Cdd:cd03256 1 IEVENLSKTYPNGKKAlKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LYIPQNP------YVFT----------ASLRENIAFYTPEasdaEIMKAIHvvSLDELvselpeGLDTIIGQGKRVLSGG 469
Cdd:cd03256 81 GMIFQQFnlierlSVLEnvlsgrlgrrSTWRSLFGLFPKE----EKQRALA--ALERV------GLLDKAYQRADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 470 QAQRIALARAFLDKTrKVMLFDEPTAHLDIETevdlKKQMLPLM------ENRLVIFATHRLHWLKE-MDYILVMHEGKL 542
Cdd:cd03256 149 QQQRVAIARALMQQP-KLILADEPVASLDPAS----SRQVMDLLkrinreEGITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
250
....*....|...
gi 543385153 543 VQQGTFDELTKEA 555
Cdd:cd03256 224 VFDGPPAELTDEV 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
330-551 |
2.12e-23 |
|
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: 100.90 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYnnQTEIGP------VSVEI-KGyEKVGIIGMSGSGKSTLINLLSGFLPPK---SGKIIIDGQKAATLNIP 399
Cdd:COG0444 2 LEVRNLKVYF--PTRRGVvkavdgVSFDVrRG-ETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 400 AWHQ------QMlyIPQNPY-----VFT--ASLRENIAFYTPeASDAEIMKaiHVVSLDELVselpeGLDtiiGQGKRV- 465
Cdd:COG0444 79 ELRKirgreiQM--IFQDPMtslnpVMTvgDQIAEPLRIHGG-LSKAEARE--RAIELLERV-----GLP---DPERRLd 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 466 -----LSGGQAQRIALARAFLdkTR-KVMLFDEPTAHLDieteVDLKKQMLPLM-----ENRL-VIFATHRLHWLKEM-D 532
Cdd:COG0444 146 rypheLSGGMRQRVMIARALA--LEpKLLIADEPTTALD----VTIQAQILNLLkdlqrELGLaILFITHDLGVVAEIaD 219
|
250
....*....|....*....
gi 543385153 533 YILVMHEGKLVQQGTFDEL 551
Cdd:COG0444 220 RVAVMYAGRIVEEGPVEEL 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
305-571 |
2.47e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.84 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 305 INELISRPmQASADLAIEPWnskseLKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSG 384
Cdd:PRK11607 1 MNDAIPRP-QAKTRKALTPL-----LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 385 KIIIDGQKAAtlNIPAWHQQMLYIPQNPYVFT-ASLRENIAFYTPE--ASDAEIMKAIH----VVSLDELVSELPEGldt 457
Cdd:PRK11607 75 QIMLDGVDLS--HVPPYQRPINMMFQSYALFPhMTVEQNIAFGLKQdkLPKAEIASRVNemlgLVHMQEFAKRKPHQ--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 458 iigqgkrvLSGGQAQRIALARAfLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLV--IFATHRLHWLKEM-DYI 534
Cdd:PRK11607 150 --------LSGGQRQRVALARS-LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVtcVMVTHDQEEAMTMaGRI 220
|
250 260 270
....*....|....*....|....*....|....*..
gi 543385153 535 LVMHEGKLVQQGTFDELTKEAGyfTKLTQEMRGTKNV 571
Cdd:PRK11607 221 AIMNRGKFVQIGEPEEIYEHPT--TRYSAEFIGSVNV 255
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
330-547 |
2.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 99.68 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQT-EIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN-IPAWHQQMLY 407
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYV-FTA-SLRENIAFyTPE---ASDAEIMKAIhvvslDELVSELpeGLDTIIGQGKRVLSGGQAQRIALArAFLD 482
Cdd:PRK13644 82 VFQNPETqFVGrTVEEDLAF-GPEnlcLPPIEIRKRV-----DRALAEI--GLEKYRHRSPKTLSGGQGQCVALA-GILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 483 KTRKVMLFDEPTAHLDIETEVDLKKQMLPLMEN-RLVIFATHRLHWLKEMDYILVMHEGKLVQQGT 547
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-537 |
5.23e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 103.96 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 55 LLIFIVCLTGRQLIDLLKDKMLETyssqevekLRQQLLNKIF-KSGQslVQSQGTGSLITMAL-YGIDEVRDYIKLIYTK 132
Cdd:PTZ00265 108 IFQFILSFISSFCMDVVTTKILKT--------LKLEFLKSVFyQDGQ--FHDNNPGSKLTSDLdFYLEQVNAGIGTKFIT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 133 VLAMMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYAAKDRASKQFgdfqkLSNN-----FIDSLRGIDTL-KY 206
Cdd:PTZ00265 178 IFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSL-----LYNNntmsiIEEALVGIRTVvSY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 207 LGLSKRYSKsiFRVSEDFRHKTMavLKVAMLSTFALDFFTTLSIAVVAVYLGFG---LLNGQLPLYP--------ALSIL 275
Cdd:PTZ00265 253 CGEKTILKK--FNLSEKLYSKYI--LKANFMESLHIGMINGFILASYAFGFWYGtriIISDLSNQQPnndfhggsVISIL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 276 --ILAPEYFLPI--RNFaSDYHATLNGKNAfkrINELISR-PMQASADLAIEPWNSKsELKLENLEFNYNNQTEI---GP 347
Cdd:PTZ00265 329 lgVLISMFMLTIilPNI-TEYMKSLEATNS---LYEIINRkPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKDVeiyKD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIII-DGQKAATLNIPAWHQQMLYIPQNPYVFTASLRENIAF- 425
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYs 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 426 ------------YTPEAS--------------------------------------------DAEIMKAIHVVSLDELVS 449
Cdd:PTZ00265 484 lyslkdlealsnYYNEDGndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVS 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 450 ELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLDIETEVDLKKQMLPLM--ENRLVIFATHRLHW 527
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAII-RNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLST 642
|
570
....*....|
gi 543385153 528 LKEMDYILVM 537
Cdd:PTZ00265 643 IRYANTIFVL 652
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
330-551 |
6.00e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 97.76 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQK--AATLNIPAWHQQMLY 407
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltDSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVF---TAslRENIAF-------YTPEASDAEIMKAIHVVSLDELVSELPegldtiiGQgkrvLSGGQAQRIALA 477
Cdd:COG1126 82 VFQQFNLFphlTV--LENVTLapikvkkMSKAEAEERAMELLERVGLADKADAYP-------AQ----LSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 478 RAfLDKTRKVMLFDEPTAHLDIET--EV-----DLKKqmlplmENRLVIFATHrlhwlkEM-------DYILVMHEGKLV 543
Cdd:COG1126 149 RA-LAMEPKVMLFDEPTSALDPELvgEVldvmrDLAK------EGMTMVVVTH------EMgfarevaDRVVFMDGGRIV 215
|
....*...
gi 543385153 544 QQGTFDEL 551
Cdd:COG1126 216 EEGPPEEF 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
349-546 |
8.75e-23 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 96.79 E-value: 8.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 349 SVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNpyVFT-ASLRENIAF-- 425
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENN--LFAhLTVEQNVGLgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 426 -----YTPEASDAeIMKAIHVVSLDELVSELPegldtiigqgkRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLDie 500
Cdd:cd03298 96 spglkLTAEDRQA-IEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLV-RDKPVLLLDEPFAALD-- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 543385153 501 teVDLKKQMLPLM-----ENRL-VIFATHRLHWLKEM-DYILVMHEGKLVQQG 546
Cdd:cd03298 161 --PALRAEMLDLVldlhaETKMtVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
328-555 |
1.19e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 328 SELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLY 407
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVFTA-SLRENIAF-YTP---------EASDAEIMKAIHVVSLDELVSelpegldtiigqgKRV--LSGGQAQRI 474
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYgRSPwlslwgrlsAEDNARVNQAMEQTRINHLAD-------------RRLtdLSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 475 ALARAFLDKTRKVMLfDEPTAHLDIETEVDLKKQMLPL-MENRLVIFATHRLHWL-KEMDYILVMHEGKLVQQGTFDELT 552
Cdd:PRK11231 148 FLAMVLAQDTPVVLL-DEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVM 226
|
...
gi 543385153 553 KEA 555
Cdd:PRK11231 227 TPG 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
357-551 |
1.24e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.95 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 357 KVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNP--YVFTASLRENIAF------YTP 428
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFgpinlgLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 429 EASDAEIMKAIHVVSLDELVSELPEGldtiigqgkrvLSGGQAQRIALArAFLDKTRKVMLFDEPTAHLDIETEVDLKKQ 508
Cdd:PRK13652 112 ETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIA-GVIAMEPQVLVLDEPTAGLDPQGVKELIDF 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 543385153 509 M--LPLMENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:PRK13652 180 LndLPETYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
348-551 |
1.47e-22 |
|
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: 97.33 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN-----------IPAWHQQMLYIPQNpyvft 416
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrelrrkkISMVFQSFALLPHR----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 417 aSLRENIAF------YTPEASDAEIMKAIHVVSLdelvselpEG-LDTIIGQgkrvLSGGQAQRIALARAfLDKTRKVML 489
Cdd:cd03294 118 -TVLENVAFglevqgVPRAEREERAAEALELVGL--------EGwEHKYPDE----LSGGMQQRVGLARA-LAVDPDILL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 490 FDEPTAHLDIETEVDLKKQMLPL--MENRLVIFATHRL-HWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
348-546 |
2.46e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 102.16 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIiidgqkaatlnipaWHQQML-YIPQNPYVFTASLRENIAFY 426
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERSIaYVPQQAWIMNATVRGNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 427 TPEASdAEIMKAIHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLDIET-EVDL 505
Cdd:PTZ00243 745 DEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVY-ANRDVYLLDDPLSALDAHVgERVV 822
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 543385153 506 KKQMLPLMENRLVIFATHRLHWLKEMDYILVMHEGKLVQQG 546
Cdd:PTZ00243 823 EECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
330-543 |
2.94e-22 |
|
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: 93.65 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKaatlnipawhqqmlyip 409
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 qnpyvftaslrenIAFYTP-EASDAEImkaihvvsldelvselpegldTIIGQgkrvLSGGQAQRIALARAFLDKTRkVM 488
Cdd:cd03216 64 -------------VSFASPrDARRAGI---------------------AMVYQ----LSVGERQMVEIARALARNAR-LL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543385153 489 LFDEPTAHLDiETEVDlkkQMLPLMEnRL------VIFATHRLHWLKEM-DYILVMHEGKLV 543
Cdd:cd03216 105 ILDEPTAALT-PAEVE---RLFKVIR-RLraqgvaVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
330-551 |
6.40e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 95.67 E-value: 6.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQT---------EIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPA 400
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 401 WHQQMLYIPQNPY-----------VFTASLRENIAFyTPEASDAEIMKAIHVVSLdelvseLPEGLDTIIgqgkRVLSGG 469
Cdd:COG4167 85 RCKHIRMIFQDPNtslnprlnigqILEEPLRLNTDL-TAEEREERIFATLRLVGL------LPEHANFYP----HMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 470 QAQRIALARAF-LDKtrKVMLFDEPTAHLDIEtevdLKKQMLPLM---ENRL---VIFATHRLHWLKEM-DYILVMHEGK 541
Cdd:COG4167 154 QKQRVALARALiLQP--KIIIADEALAALDMS----VRSQIINLMlelQEKLgisYIYVSQHLGIVKHIsDKVLVMHQGE 227
|
250
....*....|
gi 543385153 542 LVQQGTFDEL 551
Cdd:COG4167 228 VVEYGKTAEV 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
330-551 |
7.57e-22 |
|
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: 94.53 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIpawHQQ----M 405
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM---HKRarlgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LYIPQNPYVFTA-SLRENI--AFYTPEASDAEIMKaihvvSLDELVSELpeGLDTIIGQGKRVLSGGQAQRIALARAfLD 482
Cdd:cd03218 78 GYLPQEASIFRKlTVEENIlaVLEIRGLSKKEREE-----KLEELLEEF--HITHLRKSKASSLSGGERRRVEIARA-LA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 483 KTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFAT-HRLH-WLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
330-514 |
8.38e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 8.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQteigPV--SVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKaATLNIPAwhQQ--- 404
Cdd:PRK10771 2 LKLTDITWLYHHL----PMrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPS--RRpvs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 MLYIPQNpyVFT-ASLRENIAF-YTP----EASDAEIMKAI-HVVSLDELVSELPegldtiiGQgkrvLSGGQAQRIALA 477
Cdd:PRK10771 75 MLFQENN--LFShLTVAQNIGLgLNPglklNAAQREKLHAIaRQMGIEDLLARLP-------GQ----LSGGQRQRVALA 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 543385153 478 RAFLdKTRKVMLFDEPTAHLDIEtevdLKKQMLPLME 514
Cdd:PRK10771 142 RCLV-REQPILLLDEPFSALDPA----LRQEMLTLVS 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
330-542 |
8.42e-22 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 93.75 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQK--AATLNIPAWHQQMLY 407
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPYVF---TAslRENIAF-------YTPEASDAEIMKAIHVVSLDELVSELPegldtiigqgkRVLSGGQAQRIALA 477
Cdd:cd03262 81 VFQQFNLFphlTV--LENITLapikvkgMSKAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 478 RAfLDKTRKVMLFDEPTAHLDIEtevdLKKQMLPLM-----ENRLVIFATHRLHWLKEM-DYILVMHEGKL 542
Cdd:cd03262 148 RA-LAMNPKVMLFDEPTSALDPE----LVGEVLDVMkdlaeEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
330-554 |
9.97e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.80 E-value: 9.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaatlNIPAW-HQQM--- 405
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-----PLAAWsPWELarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 ---LyiPQNPYV---FTAslRENIA------FYTPEASDAEIMKAIHVVSLDELVSEL-PEgldtiigqgkrvLSGGQAQ 472
Cdd:COG4559 77 ravL--PQHSSLafpFTV--EEVVAlgraphGSSAAQDRQIVREALALVGLAHLAGRSyQT------------LSGGEQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 473 RIALARAFL------DKTRKVMLFDEPTAHLDIetevdlkKQMLPLME--NRL------VIFATHRLHwLKEM--DYILV 536
Cdd:COG4559 141 RVQLARVLAqlwepvDGGPRWLFLDEPTSALDL-------AHQHAVLRlaRQLarrgggVVAVLHDLN-LAAQyaDRILL 212
|
250
....*....|....*....
gi 543385153 537 MHEGKLVQQGTFDE-LTKE 554
Cdd:COG4559 213 LHQGRLVAQGTPEEvLTDE 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
348-550 |
1.09e-21 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 94.04 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLniPAwHQqmlyIP--------QNPYVFTA-S 418
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL--PP-HE----IArlgigrtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 419 LRENI----------------AFYTPEASDAEIMKAIHVVSLDELvselpegLDTIIGQgkrvLSGGQAQRIALARAFLd 482
Cdd:cd03219 92 VLENVmvaaqartgsglllarARREEREARERAEELLERVGLADL-------ADRPAGE----LSYGQQRRLEIARALA- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 483 kTR-KVMLFDEPTAHLDIETEVDLKKQMLPLMENRL-VIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDE 550
Cdd:cd03219 160 -TDpKLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
348-552 |
1.30e-21 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 93.34 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATlNIPAWHQQMLYIPQNPYVFTA-SLRENIAFY 426
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVREHLRFY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 427 TpeasdaeIMKAIHVVSLDELVSELPEGLDTIIGQGKRV--LSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVD 504
Cdd:cd03263 100 A-------RLKGLPKSEIKEEVELLLRVLGLTDKANKRArtLSGGMKRKLSLAIALIGGP-SVLLLDEPTSGLDPASRRA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 543385153 505 LKKQMLPLMENRLVIFATHRLHwlkEM----DYILVMHEGKLVQQGTFDELT 552
Cdd:cd03263 172 IWDLILEVRKGRSIILTTHSMD---EAealcDRIAIMSDGKLRCIGSPQELK 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
330-554 |
2.14e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.68 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ-----KAATLnipAWHQQ 404
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwSPAEL---ARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 MLyiPQNPYV-FTASLRENIAF------YTPEASDAEIMKAIHVVSLDELVSEL-PEgldtiigqgkrvLSGGQAQRIAL 476
Cdd:PRK13548 80 VL--PQHSSLsFPFTVEEVVAMgraphgLSRAEDDALVAAALAQVDLAHLAGRDyPQ------------LSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 477 ARAFL-----DKTRKVMLFDEPTAHLDI---ETEVDLKKQmLPLMENRLVIFATHRL----HWlkeMDYILVMHEGKLVQ 544
Cdd:PRK13548 146 ARVLAqlwepDGPPRWLLLDEPTSALDLahqHHVLRLARQ-LAHERGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVA 221
|
250
....*....|.
gi 543385153 545 QGTFDE-LTKE 554
Cdd:PRK13548 222 DGTPAEvLTPE 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
356-523 |
7.59e-21 |
|
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: 90.63 E-value: 7.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 356 EKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNiPAWHQQMLYIPQNPYVFTA-SLRENIAFYTPEASDAE 434
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGHAPGIKTTlSVLENLRFWHADHSDEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 435 IMKAIHVVSLDELVselpeglDTIIGQgkrvLSGGQAQRIALARAFLDKtRKVMLFDEPTAHLDIETEVDLKKQMLP-LM 513
Cdd:cd03231 106 VEEALARVGLNGFE-------DRPVAQ----LSAGQQRRVALARLLLSG-RPLWILDEPTTALDKAGVARFAEAMAGhCA 173
|
170
....*....|
gi 543385153 514 ENRLVIFATH 523
Cdd:cd03231 174 RGGMVVLTTH 183
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
325-547 |
8.60e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 8.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 325 NSKSELKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWH 402
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATyaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQNP---YVfTASLRENIAFYTPEasdaeimkaiHVVSLDELVSELPEGLDTI-----IGQGKRVLSGGQAQRI 474
Cdd:PRK13635 81 RQVGMVFQNPdnqFV-GATVQDDVAFGLEN----------IGVPREEMVERVDQALRQVgmedfLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 475 ALArAFLDKTRKVMLFDEPTAHLD-------IETEVDLKKQmlplmENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGT 547
Cdd:PRK13635 150 AIA-GVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQ-----KGITVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
330-551 |
1.42e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.10 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE---IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQML 406
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkytLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 407 YIPQNP---YVfTASLRENIAFYTPEASdaeimkaihvVSLDELVSELPEGLDTIIGQGKRV-----LSGGQAQRIALAR 478
Cdd:PRK13650 85 MVFQNPdnqFV-GATVEDDVAFGLENKG----------IPHEEMKERVNEALELVGMQDFKEreparLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 479 AFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLME--NRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:PRK13650 154 AVAMRP-KIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
325-498 |
2.82e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.77 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 325 NSKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQ 404
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 MLYIPQNPYVFTASLRENIAFYTPEASDAEIMKAIhvvsLDELVS-ELPEgldTIIGQGKRVLSGGQAQRIALAR--AFL 481
Cdd:PRK10247 83 VSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIF----LDDLERfALPD---TILTKNIAELSGGEKQRISLIRnlQFM 155
|
170
....*....|....*..
gi 543385153 482 DktrKVMLFDEPTAHLD 498
Cdd:PRK10247 156 P---KVLLLDEITSALD 169
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
330-551 |
3.74e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.09 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIpawhQQ----M 405
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI----QQrdicM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LYipQNPYVFT-ASLRENIAFytpeasdAEIMKAihvVSLDELVSELPEGLDTI--IGQGKRV---LSGGQAQRIALARA 479
Cdd:PRK11432 83 VF--QSYALFPhMSLGENVGY-------GLKMLG---VPKEERKQRVKEALELVdlAGFEDRYvdqISGGQQQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 480 FLDKTrKVMLFDEPTAHLDieteVDLKKQM---LPLMENRLVIFATHRLHWLKEM----DYILVMHEGKLVQQGTFDEL 551
Cdd:PRK11432 151 LILKP-KVLLFDEPLSNLD----ANLRRSMrekIRELQQQFNITSLYVTHDQSEAfavsDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
347-542 |
3.92e-20 |
|
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: 88.26 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 347 PVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQ-MLYIPQNPY----VFTASLRE 421
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKreglVLDLSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 422 NIAFytpeasdaeimkaihvvsldelvselpegldtiigqgKRVLSGGQAQRIALARAFLDKTRkVMLFDEPTAHLDIET 501
Cdd:cd03215 98 NIAL-------------------------------------SSLLSGGNQQKVVLARWLARDPR-VLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 543385153 502 EVDLKKQMLPL-MENRLVIFATHRLHWLKEM-DYILVMHEGKL 542
Cdd:cd03215 140 KAEIYRLIRELaDAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
330-550 |
4.73e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIdgqkAATLNIPawhqqmlYIP 409
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL----GETVKIG-------YFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVF--TASLRENIAFYTPEASDaeimkaIHVVSLdelvseL------PEGLDTIIGqgkrVLSGGQAQRIALARAFL 481
Cdd:COG0488 385 QHQEELdpDKTVLDELRDGAPGGTE------QEVRGY------LgrflfsGDDAFKPVG----VLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 482 DKTrKVMLFDEPTAHLDIETevdlkKQMLplmENRL------VIFATHRLHWLKEM-DYILVMHEGKLVQ-QGTFDE 550
Cdd:COG0488 449 SPP-NVLLLDEPTNHLDIET-----LEAL---EEALddfpgtVLLVSHDRYFLDRVaTRILEFEDGGVREyPGGYDD 516
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
19-305 |
5.80e-20 |
|
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: 90.30 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 19 LAVLEVLQAFLIIGQALSLSAVLTTLWQGKKLN--WQYLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIF 96
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSllLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 97 KSGQSLVQSQGTGSLITMALYGIDEVRDYIKLIYTKVLAMMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYAA 176
Cdd:cd07346 84 RLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 177 KdRASKQFGD-FQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAV 255
Cdd:cd07346 164 R-KASREVREsLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 543385153 256 YLGFGLLNGQLPLYPALSILILAPEYFLPIRNFASDYHATLNGKNAFKRI 305
Cdd:cd07346 243 YGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
358-558 |
1.09e-19 |
|
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: 93.47 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 358 VGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAatlnipawhqqmlYIPQNPYVFTASLRENIAFYTP--EASDAEI 435
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA-------------YVPQQAWIQNDSLRENILFGKAlnEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 436 MKAIHVVSLDELvseLPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLP---L 512
Cdd:TIGR00957 734 LEACALLPDLEI---LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA-DIYLFDDPLSAVDAHVGKHIFEHVIGpegV 809
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 543385153 513 MENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTKEAGYF 558
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
323-551 |
1.11e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.08 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 323 PWNSKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWH 402
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQN-PYVFTASLRENIAF--YtP--------EASDAE-IMKAIHVVSLDELVSELpegLDTiigqgkrvLSGGQ 470
Cdd:PRK10575 85 RKVAYLPQQlPAAEGMTVRELVAIgrY-PwhgalgrfGAADREkVEEAISLVGLKPLAHRL---VDS--------LSGGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 471 AQRIALARAFLDKTRkVMLFDEPTAHLDIETEVDLKKQMLPLMENR--LVIFATHRLHW-LKEMDYILVMHEGKLVQQGT 547
Cdd:PRK10575 153 RQRAWIAMLVAQDSR-CLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMaARYCDYLVALRGGEMIAQGT 231
|
....
gi 543385153 548 FDEL 551
Cdd:PRK10575 232 PAEL 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
347-547 |
1.25e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.08 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 347 PVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNP-----------YVF 415
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqrisQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 416 TASLRENIAFyTPEASDAEIMKAIHVVSL-DELVSELPEgldtiigqgkrVLSGGQAQRIALARAFLDKTrKVMLFDEPT 494
Cdd:PRK15112 111 DFPLRLNTDL-EPEQREKQIIETLRQVGLlPDHASYYPH-----------MLAPGQKQRLGLARALILRP-KVIIADEAL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 495 AHLDIETEVDLKKQMLPLMENRLV--IFATHRLHWLKEM-DYILVMHEGKLVQQGT 547
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHIsDQVLVMHQGEVVERGS 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
348-551 |
1.33e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 90.18 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAW---HQQMLYIPQNPYvftASL--Ren 422
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDPY---ASLnpR-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 423 iafYTPEASDAEIMKaIH-VVS---LDELVSELPE--GLDTiiGQGKRV---LSGGQAQRIALARAFLDKTRKVMLfDEP 493
Cdd:COG4608 112 ---MTVGDIIAEPLR-IHgLASkaeRRERVAELLElvGLRP--EHADRYpheFSGGQRQRIGIARALALNPKLIVC-DEP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 494 TAHLDieteVDLKKQMLPLME---NRL---VIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:COG4608 185 VSALD----VSIQAQVLNLLEdlqDELgltYLFISHDLSVVRHIsDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
330-524 |
1.48e-19 |
|
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: 86.05 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNY-NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIdgqkaatlnipAWHQQMLYI 408
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 409 PQNPYVFTASLRENIAFytpeasdaeimkaihvvsldelvselPEGldtiigqgkRVLSGGQAQRIALARAFLDKTRKVM 488
Cdd:cd03223 70 PQRPYLPLGTLREQLIY--------------------------PWD---------DVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*...
gi 543385153 489 LfDEPTAHLDIETEvdlkKQMLPLMENRL--VIFATHR 524
Cdd:cd03223 115 L-DEATSALDEESE----DRLYQLLKELGitVISVGHR 147
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
360-540 |
2.48e-19 |
|
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: 87.00 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 360 IIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQ----MLYIPQNPYVFTASLRENIAFYTPeaSDAEI 435
Cdd:cd03290 32 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVEENITFGSP--FNKQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 436 MKA-IHVVSLDELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRKVMLfDEPTAHLDIETEVDLKKQ-MLPLM 513
Cdd:cd03290 110 YKAvTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL-DDPFSALDIHLSDHLMQEgILKFL 188
|
170 180
....*....|....*....|....*....
gi 543385153 514 EN--RLVIFATHRLHWLKEMDYILVMHEG 540
Cdd:cd03290 189 QDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
330-554 |
2.62e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.22 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE------IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATL-NIPAWH 402
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQNP--YVFTASLRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPEgldtiigqgkrVLSGGQAQRI 474
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFgpenlgIPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 475 ALArAFLDKTRKVMLFDEPTAHLD-------IETEVDLKKQmlplmENRLVIFATHRLHWLKEMDYILVMHEGKLVQQGT 547
Cdd:PRK13633 154 AIA-GILAMRPECIIFDEPTAMLDpsgrrevVNTIKELNKK-----YGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
....*..
gi 543385153 548 FDELTKE 554
Cdd:PRK13633 228 PKEIFKE 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
347-544 |
2.91e-19 |
|
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: 87.10 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 347 PVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN------IPAWH-----QQMLYIPQnpyvF 415
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararLRARHvgfvfQSFQLLPT----L 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 416 TAslRENIAFYTPEASDAEIMK----AIHVVSLDELVSELPegldtiigqgkRVLSGGQAQRIALARAFLdkTRKVMLF- 490
Cdd:COG4181 106 TA--LENVMLPLELAGRRDARAraraLLERVGLGHRLDHYP-----------AQLSGGEQQRVALARAFA--TEPAILFa 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 491 DEPTAHLDIETevdlKKQMLPLME--NR-----LVIfATHRLHWLKEMDYILVMHEGKLVQ 544
Cdd:COG4181 171 DEPTGNLDAAT----GEQIIDLLFelNRergttLVL-VTHDPALAARCDRVLRLRAGRLVE 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
348-554 |
6.44e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQK--------AATLNIPAWHQQMLYIPQnpyvftASL 419
Cdd:COG1129 23 VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvrfrsprdAQAAGIAIIHQELNLVPN------LSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 420 RENIAFYTP--------------EAsdAEIMKAIHV-VSLDELVSELpegldtiigqgkrvlSGGQAQRIALARAfLDKT 484
Cdd:COG1129 97 AENIFLGREprrgglidwramrrRA--RELLARLGLdIDPDTPVGDL---------------SVAQQQLVEIARA-LSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 485 RKVMLFDEPTAHLDiETEVD--------LKKQmlplmeNRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDELTKE 554
Cdd:COG1129 159 ARVLILDEPTASLT-EREVErlfriirrLKAQ------GVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAELTED 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
340-523 |
6.54e-19 |
|
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: 85.54 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 340 NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN---IPAWHQQMLYIPQ-NPYVF 415
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKIGVVFQdFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 416 TASLRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPEGldtiigqgkrvLSGGQAQRIALARAFLDKTrKVML 489
Cdd:cd03292 92 DRNVYENVAFalevtgVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSP-TILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 543385153 490 FDEPTAHLDIETE---VDLKKQMlplmeNRL---VIFATH 523
Cdd:cd03292 160 ADEPTGNLDPDTTweiMNLLKKI-----NKAgttVVVATH 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
328-551 |
6.79e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.34 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 328 SELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTL---INLL----SGFLppKSGKIIIDGQKAATLN--- 397
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLeqpeAGTI--RVGDITIDTARSLSQQkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 398 IPAWHQQMLYIPQNPYVFT-ASLRENI----AFYTPEASDAEIMKAihvvslDELVSELpeGLdtiigQGK-----RVLS 467
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPhRTVLENIiegpVIVKGEPKEEATARA------RELLAKV--GL-----AGKetsypRRLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 468 GGQAQRIALARAfLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQ 545
Cdd:PRK11264 147 GGQQQRVAIARA-LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQ 225
|
....*.
gi 543385153 546 GTFDEL 551
Cdd:PRK11264 226 GPAKAL 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
332-501 |
6.82e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 332 LENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKaatlnipawhqQMLYIPQN 411
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 412 PYVF-TASLRENIafytpEASDAEIMKAIHvvSLDELVSELPEGLDTIIGQGK--------------------------- 463
Cdd:COG0488 70 PPLDdDLTVLDTV-----LDGDAELRALEA--ELEELEAKLAEPDEDLERLAElqeefealggweaearaeeilsglgfp 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 543385153 464 --------RVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIET 501
Cdd:COG0488 143 eedldrpvSELSGGWRRRVALARALLSEP-DLLLLDEPTNHLDLES 187
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
348-551 |
7.27e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.83 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN---IPAWHQQMLYIPQNPYVF---TAslRE 421
Cdd:COG1135 24 VSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAARRKIGMIFQHFNLLssrTV--AE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 422 NIAFytP----EASDAEIMKaiHVVSLDELVselpeGLdtiigQGKRV-----LSGGQAQRIALARAfLdKTR-KVMLFD 491
Cdd:COG1135 102 NVAL--PleiaGVPKAEIRK--RVAELLELV-----GL-----SDKADaypsqLSGGQKQRVGIARA-L-ANNpKVLLCD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 492 EPTAHLDIETevdlKKQMLPLMEN---RL---VIFATHrlhwlkEMDYI-------LVMHEGKLVQQGTFDEL 551
Cdd:COG1135 166 EATSALDPET----TRSILDLLKDinrELgltIVLITH------EMDVVrricdrvAVLENGRIVEQGPVLDV 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
348-546 |
8.08e-19 |
|
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: 85.40 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPP---KSGKIIIDGQKaatLNIPAWHQQMLYIPQNPY-VFTASLRENI 423
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP---RKPDQFQKCVAYVRQDDIlLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 424 AFYTP-----EASDAEIMKAIHVVSLDELVselpeglDTIIGqGKRV--LSGGQAQRIALARAFLdKTRKVMLFDEPTAH 496
Cdd:cd03234 103 TYTAIlrlprKSSDAIRKKRVEDVLLRDLA-------LTRIG-GNLVkgISGGERRRVSIAVQLL-WDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 497 LD-------IETEVDLKKqmlplmENRLVIFATH--RLHWLKEMDYILVMHEGKLVQQG 546
Cdd:cd03234 174 LDsftalnlVSTLSQLAR------RNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
348-523 |
1.16e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.54 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAwhqQMLYI-PQNPYVFTASLRENIAFY 426
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE---ACHYLgHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 427 --TPEASDAEIMKAIHVVSLDeLVSELPEGldtiigqgkrVLSGGQAQRIALARaFLDKTRKVMLFDEPTAHLDIETevd 504
Cdd:PRK13539 98 aaFLGGEELDIAAALEAVGLA-PLAHLPFG----------YLSAGQKRRVALAR-LLVSNRPIWILDEPTAALDAAA--- 162
|
170 180
....*....|....*....|....
gi 543385153 505 lKKQMLPLMENRL-----VIFATH 523
Cdd:PRK13539 163 -VALFAELIRAHLaqggiVIAATH 185
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
348-551 |
2.06e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.68 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQ-----QMLYipQNPYvftASL--R 420
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsdiQMIF--QDPL---ASLnpR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 421 ENIA--------FYTPEASDAEIMKAIHVVSLDelVSELPEgldtIIGQGKRVLSGGQAQRIALARAFLDKTrKVMLFDE 492
Cdd:PRK15079 115 MTIGeiiaeplrTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEP-KLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 493 PTAHLD--IETEV-----DLKKQM-LPLmenrlvIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:PRK15079 188 PVSALDvsIQAQVvnllqQLQREMgLSL------IFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
330-554 |
2.24e-18 |
|
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: 84.02 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaatlNIPAW--HQQ--- 404
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR-----DITGLppHERara 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 -MLYIPQNPYVF-TASLRENI--AFYTPEASDAEImkaihvvSLDELVSELPEgLDTIIGQGKRVLSGGQAQRIALARAF 480
Cdd:cd03224 76 gIGYVPEGRRIFpELTVEENLllGAYARRRAKRKA-------RLERVYELFPR-LKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 481 LDKtRKVMLFDEPTAHL------DIETEV-DLKKQ---MLpLMEnrlvifatHRLHWLKEM-DYILVMHEGKLVQQGTFD 549
Cdd:cd03224 148 MSR-PKLLLLDEPSEGLapkiveEIFEAIrELRDEgvtIL-LVE--------QNARFALEIaDRAYVLERGRVVLEGTAA 217
|
....*
gi 543385153 550 ELTKE 554
Cdd:cd03224 218 ELLAD 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
342-554 |
2.51e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.60 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 342 QTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLpPKSGKIIIDGQKAATLNIPAWHQQMLYIPQN-PYVFTASLR 420
Cdd:PRK03695 9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 421 ENIAFYTPE-ASDAEIMKAIHVVSldELVsELPEGLDTIIGQgkrvLSGGQAQRIALARAFLDKTR------KVMLFDEP 493
Cdd:PRK03695 88 QYLTLHQPDkTRTEAVASALNEVA--EAL-GLDDKLGRSVNQ----LSGGEWQRVRLAAVVLQVWPdinpagQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543385153 494 TAHLDIETEVDLkKQMLPLM--ENRLVIFATHRL-HWLKEMDYILVMHEGKLVQQGTFDELTKE 554
Cdd:PRK03695 161 MNSLDVAQQAAL-DRLLSELcqQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
348-551 |
2.52e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 88.20 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTL----INLLsgflpPKSGKIIIDGQKAATLNIPAW-----HQQMLYipQNPYvftAS 418
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALrplrrRMQVVF--QDPF---GS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 419 L----------RENIAFYTPEASDAE----IMKAIHVVSLDelvselPEGLDtiigqgkRV---LSGGQAQRIALARAFL 481
Cdd:COG4172 375 LsprmtvgqiiAEGLRVHGPGLSAAErrarVAEALEEVGLD------PAARH-------RYpheFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 482 DKTRKVMLfDEPTAHLDieteVDLKKQMLPLM-----ENRLV-IFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:COG4172 442 LEPKLLVL-DEPTSALD----VSVQAQILDLLrdlqrEHGLAyLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQV 513
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
346-555 |
2.97e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.51 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 346 GPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKsGKIIIDGQKAATLNIPAWHQQMLYIPQN-PYVFTASLRENIA 424
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 425 FYTP-EASDAEIMKAIHVVSlDELvsELPEGLDTIIGQgkrvLSGGQAQRIALARAFL------DKTRKVMLFDEPTAHL 497
Cdd:COG4138 92 LHQPaGASSEAVEQLLAQLA-EAL--GLEDKLSRPLTQ----LSGGEWQRVRLAAVLLqvwptiNPEGQLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 498 DIETEVDLKKQmlpLME----NRLVIFATHRL-HWLKEMDYILVMHEGKLVQQGTFDELTKEA 555
Cdd:COG4138 165 DVAQQAALDRL---LRElcqqGITVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVMTPE 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
348-551 |
4.51e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.60 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAatlNIPAWH------------QQMLYIPQnpyvF 415
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV---NDPKVDerlirqeagmvfQQFYLFPH----L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 416 TAslRENIAF---YTPEASDAEimkaihvvsldelVSELPEGLDTIIGQGKRV------LSGGQAQRIALARAFLDKTrK 486
Cdd:PRK09493 93 TA--LENVMFgplRVRGASKEE-------------AEKQARELLAKVGLAERAhhypseLSGGQQQRVAIARALAVKP-K 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 487 VMLFDEPTAHLDIEtevdLKKQMLPLM-----ENRLVIFATHRLHWLKEMDYILV-MHEGKLVQQGTFDEL 551
Cdd:PRK09493 157 LMLFDEPTSALDPE----LRHEVLKVMqdlaeEGMTMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVL 223
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
359-554 |
6.28e-18 |
|
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: 83.71 E-value: 6.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 359 GIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQ-NPYVFTASLRENIA---------FYTP 428
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVEQdSDTAVPLTVRDVVAlgriphrslWAGD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 429 EASDAEImkAIHVVSLDELVSELPEGLDTiigqgkrvLSGGQAQRIALARAFLDKTRkVMLFDEPTAHLDIETEVDLKKQ 508
Cdd:TIGR03873 111 SPHDAAV--VDRALARTELSHLADRDMST--------LSGGERQRVHVARALAQEPK-LLLLDEPTNHLDVRAQLETLAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 543385153 509 MLPLMENRL-VIFATHRL-HWLKEMDYILVMHEGKLVQQGTFDE-LTKE 554
Cdd:TIGR03873 180 VRELAATGVtVVAALHDLnLAASYCDHVVVLDGGRVVAAGPPREvLTPA 228
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
21-266 |
7.07e-18 |
|
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: 83.85 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 21 VLEVLQAFLIIGQALSLSAVLTTLWQGKKLNWQ----YLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIF 96
Cdd:pfam00664 6 LLAILSGAISPAFPLVLGRILDVLLPDGDPETQalnvYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 97 KSGQSLVQSQGTGSLITMALYGIDEVRDYIKLIYTKVLAMMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYAA 176
Cdd:pfam00664 86 RQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 177 KDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVY 256
Cdd:pfam00664 166 RKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWF 245
|
250
....*....|
gi 543385153 257 LGFGLLNGQL 266
Cdd:pfam00664 246 GAYLVISGEL 255
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
330-546 |
9.40e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 81.88 E-value: 9.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKaATLNIPAWhQQMLYIP 409
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEAL-RRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVFTA-SLRENIAFYT--PEASDAEIMKAIHVVsldelvselpeGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRK 486
Cdd:cd03268 79 EAPGFYPNlTARENLRLLArlLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543385153 487 VMLfDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQG 546
Cdd:cd03268 148 LIL-DEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
330-554 |
1.01e-17 |
|
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: 82.83 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGK-IIIDGQKAATLNIPAWHQQM--- 405
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIglv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 -----LYIPQNPYV-------FTASlrenIAFYtPEASDAEIMKAihvvslDELVSELpeGLDTIIGQGKRVLSGGQAQR 473
Cdd:COG1119 84 spalqLRFPRDETVldvvlsgFFDS----IGLY-REPTDEQRERA------RELLELL--GLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 474 IALARAFLdKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRL--VIFATHRLH-WLKEMDYILVMHEGKLVQQGTFDE 550
Cdd:COG1119 151 VLIARALV-KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAptLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKEE 229
|
....*
gi 543385153 551 -LTKE 554
Cdd:COG1119 230 vLTSE 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
348-550 |
1.17e-17 |
|
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: 82.78 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLniPAwHQqmlyIP--------QNPYVFTA-S 418
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL--PP-HR----IArlgiartfQNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 419 LRENIA---------------FYTP------EASDAEIMKAIHVVSLDELVSELPegldtiigqgkRVLSGGQAQRIALA 477
Cdd:COG0411 96 VLENVLvaaharlgrgllaalLRLPrarreeREARERAEELLERVGLADRADEPA-----------GNLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 478 RAFLdkTR-KVMLFDEPTAHLDI-ETE--VDLKKQmLPLMENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDE 550
Cdd:COG0411 165 RALA--TEpKLLLLDEPAAGLNPeETEelAELIRR-LRDERGITILLIEHDMDLVMGLaDRIVVLDFGRVIAEGTPAE 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-551 |
1.26e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.65 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 327 KSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGF--LPPK---SGKIIIDGQKAATLNIPAW 401
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 402 HQ--QMLYIPQNPyVFTASLRENIAFYTP----EASDAEIMKAIH-VVSLDELVSELPEGLDTIIGQgkrvLSGGQAQRI 474
Cdd:PRK14247 81 RRrvQMVFQIPNP-IPNLSIFENVALGLKlnrlVKSKKELQERVRwALEKAQLWDEVKDRLDAPAGK----LSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 475 ALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:PRK14247 156 CIARALAFQP-EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
348-546 |
1.43e-17 |
|
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: 81.65 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAwHQQMLYIPQNPYVFT-ASLRENIAFY 426
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRLGFVSDSTGLYDrLTARENLEYF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 427 TpeasdaeimkAIHVVSLDEL---VSELPEGLDTIIGQGKRV--LSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIET 501
Cdd:cd03266 103 A----------GLYGLKGDELtarLEELADRLGMEELLDRRVggFSTGMRQKVAIARALVHDP-PVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 543385153 502 EVDLKKQMLPLME-NRLVIFATHRLHWLKEM-DYILVMHEGKLVQQG 546
Cdd:cd03266 172 TRALREFIRQLRAlGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
296-555 |
1.73e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 296 LNGKNAFKRINELISRPMqaSADLAIEPWNSK-SELKLENLEFNYNNQT-EIGPVSVEIKGYEKVGIIGMSGSGKSTLIN 373
Cdd:PRK10522 290 LSAQVAFNKLNKLALAPY--KAEFPRPQAFPDwQTLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 374 LLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPYVFTASLreniafyTPEASDAEimkaihvvslDELVSELPE 453
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL-------GPEGKPAN----------PALVEKWLE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 454 GL---DTIIGQGKRV----LSGGQAQRIALARAFLDKtRKVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFA-THR 524
Cdd:PRK10522 431 RLkmaHKLELEDGRIsnlkLSKGQKKRLALLLALAEE-RDILLLDEWAADQDPHFRREFYQVLLPLLqEMGKTIFAiSHD 509
|
250 260 270
....*....|....*....|....*....|.
gi 543385153 525 LHWLKEMDYILVMHEGKLVqqgtfdELTKEA 555
Cdd:PRK10522 510 DHYFIHADRLLEMRNGQLS------ELTGEE 534
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
330-541 |
2.59e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.64 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDgqkaATLNIPawhqqmlYIP 409
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIG-------YFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QnpyvftaslreniafytpeasdaeimkaihvvsldelvselpegldtiigqgkrvLSGGQAQRIALARAFLDKTrKVML 489
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENP-NLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 543385153 490 FDEPTAHLDIETeVDLKKQMLpLMENRLVIFATHRLHWLKEM-DYILVMHEGK 541
Cdd:cd03221 94 LDEPTNHLDLES-IEALEEAL-KEYPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
325-547 |
6.15e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.24 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 325 NSKSELKLENLEFNY---NNQTEI-GPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPA 400
Cdd:PRK11629 1 MNKILLQCDNLCKRYqegSVQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 401 ----WHQQMLYIPQNPYV---FTAslRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPEGldtiigqgkrvLS 467
Cdd:PRK11629 81 kaelRNQKLGFIYQFHHLlpdFTA--LENVAMplligkKKPAEINSRALEMLAAVGLEHRANHRPSE-----------LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 468 GGQAQRIALARAFLDKTRKVmLFDEPTAHLDIETeVDLKKQMLPLMENR-----LVIfaTHRLHWLKEMDYILVMHEGKL 542
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLV-LADEPTGNLDARN-ADSIFQLLGELNRLqgtafLVV--THDLQLAKRMSRQLEMRDGRL 223
|
....*
gi 543385153 543 VQQGT 547
Cdd:PRK11629 224 TAELS 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
330-551 |
6.32e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 6.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQML-YI 408
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIgYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 409 PQNPYVF-----------TASLRENIAFYTPEASDAEIMKAIHVVSLDElvselpegldtIIGQGkrvLSGGQAQRIALA 477
Cdd:PRK10895 84 PQEASIFrrlsvydnlmaVLQIRDDLSAEQREDRANELMEEFHIEHLRD-----------SMGQS---LSGGERRRVEIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 478 RAfLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHrlHWLKEM----DYILVMHEGKLVQQGTFDEL 551
Cdd:PRK10895 150 RA-LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITD--HNVRETlavcERAYIVSQGHLIAHGTPTEI 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
347-547 |
6.60e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.16 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 347 PVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIP---AWHQQMLYIPQNPY------VFta 417
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrKARRQIGMIFQHFNllssrtVF-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 418 slrENIAFytP-EA---SDAEIMKaiHVVSLDELVsELPEGLDTIIGQgkrvLSGGQAQRIALARAfLDKTRKVMLFDEP 493
Cdd:PRK11153 101 ---DNVAL--PlELagtPKAEIKA--RVTELLELV-GLSDKADRYPAQ----LSGGQKQRVAIARA-LASNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 494 TAHLDIETevdlKKQMLPLME--NRL----VIFATHrlhwlkEMDYI-------LVMHEGKLVQQGT 547
Cdd:PRK11153 168 TSALDPAT----TRSILELLKdiNRElgltIVLITH------EMDVVkricdrvAVIDAGRLVEQGT 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
351-500 |
7.67e-17 |
|
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: 80.14 E-value: 7.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 351 EIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAAtlnipawhqqmlYIPQnpYV---FTASLRENIA--- 424
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------------YKPQ--YIkadYEGTVRDLLSsit 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 425 --FYTPEASDAEIMKaihvvsldelvselPEGLDTIIGQGKRVLSGGQAQRIALArAFLDKTRKVMLFDEPTAHLDIE 500
Cdd:cd03237 87 kdFYTHPYFKTEIAK--------------PLQIEQILDREVPELSGGELQRVAIA-ACLSKDADIYLLDEPSAYLDVE 149
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
348-554 |
1.18e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.93 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIII--------------DGQKAATLNIPAWHQQMLYIPQNPY 413
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpDGRGRAKRYIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 414 VftASLRENIAFYTPEasDAEIMKAIHVVSL-----DELVSELPEGLDTiigqgkrvLSGGQAQRIALARAFLDKTRKVM 488
Cdd:TIGR03269 383 L--DNLTEAIGLELPD--ELARMKAVITLKMvgfdeEKAEEILDKYPDE--------LSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 489 LfDEPTAHLDIETEVDLKKQMLPLME--NRLVIFATHrlhwlkEMDYIL-------VMHEGKLVQQGTFDELTKE 554
Cdd:TIGR03269 451 L-DEPTGTMDPITKVDVTHSILKAREemEQTFIIVSH------DMDFVLdvcdraaLMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
332-564 |
1.21e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.44 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 332 LENLEFNYNNQT-----EIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKaatlnIPA------ 400
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYA-----IPAnlkkik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 401 ----WHQQMLYIPQNP--YVFTASLRENIAFytpeasdaeimKAIHV-VSLDELVSELPEGLDTI------IGQGKRVLS 467
Cdd:PRK13645 84 evkrLRKEIGLVFQFPeyQLFQETIEKDIAF-----------GPVNLgENKQEAYKKVPELLKLVqlpedyVKRSPFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 468 GGQAQRIALArAFLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMEN--RLVIFATHRL-HWLKEMDYILVMHEGKLVQ 544
Cdd:PRK13645 153 GGQKRRVALA-GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMdQVLRIADEVIVMHEGKVIS 231
|
250 260
....*....|....*....|
gi 543385153 545 QGTFDELTKEAGYFTKLTQE 564
Cdd:PRK13645 232 IGSPFEIFSNQELLTKIEID 251
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
348-554 |
1.68e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.28 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNipAWHQQMLYIPQNPYVFT-ASLRENIAF- 425
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH--ARDRKVGFVFQHYALFRhMTVFDNIAFg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 426 ---------YTPEASDAEIMKAIHVVSLDELVSELPEGldtiigqgkrvLSGGQAQRIALARAfLDKTRKVMLFDEPTAH 496
Cdd:PRK10851 99 ltvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVALARA-LAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 497 LDIETEVDLKKQMLPLMENR--LVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDELTKE 554
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQVWRE 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
330-547 |
2.19e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.28 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE-----IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKI----IIDGQKAATLNIPA 400
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 401 WHQQ------------MLYIPQNP--YVFTASLRENIAFyTPEA-----SDAEIMKAIHVVSLdelvselpeGLD-TIIG 460
Cdd:PRK13631 102 NPYSkkiknfkelrrrVSMVFQFPeyQLFKDTIEKDIMF-GPVAlgvkkSEAKKLAKFYLNKM---------GLDdSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 461 QGKRVLSGGQAQRIALArAFLDKTRKVMLFDEPTAHLDIETEvdlkKQMLPLM-----ENRLVIFATHRL-HWLKEMDYI 534
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIA-GILAIQPEILIFDEPTAGLDPKGE----HEMMQLIldakaNNKTVFVITHTMeHVLEVADEV 246
|
250
....*....|...
gi 543385153 535 LVMHEGKLVQQGT 547
Cdd:PRK13631 247 IVMDKGKILKTGT 259
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
325-555 |
2.20e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.41 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 325 NSKSELKLENLEFNYNNQT--EIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWH 402
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQNP-YVFTASL-RENIAFYTPEasdaeimkaiHVVSLDELVSELPEGLDTIIGQGKR-----VLSGGQAQRIA 475
Cdd:PRK13648 83 KHIGIVFQNPdNQFVGSIvKYDVAFGLEN----------HAVPYDEMHRRVSEALKQVDMLERAdyepnALSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 476 LArAFLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLV--IFATHRLHWLKEMDYILVMHEGKLVQQGTFDELTK 553
Cdd:PRK13648 153 IA-GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItiISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
..
gi 543385153 554 EA 555
Cdd:PRK13648 232 HA 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
330-563 |
2.27e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.28 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ--KAATLNIPAWHQQMLY 407
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNP--YVFTASLRENIAFYTPEASDAEimkaihvvslDELVSELPEGLDTIIGQGKR-----VLSGGQAQRIALARAF 480
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPE----------AEITRRVDEALTLVDAQHFRhqpiqCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 481 LDKTRkVMLFDEPTAHLDIETevdlKKQMLPLM-----ENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQG------TF 548
Cdd:PRK13638 152 VLQAR-YLLLDEPTAGLDPAG----RTQMIAIIrrivaQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGapgevfAC 226
|
250
....*....|....*
gi 543385153 549 DELTKEAGyftkLTQ 563
Cdd:PRK13638 227 TEAMEQAG----LTQ 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
333-551 |
2.37e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 78.18 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 333 ENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAA--TLNIpawHQQMLYIPQ 410
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVrePREV---RRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 411 NPYV---FTAslRENIafytpeasdaEIMKAIHVVS---LDELVSELPEGLDTIIGQGKRV--LSGGQAQRIALARAFLd 482
Cdd:cd03265 81 DLSVddeLTG--WENL----------YIHARLYGVPgaeRRERIDELLDFVGLLEAADRLVktYSGGMRRRLEIARSLV- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543385153 483 KTRKVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFAThrLHWLKEM----DYILVMHEGKLVQQGTFDEL 551
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeEFGMTILLT--THYMEEAeqlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
330-525 |
2.45e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYIP 409
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYV-FTASLRENIAF-YTP---------EASDAEIMKAIHVVSLDELVSelpegldtiigQGKRVLSGGQAQRIALAR 478
Cdd:PRK09536 84 QDTSLsFEFDVRQVVEMgRTPhrsrfdtwtETDRAAVERAMERTGVAQFAD-----------RPVTSLSGGERQRVLLAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 543385153 479 AFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMEN-RLVIFATHRL 525
Cdd:PRK09536 153 ALAQAT-PVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDL 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
360-555 |
3.26e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 360 IIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLY-IPQNPYVF-TASLRENIAFYTPEASDAEimk 437
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYlVPQEPLLFpNLSVKENILFGLPKRQASM--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 438 aihvVSLDELVSELPEGLDTIIGQGkrVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLD-IETEvDLKKQMLPLMENR 516
Cdd:PRK15439 119 ----QKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLM-RDSRILILDEPTASLTpAETE-RLFSRIRELLAQG 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 543385153 517 L-VIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDELTKEA 555
Cdd:PRK15439 191 VgIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADLSTDD 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
330-554 |
3.81e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.23 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEF-NYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQ-MLY 407
Cdd:COG3845 258 LEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IPQNPY----VFTASLRENIA---FYTPEASDAEIM--KAIHVVSlDELVSEL---PEGLDTIIGQgkrvLSGGQAQRIA 475
Cdd:COG3845 338 IPEDRLgrglVPDMSVAENLIlgrYRRPPFSRGGFLdrKAIRAFA-EELIEEFdvrTPGPDTPARS----LSGGNQQKVI 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 476 LARAfLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRL-VIFATHRLHWLKEM-DYILVMHEGKLVqqGTFD--EL 551
Cdd:COG3845 413 LARE-LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAaVLLISEDLDEILALsDRIAVMYEGRIV--GEVPaaEA 489
|
...
gi 543385153 552 TKE 554
Cdd:COG3845 490 TRE 492
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
330-546 |
1.01e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 76.17 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAAtlniPAWHQQMLYIP 409
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 -----------QNPYVFTASLREniafYTPEASDAEIMKAIHVVSLDELvselpegldtiigQGKRV--LSGGQAQRIAL 476
Cdd:cd03269 77 eerglypkmkvIDQLVYLAQLKG----LKKEEARRRIDEWLERLELSEY-------------ANKRVeeLSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 477 ARAFLDKTrKVMLFDEPTAHLD-IETEVdLKKQMLPLMEN-RLVIFATHRLHWLKEM-DYILVMHEGKLVQQG 546
Cdd:cd03269 140 IAAVIHDP-ELLILDEPFSGLDpVNVEL-LKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
342-544 |
1.04e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 342 QTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQ-----QMlyipqnpyVFT 416
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQM--------VFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 417 ASLRENIAFYTPEASDAEIMKaiHVVSLDEL-----VSEL-------PEGLDTIIGQgkrvLSGGQAQRIALARAfLDKT 484
Cdd:PRK10419 97 DSISAVNPRKTVREIIREPLR--HLLSLDKAerlarASEMlravdldDSVLDKRPPQ----LSGGQLQRVCLARA-LAVE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 485 RKVMLFDEPTAHLDIEtevdLKKQMLPLMEnRL-------VIFATHRLHWLKEM-DYILVMHEGKLVQ 544
Cdd:PRK10419 170 PKLLILDEAVSNLDLV----LQAGVIRLLK-KLqqqfgtaCLFITHDLRLVERFcQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
329-555 |
1.09e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.75 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 329 ELKLENLEFNYNNQT-----EIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKI-----IIDGQKAATlNI 398
Cdd:PRK13634 2 DITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigerVITAGKKNK-KL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 399 PAWHQQMLYIPQNP--YVFTASLRENIAF------YTPEASDAEIMKAIHVVSLDELVSElpegldtiigQGKRVLSGGQ 470
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETVEKDICFgpmnfgVSEEDAKQKAREMIELVGLPEELLA----------RSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 471 AQRIALArAFLDKTRKVMLFDEPTAHLDIETevdlKKQMLPLME------NRLVIFATHRLH-WLKEMDYILVMHEGKLV 543
Cdd:PRK13634 151 MRRVAIA-GVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSMEdAARYADQIVVMHKGTVF 225
|
250
....*....|..
gi 543385153 544 QQGTFDELTKEA 555
Cdd:PRK13634 226 LQGTPREIFADP 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-543 |
1.55e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.66 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLE--FNYNNQTEI----GpVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaatlNIPAW-- 401
Cdd:COG1101 2 LELKNLSktFNPGTVNEKraldG-LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-----DVTKLpe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 402 HQQMLYIP---QNPYVFTA---SLRENIAF-----------YTPEASDAEIMKaihvvsldELVSELPEGL----DTIIG 460
Cdd:COG1101 76 YKRAKYIGrvfQDPMMGTApsmTIEENLALayrrgkrrglrRGLTKKRRELFR--------ELLATLGLGLenrlDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 461 QgkrvLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIET--EV-DLKKQMLPlmENRL-VIFATHRL-HWLKEMDYIL 535
Cdd:COG1101 148 L----LSGGQRQALSLLMATLTKP-KLLLLDEHTAALDPKTaaLVlELTEKIVE--ENNLtTLMVTHNMeQALDYGNRLI 220
|
....*...
gi 543385153 536 VMHEGKLV 543
Cdd:COG1101 221 MMHEGRII 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
330-533 |
2.04e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.99 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATlNIPAWHQQMLYIP 409
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 Q----NPYVftaSLRENIAFYTPEASDA-EIMKAIHVVSLDELVsELPEGLdtiigqgkrvLSGGQAQRIALARAFLDKT 484
Cdd:PRK13540 81 HrsgiNPYL---TLRENCLYDIHFSPGAvGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 543385153 485 rKVMLFDEPTAHLDietEVDLKKQMLPLMENR----LVIFATHRLHWLKEMDY 533
Cdd:PRK13540 147 -KLWLLDEPLVALD---ELSLLTIITKIQEHRakggAVLLTSHQDLPLNKADY 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
330-555 |
2.24e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLefnyNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIP-AWHQQMLYI 408
Cdd:COG1129 257 LEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 409 P----QNPYVFTASLRENIAFytpeASDAEIMKAIhVVSL-------DELVSEL---PEGLDTIIGQgkrvLSGGQAQRI 474
Cdd:COG1129 333 PedrkGEGLVLDLSIRENITL----ASLDRLSRGG-LLDRrreralaEEYIKRLrikTPSPEQPVGN----LSGGNQQKV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 475 ALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMlplmeNRL------VIFATHRLHWLKEM-DYILVMHEGKLVqqGT 547
Cdd:COG1129 404 VLAKWLATDP-KVLILDEPTRGIDVGAKAEIYRLI-----RELaaegkaVIVISSELPELLGLsDRILVMREGRIV--GE 475
|
250
....*....|
gi 543385153 548 F--DELTKEA 555
Cdd:COG1129 476 LdrEEATEEA 485
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
348-546 |
3.06e-15 |
|
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: 74.51 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPP--KSGKIIIDGQKaatLNIPAWHQQMLYIPQNPYVF-TASLRENIA 424
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRP---LDKRSFRKIIGYVPQDDILHpTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 425 FytpeasDAEImkaihvvsldelvselpegldtiigqgkRVLSGGQAQRIALARAFLDKTRkVMLFDEPTAHLDIETEVD 504
Cdd:cd03213 105 F------AAKL----------------------------RGLSGGERKRVSIALELVSNPS-LLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 543385153 505 LkkqMLPLM----ENRLVIFATHRLHWL--KEMDYILVMHEGKLVQQG 546
Cdd:cd03213 150 V---MSLLRrladTGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-551 |
3.47e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.84 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKS-----GKIIIDGQK--AATLNIPAWH 402
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNiyERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQNPYVFTASLRENIAFytpeasDAEIMKAIHVVSLDELV------SELPEGLDTIIGQGKRVLSGGQAQRIAL 476
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAY------GVKIVGWRPKLEIDDIVesalkdADLWDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 477 ARAFLDKTrKVMLFDEPTAHLDIETEVDLKK--QMLPLMENRLVIFATHRLHWLKEM-DYILVMHE-----GKLVQQGTF 548
Cdd:PRK14258 162 ARALAVKP-KVLLMDEPCFGLDPIASMKVESliQSLRLRSELTMVIVSHNLHQVSRLsDFTAFFKGnenriGQLVEFGLT 240
|
...
gi 543385153 549 DEL 551
Cdd:PRK14258 241 KKI 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
348-545 |
3.83e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 75.61 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN---IPAWHQQMLYIPQNPY-------VFTA 417
Cdd:TIGR02769 30 VSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDSPsavnprmTVRQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 418 SLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGLdtiigqgKRVLSGGQAQRIALARAfLDKTRKVMLFDEPTAHL 497
Cdd:TIGR02769 110 IIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKL-------PRQLSGGQLQRINIARA-LAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 543385153 498 DIETEVDLKKQMLPLME--NRLVIFATHRLHWLKEM-DYILVMHEGKLVQQ 545
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEE 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
348-551 |
4.89e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 75.22 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTL---INLLSgflPPKSGKIIIDGQKAAT------LNIPAWHQQMLYIPQN-PYVFTA 417
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFlrcINLLE---TPDSGEIRVGGEEIRLkpdrdgELVPADRRQLQRIRTRlGMVFQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 418 -------SLRENIafytpeasdaeiMKA-IHV--VSLDELVSELPEGLDTIIGQGKR-----VLSGGQAQRIALARAfLD 482
Cdd:COG4598 104 fnlwshmTVLENV------------IEApVHVlgRPKAEAIERAEALLAKVGLADKRdaypaHLSGGQQQRAAIARA-LA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 483 KTRKVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHrlhwlkEMDY-------ILVMHEGKLVQQGTFDEL 551
Cdd:COG4598 171 MEPEVMLFDEPTSALDPELVGEVLKVMRDLAeEGRTMLVVTH------EMGFardvsshVVFLHQGRIEEQGPPAEV 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
348-547 |
5.72e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.16 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQ-----QMLYipQNPYvftASL--R 420
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLlrqkiQIVF--QNPY---GSLnpR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 421 ENIAFYTPEA-------SDAEimKAIHVVSLDELVSELPEgldtiigQGKR---VLSGGQAQRIALARAF-LDKtrKVML 489
Cdd:PRK11308 109 KKVGQILEEPllintslSAAE--RREKALAMMAKVGLRPE-------HYDRyphMFSGGQRQRIAIARALmLDP--DVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 490 FDEPTAHLDieteVDLKKQMLPLM-----ENRLV-IFATHRLHWLKEM-DYILVMHEGKLVQQGT 547
Cdd:PRK11308 178 ADEPVSALD----VSVQAQVLNLMmdlqqELGLSyVFISHDLSVVEHIaDEVMVMYLGRCVEKGT 238
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
330-551 |
5.83e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.50 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE-IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ-----KAATLNIpawHQ 403
Cdd:PRK13639 2 LETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydKKSLLEV---RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 404 QMLYIPQNP--YVFTASLRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPEGldtiigqgkrvLSGGQAQRIA 475
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFgplnlgLSKEEVEKRVKEALKAVGMEGFENKPPHH-----------LSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 476 LArAFLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRL-VIFATHRLHWL-KEMDYILVMHEGKLVQQGTFDEL 551
Cdd:PRK13639 148 IA-GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGItIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
330-551 |
6.41e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE-IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKA--ATLNIPAWHQQML 406
Cdd:PRK13636 6 LKVEELNYNYSDGTHaLKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 407 YIPQNP--YVFTASLRENIAF--YTPEASDAEIMKAIHVVSLDELVSELPEgldtiigQGKRVLSGGQAQRIALArAFLD 482
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDVSFgaVNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIA-GVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 483 KTRKVMLFDEPTAHLD---IETEVDLKKQMLPLMENRLVIfATHRLHWLK-EMDYILVMHEGKLVQQGTFDEL 551
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgVSEIMKLLVEMQKELGLTIII-ATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
360-550 |
7.81e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.07 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 360 IIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ----KAATLNIPAWHQQMLYIPQNPYVFTA-SLRENIAFYTPEASDAE 434
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdAEKGICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 435 IMKAIHVVSLDELVSELPegldtiigqgkRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETevdlKKQMLPLME 514
Cdd:PRK11144 109 FDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAP-ELLLMDEPLASLDLPR----KRELLPYLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 543385153 515 nRL-------VIFATHRL-HWLKEMDYILVMHEGKLVQQGTFDE 550
Cdd:PRK11144 173 -RLareinipILYVSHSLdEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
330-551 |
9.94e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.74 E-value: 9.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGP---VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQML 406
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 407 YIPQNP--YVFTASLRENIAFytpEASDAEIMKAIHVVSLDELVSELpEGLDTIIGQGKRvLSGGQAQRIALArAFLDKT 484
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAF---GMENQGIPREEMIKRVDEALLAV-NMLDFKTREPAR-LSGGQKQRVAVA-GIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 485 RKVMLFDEPTAHLDIETEVDLKKQMLPLME--NRLVIFATHRLHWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
325-551 |
1.05e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.24 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 325 NSKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ-------KAATLN 397
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 398 IPAWHQQMLYIPQNPYVFtaslrENIAFYTPEASDAEIMKA-IHVVSLDElvSELPE---------GLDTIiGQGKRV-- 465
Cdd:PRK10619 81 VADKNQLRLLRTRLTMVF-----QHFNLWSHMTVLENVMEApIQVLGLSK--QEAREravkylakvGIDER-AQGKYPvh 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 466 LSGGQAQRIALARAfLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMEN-RLVIFATHRLHWLKEM-DYILVMHEGKLV 543
Cdd:PRK10619 153 LSGGQQQRVSIARA-LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIE 231
|
....*...
gi 543385153 544 QQGTFDEL 551
Cdd:PRK10619 232 EEGAPEQL 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-559 |
1.06e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 74.76 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKaatlnipawhqqmlyip 409
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 qnpyvFTASLRENIAfYTPE----------------------ASDAEIMKAIHVVsLDELvsELPEGLDtiigqgKRV-- 465
Cdd:COG4152 65 -----LDPEDRRRIG-YLPEerglypkmkvgeqlvylarlkgLSKAEAKRRADEW-LERL--GLGDRAN------KKVee 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 466 LSGGQAQRIALARAFLDKTrKVMLFDEPTAHLD-IETEVdLKKQMLPLMEN-RLVIFATHRLHWLKEM-DYILVMHEGKL 542
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDP-ELLILDEPFSGLDpVNVEL-LKDVIRELAAKgTTVIFSSHQMELVEELcDRIVIINKGRK 207
|
250
....*....|....*..
gi 543385153 543 VQQGTFDELTKEAGYFT 559
Cdd:COG4152 208 VLSGSVDEIRRQFGRNT 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
349-523 |
1.37e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.53 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 349 SVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNiPAWHQQMLYIPQNPYV---FTAslRENIAF 425
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPGIkteLTA--LENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 426 YTP---EASDAEIMKAIHVVSLDElVSELPegldtiigqgKRVLSGGQAQRIALARAFLDKtRKVMLFDEP-TAhLDiet 501
Cdd:PRK13538 98 YQRlhgPGDDEALWEALAQVGLAG-FEDVP----------VRQLSAGQQRRVALARLWLTR-APLWILDEPfTA-ID--- 161
|
170 180 190
....*....|....*....|....*....|.
gi 543385153 502 evdlkKQMLPLMENRL---------VIFATH 523
Cdd:PRK13538 162 -----KQGVARLEALLaqhaeqggmVILTTH 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
325-564 |
1.53e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.53 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 325 NSKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTL---IN----LLSGFlppK-SGKIIIDGQK--AA 394
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLlrcLNrmndLIPGA---RvEGEILLDGEDiyDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 395 TLNIPAWHQQMLYIPQNPYVFTASLRENIAF---YTPEASDAEimkaihvvsLDELVSE------LPE---------GLD 456
Cdd:COG1117 84 DVDVVELRRRVGMVFQKPNPFPKSIYDNVAYglrLHGIKSKSE---------LDEIVEEslrkaaLWDevkdrlkksALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 457 tiigqgkrvLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLD-IETE------VDLKKQMlplmenrLVIFATHRlhwlk 529
Cdd:COG1117 155 ---------LSGGQQQRLCIARALAVEP-EVLLMDEPTSALDpISTAkieeliLELKKDY-------TIVIVTHN----- 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 543385153 530 eM-------DYILVMHEGKLVQQGTFDELtkeagyFT----KLTQE 564
Cdd:COG1117 213 -MqqaarvsDYTAFFYLGELVEFGPTEQI------FTnpkdKRTED 251
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
328-523 |
1.61e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 73.74 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 328 SELKLENLEFNYNNQTEIGP----VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDG------------- 390
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPalqdVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvpvtgpgadrgvv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 391 -QKAATLniPaWhqqmlyipqnpyvftASLRENIAF------YTPEASDAEIMKAIHVVSLDELvselpegldtiigQGK 463
Cdd:COG4525 82 fQKDALL--P-W---------------LNVLDNVAFglrlrgVPKAERRARAEELLALVGLADF-------------ARR 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 464 RV--LSGGQAQRIALARAFLDKTRkVMLFDEPTAHLDIETevdlKKQMLPLM------ENRLVIFATH 523
Cdd:COG4525 131 RIwqLSGGMRQRVGIARALAADPR-FLLMDEPFGALDALT----REQMQELLldvwqrTGKGVFLITH 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
326-551 |
1.80e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.87 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 326 SKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQK---------AATL 396
Cdd:PRK10253 4 SVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 397 NIPAWH---------QQMLYIPQNPY--VFTASLRENiafytpEASDAEIMKAIhvvsldelvselpeGLDTIIGQGKRV 465
Cdd:PRK10253 84 GLLAQNattpgditvQELVARGRYPHqpLFTRWRKED------EEAVTKAMQAT--------------GITHLADQSVDT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 466 LSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFAThRLHWLKE----MDYILVMHEGK 541
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQET-AIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAA-VLHDLNQacryASHLIALREGK 221
|
250
....*....|
gi 543385153 542 LVQQGTFDEL 551
Cdd:PRK10253 222 IVAQGAPKEI 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
348-546 |
2.13e-14 |
|
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: 72.75 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGqkaatlNIPaWHQQMLYIPQNPYVFTAslRENIAFYT 427
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVP-WKRRKKFLRRIGVVFGQ--KTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 428 PEASDAEIMKAIHVVSLDEL---VSELPEGLDT--IIGQGKRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETE 502
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFkkrLDELSELLDLeeLLDTPVRQLSLGQRMRAEIAAALLHEP-EILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 543385153 503 VDLKKQMLPLMENR--LVIFATHRLHWLKEM-DYILVMHEGKLVQQG 546
Cdd:cd03267 190 ENIRNFLKEYNRERgtTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
348-550 |
3.43e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPA-WHQQMlyipqnpyvftaSLRENIAFY 426
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELGAgFHPEL------------TGRENIYLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 427 tpeA-----SDAEIMKAIhvvslDELV--SELPEGLDTIIgqgkRVLSGGQAQRIALA--------------------RA 479
Cdd:COG1134 113 ---GrllglSRKEIDEKF-----DEIVefAELGDFIDQPV----KTYSSGMRARLAFAvatavdpdillvdevlavgdAA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543385153 480 FLDKTRKVMLfdeptahldietevDLKKQmlplmeNRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDE 550
Cdd:COG1134 181 FQKKCLARIR--------------ELRES------GRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEE 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
348-554 |
3.77e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQK--------AATLNIPAWHQQ-MLyIPqnpyVFTAs 418
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrirsprdAIALGIGMVHQHfML-VP----NLTV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 419 lRENIAFYTPEASDAEI-MKAIHvvsldELVSELPE--GL----DTIIGQgkrvLSGGQAQRIALARAFLDKTRkVMLFD 491
Cdd:COG3845 98 -AENIVLGLEPTKGGRLdRKAAR-----ARIRELSEryGLdvdpDAKVED----LSVGEQQRVEILKALYRGAR-ILILD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 492 EPTAHL-DIETEvDLKKQMlplmeNRL------VIFATHRLHWLKEM-DYILVMHEGKLVqqGTFD--ELTKE 554
Cdd:COG3845 167 EPTAVLtPQEAD-ELFEIL-----RRLaaegksIIFITHKLREVMAIaDRVTVLRRGKVV--GTVDtaETSEE 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-551 |
4.35e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.39 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 340 NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIID------GQKAATLNIPAWHQQMLYIPQNPY 413
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 414 VFT-ASLRENIAF--YTPEASDAEIMKAIHVVSLDE--LVSELPEGLDTIIGQgkrvLSGGQAQRIALARAFLDKTrKVM 488
Cdd:PRK14246 101 PFPhLSIYDNIAYplKSHGIKEKREIKKIVEECLRKvgLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKP-KVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543385153 489 LFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEI 239
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
330-551 |
5.97e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 71.55 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNnQTEI--GpVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaATLNIPAW---HQQ 404
Cdd:COG0410 4 LEVENLHAGYG-GIHVlhG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE--DITGLPPHriaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 MLYIPQNPYVFTA-SLREN--IAFYTPeASDAEIMKAIhvvsldELVSEL-PEgLDTIIGQGKRVLSGGQAQRIALARAF 480
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENllLGAYAR-RDRAEVRADL------ERVYELfPR-LKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 481 LdkTR-KVMLFDEPTAHL------DI-ETEVDLKKQMLPlmenrlVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:COG0410 152 M--SRpKLLLLDEPSLGLapliveEIfEIIRRLNREGVT------ILLVEQNARFALEIaDRAYVLERGRIVLEGTAAEL 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
330-547 |
6.12e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLI---NLLSGflpPKSGKIIIDGQKAATLNIPAwHQQML 406
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLrvlNLLEM---PRSGTLNIAGNHFDFSKTPS-DKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 407 YIPQN-PYVFTA-------SLREN-------IAFYTPEASDAEIMKAIHVVSLDELVSELPEGLdtiigqgkrvlSGGQA 471
Cdd:PRK11124 79 ELRRNvGMVFQQynlwphlTVQQNlieapcrVLGLSKDQALARAEKLLERLRLKPYADRFPLHL-----------SGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 472 QRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLV-IFATHRLHWLKEM-DYILVMHEGKLVQQGT 547
Cdd:PRK11124 148 QRVAIARALMMEP-QVLLFDEPTAALDPEITAQIVSIIRELAETGITqVIVTHEVEVARKTaSRVVYMENGHIVEQGD 224
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
340-502 |
6.32e-14 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 74.79 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 340 NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGkiiidgqkaaTLNIPAwHQQMLYIPQNPYVFTASL 419
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG----------RLTKPA-KGKLFYVPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 420 RENIA-------FYTPEASDAEIMKAIHVVSLDELVSElpEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRKVMLfDE 492
Cdd:TIGR00954 532 RDQIIypdssedMKRRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAIL-DE 608
|
170
....*....|
gi 543385153 493 PTAHLDIETE 502
Cdd:TIGR00954 609 CTSAVSVDVE 618
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
350-566 |
6.84e-14 |
|
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: 75.05 E-value: 6.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 350 VEIKGYEK--VGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATlNIPAWHQQMLYIPQNPYVF-TASLRENIAFY 426
Cdd:TIGR01257 949 LNITFYENqiTAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFhHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 427 TPEASDAEIMKAIHVVSLDElvselPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLK 506
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLE-----DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA-KVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 507 KQMLPLMENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGT--FDELTKEAGYFTKLTQEMR 566
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTplFLKNCFGTGFYLTLVRKMK 1164
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
330-555 |
6.85e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.08 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE-IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLYI 408
Cdd:PRK13647 5 IEVEDLHFRYKDGTKaLKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 409 PQNP--YVFTASLRENIAF------YTPEASDAEIMKAIHVVSLDELVSELPEGldtiigqgkrvLSGGQAQRIALArAF 480
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFgpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIA-GV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 481 LDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMEN-RLVIFATHRLHWLKE-MDYILVMHEGKLVQQGTFDELTKEA 555
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
348-546 |
7.97e-14 |
|
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: 71.02 E-value: 7.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQQMLyipqnpyvftaSLRENIAFYT 427
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFNPEL-----------TGRENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 428 PE--ASDAEIMKAIhvvslDELV--SELPEGLDTIIgqgkRVLSGGQAQRIALARAfLDKTRKVMLFDEPTAHLDIETev 503
Cdd:cd03220 110 RLlgLSRKEIDEKI-----DEIIefSELGDFIDLPV----KTYSSGMKARLAFAIA-TALEPDILLIDEVLAVGDAAF-- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 543385153 504 dlKKQMLPLMENRL-----VIFATHRLHWLKEM-DYILVMHEGKLVQQG 546
Cdd:cd03220 178 --QEKCQRRLRELLkqgktVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
329-555 |
1.15e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.04 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 329 ELKLENLEFNYNNQTE-----IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIII---DGQKAATLNIPA 400
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPtelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 401 WHQQMLYIpQNPYV------------------------FTASLRENIAF------YTPEASDAEIMKAIHVVSLDElvSE 450
Cdd:PRK13651 82 KVLEKLVI-QKTRFkkikkikeirrrvgvvfqfaeyqlFEQTIEKDIIFgpvsmgVSKEEAKKRAAKYIELVGLDE--SY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 451 LPegldtiigQGKRVLSGGQAQRIALArAFLDKTRKVMLFDEPTAHLDIETEVDlkkqMLPLMEN-----RLVIFATHRL 525
Cdd:PRK13651 159 LQ--------RSPFELSGGQKRRVALA-GILAMEPDFLVFDEPTAGLDPQGVKE----ILEIFDNlnkqgKTIILVTHDL 225
|
250 260 270
....*....|....*....|....*....|..
gi 543385153 526 -HWLKEMDYILVMHEGKLVQQG-TFDELTKEA 555
Cdd:PRK13651 226 dNVLEWTKRTIFFKDGKIIKDGdTYDILSDNK 257
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
330-543 |
1.45e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.60 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE----IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQ-- 403
Cdd:PRK10535 5 LELKDIRRSYPSGEEqvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 404 --QMLYIPQN----PYVFTASLRENIAFYTPEASDAEIMKAIhvvsldELVSELpeGLDTIIGQGKRVLSGGQAQRIALA 477
Cdd:PRK10535 85 reHFGFIFQRyhllSHLTAAQNVEVPAVYAGLERKQRLLRAQ------ELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 478 RAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMEN-RLVIFATHRLHWLKEMDYILVMHEGKLV 543
Cdd:PRK10535 157 RALMNGG-QVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
330-565 |
1.53e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 71.37 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKS---GKIIIDGQKAATLNIPAWHQQ 404
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpaLNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 MLYIPQNP---YVfTASLRENIAF--YTPEASDAEIMKAIHVVsldelVSELpeGLDTIIGQGKRVLSGGQAQRIALArA 479
Cdd:PRK13640 86 VGIVFQNPdnqFV-GATVGDDVAFglENRAVPRPEMIKIVRDV-----LADV--GMLDYIDSEPANLSGGQKQRVAIA-G 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 480 FLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFA-THRLHWLKEMDYILVMHEGKLVQQGT----FD--EL 551
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISiTHDIDEANMADQVLVLDDGKLLAQGSpveiFSkvEM 236
|
250
....*....|....*...
gi 543385153 552 TKEAG----YFTKLTQEM 565
Cdd:PRK13640 237 LKEIGldipFVYKLKNKL 254
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
330-571 |
1.62e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.91 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGF--LPPKSGKII-----------IDGQKAATL 396
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 397 NIPAWHQQM------LYIPQNPYvfTASLRENI--------AFYTPEASDAEIMKAIHVV--SLDELVSELPEGLDTI-- 458
Cdd:TIGR03269 81 PCPVCGGTLepeevdFWNLSDKL--RRRIRKRIaimlqrtfALYGDDTVLDNVLEALEEIgyEGKEAVGRAVDLIEMVql 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 459 ---IGQGKRVLSGGQAQRIALARAfLDKTRKVMLFDEPTAHLDIETeVDLKKQML--PLMENRLVIFATHrlHWLKEM-- 531
Cdd:TIGR03269 159 shrITHIARDLSGGEKQRVVLARQ-LAKEPFLFLADEPTGTLDPQT-AKLVHNALeeAVKASGISMVLTS--HWPEVIed 234
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 543385153 532 --DYILVMHEGKLVQQGTFDELTKEagyFTKLTQEMRGTKNV 571
Cdd:TIGR03269 235 lsDKAIWLENGEIKEEGTPDEVVAV---FMEGVSEVEKECEV 273
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
349-551 |
1.86e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.37 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 349 SVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN-----------IPAWHQQMLYIPQNPYVFTA 417
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrevrrkkIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 418 SLRENIAFYTPEASDAEIMKAIHVVSLDELVSELPEGldtiigqgkrvLSGGQAQRIALARAfLDKTRKVMLFDEPTAHL 497
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARA-LAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 498 D--IETEVDLKKQMLPLMENRLVIFATHRL-HWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:PRK10070 196 DplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
348-546 |
1.86e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKST----LINLLsgflpPKSGKIIIDGQKAATLN----IPAWHQ-QMLYipQNPY----- 413
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNrrqlLPVRHRiQVVF--QDPNsslnp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 414 ------VFTASLRENIAFYTPEASDAEIMKAIHVVSLD-ELVSELPEGLdtiigqgkrvlSGGQAQRIALARAFLDKTRK 486
Cdd:PRK15134 378 rlnvlqIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEF-----------SGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 487 VMLfDEPTAHLDieteVDLKKQMLPLM-----ENRLV-IFATHRLHWLKEMDY-ILVMHEGKLVQQG 546
Cdd:PRK15134 447 IIL-DEPTSSLD----KTVQAQILALLkslqqKHQLAyLFISHDLHVVRALCHqVIVLRQGEVVEQG 508
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
348-561 |
2.17e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPP---KSGKIIIDGQKaatLNIPAWHQQMLYIPQNPyVFTASL--REN 422
Cdd:TIGR00955 44 VSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMP---IDAKEMRAISAYVQQDD-LFIPTLtvREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 423 IAFYTPEASDAEIMKAIHVVSLDELVSELpeGL----DTIIGQGKRV--LSGGQAQRIALARAFLDKTrKVMLFDEPTAH 496
Cdd:TIGR00955 120 LMFQAHLRMPRRVTKKEKRERVDEVLQAL--GLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDP-PLLFCDEPTSG 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 497 LDIETEVDLKKQMLPL-MENRLVIFATH----RLHWLkeMDYILVMHEGKLVQQGTFDELTKeagYFTKL 561
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLaQKGKTIICTIHqpssELFEL--FDKIILMAEGRVAYLGSPDQAVP---FFSDL 261
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
332-547 |
2.53e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.54 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 332 LENLEFNYNNQTEI-GP----VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ--KAATLN--IPAWH 402
Cdd:PRK13649 5 LQNVSYTYQAGTPFeGRalfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTliTSTSKNkdIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQNP--YVFTASLRENIAF------YTPEASDAEIMKAIHVVSLDElvselpegldTIIGQGKRVLSGGQAQRI 474
Cdd:PRK13649 85 KKVGLVFQFPesQLFEETVLKDVAFgpqnfgVSQEEAEALAREKLALVGISE----------SLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 475 ALArAFLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVI-FATHRLHWLKEM-DYILVMHEGKLVQQGT 547
Cdd:PRK13649 155 AIA-GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIvLVTHLMDDVANYaDFVYVLEKGKLVLSGK 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
328-498 |
4.89e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.90 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 328 SELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIpawHQQ--- 404
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM---HKRarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 -MLYIPQNPYVFTA-SLRENI--AFYTPEASDAEIMKAihvvsLDELVSELpeGLDTIIGQGKRVLSGGQAQRIALARAF 480
Cdd:COG1137 79 gIGYLPQEASIFRKlTVEDNIlaVLELRKLSKKEREER-----LEELLEEF--GITHLRKSKAYSLSGGERRRVEIARAL 151
|
170
....*....|....*....
gi 543385153 481 LdkTR-KVMLFDEPTAHLD 498
Cdd:COG1137 152 A--TNpKFILLDEPFAGVD 168
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
330-560 |
5.45e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.47 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE-----IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ----KAATLNIPA 400
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 401 WHQQMLYIPQNPYV--FTASLRENIAF------YTPEASDAEIMKAIHVVSLDElvselpegldTIIGQGKRVLSGGQAQ 472
Cdd:PRK13641 83 LRKKVSLVFQFPEAqlFENTVLKDVEFgpknfgFSEDEAKEKALKWLKKVGLSE----------DLISKSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 473 RIALARAFLDKTrKVMLFDEPTAHLDIETevdlKKQMLPLMEN-----RLVIFATHRLHWLKE-MDYILVMHEGKLVQQG 546
Cdd:PRK13641 153 RVAIAGVMAYEP-EILCLDEPAAGLDPEG----RKEMMQLFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKLIKHA 227
|
250
....*....|....
gi 543385153 547 TFDELTKEAGYFTK 560
Cdd:PRK13641 228 SPKEIFSDKEWLKK 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
348-543 |
6.86e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN---IPAWHQQMLYIPQNPYVFT-ASLRENI 423
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHHLLMdRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 424 AfytpeasdaeIMKAIHVVSLDELVSELPEGLDTI--IGQGKRV---LSGGQAQRIALARAFLDKTrKVMLFDEPTAHLD 498
Cdd:PRK10908 101 A----------IPLIIAGASGDDIRRRVSAALDKVglLDKAKNFpiqLSGGEQQRVGIARAVVNKP-AVLLADEPTGNLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 543385153 499 IEtevdLKKQMLPLME--NRL---VIFATHRLHWLKEMDY-ILVMHEGKLV 543
Cdd:PRK10908 170 DA----LSEGILRLFEefNRVgvtVLMATHDIGLISRRSYrMLTLSDGHLH 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
329-547 |
1.36e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 67.73 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 329 ELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQK---AATLNipawHQQM 405
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPS----EKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LYIPQN-PYVFTA-------SLREN-------IAFYTPEASDAEIMKAIHVVSLDELVSELPegldtiigqgkRVLSGGQ 470
Cdd:COG4161 78 RLLRQKvGMVFQQynlwphlTVMENlieapckVLGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 471 AQRIALARAFLDKTRkVMLFDEPTAHLDIETEVDLKKQMLPLMENRLV-IFATHRLHWLKEM-DYILVMHEGKLVQQGT 547
Cdd:COG4161 147 QQRVAIARALMMEPQ-VLLFDEPTAALDPEITAQVVEIIRELSQTGITqVIVTHEVEFARKVaSQVVYMEKGRIIEQGD 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
339-537 |
1.38e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.49 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 339 YNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAatlniPAwhqqmlYIPQN---PYVF 415
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR-----VA------YVPQRsevPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 416 TASLRENIA---------FYTPEASD-AEIMKAihvvsLDELvselpeGLDTIIGQGKRVLSGGQAQRIALARAFLDKTR 485
Cdd:NF040873 71 PLTVRDLVAmgrwarrglWRRLTRDDrAAVDDA-----LERV------GLADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 543385153 486 kVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEMDYILVM 537
Cdd:NF040873 140 -LLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
330-547 |
1.42e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.10 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTE-IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATL-----NIPawhq 403
Cdd:PRK11650 4 LKLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELepadrDIA---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 404 qMLYipQN----PYVftaSLRENIAfY------TPEAS-DAEIMKAIHVVSLDELVSELPegldtiigqgkRVLSGGQAQ 472
Cdd:PRK11650 80 -MVF--QNyalyPHM---SVRENMA-YglkirgMPKAEiEERVAEAARILELEPLLDRKP-----------RELSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 473 RIALARAFLdktR--KVMLFDEPTAHLDIEtevdLKKQM---LPLMENRL---VIFATHrlHWLKEM---DYILVMHEGK 541
Cdd:PRK11650 142 RVAMGRAIV---RepAVFLFDEPLSNLDAK----LRVQMrleIQRLHRRLkttSLYVTH--DQVEAMtlaDRVVVMNGGV 212
|
....*.
gi 543385153 542 LVQQGT 547
Cdd:PRK11650 213 AEQIGT 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
325-525 |
2.00e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 325 NSKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLI---NLLSGFLPP--KSGKIIIDGQK--AATLN 397
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNlyAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 398 IPAWHQQMLYIPQNPYVFTASLRENIAFytpeasDAEIMKaiHVVSLDELV------SELPEGLDTIIGQGKRVLSGGQA 471
Cdd:PRK14243 86 PVEVRRRIGMVFQKPNPFPKSIYDNIAY------GARING--YKGDMDELVerslrqAALWDEVKDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 543385153 472 QRIALARAfLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRL 525
Cdd:PRK14243 158 QRLCIARA-IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
348-501 |
2.37e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.73 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN------IPAWH-----QQMLYIPqnpyvfT 416
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearakLRAKHvgfvfQSFMLIP------T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 417 ASLRENI---AFYTPEASDAEIMKAIhvvsldELVSELpegldtiiGQGKRV------LSGGQAQRIALARAFldKTRKV 487
Cdd:PRK10584 103 LNALENVelpALLRGESSRQSRNGAK------ALLEQL--------GLGKRLdhlpaqLSGGEQQRVALARAF--NGRPD 166
|
170
....*....|....*
gi 543385153 488 MLF-DEPTAHLDIET 501
Cdd:PRK10584 167 VLFaDEPTGNLDRQT 181
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
358-537 |
2.76e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 358 VGIIGMSGSGKSTLINLLSGFLPPKSGKI--------IID---G-------QKAATLNIPAWHQ-QmlYIPQNPYVFTAS 418
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKrfrGtelqnyfKKLYNGEIKVVHKpQ--YVDLIPKVFKGK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 419 LREniafytpeasdaEIMKAIHVVSLDELVSELpeGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLD 498
Cdd:PRK13409 180 VRE------------LLKKVDERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAALL-RDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 543385153 499 IETEVDLKKQMLPLMENRLVIFATHRLHWLKEM-DYILVM 537
Cdd:PRK13409 245 IRQRLNVARLIRELAEGKYVLVVEHDLAVLDYLaDNVHIA 284
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
84-266 |
3.13e-12 |
|
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: 67.45 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 84 VEKLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYIKLIYTKVLAMMIIPILLFIAMLFINWQSALGLLLMYP 163
Cdd:cd18552 71 VRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 164 LIVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALD 243
Cdd:cd18552 151 LAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME 230
|
170 180
....*....|....*....|...
gi 543385153 244 FFTTLSIAVVAVYLGFGLLNGQL 266
Cdd:cd18552 231 LLGAIAIALVLWYGGYQVISGEL 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
348-567 |
3.98e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaatlnipawhqqmlyipqnPYVF---TASLRENIA 424
Cdd:PRK11288 23 ISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ--------------------EMRFastTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 425 F------YTPEASDAE-IM-----KAIHVVSLDELVSELPEGLDTI---IGQGKRV--LSGGQAQRIALARAfLDKTRKV 487
Cdd:PRK11288 83 IiyqelhLVPEMTVAEnLYlgqlpHKGGIVNRRLLNYEAREQLEHLgvdIDPDTPLkyLSIGQRQMVEIAKA-LARNARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 488 MLFDEPTAHLDI-ETEV------DLKKqmlplmENRLVIFATHRLHWLKEM-DYILVMHEGKLVQqgTFD---ELTKEag 556
Cdd:PRK11288 162 IAFDEPTSSLSArEIEQlfrvirELRA------EGRVILYVSHRMEEIFALcDAITVFKDGRYVA--TFDdmaQVDRD-- 231
|
250
....*....|.
gi 543385153 557 yftKLTQEMRG 567
Cdd:PRK11288 232 ---QLVQAMVG 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
348-551 |
5.16e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 68.17 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKS----TLINLLSGFLPPKSGKIIIDGQKAATLNIPAWHQ----QMLYIPQ------NPy 413
Cdd:COG4172 29 VSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQepmtslNP- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 414 VFT--ASLRENIAFY---TPEASDAEIMKAIHVVSLDElvselPEgldtiigqgKRV------LSGGQAQRIALARAFLD 482
Cdd:COG4172 108 LHTigKQIAEVLRLHrglSGAAARARALELLERVGIPD-----PE---------RRLdayphqLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 483 KTrKVMLFDEPTAHLDieteVDLKKQMLPLMEN---RL---VIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:COG4172 174 EP-DLLIADEPTTALD----VTVQAQILDLLKDlqrELgmaLLLITHDLGVVRRFaDRVAVMRQGEIVEQGPTAEL 244
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
330-558 |
6.36e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.68 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGP-----VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKI----IIDGQKAATLNIPA 400
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASralfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 401 WHQQMLYIPQNP--YVFTASLRENIAF------YTPEASDAEIMKAIHVVSLDELVSElpegldtiigQGKRVLSGGQAQ 472
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFgpqnfgIPKEKAEKIAAEKLEMVGLADEFWE----------KSPFELSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 473 RIALArAFLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMEN-RLVIFATHRLHWLKE-MDYILVMHEGKLVQQGTFDE 550
Cdd:PRK13643 152 RVAIA-GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
....*...
gi 543385153 551 LTKEAGYF 558
Cdd:PRK13643 231 VFQEVDFL 238
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
330-513 |
7.53e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.88 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQK----AATLNIPAWHQQM 405
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LyipqnPYvftASLRENIAFYTPEASdaeIMKAIHVVSLDELVSELpeGLDtiiGQGKRV---LSGGQAQRIALARAfLD 482
Cdd:PRK11248 82 L-----PW---RNVQDNVAFGLQLAG---VEKMQRLEIAHQMLKKV--GLE---GAEKRYiwqLSGGQRQRVGIARA-LA 144
|
170 180 190
....*....|....*....|....*....|.
gi 543385153 483 KTRKVMLFDEPTAHLDIETevdlKKQMLPLM 513
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFT----REQMQTLL 171
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
358-499 |
1.09e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.50 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 358 VGIIGMSGSGKSTLINLLSGFLPPKSGKI--------IID---G-------QKAATLNIPAWH--QQMLYIPQnpyVFTA 417
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKrfrGtelqdyfKKLANGEIKVAHkpQYVDLIPK---VFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 418 SLRENIafytpEASDaEIMKaihvvsLDELVSELpeGLDTIIGQGKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHL 497
Cdd:COG1245 179 TVRELL-----EKVD-ERGK------LDELAEKL--GLENILDRDISELSGGELQRVAIAAALL-RDADFYFFDEPSSYL 243
|
..
gi 543385153 498 DI 499
Cdd:COG1245 244 DI 245
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
330-549 |
1.46e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.95 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIII---DGQKAATLNIPAWHQQML 406
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 407 ------YIPQNPyvfTASLRENIafyTPEASDAEIMKAIHVVSLDELVSELPEGLDTI-IGQGK-----RVLSGGQAQRI 474
Cdd:PRK11701 87 lrtewgFVHQHP---RDGLRMQV---SAGGNIGERLMAVGARHYGDIRATAGDWLERVeIDAARiddlpTTFSGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 475 ALARAFLDKTRKVmLFDEPTAHLDieteVDLKKQMLPLM-----ENRL-VIFATH-----RLhwLKemDYILVMHEGKLV 543
Cdd:PRK11701 161 QIARNLVTHPRLV-FMDEPTGGLD----VSVQARLLDLLrglvrELGLaVVIVTHdlavaRL--LA--HRLLVMKQGRVV 231
|
....*.
gi 543385153 544 QQGTFD 549
Cdd:PRK11701 232 ESGLTD 237
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
360-551 |
1.50e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.17 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 360 IIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaatlNIPAWHQQMLY--------IPQNPYVFT-ASLRENIAFYTPEA 430
Cdd:PRK11831 38 IMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE-----NIPAMSRSRLYtvrkrmsmLFQSGALFTdMNVFDNVAYPLREH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 431 SD--AEIMKAIHVVSLDELvselpeGLDTIIGQGKRVLSGGQAQRIALARAF-LDKtrKVMLFDEPTAHLDIETEVDLKK 507
Cdd:PRK11831 113 TQlpAPLLHSTVMMKLEAV------GLRGAAKLMPSELSGGMARRAALARAIaLEP--DLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 543385153 508 QMLPLMENRLV--IFATHRL-HWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:PRK11831 185 LISELNSALGVtcVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
348-541 |
2.48e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKS--GKIIIDGQ--KAATLN------IPAWHQQMLYIPQnpyvftA 417
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEelQASNIRdteragIAIIHQELALVKE------L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 418 SLRENIaFYTPEASDAEIM--KAIHVVSlDELVSELpeGLDtiIGQGKRV--LSGGQAQRIALARAfLDKTRKVMLFDEP 493
Cdd:PRK13549 98 SVLENI-FLGNEITPGGIMdyDAMYLRA-QKLLAQL--KLD--INPATPVgnLGLGQQQLVEIAKA-LNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 494 TAHL-DIETEV------DLKKQmlplmeNRLVIFATHRLHWLKEM-DYILVMHEGK 541
Cdd:PRK13549 171 TASLtESETAVlldiirDLKAH------GIACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
340-546 |
2.58e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.52 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 340 NNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ---KAATLNIPAwhqqmlYIPQNPYV-- 414
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrQALQKNLVA------YVPQSEEVdw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 415 -FTAsLRENIAFY----------TPEASDAEIM-KAIHVVSLDELVSELpegldtiIGQgkrvLSGGQAQRIALARAfLD 482
Cdd:PRK15056 92 sFPV-LVEDVVMMgryghmgwlrRAKKRDRQIVtAALARVDMVEFRHRQ-------IGE----LSGGQKKRVFLARA-IA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 483 KTRKVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEM-DYIlVMHEGKLVQQG 546
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFcDYT-VMVKGTVLASG 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
348-542 |
4.92e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPA-WHQQMLYIPQNPYV----FTASLREN 422
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRQSsglyLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 423 I--------AFYTPEASDAEIMKAIHvVSLDELVSElpegldtiIGQGKRVLSGGQAQRIALARAfLDKTRKVMLFDEPT 494
Cdd:PRK15439 362 VcalthnrrGFWIKPARENAVLERYR-RALNIKFNH--------AEQAARTLSGGNQQKVLIAKC-LEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 543385153 495 AHLDIETEVDLKKQMLPLME-NRLVIFATHRLHWLKEM-DYILVMHEGKL 542
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAqNVAVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
351-519 |
5.92e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 351 EIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDgqkaatLNIPawhqqmlYIPQnpYV---FTASLRENIAFYT 427
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKIS-------YKPQ--YIspdYDGTVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 428 PEASD-----AEIMKaihvvsldelvselPEGLDTIIGQGKRVLSGGQAQRIALArAFLDKTRKVMLFDEPTAHLDIETE 502
Cdd:COG1245 427 TDDFGssyykTEIIK--------------PLGLEKLLDKNVKDLSGGELQRVAIA-ACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180
....*....|....*....|.
gi 543385153 503 VDLKKQMLPLMENR----LVI 519
Cdd:COG1245 492 LAVAKAIRRFAENRgktaMVV 512
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
351-519 |
9.12e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 9.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 351 EIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDgqkaatLNIPawhqqmlYIPQnpYV---FTASLRENIAFYT 427
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIS-------YKPQ--YIkpdYDGTVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 428 PEASD----AEIMKaihvvsldelvselPEGLDTIIGQGKRVLSGGQAQRIALArAFLDKTRKVMLFDEPTAHLDIETEV 503
Cdd:PRK13409 426 DDLGSsyykSEIIK--------------PLQLERLLDKNVKDLSGGELQRVAIA-ACLSRDADLYLLDEPSAHLDVEQRL 490
|
170 180
....*....|....*....|
gi 543385153 504 DLKKQMLPLMENR----LVI 519
Cdd:PRK13409 491 AVAKAIRRIAEEReataLVV 510
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
348-546 |
1.00e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.51 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNiPA-------WHQQMLYipqnPYVftaSLR 420
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-PAergvgmvFQSYALY----PHL---SVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 421 ENIAF--YTPEASDAEIMKAIHVVS----LDELVSELPegldtiigqgkRVLSGGQAQRIALARAFLDKTrKVMLFDEPT 494
Cdd:PRK11000 94 ENMSFglKLAGAKKEEINQRVNQVAevlqLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEP-SVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 495 AHLDIETEVDLKKQMLPLME--NRLVIFATH-RLHWLKEMDYILVMHEGKLVQQG 546
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
330-525 |
1.06e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTL---INLLSGFLP--PKSGKIIIDGQ-----KAATLNIp 399
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsINRMNDLNPevTITGSIVYNGHniyspRTDTVDL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 400 awHQQMLYIPQNPYVFTASLRENIAF-------YTPEASDAEIMKAIHVVSL-DELVSELPeglDTIIGqgkrvLSGGQA 471
Cdd:PRK14239 85 --RKEIGMVFQQPNPFPMSIYENVVYglrlkgiKDKQVLDEAVEKSLKGASIwDEVKDRLH---DSALG-----LSGGQQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 543385153 472 QRIALARAfLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRL 525
Cdd:PRK14239 155 QRVCIARV-LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
360-561 |
1.21e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.49 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 360 IIGMSGSGKSTLINLLSGFLPPKSGKIIIDG----QKAATLNIPAWHQQMLYIPQNP--YVFTASLRENIAFyTPEASDA 433
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRPVRKRIGMVFQFPesQLFEDTVEREIIF-GPKNFKM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 434 EIMKAIHVVSldELVSELPEGLDtIIGQGKRVLSGGQAQRIALArAFLDKTRKVMLFDEPTAHLDIETEVDLKK--QMLP 511
Cdd:PRK13646 117 NLDEVKNYAH--RLLMDLGFSRD-VMSQSPFQMSGGQMRKIAIV-SILAMNPDIIVLDEPTAGLDPQSKRQVMRllKSLQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 543385153 512 LMENRLVIFATHRLHWL-KEMDYILVMHEGKLVQQGTFDELTKEAGYFTKL 561
Cdd:PRK13646 193 TDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
348-551 |
1.71e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.64 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPP----KSGKIIIDGQKAATLNIPAWHqqMLYIPQNP-------YVFT 416
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRK--IATIMQNPrsafnplHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 417 ASLRENIAFYTPEASDAEIMKAIHVVSLDElvselpegldtiigqGKRVL-------SGGQAQRIALARAFLDKTrKVML 489
Cdd:PRK10418 100 THARETCLALGKPADDATLTAALEAVGLEN---------------AARVLklypfemSGGMLQRMMIALALLCEA-PFII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 490 FDEPTAHLDIETEVDLKKQMLPLMENRL--VIFATH------RLhwlkeMDYILVMHEGKLVQQGTFDEL 551
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHdmgvvaRL-----ADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
357-501 |
1.78e-10 |
|
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: 63.42 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 357 KVGIIGMSGSGKSTLINLLSGFLPPKSGKiiidgqkaatlnipAWHQQML---YIPQNPYV-FTASLRENI--------- 423
Cdd:TIGR03719 33 KIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------------ARPQPGIkvgYLPQEPQLdPTKTVRENVeegvaeikd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 424 ----------AFYTPEAS-------DAEIMKAIHVVSLDELVSEL---------PEGlDTIIGqgkrVLSGGQAQRIALA 477
Cdd:TIGR03719 99 aldrfneisaKYAEPDADfdklaaeQAELQEIIDAADAWDLDSQLeiamdalrcPPW-DADVT----KLSGGERRRVALC 173
|
170 180
....*....|....*....|....
gi 543385153 478 RAFLDKTrKVMLFDEPTAHLDIET 501
Cdd:TIGR03719 174 RLLLSKP-DMLLLDEPTNHLDAES 196
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
80-266 |
1.94e-10 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 62.04 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 80 SSQEVEK-LRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYIKLIytkVLAMM---IIPILLFIAMLFINWQSA 155
Cdd:cd18541 67 ASRRIEYdLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPG---ILYLVdalFLGVLVLVMMFTISPKLT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 156 LGLLLMYPLIVLFMIILGyaakDRASKQFGD----FQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAV 231
Cdd:cd18541 144 LIALLPLPLLALLVYRLG----KKIHKRFRKvqeaFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRL 219
|
170 180 190
....*....|....*....|....*....|....*
gi 543385153 232 LKVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQL 266
Cdd:cd18541 220 ARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTI 254
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
330-554 |
4.83e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLP----------------PKSGKIIIDGQKA 393
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshiellgrtvQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 394 ATLNIPAWHQ----QMLYIPQNPYV----FTASLRENIAFYTPEASDaEIMKAIHVVsldelvselpeGLDTIIGQGKRV 465
Cdd:PRK09984 85 RANTGYIFQQfnlvNRLSVLENVLIgalgSTPFWRTCFSWFTREQKQ-RALQALTRV-----------GMVHFAHQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 466 LSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENR--LVIFATHRLHW-LKEMDYILVMHEGKL 542
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQA-KVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYaLRYCERIVALRQGHV 231
|
250
....*....|..
gi 543385153 543 VQQGTFDELTKE 554
Cdd:PRK09984 232 FYDGSSQQFDNE 243
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
332-526 |
5.64e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 332 LENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaatLNIPawhqqmlYIPQN 411
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----LRIG-------YVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 412 PYVfTASLRENIAFYT---PEASDAEIMKAIHVVSLDELvselpegldtiIGQGKRVLSGGQAQRIALARAFLDKTrKVM 488
Cdd:PRK09544 76 LYL-DTTLPLTVNRFLrlrPGTKKEDILPALKRVQAGHL-----------IDAPMQKLSGGETQRVLLARALLNRP-QLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 543385153 489 LFDEPTAHLDIETEV---DLKKQMLPLMeNRLVIFATHRLH 526
Cdd:PRK09544 143 VLDEPTQGVDVNGQValyDLIDQLRREL-DCAVLMVSHDLH 182
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
52-289 |
7.62e-10 |
|
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: 60.09 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 52 WQYLLIFIVCLTGRQLIDLLKDkMLETYSSQEV-EKLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDyiklIY 130
Cdd:cd18544 41 LLLALLYLGLLLLSFLLQYLQT-YLLQKLGQRIiYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNE----LF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 131 TKVLAMMIIPILL----FIAMLFINWQSALGLLLMYPLIVLFMIILGYAAKD--RASKqfgdfQKLS--NNFI-DSLRGI 201
Cdd:cd18544 116 TSGLVTLIGDLLLligiLIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKayREVR-----EKLSrlNAFLqESISGM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 202 DTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQLplypALSILILAPEY 281
Cdd:cd18544 191 SVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAV----TLGVLYAFIQY 266
|
250
....*....|..
gi 543385153 282 ----FLPIRNFA 289
Cdd:cd18544 267 iqrfFRPIRDLA 278
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
323-500 |
1.12e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.71 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 323 PWNSKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLNIPawh 402
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQNPYVFT-ASLRENIAFytpeasdaeiMKAIHvvslDELVSELPEGLDTIIGQGK------RVLSGGQAQRIA 475
Cdd:PRK13543 82 RFMAYLGHLPGLKAdLSTLENLHF----------LCGLH----GRRAKQMPGSALAIVGLAGyedtlvRQLSAGQKKRLA 147
|
170 180
....*....|....*....|....*
gi 543385153 476 LARAFLDKTrKVMLFDEPTAHLDIE 500
Cdd:PRK13543 148 LARLWLSPA-PLWLLDEPYANLDLE 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
330-543 |
1.35e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLP--PKSGKIIIDGQ--KAATLN------IP 399
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSplKASNIRdteragIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 400 AWHQQMLYIPQnpyvftASLRENIAFYTPEASDAEIMK-AIHVVSLDELVSELPEGLDTI---IGQgkrvLSGGQAQRIA 475
Cdd:TIGR02633 82 IIHQELTLVPE------LSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLRELQLDADNVtrpVGD----YGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 476 LARAfLDKTRKVMLFDEPTAHL-DIETEV------DLKKQmlplmeNRLVIFATHRLHWLKEM-DYILVMHEGKLV 543
Cdd:TIGR02633 152 IAKA-LNKQARLLILDEPSSSLtEKETEIlldiirDLKAH------GVACVYISHKLNEVKAVcDTICVIRDGQHV 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
348-554 |
1.39e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPK-SGKIIIDGQKAATLN-IPAWHQQMLYIPQN-------PYV---- 414
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivPILgvgk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 415 -FTASLRENIAFYTPEASDAE---IMKAIHVVSLDELVSELPegldtiIGQgkrvLSGGQAQRIALARAFLDKTRkVMLF 490
Cdd:TIGR02633 359 nITLSVLKSFCFKMRIDAAAElqiIGSAIQRLKVKTASPFLP------IGR----LSGGNQQKAVLAKMLLTNPR-VLIL 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 491 DEPTAHLDIETEVDLKKQMLPLMEN--RLVIFATHRLHWLKEMDYILVMHEGKLvqQGTF--DELTKE 554
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEgvAIIVVSSELAEVLGLSDRVLVIGEGKL--KGDFvnHALTQE 493
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-538 |
1.61e-09 |
|
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: 58.92 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 358 VGIIGMSGSGKSTLINLLSGFLPPKSGKI--------IIDGQKAATLNIpaWHQQML-----------YIPQNPYVFTAS 418
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEFRGSELQN--YFTKLLegdvkvivkpqYVDLIPKAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 419 LRENIafytpEASDAEIMkaihvvsLDELVSELpeGLDTIIGQGKRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLD 498
Cdd:cd03236 107 VGELL-----KKKDERGK-------LDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDA-DFYFFDEPSSYLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 543385153 499 IETEVDLKKQMLPLME-NRLVIFATHRLHWLKEM-DYILVMH 538
Cdd:cd03236 172 IKQRLNAARLIRELAEdDNYVLVVEHDLAVLDYLsDYIHCLY 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
330-500 |
1.61e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIiidgQKAATLNIPawhqqmlYIP 409
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSENANIG-------YYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QNPYVFTA---SLRENIAFYTPEASDAEIMKAIhvvsLDELvseLPEGLDtiIGQGKRVLSGGQAQRIALARAFLDKTrK 486
Cdd:PRK15064 389 QDHAYDFEndlTLFDWMSQWRQEGDDEQAVRGT----LGRL---LFSQDD--IKKSVKVLSGGEKGRMLFGKLMMQKP-N 458
|
170
....*....|....
gi 543385153 487 VMLFDEPTAHLDIE 500
Cdd:PRK15064 459 VLVMDEPTNHMDME 472
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
348-562 |
2.44e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.95 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGqkaatlNIPaWHQQMlyipqnpyvftaSLRENIAF-- 425
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG------YVP-FKRRK------------EFARRIGVvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 426 --------YTPeASDA-EIMKAIHVVS-------LDELVSELpeGLDTIIGQGKRVLSGGQAQRIALARAFLDKTrKVML 489
Cdd:COG4586 102 gqrsqlwwDLP-AIDSfRLLKAIYRIPdaeykkrLDELVELL--DLGELLDTPVRQLSLGQRMRCELAAALLHRP-KILF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 490 FDEPTAHLDIETEV-------DLKKQmlplmENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDELTKEAGYFTKL 561
Cdd:COG4586 178 LDEPTIGLDVVSKEaireflkEYNRE-----RGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFGPYKTI 252
|
.
gi 543385153 562 T 562
Cdd:COG4586 253 V 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
330-557 |
2.52e-09 |
|
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: 57.15 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPK--SGKIIIDGQKaaTLNIPAWHQQMLY 407
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGED--ITDLPPEERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 408 IpqnpyvftaslreNIAFYTPEAsdaeimkaIHVVSLDELVSELPEGLdtiigqgkrvlSGGQAQRIALARAFLDKTRKV 487
Cdd:cd03217 79 I-------------FLAFQYPPE--------IPGVKNADFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 488 MLfDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEM--DYILVMHEGKLVQQGTFD--ELTKEAGY 557
Cdd:cd03217 127 IL-DEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
348-554 |
2.62e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQK--------AATLNIPAWHQQM-----LYIPQNPYV 414
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhklAAQLGIGIIYQELsvideLTVLENLYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 415 FTASLRE----NIAFYTPEASDAEIMK---AIHvVSLDELVSElpegldtiigqgkrvLSGGQAQRIALARAFLDKTrKV 487
Cdd:PRK09700 104 GRHLTKKvcgvNIIDWREMRVRAAMMLlrvGLK-VDLDEKVAN---------------LSISHKQMLEIAKTLMLDA-KV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 488 MLFDEPTAHLdIETEVDlkkQMLPLM-----ENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDELTKE 554
Cdd:PRK09700 167 IIMDEPTSSL-TNKEVD---YLFLIMnqlrkEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
330-515 |
3.59e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIidgQKAATLNIPAWHQQMLYip 409
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---AGTAPLAEAREDTRLMF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 QN----PYvftASLRENIAF-----YTPEAsdaeiMKAIHVVSLDELVSELPEGLdtiigqgkrvlSGGQAQRIALARAF 480
Cdd:PRK11247 88 QDarllPW---KKVIDNVGLglkgqWRDAA-----LQALAAVGLADRANEWPAAL-----------SGGQKQRVALARAL 148
|
170 180 190
....*....|....*....|....*....|....*
gi 543385153 481 LDKTRkVMLFDEPTAHLDIETEVdlkkQMLPLMEN 515
Cdd:PRK11247 149 IHRPG-LLLLDEPLGALDALTRI----EMQDLIES 178
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
358-501 |
3.96e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 358 VGIIGMSGSGKSTLINLLSGFLPPKSGKIIIdGQKAatlnipawhqQMLYIPQNpyvftaslRENIAfytPEASDAEimk 437
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVDQS--------RDALD---PNKTVWE--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 438 aihVVSldelvselpEGLDTI-IG-------------------QGKRV--LSGGQAQRIALArafldKTRK----VMLFD 491
Cdd:PRK11819 408 ---EIS---------GGLDIIkVGnreipsrayvgrfnfkggdQQKKVgvLSGGERNRLHLA-----KTLKqggnVLLLD 470
|
170
....*....|
gi 543385153 492 EPTAHLDIET 501
Cdd:PRK11819 471 EPTNDLDVET 480
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
356-531 |
5.00e-09 |
|
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: 55.07 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 356 EKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIdgqkaatlnipawhqqmlyipqnpyvftaslreniafytpeasdaei 435
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIY----------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 436 mkaihvVSLDELVSELPEGL-DTIIGQGKRVLSGGQAQRIALARAfLDKTRKVMLFDEPTAHLDIETEVDL-------KK 507
Cdd:smart00382 36 ------IDGEDILEEVLDQLlLIIVGGKKASGSGELRLRLALALA-RKLKPDVLILDEITSLLDAEQEALLllleelrLL 108
|
170 180
....*....|....*....|....
gi 543385153 508 QMLPLMENRLVIFATHRLHWLKEM 531
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
348-555 |
6.76e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGqKAATLNIPawhQQML-----YIPQNP----YVFTAS 418
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG-HEVVTRSP---QDGLangivYISEDRkrdgLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 419 LRENIAFytpEASDAEIMKAIHVVSLDE--LVSELPE-------GLDTIIGqgkrVLSGGQAQRIALARAFLdkTR-KVM 488
Cdd:PRK10762 347 VKENMSL---TALRYFSRAGGSLKHADEqqAVSDFIRlfniktpSMEQAIG----LLSGGNQQKVAIARGLM--TRpKVL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 489 LFDEPTAHLDieteVDLKKQMLPLM-----ENRLVIFATHRLHWLKEM-DYILVMHEGKLvqQGTFD--ELTKEA 555
Cdd:PRK10762 418 ILDEPTRGVD----VGAKKEIYQLInqfkaEGLSIILVSSEMPEVLGMsDRILVMHEGRI--SGEFTreQATQEK 486
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
325-551 |
7.58e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.92 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 325 NSKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLniPAwHQ- 403
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PG-HQi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 404 ----------------QM-----LYIPQNPYVFTASLREniAFYTPEASDAE---IMKAIHvvSLDELvselpeGLDTII 459
Cdd:PRK11300 78 armgvvrtfqhvrlfrEMtvienLLVAQHQQLKTGLFSG--LLKTPAFRRAEseaLDRAAT--WLERV------GLLEHA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 460 GQGKRVLSGGQAQRIALARAFLDKTRKVMLfDEPTAHLDIETEVDLKKQMLPLME--NRLVIFATHRLHWLKEM-DYILV 536
Cdd:PRK11300 148 NRQAGNLAYGQQRRLEIARCMVTQPEILML-DEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGIsDRIYV 226
|
250
....*....|....*
gi 543385153 537 MHEGKLVQQGTFDEL 551
Cdd:PRK11300 227 VNQGTPLANGTPEEI 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
348-564 |
9.44e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGqKAATLNIP--AWHQQMLYIPQ----NPYVFTASLRE 421
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG-KDISPRSPldAVKKGMAYITEsrrdNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 422 NIAFyTPEASDAEIMKAIHVV--SLDELVSELPEGLDTI----IGQGKRVLSGGQAQRIALARaFLDKTRKVMLFDEPTA 495
Cdd:PRK09700 361 NMAI-SRSLKDGGYKGAMGLFheVDEQRTAENQRELLALkchsVNQNITELSGGNQQKVLISK-WLCCCPEVIIFDEPTR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543385153 496 HLDIETEVDLKKQMLPLMEN-RLVIFATHRL-HWLKEMDYILVMHEGKLVQQGT-FDELTKEAGYFTKLTQE 564
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRLTQILTnRDDMSEEEIMAWALPQE 510
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
357-501 |
1.06e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 357 KVGIIGMSGSGKSTLINLLSGFLPPKSGKiiidgqkaatlnipAWHQQML---YIPQNPYV-FTASLRENI--------- 423
Cdd:PRK11819 35 KIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------------ARPAPGIkvgYLPQEPQLdPEKTVRENVeegvaevka 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 424 ----------AFYTPEASDAEIMK-------AIHVVSLDELVSEL---------PEGlDTIIGqgkrVLSGGQAQRIALA 477
Cdd:PRK11819 101 aldrfneiyaAYAEPDADFDALAAeqgelqeIIDAADAWDLDSQLeiamdalrcPPW-DAKVT----KLSGGERRRVALC 175
|
170 180
....*....|....*....|....
gi 543385153 478 RAFLDKTrKVMLFDEPTAHLDIET 501
Cdd:PRK11819 176 RLLLEKP-DMLLLDEPTNHLDAES 198
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
330-551 |
1.14e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkaatlNIPAWH------Q 403
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK-----DITDWQtakimrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 404 QMLYIPQNPYVFT-ASLRENIAFYTPEASDAEIMKAIhvvsldELVSELPEGLDTIIGQGKRVLSGGQAQRIALARAFLD 482
Cdd:PRK11614 81 AVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERI------KWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543385153 483 KTRkVMLFDEPT---AHLDIETEVDLKKQmlpLMENRLVIFATHR--LHWLKEMDYILVMHEGKLVQQGTFDEL 551
Cdd:PRK11614 155 QPR-LLLLDEPSlglAPIIIQQIFDTIEQ---LREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
305-554 |
1.50e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.76 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 305 INELISRPMQASADLAIEpwnskselkLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSG 384
Cdd:PRK13536 26 ISEAKASIPGSMSTVAID---------LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 385 KIIIdgqkaatLNIPAWHQQML------YIPQNPYV---FTAslRENIAFYTP--EASDAEIMKAIHvvSLDELvSELPE 453
Cdd:PRK13536 97 KITV-------LGVPVPARARLararigVVPQFDNLdleFTV--RENLLVFGRyfGMSTREIEAVIP--SLLEF-ARLES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 454 GLDTIIGQgkrvLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEM- 531
Cdd:PRK13536 165 KADARVSD----LSGGMKRRLTLARALINDP-QLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLc 239
|
250 260
....*....|....*....|...
gi 543385153 532 DYILVMHEGKLVQQGTFDELTKE 554
Cdd:PRK13536 240 DRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
326-551 |
1.64e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 56.35 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 326 SKSELKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKaatlnIP--AWHQ 403
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP-----VPsrARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 404 QMLY--IPQ----NPyvfTASLRENIAFYTPE--ASDAEIMKAihVVSLDELvSELPEGLDTIIGQgkrvLSGGQAQRIA 475
Cdd:PRK13537 79 RQRVgvVPQfdnlDP---DFTVRENLLVFGRYfgLSAAAARAL--VPPLLEF-AKLENKADAKVGE----LSGGMKRRLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 476 LARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFAThrLHWLKEM----DYILVMHEGKLVQQGTFDEL 551
Cdd:PRK13537 149 LARALVNDP-DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLT--THFMEEAerlcDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
348-546 |
2.11e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATLN---IPAWHQQMLYIPQNPYvftASL--REN 422
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY---ASLdpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 423 IAFytpeasdaEIMKAIHVVSL------DELVSELPEGLDTIIGQGKRV---LSGGQAQRIALARAfLDKTRKVMLFDEP 493
Cdd:PRK10261 420 VGD--------SIMEPLRVHGLlpgkaaAARVAWLLERVGLLPEHAWRYpheFSGGQRQRICIARA-LALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 494 TAHLDIETEVDLKKQMLPLMENRLV--IFATHRLHWLKEMDY-ILVMHEGKLVQQG 546
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHrVAVMYLGQIVEIG 546
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
330-551 |
2.20e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPV----SVEIKGYEKVGIIGMSGSGKS----TLINLLSGflPP---KSGKIIIDGQKAATLNI 398
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVvndvSLQIEAGETLALVGESGSGKSvtalSILRLLPS--PPvvyPSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 399 PAWHQ----QMLYIPQNPYVftaSLReniAFYTPEASDAEIMKAIHVVSLDELVSELPEGLDTI-IGQGKR-------VL 466
Cdd:PRK15134 84 QTLRGvrgnKIAMIFQEPMV---SLN---PLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVgIRQAAKrltdyphQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 467 SGGQAQRIALARAFLdkTR-KVMLFDEPTAHLDieteVDLKKQMLPLME------NRLVIFATHRLHWLKEM-DYILVMH 538
Cdd:PRK15134 158 SGGERQRVMIAMALL--TRpELLIADEPTTALD----VSVQAQILQLLRelqqelNMGLLFITHNLSIVRKLaDRVAVMQ 231
|
250
....*....|...
gi 543385153 539 EGKLVQQGTFDEL 551
Cdd:PRK15134 232 NGRCVEQNRAATL 244
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
52-266 |
2.52e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 55.52 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 52 WQYLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIfksgQSL-----VQSQgTGSLITMALYGIDEVRDYI 126
Cdd:cd18542 39 WLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHL----QRLsfsfhDKAR-TGDLMSRCTSDVDTIRRFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 127 KLIYTKVLAMMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYAAK---DRASKQFGdfqKLSNNFIDSLRGIDT 203
Cdd:cd18542 114 AFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRpafEEIREQEG---ELNTVLQENLTGVRV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 204 LKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQL 266
Cdd:cd18542 191 VKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEI 253
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
311-501 |
2.67e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 311 RPMQASADLAIEPWNSKSEL--KLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIII 388
Cdd:PRK11147 299 REVMGTAKMQVEEASRSGKIvfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 389 dGQKaatLNIpAWHQQmlyipqnpyvFTASL------RENIAfytpeASDAEIM---KAIHVVSL--DELVSelPEGLDT 457
Cdd:PRK11147 379 -GTK---LEV-AYFDQ----------HRAELdpektvMDNLA-----EGKQEVMvngRPRHVLGYlqDFLFH--PKRAMT 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 543385153 458 IIgqgkRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLDIET 501
Cdd:PRK11147 437 PV----KALSGGERNRLLLARLFL-KPSNLLILDEPTNDLDVET 475
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
348-551 |
3.48e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKS----TLINLL--SG--------FLPPKSGKIIIDGQKAATLNIPAWHQQMLYIPQNPY 413
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmLLRRRSRQVIELSEQSAAQMRHVRGADMAMIFQEPM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 414 -----VFTA--SLRENIAFYTPEASDAEIMKAIHVvsLDELvsELPEGlDTIIGQGKRVLSGGQAQRIALARAfLDKTRK 486
Cdd:PRK10261 115 tslnpVFTVgeQIAESIRLHQGASREEAMVEAKRM--LDQV--RIPEA-QTILSRYPHQLSGGMRQRVMIAMA-LSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 487 VMLFDEPTAHLDIETEVDLKkQMLPLMENRL---VIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQIL-QLIKVLQKEMsmgVIFITHDMGVVAEIaDRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
52-268 |
3.56e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 55.21 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 52 WQYLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYIK--LI 129
Cdd:cd18563 43 LLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSdgLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 130 YTKVLAMMIIPILlfIAMLFINWQSALGLLLMYPLIVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGL 209
Cdd:cd18563 123 DFLTNILMIIGIG--VVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQ 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 210 SKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQLPL 268
Cdd:cd18563 201 EKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTL 259
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-569 |
4.23e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.72 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 334 NLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLL-------SGFlpPKSGKIIIDGQKAATL-NIPAWHQQM 405
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGY--RYSGDVLLGGRSIFNYrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 406 LYIPQNPYVFTASLRENI--AFYTPEASDAEIMKAIHVVSLDELvsELPEGLDTIIGQGKRVLSGGQAQRIALARAfLDK 483
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVlaGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLART-LAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 484 TRKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL------TKEAG 556
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLfsspkhAETAR 260
|
250
....*....|...
gi 543385153 557 YFTKLTQEMRGTK 569
Cdd:PRK14271 261 YVAGLSGDVKDAK 273
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
347-554 |
4.26e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 347 PVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGqKAATLNIP--AWHQQMLYIP----QNPYVFTASLR 420
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG-KPIDIRSPrdAIRAGIMLCPedrkAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 421 ENIA-----FYTP---------EASDAE--IMK-AIHVVSLDELVselpegldtiigqgkRVLSGGQAQRIALARaFLDK 483
Cdd:PRK11288 350 DNINisarrHHLRagclinnrwEAENADrfIRSlNIKTPSREQLI---------------MNLSGGNQQKAILGR-WLSE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 484 TRKVMLFDEPTAHLDI--ETEV-----DLKKQmlplmeNRLVIFATHRlhwLKEM----DYILVMHEGKLVqqgtfDELT 552
Cdd:PRK11288 414 DMKVILLDEPTRGIDVgaKHEIynviyELAAQ------GVAVLFVSSD---LPEVlgvaDRIVVMREGRIA-----GELA 479
|
..
gi 543385153 553 KE 554
Cdd:PRK11288 480 RE 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
358-501 |
5.28e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.71 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 358 VGIIGMSGSGKSTLINLLSGFLPPKSGKIIIdgqkAATLnipawhqQMLYIPQNpyvftaslRENIafyTPEASDAEimk 437
Cdd:TIGR03719 351 VGVIGPNGAGKSTLFRMITGQEQPDSGTIEI----GETV-------KLAYVDQS--------RDAL---DPNKTVWE--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 438 aihvvsldelvsELPEGLDTI-IG-------------------QGKRV--LSGGQAQRIALARAfLDKTRKVMLFDEPTA 495
Cdd:TIGR03719 406 ------------EISGGLDIIkLGkreipsrayvgrfnfkgsdQQKKVgqLSGGERNRVHLAKT-LKSGGNVLLLDEPTN 472
|
....*.
gi 543385153 496 HLDIET 501
Cdd:TIGR03719 473 DLDVET 478
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
348-544 |
6.75e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDgqkaatlnipawhqqmlyIPQNPYVFTASLRENIAfyt 427
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLIDAIG--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 428 PEASDAEIMKAIHVVSLDELVSELpegldtiigqgKRV--LSGGQAQRIALARAfLDKTRKVMLFDEPTAHLDIETEVDL 505
Cdd:COG2401 108 RKGDFKDAVELLNAVGLSDAVLWL-----------RRFkeLSTGQKFRFRLALL-LAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 543385153 506 KKQMLPLMENRLV--IFATHR---LHWLKEmDYILVMHEGKLVQ 544
Cdd:COG2401 176 ARNLQKLARRAGItlVVATHHydvIDDLQP-DLLIFVGYGGVPE 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
356-501 |
7.60e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 356 EKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ-KAATLnipawhqqmlyiPQNP--------YVFTAslrENIAfy 426
Cdd:PRK11147 30 ERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARL------------QQDPprnvegtvYDFVA---EGIE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 427 tpeaSDAEIMKAIHVVSL-------DELVSELPEGLDTIIGQG-----KRV-----------------LSGGQAQRIALA 477
Cdd:PRK11147 93 ----EQAEYLKRYHDISHlvetdpsEKNLNELAKLQEQLDHHNlwqleNRInevlaqlgldpdaalssLSGGWLRKAALG 168
|
170 180
....*....|....*....|....
gi 543385153 478 RAfLDKTRKVMLFDEPTAHLDIET 501
Cdd:PRK11147 169 RA-LVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
330-542 |
7.84e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIdgQKAATLNIPAWHQqmlyip 409
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--AKGIKLGYFAQHQ------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 410 qnpyvftaslrenIAFYTPEASDAEimkaiHVVSL--DELVSELPEGLDTIIGQGKRV------LSGGQAQRIALARAFL 481
Cdd:PRK10636 385 -------------LEFLRADESPLQ-----HLARLapQELEQKLRDYLGGFGFQGDKVteetrrFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543385153 482 DKTrKVMLFDEPTAHLDIETEVDLKKQMLPLmENRLVIfATHRLHWLKE-MDYILVMHEGKL 542
Cdd:PRK10636 447 QRP-NLLLLDEPTNHLDLDMRQALTEALIDF-EGALVV-VSHDRHLLRStTDDLYLVHDGKV 505
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
348-547 |
9.68e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.39 E-value: 9.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLsgFLPPKSGKIIIDGQKAATLNIPAWHQQ---MLYIPQNP-----------Y 413
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSLINDT--LYPALARRLHLKKEQPGNHDRIEGLEHidkVIVIDQSPigrtprsnpatY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 414 --VFTaSLRE------NIAFYTPEAsdAEIM---KAIHVVsLDELVSELPE------------------GLDTI-IGQGK 463
Cdd:cd03271 92 tgVFD-EIRElfcevcKGKRYNRET--LEVRykgKSIADV-LDMTVEEALEffenipkiarklqtlcdvGLGYIkLGQPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 464 RVLSGGQAQRIALARAFLDKTRKVMLF--DEPTAHLDIEtevDLKKqmlpLME--NRL------VIFATHRLHWLKEMDY 533
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRSTGKTLYilDEPTTGLHFH---DVKK----LLEvlQRLvdkgntVVVIEHNLDVIKCADW 240
|
250 260
....*....|....*....|
gi 543385153 534 ILVM------HEGKLVQQGT 547
Cdd:cd03271 241 IIDLgpeggdGGGQVVASGT 260
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
454-551 |
1.13e-07 |
|
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: 55.02 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 454 GLDTI-IGQGKRVLSGGQAQRIALARAFL--DKTRKVMLFDEPTAHLDIEtevDLKKqmlpLME--NRL------VIFAT 522
Cdd:TIGR00630 817 GLGYIrLGQPATTLSGGEAQRIKLAKELSkrSTGRTLYILDEPTTGLHFD---DIKK----LLEvlQRLvdkgntVVVIE 889
|
90 100 110
....*....|....*....|....*....|....*
gi 543385153 523 HRLHWLKEMDYILVM------HEGKLVQQGTFDEL 551
Cdd:TIGR00630 890 HNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
348-554 |
2.03e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKS-GKIIIDGQKAATLNipawhqqmlyiPQNpyvftaSLRENIAfY 426
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRN-----------PQQ------AIAQGIA-M 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 427 TPE-------ASDAEIMKAIHVVSLDELV--SELPEG--LDTIIGQGKRV-------------LSGGQAQRIALARAFLD 482
Cdd:PRK13549 343 VPEdrkrdgiVPVMGVGKNITLAALDRFTggSRIDDAaeLKTILESIQRLkvktaspelaiarLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 483 KTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRL-VIFATHRLHWLKEM-DYILVMHEGKLvqQGTF--DELTKE 554
Cdd:PRK13549 423 NP-KILILDEPTRGIDVGAKYEIYKLINQLVQQGVaIIVISSELPEVLGLsDRVLVMHEGKL--KGDLinHNLTQE 495
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
325-570 |
2.85e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 325 NSKSELKLENLEFNYNNQTE--IGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAATlNIPAWH 402
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSSpaVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 403 QQMLYIPQnpyvFTA-----SLRENIAFYTP-EASDAEIMKAIHVVSLDELvselpeGLDTIIGQGKRVLSGGQAQRIAL 476
Cdd:TIGR01257 2012 QNMGYCPQ----FDAiddllTGREHLYLYARlRGVPAEEIEKVANWSIQSL------GLSLYADRLAGTYSGGNKRKLST 2081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 477 ARAfLDKTRKVMLFDEPTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDELTKE 554
Cdd:TIGR01257 2082 AIA-LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHLKSK 2160
|
250
....*....|....*.
gi 543385153 555 AGYFTKLTQEMRGTKN 570
Cdd:TIGR01257 2161 FGDGYIVTMKIKSPKD 2176
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
348-498 |
2.98e-07 |
|
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: 51.67 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQkAATLNIP-AWHQQMLYIpqnpyvftasLRENIAFY 426
Cdd:COG4778 30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHD-GGWVDLAqASPREILAL----------RRRTIGYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 427 TpeasdaEIMKAIHVVSLDELVSE----LPEGLDTIIGQGKRVL-----------------SGGQAQRIALARAFLDKTR 485
Cdd:COG4778 99 S------QFLRVIPRVSALDVVAEplleRGVDREEARARARELLarlnlperlwdlppatfSGGEQQRVNIARGFIADPP 172
|
170
....*....|...
gi 543385153 486 kVMLFDEPTAHLD 498
Cdd:COG4778 173 -LLLLDEPTASLD 184
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-546 |
2.99e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 330 LKLENLEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPK-----SGKIIIDGQKAATLNIPAWHQQ 404
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 405 ----MLYIPQNPYVFTaSLRENIAF--------YTPEASDAEIMKAIHVVSLDElvsELPEGLDTIIGQgkrvLSGGQAQ 472
Cdd:PRK14267 85 revgMVFQYPNPFPHL-TIYDNVAIgvklnglvKSKKELDERVEWALKKAALWD---EVKDRLNDYPSN----LSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 473 RIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLMENRLVIFATHR-LHWLKEMDYILVMHEGKLVQQG 546
Cdd:PRK14267 157 RLVIARALAMKP-KILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
357-553 |
3.37e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 357 KVGIIGMSGSGKSTLINLLSGFLPPKSGKIIidgqKAATLNIPAWHQQmlyipqnpYVFTASLRENIAFYtpeasdaeIM 436
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTVF----RSAKVRMAVFSQH--------HVDGLDLSSNPLLY--------MM 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 437 KAIHVVSLDELVSELpeGLDTIIG----QGKRVLSGGQAQRIALARAFLDKTRkVMLFDEPTAHLDIETeVDLKKQMLPL 512
Cdd:PLN03073 597 RCFPGVPEQKLRAHL--GSFGVTGnlalQPMYTLSGGQKSRVAFAKITFKKPH-ILLLDEPSNHLDLDA-VEALIQGLVL 672
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 543385153 513 MENRlVIFATHRLHWLK-EMDYILVMHEGKLVQ-QGTFDELTK 553
Cdd:PLN03073 673 FQGG-VLMVSHDEHLISgSVDELWVVSEGKVTPfHGTFHDYKK 714
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
351-548 |
3.71e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.26 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 351 EIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKAAtlnipawhqqmlYIPQnpyvftaslreniafytpea 430
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------YKPQ-------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 431 sdaeimkaihvvsldelvselpegldtiigqgKRVLSGGQAQRIALARAFLdKTRKVMLFDEPTAHLDIETEVDLKKQML 510
Cdd:cd03222 69 --------------------------------YIDLSGGELQRVAIAAALL-RNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 543385153 511 PLMEN--RLVIFATHRLHWLKEMDYILVMHEGKLVQQGTF 548
Cdd:cd03222 116 RLSEEgkKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIA 155
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
356-551 |
4.78e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.03 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 356 EKVGIIGMSGSGKSTLINLLSGFLPPK---SGKIIIDGQKaaTLNIPAWH------QQMLYIPQ------NPYV-FTASL 419
Cdd:PRK09473 43 ETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGRE--ILNLPEKElnklraEQISMIFQdpmtslNPYMrVGEQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 420 RENIAFYTpEASDAEIMKAiHVVSLDELvsELPEGLdtiigqgKRV------LSGGQAQRIALARAFLDKTrKVMLFDEP 493
Cdd:PRK09473 121 MEVLMLHK-GMSKAEAFEE-SVRMLDAV--KMPEAR-------KRMkmypheFSGGMRQRVMIAMALLCRP-KLLIADEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 494 TAHLDieteVDLKKQMLPLME------NRLVIFATHRLHWLKEM-DYILVMHEGKLVQQGTFDEL 551
Cdd:PRK09473 189 TTALD----VTVQAQIMTLLNelkrefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDV 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
356-546 |
1.65e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 356 EKVGIIGMSGSGKSTLINLLSGFLPPKS--GKIIIDGQKAATLNIpawhQQMLYIPQNPYVFT-ASLRENIAFYTPEASD 432
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL----KRTGFVTQDDILYPhLTVRETLVFCSLLRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 433 AEIMKAIHVVSLDELVSELpeGL----DTIIGQG-KRVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKK 507
Cdd:PLN03211 171 KSLTKQEKILVAESVISEL--GLtkceNTIIGNSfIRGISGGERKRVSIAHEMLINP-SLLILDEPTSGLDATAAYRLVL 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 543385153 508 QMLPLMEN-RLVIFATH----RLHWLkeMDYILVMHEGKLVQQG 546
Cdd:PLN03211 248 TLGSLAQKgKTIVTSMHqpssRVYQM--FDSVLVLSEGRCLFFG 289
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
52-305 |
3.99e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 48.69 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 52 WQYLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIFKSGQSLVQSQGTGSLITMAlygIDEVrDYIKLIYT 131
Cdd:cd18778 40 LGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRV---INDV-ANVERLIA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 132 KVLAMMIIPILLF----IAMLFINWQsaLGLLLMYPLIVLFMIILGYAAK-----DRASKQFGDfqkLSNNFIDSLRGID 202
Cdd:cd18778 116 DGIPQGITNVLTLvgvaIILFSINPK--LALLTLIPIPFLALGAWLYSKKvrpryRKVREALGE---LNALLQDNLSGIR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 203 TLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQLPLYPALSILILAPEYF 282
Cdd:cd18778 191 EIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFY 270
|
250 260
....*....|....*....|...
gi 543385153 283 LPIRNFASDYHATLNGKNAFKRI 305
Cdd:cd18778 271 EPITSLHGLNEMLQRALAGAERV 293
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
331-393 |
5.27e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 5.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543385153 331 KLENLEFNY--NNqteigpVSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQKA 393
Cdd:PRK13545 30 RSKDGEYHYalNN------ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAA 88
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
466-554 |
6.62e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.20 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 466 LSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLM--ENRLVIFATHRLHWLKEM-DYILVMHEGKL 542
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRP-KLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEAaHKIIVMYAGQV 232
|
90
....*....|..
gi 543385153 543 VQQGTFDELTKE 554
Cdd:PRK11022 233 VETGKAHDIFRA 244
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
335-546 |
9.73e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 335 LEFNYNNQTEIGPVSVEIKGYEKVGIIGMSGSGKSTLINllsgflppksgkiiidgqkaatlnipawhqqmlyipqnpYV 414
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------------------------------EG 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 415 FTASLRENIAFYTPEASDAEImkaihvVSLDELVSELPEGLDTI-IGQGKRVLSGGQAQRIALAR-AFLDKTRKVMLFDE 492
Cdd:cd03238 42 LYASGKARLISFLPKFSRNKL------IFIDQLQFLIDVGLGYLtLGQKLSTLSGGELQRVKLASeLFSEPPGTLFILDE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 493 PTAHLDIETEVDLKKQMLPLM-ENRLVIFATHRLHWLKEMDYILVM------HEGKLVQQG 546
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
348-501 |
9.97e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 348 VSVEIKGYEKVGIIGMSGSGKSTLINLLSGFLPPKSGKIIID-GQKAATLN--------------IPAWHQQMLYIPQnp 412
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRqdqfafeeftvldtVIMGHTELWEVKQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 413 yvftaslrENIAFYT-PEASDAEIMKAIHVVS----LD---------ELVSEL--PE----GLDTIIGQGKRVlsggqaq 472
Cdd:PRK15064 98 --------ERDRIYAlPEMSEEDGMKVADLEVkfaeMDgytaearagELLLGVgiPEeqhyGLMSEVAPGWKL------- 162
|
170 180 190
....*....|....*....|....*....|
gi 543385153 473 RIALARA-FLDKtrKVMLFDEPTAHLDIET 501
Cdd:PRK15064 163 RVLLAQAlFSNP--DILLLDEPTNNLDINT 190
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
119-266 |
1.02e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 47.58 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 119 IDEVRDYikLIYTKVLAMMIIP--ILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYAAKdRASKQFGDFQKLSNNF-I 195
Cdd:cd18566 108 LEQIREF--LTGQALLALLDLPfvLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR-RALKERSRADERRQNFlI 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543385153 196 DSLRGIDTLKYLGLSKRYSKSIFRVSEdfrHKTMAVLKVAMLSTFALDFFTTLSIAVVAVYLGFG---LLNGQL 266
Cdd:cd18566 185 ETLTGIHTIKAMAMEPQMLRRYERLQA---NAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGallVINGDL 255
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
141-266 |
1.67e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 46.78 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 141 ILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKsifRV 220
Cdd:cd18568 130 FIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRW---RW 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 543385153 221 SEDFRHKTMAVLKVAMLS---TFALDFFTTLSIAVVaVYLGFGL-LNGQL 266
Cdd:cd18568 207 ENKFAKALNTRFRGQKLSivlQLISSLINHLGTIAV-LWYGAYLvISGQL 255
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
56-266 |
1.76e-05 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 46.67 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 56 LIFIVCLTGRQLIDLLKDKMLeTYSSQEVEK-LRQQLLNKIFKSGQSLVQSQGTGSLITMaLYGIDEVRDYIKLIYTKVL 134
Cdd:cd18570 46 IGLILLYLFQSLLSYIRSYLL-LKLSQKLDIrLILGYFKHLLKLPLSFFETRKTGEIISR-FNDANKIREAISSTTISLF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 135 AMMIIPILLFIAMLFINWQsaLGLLLMypLIVLFMIILGYAAKDRASKQFGDFQ----KLSNNFIDSLRGIDTLKYLGLS 210
Cdd:cd18570 124 LDLLMVIISGIILFFYNWK--LFLITL--LIIPLYILIILLFNKPFKKKNREVMesnaELNSYLIESLKGIETIKSLNAE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 543385153 211 KRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQL 266
Cdd:cd18570 200 EQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQL 255
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
52-266 |
3.41e-05 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 45.86 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 52 WQYLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIfksgQSL----VQSQGTGSLITMALYGIDEVRDYIK 127
Cdd:cd18547 45 LRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKL----QRLplsyFDTHSHGDIMSRVTNDVDNISQALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 128 LIYTKVLAMMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYaakdRASKQFGDFQKLS---NNFID-SLRGIDT 203
Cdd:cd18547 121 QSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAK----RSQKYFRKQQKALgelNGYIEeMISGQKV 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 204 LKYLGLSKrysksifRVSEDFRHKTMAVLKVAMLSTF-------ALDFFTTLSIAVVAVYLGFGLLNGQL 266
Cdd:cd18547 197 VKAFNREE-------EAIEEFDEINEELYKASFKAQFysgllmpIMNFINNLGYVLVAVVGGLLVINGAL 259
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
134-289 |
3.75e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 45.93 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 134 LAMMIIpilLFIAMLFINWQSALGLLLMYPLIVLFMI-----ILGYAAKDRA--SkqfgdfqKLSNNFIDSLRGIDTLKY 206
Cdd:cd18540 127 ITYMIG---ILIVMLILNWKLALIVLAVVPVLAVVSIyfqkkILKAYRKVRKinS-------RITGAFNEGITGAKTTKT 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 207 LGLSKRYSKSIFRVSEDFRHKTMavlKVAMLSTF---ALDFFTTLSIAVVAVYLGFGLLNGQLpLYPALSILI-LAPEYF 282
Cdd:cd18540 197 LVREEKNLREFKELTEEMRRASV---RAARLSALflpIVLFLGSIATALVLWYGGILVLAGAI-TIGTLVAFIsYATQFF 272
|
....*..
gi 543385153 283 LPIRNFA 289
Cdd:cd18540 273 EPIQQLA 279
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
360-497 |
3.87e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 360 IIGMSGSGKSTLINLLSGFLPPKS--GKIIIDGQKAATLNIPA--------WHQQMLYIPQnpyvftASLRENIaFYTPE 429
Cdd:NF040905 32 LCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDsealgiviIHQELALIPY------LSIAENI-FLGNE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543385153 430 AS-------DAEIMKA---IHVVSLDelvsELPEGLDTIIGQGKRvlsggqaQRIALARAfLDKTRKVMLFDEPTAHL 497
Cdd:NF040905 105 RAkrgvidwNETNRRArelLAKVGLD----ESPDTLVTDIGVGKQ-------QLVEIAKA-LSKDVKLLILDEPTAAL 170
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
360-535 |
4.23e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.91 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 360 IIGMSGSGKSTLINLLS----GFLPPKS------GKIIIDGQKAATLNIPAWHQQmlyipQNPYVFTASLR--ENIAFyt 427
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPNSkggahdPKLIREGEVRAQVKLAFENAN-----GKKYTITRSLAilENVIF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 428 peasdaeimkaihvVSLDELVSELPEGLDTiigqgkrvLSGGQ------AQRIALARAFLDKTRKVMLfDEPTAHLDIEt 501
Cdd:cd03240 100 --------------CHQGESNWPLLDMRGR--------CSGGEkvlaslIIRLALAETFGSNCGILAL-DEPTTNLDEE- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 543385153 502 evDLKKQMLPLME------NRLVIFATHRLHWLKEMDYIL 535
Cdd:cd03240 156 --NIEESLAEIIEerksqkNFQLIVITHDEELVDAADHIY 193
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
87-268 |
6.92e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 44.89 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 87 LRQQLLNKIFKSGQSLVQSQGTGSLITMaLYGIDEVRDYI-KLIYTKVLAMMIIPILLFIaMLFINWQSALGLLLMYPLI 165
Cdd:cd18782 77 LGGTIIDHLLRLPLGFFDKRPVGELSTR-ISELDTIRGFLtGTALTTLLDVLFSVIYIAV-LFSYSPLLTLVVLATVPLQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 166 VLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSkrySKSIFRVSEDFRHKTMAVLKVAMLSTFA---- 241
Cdd:cd18782 155 LLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAE---LKARWRWQNRYARSLGEGFKLTVLGTTSgsls 231
|
170 180
....*....|....*....|....*....
gi 543385153 242 --LDFFTTLSIAVVAVYLgfgLLNGQLPL 268
Cdd:cd18782 232 qfLNKLSSLLVLWVGAYL---VLRGELTL 257
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
125-278 |
1.94e-04 |
|
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: 43.62 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 125 YIKLIYTKVLAMMIIpILLFIAMLFINWQSALGLLLMYPLIVLFMIILGYAAKDRASKQFGDFQ-KLSNNFIDSLRGIDT 203
Cdd:cd18585 109 YLRVLSPPVVALLVI-LATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLGKKIGQQLVQLRaELRTELVDGLQGMAE 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543385153 204 LKYLGLSKRYSKSIFRVSEDF--RHKTMAVLKVamLSTFALDFFTTLSIAVVAVYLGFGLLNGQLPlYPALSILILA 278
Cdd:cd18585 188 LLIFGALERQRQQLEQLSDALikEQRRLARLSG--LSQALMILLSGLTVWLVLWLGAPLVQNGALD-GALLAMLVFA 261
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
325-391 |
1.95e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 1.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 325 NSKSELKlENLEFNYNNQTEIGPVSVEIKGYEK--VGIIGMSGSGKSTLINLLSGFLPPKSGKIIIDGQ 391
Cdd:PRK13546 19 TNKERMK-DALIPKHKNKTFFALDDISLKAYEGdvIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE 86
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
454-518 |
3.03e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 3.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543385153 454 GLDTI-IGQGKRVLSGGQAQRIALARaFLDK--TRKVM-LFDEPTA--HLDietevDLKKqmlpLME--NRLV 518
Cdd:COG0178 814 GLGYIkLGQPATTLSGGEAQRVKLAS-ELSKrsTGKTLyILDEPTTglHFH-----DIRK----LLEvlHRLV 876
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
134-266 |
7.66e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 41.71 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 134 LAMMIIPILLF----IAMLFINWQSALGLLLMYPLIVLFMII------LGY-AAKDRASKQFGDFQklsnnfiDSLRGID 202
Cdd:cd18546 117 LVQLVVSLLTLvgiaVVLLVLDPRLALVALAALPPLALATRWfrrrssRAYrRARERIAAVNADLQ-------ETLAGIR 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543385153 203 TLKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQL 266
Cdd:cd18546 190 VVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTL 253
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
131-267 |
8.92e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 41.39 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 131 TKVLAMMIIPILLFIA----MLFINWQSALGLLLMYPLIVLFMIILGYAAKdRASKQFGDFQKLSNNFID-SLRGIDTLK 205
Cdd:cd18557 111 TDNLSQLLRNILQVIGgliiLFILSWKLTLVLLLVIPLLLIASKIYGRYIR-KLSKEVQDALAKAGQVAEeSLSNIRTVR 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543385153 206 YLGlskRYSKSIFRvsedFRHKTMAVLKVAMLSTFAL-------DFFTTLSIAVVAVYLGFGLLNGQLP 267
Cdd:cd18557 190 SFS---AEEKEIRR----YSEALDRSYRLARKKALANalfqgitSLLIYLSLLLVLWYGGYLVLSGQLT 251
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
130-274 |
9.80e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 41.40 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 130 YTKVLAMMIIPILLFIAMLFINWQSALGLLLMYPLIVLFMIIlgYAAK-----DRASKQFGDFQ-KLSNNfidsLRGIDT 203
Cdd:cd18565 132 ANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYW--FQRRiepryRAVREAVGDLNaRLENN----LSGIAV 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543385153 204 LKYLGLSKRYSKSIFRVSEDFRHKTMAVLKVAMLSTFALDFFTTLSIAVVAVYLGFGLLNGQLPLYPALSI 274
Cdd:cd18565 206 IKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV 276
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
454-559 |
1.10e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 454 GLDTI-IGQGKRVLSGGQAQRIALARaFLDKT---RKVMLFDEPTAHLDIEtevDLKKqmlpLME--NRLV------IFA 521
Cdd:PRK00349 818 GLGYIkLGQPATTLSGGEAQRVKLAK-ELSKRstgKTLYILDEPTTGLHFE---DIRK----LLEvlHRLVdkgntvVVI 889
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 543385153 522 THRLHWLKEMDYILVM------HEGKLVQQGTFDELTKEAGYFT 559
Cdd:PRK00349 890 EHNLDVIKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEASYT 933
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
357-377 |
1.16e-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: 38.75 E-value: 1.16e-03
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
86-292 |
1.22e-03 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 40.91 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 86 KLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYIKLIYTKVLAMMIIPILLFIAMLFINWQSALGLLLMYPLI 165
Cdd:cd18545 74 DLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 166 VLFMIILGYAAKdRASKQFGdfQKLSN---NFIDSLRGIDTLKYLGlSKRYSKSIF-RVSEDFRHKTMAVLKVAMLSTFA 241
Cdd:cd18545 154 VLVVFLLRRRAR-KAWQRVR--KKISNlnaYLHESISGIRVIQSFA-REDENEEIFdELNRENRKANMRAVRLNALFWPL 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 543385153 242 LDFFTTLSIAVVAVYLGFGLLNGQLPLYPALSILILAPEYFLPIRNFASDY 292
Cdd:cd18545 230 VELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFY 280
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
86-245 |
1.72e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 40.54 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 86 KLRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYI--KL-IYTKVLAMMIIpiLLFIAMLFiNWQSALGLLLMY 162
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIgeKLgLLIQSLSTFIA--GFIIAFIY-SWKLTLVLLATL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 163 PLIVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLG----LSKRYSKSIFRVSEDFRHK------TMAVL 232
Cdd:cd18577 158 PLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGgeekEIKRYSKALEKARKAGIKKglvsglGLGLL 237
|
170
....*....|...
gi 543385153 233 KVAMLSTFALDFF 245
Cdd:cd18577 238 FFIIFAMYALAFW 250
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
464-554 |
1.91e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 464 RVLSGGQAQRIALARAFLDKTrKVMLFDEPTAHLDIETEVDLKKQMLPLmeNRLVIFATHRLHWLKE-MDYILVMHEGKL 542
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEP-DLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSHAREFLNTvVTDILHLHGQKL 419
|
90
....*....|....*
gi 543385153 543 VQ-QGTFD--ELTKE 554
Cdd:PLN03073 420 VTyKGDYDtfERTRE 434
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
351-501 |
2.62e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 351 EIKGYEKVGII----GMSGSGKSTLINLLSGflpPKSGKIIIDG---------QKAATLNIPAWHQQMLYIPQ----NPY 413
Cdd:TIGR00956 781 NVDGWVKPGTLtalmGASGAGKTTLLNVLAE---RVTTGVITGGdrlvngrplDSSFQRSIGYVQQQDLHLPTstvrESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 414 VFTASLREniafyTPEASDAEIMKaiHVVSLDELVsELPEGLDTIIGQGKRVLSGGQAQRIALARAFLDKTRKVMLFDEP 493
Cdd:TIGR00956 858 RFSAYLRQ-----PKSVSKSEKME--YVEEVIKLL-EMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFLDEP 929
|
....*...
gi 543385153 494 TAHLDIET 501
Cdd:TIGR00956 930 TSGLDSQT 937
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
87-266 |
2.70e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 40.16 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 87 LRQQLLNKIFKSGQSLVQSQGTGSLITMALYGIDEVRDYIkliyTKVLAMMIIPILLFIA----MLFINWQSALGLLLMY 162
Cdd:cd18576 71 LRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTL----TTTLAEFLRQILTLIGgvvlLFFISWKLTLLMLATV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 163 PLIVLFMIILGYAAKdRASKQFGDFQKLSNNFID-SLRGIDTLKYLG----LSKRYSKSIfrvsEDFRHKTMAVLKV-AM 236
Cdd:cd18576 147 PVVVLVAVLFGRRIR-KLSKKVQDELAEANTIVEeTLQGIRVVKAFTredyEIERYRKAL----ERVVKLALKRARIrAL 221
|
170 180 190
....*....|....*....|....*....|
gi 543385153 237 LSTFaLDFFTTLSIAVVAVYLGFGLLNGQL 266
Cdd:cd18576 222 FSSF-IIFLLFGAIVAVLWYGGRLVLAGEL 250
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
29-260 |
3.20e-03 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 39.72 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 29 LIIGQALSLSAVLTTLWQ------------GKKLNWQYLLIFIVCLTGRQLIDLLKDKMLETYSSQEVEKLRQQLLNKIF 96
Cdd:cd18551 1 LILALLLSLLGTAASLAQpllvknlidalsAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 97 KSGQSLVQSQGTGSLITMALYGIDEVRDYIkliyTKVLAMMIIPILLFIA----MLFINWQSALGLLLMYPLIVLFMIIL 172
Cdd:cd18551 81 RLPVSFFDRRRSGDLVSRVTNDTTLLRELI----TSGLPQLVTGVLTVVGavvlMFLLDWVLTLVTLAVVPLAFLIILPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 173 G---YAAKDRASKQFGDFqklSNNFIDSLRGIDTLKYLGLSKRYSKsifRVSEDFRHKTMAVLKVAMLSTFALDFFTTLS 249
Cdd:cd18551 157 GrriRKASKRAQDALGEL---SAALERALSAIRTVKASNAEERETK---RGGEAAERLYRAGLKAAKIEALIGPLMGLAV 230
|
250
....*....|.
gi 543385153 250 IAVVAVYLGFG 260
Cdd:cd18551 231 QLALLVVLGVG 241
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
87-258 |
4.76e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 39.30 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 87 LRQQLLNKIfksgQSL----VQSQGTGSLITmalygidevR-----DYIKLIYTKVLAMMII-PILLFIAM---LFINWQ 153
Cdd:cd18548 74 LRKDLFEKI----QSFsfaeIDKFGTSSLIT---------RltndvTQVQNFVMMLLRMLVRaPIMLIGAIimaFRINPK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543385153 154 SALGLLLMYPLIVLFMIILGYAAKDRASKQFGDFQKLSNNFIDSLRGIDTLKYLGLSKRYSKSIFRVSEDFRHKTMAVLK 233
Cdd:cd18548 141 LALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGR 220
|
170 180
....*....|....*....|....*
gi 543385153 234 VAMLSTFALDFFTTLSIAVVaVYLG 258
Cdd:cd18548 221 LMALLNPLMMLIMNLAIVAI-LWFG 244
|
|
| |
