|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-561 |
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: 669.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 2 IDKRLFKL-PGIKPLFKMLAGLTVLQAFMILFQAIFLAKVLVLSW-QRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLD 79
Cdd:COG4988 4 LDKRLKRLaRGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 80 RYATKTTEDLRQKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIV 159
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 160 LVLVFPIIILFMIILGYAAKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAIL 239
Cdd:COG4988 164 LLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 240 STFALDWFTTLSIAILAVFLGLALMNGTLPLYPALVTLILAPEYFLPLRDFASDYHATLNGKNAFQQTLDILAIPTVTDR 319
Cdd:COG4988 244 SSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 320 TLLPAFTWNEQSRLTIQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQL 399
Cdd:COG4988 324 AGTAPLPAAGPPSIELEDVSFSYPG--GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 400 PHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQR 479
Cdd:COG4988 402 SDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 480 IMLARAFLvQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQ 559
Cdd:COG4988 482 LALARALL-RDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560
|
..
gi 2468565974 560 KQ 561
Cdd:COG4988 561 KN 562
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-543 |
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: 541.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 12 IKPLFKMLAGLTVLQAFMILFQAIFLAKVLVLSWQRK-GLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLR 90
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGePLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 91 QKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLVLVFPIIILF 170
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 171 MIILGYAAKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTL 250
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 251 SIAILAVFLGLALMNGTLPLYPALVTLILAPEYFLPLRDFASDYHATLNGKNAFQQTLDILAIPTVTDRTLLPAfTWNEQ 330
Cdd:TIGR02857 241 SVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPV-TAAPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 331 SRLTIQHLNFQYDDTMdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ 410
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLvQQ 490
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFL-RD 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 491 RHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVL 543
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-571 |
1.01e-120 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 368.79 E-value: 1.01e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 12 IKPLFKMLAGLTVLQAFMILFQAIFLAKVL-VLSWQRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLR 90
Cdd:PRK11174 20 AKRWLNLSILLGFLSGLLLIAQAWLLATILqALIIENIPREALLPPFILLILLFVLRALLAWLRERVGFKAGQHIRQQIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 91 QKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLVLVFPIIILF 170
Cdd:PRK11174 100 QQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTAPLIPLF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 171 MIILGYAAKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTL 250
Cdd:PRK11174 180 MALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 251 SIAILAVFLGLALMN--------GTLPLYPALVTLILAPEYFLPLRDFASDYHATLNGKNAFQQTLDILAIPTVTDRTLL 322
Cdd:PRK11174 260 SIALVAVYFGFSYLGelnfghygTGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 323 PAFTWNEQSRLTIQHLN-FQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFvIPQTGNIQLNGHQLPH 401
Cdd:PRK11174 340 KELASNDPVTIEAEDLEiLSPDG---KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 402 LAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIM 481
Cdd:PRK11174 416 LDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLA 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQlLQKQ 561
Cdd:PRK11174 496 LARA-LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAE-LSQA 573
|
570
....*....|
gi 2468565974 562 HGPFFELTSH 571
Cdd:PRK11174 574 GGLFATLLAH 583
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-568 |
1.04e-114 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 352.93 E-value: 1.04e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 4 KRLFK-LPGIKPLFKMLAGLTVLQAFMILFQAIFLAKVLVLSWQRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYA 82
Cdd:COG1132 10 RRLLRyLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 83 TKTTEDLRQKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLVL 162
Cdd:COG1132 90 QRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 163 VFPIIILFMIILGYAAKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTF 242
Cdd:COG1132 170 VLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 243 ALDWFTTLSIAILAVFLGLALMNGTLPLyPALVTLILAPEYFL-PLRDFASDYHATLNGKNAFQQTLDILAIP-TVTDRT 320
Cdd:COG1132 250 LMELLGNLGLALVLLVGGLLVLSGSLTV-GDLVAFILYLLRLFgPLRQLANVLNQLQRALASAERIFELLDEPpEIPDPP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 321 LLPAFTwNEQSRLTIQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLP 400
Cdd:COG1132 329 GAVPLP-PVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 401 HLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRI 480
Cdd:COG1132 406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 481 MLARAFLvQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQk 560
Cdd:COG1132 486 AIARALL-KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA- 563
|
....*...
gi 2468565974 561 QHGPFFEL 568
Cdd:COG1132 564 RGGLYARL 571
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
19-306 |
8.31e-107 |
|
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: 322.44 E-value: 8.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 19 LAGLTVLQAFMILFQAIFLAKVLVLSW-QRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLAQV 97
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFlEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 98 YTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLVLVFPIIILFMIILGYA 177
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 178 AKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTLSIAILAV 257
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2468565974 258 FLGLALMNGTLPLYPALVTLILAPEYFLPLRDFASDYHATLNGKNAFQQ 306
Cdd:cd18584 241 YIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAER 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-568 |
8.57e-98 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 312.92 E-value: 8.57e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 18 MLAGL--TVLQAFMILFQAIFLAKVLVlswqRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLA 95
Cdd:COG2274 162 LLASLliNLLALATPLFTQVVIDRVLP----NQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 96 QVYTTGAAMIAQKGSGNIVTNALDgMDEVNNYF-NLILSKFMNMMIIpWILLVYIFWQNLTSGIVLVLVFPIIILFMIIL 174
Cdd:COG2274 238 HLLRLPLSFFESRSVGDLASRFRD-VESIREFLtGSLLTALLDLLFV-LIFLIVLFFYSPPLALVVLLLIPLYVLLGLLF 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 175 GYAAKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTLSIAI 254
Cdd:COG2274 316 QPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 255 LAVFLGLALMNGTLPL-----YPALVTLILAPeyFLPLRDFASDYHATlngKNAFQQTLDILAIPTVTDRTLLPAFTWNE 329
Cdd:COG2274 396 LLWLGAYLVIDGQLTLgqliaFNILSGRFLAP--VAQLIGLLQRFQDA---KIALERLDDILDLPPEREEGRSKLSLPRL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 330 QSRLTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQ 409
Cdd:COG2274 471 KGDIELENVSFRYPGDSPPV-LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 410 QFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQ 489
Cdd:COG2274 550 QIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARA-LLR 628
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 490 QRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQhGPFFEL 568
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARK-GLYAEL 706
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
76-571 |
1.58e-96 |
|
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: 305.54 E-value: 1.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 76 RLLDRYAT-----KTTEDLRQKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFnLILskfmnmmIIPWI--LLVY 148
Cdd:COG4987 72 RYLERLVShdatlRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLY-LRV-------LLPLLvaLLVI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 149 IF------WQNLTSGIVLVLVFPIIILFMIILGYAAKDKASSQYAEY-VVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQ 221
Cdd:COG4987 144 LAavaflaFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAArAALRARLTDLLQGAAELAAYGALDRALARLDA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 222 VSENYRKKTLSTLRIAILSTFALDWFTTLSIAILAVFLGLALMNGTLPLyPALVTLILAP----EYFLPLRDFASdyhat 297
Cdd:COG4987 224 AEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSG-PLLALLVLAAlalfEALAPLPAAAQ----- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 298 lngknAFQQTLD----ILAIPTVTDRTLLPA--FTWNEQSRLTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSG 371
Cdd:COG4987 298 -----HLGRVRAaarrLNELLDAPPAVTEPAepAPAPGGPSLELEDVSFRYPGAGRPV-LDGLSLTLPPGERVAIVGPSG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 372 AGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLA 451
Cdd:COG4987 372 SGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 452 KFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLvQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRL 531
Cdd:COG4987 452 DWLAALPDGLDTWLGEGGRRLSGGERRRLALARALL-RDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRL 530
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2468565974 532 HWLEQMDYVLVLDNGKIAEQGPVKQLLQkQHGPFFELTSH 571
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELLA-QNGRYRQLYQR 569
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
333-547 |
8.90e-62 |
|
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: 201.46 E-value: 8.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV-LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSDTIANNIrfyqptasneevqqameqaglakfiatlpqglqtrvgeagrgISGGQAQRIMLARAFLvQQRH 492
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALL-RDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 493 ILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGK 547
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
333-568 |
4.69e-61 |
|
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: 201.69 E-value: 4.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV-LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLVQQRh 492
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 493 ILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLqKQHGPFFEL 568
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL-AQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
337-568 |
2.18e-60 |
|
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: 200.15 E-value: 2.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 337 HLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQ 416
Cdd:cd03253 5 NVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 417 KPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLVQQRhILIF 496
Cdd:cd03253 83 DTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP-ILLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 497 DEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKqHGPFFEL 568
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEM 232
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
144-564 |
1.19e-58 |
|
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: 207.80 E-value: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 144 ILLVYIFWqnltSGIVLVLVFPIIILFMIILGYAAK---DKASSQYAEYVVLSNHFL-DALRGLTTLKMLGLSKEYTHNI 219
Cdd:TIGR03375 275 LFLLVIAI----IGGPLVWVPLVAIPLILLPGLLLQrplSRLAEESMRESAQRNAVLvESLSGLETIKALNAEGRFQRRW 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 220 YQVSE-----NYRKKTLSTLriAILSTFALDWFTTLSIAILAVFLglaLMNGTLPLyPALV-TLILAPEYFLPLRDFAS- 292
Cdd:TIGR03375 351 EQTVAalarsGLKSRFLSNL--ATNFAQFIQQLVSVAIVVVGVYL---ISDGELTM-GGLIaCVMLSGRALAPLGQLAGl 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 293 --DYHATlngKNAFQQTLDILAIPT--VTDRTLLpaftwneqSRLTIQH------LNFQYDDtMDQVNLKDLNLTLQGYE 362
Cdd:TIGR03375 425 ltRYQQA---KTALQSLDELMQLPVerPEGTRFL--------HRPRLQGeiefrnVSFAYPG-QETPALDNVSLTIRPGE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 363 RVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQ 442
Cdd:TIGR03375 493 KVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEIL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 443 QAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH 522
Cdd:TIGR03375 573 RAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARA-LLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK 651
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2468565974 523 LVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQHGP 564
Cdd:TIGR03375 652 TLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLEALRKG 693
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
82-531 |
8.00e-58 |
|
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: 202.21 E-value: 8.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 82 ATKTTEDLRQKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLV 161
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 162 LVFPIIILFM-IILGYAAKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILS 240
Cdd:TIGR02868 161 AGLLLAGFVApLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 241 TFALDWFTTLSIAILAVFLGLALMNGTLPlYPALVTLILAP----EYFLPLRDfASDYHATlnGKNAFQQTLDIL----- 311
Cdd:TIGR02868 241 AALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPlaafEAFAALPA-AAQQLTR--VRAAAERIVEVLdaagp 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 312 -AIPTV-TDRTLLPaftwnEQSRLTIQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQT 389
Cdd:TIGR02868 317 vAEGSApAAGAVGL-----GKPTLELRDLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 390 GNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAG 469
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 470 RGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRL 531
Cdd:TIGR02868 470 ARLSGGERQRLALARA-LLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
331-560 |
1.58e-57 |
|
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: 192.44 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 331 SRLTIQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ 410
Cdd:cd03254 1 GEIEFENVNFSYDE--KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQ 490
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARA-MLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 491 RHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
332-552 |
8.73e-57 |
|
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: 190.11 E-value: 8.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 332 RLTIQHLNFQYDDtMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQF 411
Cdd:cd03245 2 RIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLvQQR 491
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL-NDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 492 HILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQG 552
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
334-568 |
1.45e-56 |
|
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: 190.06 E-value: 1.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 334 TIQHLNFQYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTY 413
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 414 LPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHI 493
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARA-LLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 494 LIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLqKQHGPFFEL 568
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM-AQKGVYAKL 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
144-571 |
2.56e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 193.50 E-value: 2.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 144 ILLVYIF--WQN----LTSGIVLVLVFPIIILFMIILGYAAKDKASSQYAEYVVLsnhFLDALRGLTTLKMLGLSKEYTH 217
Cdd:PRK11160 148 ILVLTIGlsFFDltlaLTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQ---LTEWLQGQAELTLFGAEDRYRQ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 218 NIYQVSENYRKktlSTLRIAILstfaldwfTTLSIAILAVFLGLALMngtlplypalVTLILA---------PEYFLPLR 288
Cdd:PRK11160 225 QLEQTEQQWLA---AQRRQANL--------TGLSQALMILANGLTVV----------LMLWLAaggvggnaqPGALIALF 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 289 DFAS----DYHATLNGknAFQQTLDILA----IPTVTDRTLLPAFTWNEQSR-----LTIQHLNFQYDDTMDQVnLKDLN 355
Cdd:PRK11160 284 VFAAlaafEALMPVAG--AFQHLGQVIAsarrINEITEQKPEVTFPTTSTAAadqvsLTLNNVSFTYPDQPQPV-LKGLS 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 356 LTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQPT 435
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPN 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 436 ASNEEVQQAMEQAGLAKFIATlPQGLQTRVGEAGRGISGGQAQRIMLARAFLvQQRHILIFDEPTAHLDIETEYALKKTM 515
Cdd:PRK11160 441 ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALL-HDAPLLLLDEPTEGLDAETERQILELL 518
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 516 VQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQhGPFFELTSH 571
Cdd:PRK11160 519 AEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQ-GRYYQLKQR 573
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-571 |
3.31e-54 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 195.73 E-value: 3.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 17 KMLAGLTVLQAFMILFQAI----FLAKVLVLSWQRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQK 92
Cdd:TIGR01193 155 KKLIVNIVIAAIIVTLISIagsyYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 93 LLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFwQNLTSGIVLVLVFPIIILFMI 172
Cdd:TIGR01193 235 YIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVR-QNMLLFLLSLLSIPVYAVIII 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 173 ILGYAAKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLsTLRIAILSTFALDWFTTLSI 252
Cdd:TIGR01193 314 LFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSF-KYQKADQGQQAIKAVTKLIL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 253 AILAVFLGLAL-MNGTLPL-----YPALVTlilapeYFL-PLRDFASDYHATLNGKNAFQQTLDILAIPTVTDRTLLPAF 325
Cdd:TIGR01193 393 NVVILWTGAYLvMRGKLTLgqlitFNALLS------YFLtPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 326 TWNEQSRLTIQHLNFQYDdtMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQD 405
Cdd:TIGR01193 467 LNNLNGDIVINDVSYSYG--YGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 406 QWQQQFTYLPQKPYLFSDTIANNIRF-YQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLAR 484
Cdd:TIGR01193 545 TLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALAR 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 485 AFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLfEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLqKQHGP 564
Cdd:TIGR01193 625 ALLTDSK-VLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGF 701
|
....*..
gi 2468565974 565 FFELTSH 571
Cdd:TIGR01193 702 YASLIHN 708
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
332-553 |
9.18e-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: 179.23 E-value: 9.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 332 RLTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQF 411
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPV-LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSDTIANNIRFYQpTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQR 491
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA-LLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 492 HILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGP 553
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 ... |
25-561 |
8.84e-52 |
|
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: 188.80 E-value: 8.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 25 LQAFMI----LFQAIfLAKVLVlswqRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLAQVYTT 100
Cdd:TIGR01846 151 LQLFALvtplLFQVV-IDKVLV----HRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 101 GAAMIAQKGSGNIVTNaldgMDEVNNYFNLILSKFMNMMIIPWILLVYI---FWQNLTSGIVLVLVFPIIILFMIILGYA 177
Cdd:TIGR01846 226 PLGYFESRRVGDTVAR----VRELEQIRNFLTGSALTVVLDLLFVVVFLavmFFYSPTLTGVVIGSLVCYALLSVFVGPI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 178 AKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTLSIAILAV 257
Cdd:TIGR01846 302 LRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLW 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 258 F-----LGLALMNGTLPLYPALVTLILAPeyFLPLRDFASDYHATLNgknAFQQTLDILAIPTVTDRTLLPAFTwNEQSR 332
Cdd:TIGR01846 382 FgahlvIGGALSPGQLVAFNMLAGRVTQP--VLRLAQLWQDFQQTGI---ALERLGDILNSPTEPRSAGLAALP-ELRGA 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEV-LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLVQQRh 492
Cdd:TIGR01846 535 VVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPR- 613
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 493 ILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
312-564 |
8.14e-50 |
|
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: 181.10 E-value: 8.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 312 AIPTVTDRTLLPAftwnEQSRLTIQHLNFQYDDTmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGN 391
Cdd:COG4618 314 AVPAEPERMPLPR----PKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 392 IQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNI-RFYQPTAsnEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGR 470
Cdd:COG4618 389 VRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFGDADP--EKVVAAAKLAGVHEMILRLPDGYDTRIGEGGA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 471 GISGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQMDYVLVLDNGKIA 549
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPR-LVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
250
....*....|....*
gi 2468565974 550 EQGPVKQLLQKQHGP 564
Cdd:COG4618 546 AFGPRDEVLARLARP 560
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
330-560 |
2.46e-49 |
|
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: 179.90 E-value: 2.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 330 QSRLTIQHLNFQYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQ 409
Cdd:TIGR02204 335 RGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 410 QFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQ 489
Cdd:TIGR02204 415 RMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARA-ILK 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 490 QRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:TIGR02204 494 DAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
336-561 |
1.00e-48 |
|
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: 178.86 E-value: 1.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 336 QHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLP 415
Cdd:COG5265 361 ENVSFGYDP--ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 416 QKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLVQQRhILI 495
Cdd:COG5265 439 QDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPP-ILI 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 496 FDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQG 583
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
333-560 |
4.10e-48 |
|
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: 167.66 E-value: 4.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:cd03252 1 ITFEHVRFRYKPDGPVI-LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRH 492
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARA-LIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 493 ILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
333-552 |
3.80e-45 |
|
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: 157.47 E-value: 3.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHqLPHLAQDQWQQQFT 412
Cdd:cd03247 1 LSINNVSFSYPEQEQQV-LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV-PVSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSDTIANNIrfyqptasneevqqameqaglakfiatlpqglqtrvgeaGRGISGGQAQRIMLARAfLVQQRH 492
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARI-LLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 493 ILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQG 552
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
56-560 |
3.53e-44 |
|
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: 164.83 E-value: 3.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 56 LAGAFFLAFLGrhGLTWIKNRLLDRYATKTTEDLRQKLLAQVYTTGAAMIAQKGSgnivtNALDGMDEVNNYFN-LILSK 134
Cdd:TIGR01842 50 VLALGLYLFLG--LLDALRSFVLVRIGEKLDGALNQPIFAASFSATLRRGSGDGL-----QALRDLDQLRQFLTgPGLFA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 135 FMNmmiIPW--ILLVYIFWQNLTSGIvLVLVFPIIILFMIILGYAAKDKASSQYAEYVVLSNHFLD-ALRGLTTLKMLGL 211
Cdd:TIGR01842 123 FFD---APWmpIYLLVCFLLHPWIGI-LALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADsALRNAEVIEAMGM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 212 SKEYTHNIYQVSENYRKKTLSTL-RIAILSTFALDWFTTLSIAILAVFLGLALMN----GTLPLYPALVTLILAPeyflp 286
Cdd:TIGR01842 199 MGNLTKRWGRFHSKYLSAQSAASdRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGeitpGMMIAGSILVGRALAP----- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 287 LRDFASDYHATLNGKNAFQQTLDILA-IPTVTDRTLLPaftwNEQSRLTIQHLNFQYDDTmDQVNLKDLNLTLQGYERVA 365
Cdd:TIGR01842 274 IDGAIGGWKQFSGARQAYKRLNELLAnYPSRDPAMPLP----EPEGHLSVENVTIVPPGG-KKPTLRGISFSLQAGEALA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 366 IIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLphlaqDQWQQQF-----TYLPQKPYLFSDTIANNIRFYQPTASNEE 440
Cdd:TIGR01842 349 IIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL-----KQWDRETfgkhiGYLPQDVELFPGTVAENIARFGENADPEK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 441 VQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLFE 520
Cdd:TIGR01842 424 IIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPK-LVVLDEPNSNLDEEGEQALANAIKALKA 502
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2468565974 521 HHL-VLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:TIGR01842 503 RGItVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
330-548 |
1.18e-43 |
|
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: 155.32 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 330 QSRLTIQHLNFQYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQ 409
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 410 QFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQ 489
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA-LIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 490 QRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKI 548
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
333-561 |
1.21e-42 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 161.34 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDdTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:PRK11176 342 IEFRNVTFTYP-GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSDTIANNIRF-YQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQR 491
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARA-LLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 492 HILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
314-559 |
3.91e-42 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 159.49 E-value: 3.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 314 PTVTDRTL-LPAftwnEQSRLTIQHLNFQYDDTmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNI 392
Cdd:PRK10789 298 PVVKDGSEpVPE----GRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 393 QLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGI 472
Cdd:PRK10789 373 RFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVML 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 473 SGGQAQRIMLARAFLVQQrHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQG 552
Cdd:PRK10789 453 SGGQKQRISIARALLLNA-EILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRG 531
|
....*..
gi 2468565974 553 PVKQLLQ 559
Cdd:PRK10789 532 NHDQLAQ 538
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
17-303 |
1.30e-40 |
|
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: 148.97 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 17 KMLAGLTVLQAFMIlfQAIFLAKVLVLSWQRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLAQ 96
Cdd:cd18561 1 SVLLGLLITALYIA--QAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 97 VYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLVLVFPIIILFMIILGY 176
Cdd:cd18561 79 LLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 177 AAKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTLSIAILA 256
Cdd:cd18561 159 LAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALAL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2468565974 257 VFLGLALMNGTLPLYPALVTLILAPEYFLPLRDFASDYHATLNGKNA 303
Cdd:cd18561 239 GVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
333-548 |
2.60e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 145.34 E-value: 2.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:COG4619 1 LELEGLSFRVGG---KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSDTIANNIRFY----QPTASNEEVQQAMEQAGLAKFIatlpqgLQTRVGEagrgISGGQAQRIMLARAfLV 488
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPfqlrERKFDRERALELLERLGLPPDI------LDKPVER----LSGGERQRLALIRA-LL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 489 QQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQM-DYVLVLDNGKI 548
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
333-560 |
4.66e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 145.59 E-value: 4.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQdQWQQQFT 412
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRFYQ------PTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARA 485
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFArlyglpRKEARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 486 fLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:COG1131 146 -LLHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
329-561 |
1.03e-39 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 152.95 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 329 EQSRLTIQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ 408
Cdd:PRK10790 337 QSGRIDIDNVSFAYRD--DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 QQFTYLPQKPYLFSDTIANNIRFYQPTaSNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLV 488
Cdd:PRK10790 415 QGVAMVQQDPVVLADTFLANVTLGRDI-SEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV-LV 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 489 QQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-547 |
3.40e-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: 142.22 E-value: 3.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVN--LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHqlphlaqdqwqqq 410
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKPYLFSDTIANNIRFYQPTaSNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLvQQ 490
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPF-DEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY-SD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 491 RHILIFDEPTAHLDIETEyalkktmVQLFEH----HL-----VLFATHRLHWLEQMDYVLVLDNGK 547
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVG-------RHIFENcilgLLlnnktRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
328-561 |
4.35e-38 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 149.49 E-value: 4.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 328 NEQSRLTIQHLNFQYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQW 407
Cdd:TIGR00958 474 NLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 408 QQQFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfL 487
Cdd:TIGR00958 554 HRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARA-L 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 488 VQQRHILIFDEPTAHLDIETEYALKKTMVqlFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
89-568 |
6.36e-38 |
|
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: 150.10 E-value: 6.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 89 LRQKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFwqnLTSGIVLVLVFPIII 168
Cdd:TIGR00957 1040 LHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVIL---LATPIAAVIIPPLGL 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 169 LFMIILGYAAKDKASSQYAEYVVLS---NHFLDALRGLTTLKMLGLSKEYTH-NIYQVSENYRKKTLSTLriailstfAL 244
Cdd:TIGR00957 1117 LYFFVQRFYVASSRQLKRLESVSRSpvySHFNETLLGVSVIRAFEEQERFIHqSDLKVDENQKAYYPSIV--------AN 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 245 DWfttLSIAI------LAVFLGLALMNGTLPLYPALVTLILA-----PEYFLPLRDFASDYHATLNGKNAFQQTLDI-LA 312
Cdd:TIGR00957 1189 RW---LAVRLecvgncIVLFAALFAVISRHSLSAGLVGLSVSyslqvTFYLNWLVRMSSEMETNIVAVERLKEYSETeKE 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 313 IPTVTDRTLLPAfTWNEQSRLTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNI 392
Cdd:TIGR00957 1266 APWQIQETAPPS-GWPPRGRVEFRNYCLRYREDLDLV-LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 393 QLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQpTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGI 472
Cdd:TIGR00957 1344 IIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFS-QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENL 1422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 473 SGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLeqMDY--VLVLDNGKIAE 550
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTK-ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI--MDYtrVIVLDKGEVAE 1499
|
490
....*....|....*...
gi 2468565974 551 QGPVKQLLQkQHGPFFEL 568
Cdd:TIGR00957 1500 FGAPSNLLQ-QRGIFYSM 1516
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
332-562 |
7.83e-38 |
|
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: 140.18 E-value: 7.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 332 RLTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQF 411
Cdd:COG1120 1 MLEAENLSVGYGGR--PV-LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYL-FSDTIANNI---------RFYQPTASNEE-VQQAMEQAGLAKFIatlpqglQTRVGEagrgISGGQAQRI 480
Cdd:COG1120 78 AYVPQEPPApFGLTVRELValgryphlgLFGRPSAEDREaVEEALERTGLEHLA-------DRPVDE----LSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 481 MLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRL-HWLEQMDYVLVLDNGKIAEQGPVKQL 557
Cdd:COG1120 147 LIARA-LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEV 225
|
....*
gi 2468565974 558 LQKQH 562
Cdd:COG1120 226 LTPEL 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
304-568 |
1.18e-37 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 147.03 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 304 FQQTLDilAIPTVTDRTLLPAFTwNEQSRLTIQHLNFQYDDTMDQVnlKDLNLTLQGYERVAIIGQSGAGKSTLLEALSG 383
Cdd:PRK13657 309 FFEVED--AVPDVRDPPGAIDLG-RVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 384 FVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLQT 463
Cdd:PRK13657 384 VFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDT 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 464 RVGEAGRGISGGQAQRIMLARAFLvQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVL 543
Cdd:PRK13657 464 VVGERGRQLSGGERQRLAIARALL-KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVF 542
|
250 260
....*....|....*....|....*
gi 2468565974 544 DNGKIAEQGPVKQLLQKQhGPFFEL 568
Cdd:PRK13657 543 DNGRVVESGSFDELVARG-GRFAAL 566
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
333-567 |
9.76e-37 |
|
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: 136.91 E-value: 9.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAqDQWQQQFT 412
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRFY------QPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARA 485
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFaelyglFDEELKKRIEELIELLGLEEFLDRRVGEL-----------STGMKKKVALARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 486 fLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQKQHG 563
Cdd:COG4555 147 -LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIGE 225
|
....
gi 2468565974 564 PFFE 567
Cdd:COG4555 226 ENLE 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
333-561 |
2.31e-36 |
|
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: 135.54 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKP--YLFSDTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLAR 484
Cdd:COG1122 79 LVFQNPddQLFAPTVEEDVAFgpenlgLPREEIRERVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 485 AfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:COG1122 148 V-LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
351-501 |
3.66e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.00 E-value: 3.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSD-TIANNI 429
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 430 RF------YQPTASNEEVQQAMEQAGLAKFIAtlpqglqTRVGEAGRGISGGQAQRIMLARAFLVQQRhILIFDEPTA 501
Cdd:pfam00005 81 RLglllkgLSKREKDARAEEALEKLGLGDLAD-------RPVGERPGTLSGGQRQRVAIARALLTKPK-LLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
333-548 |
4.61e-35 |
|
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: 130.03 E-value: 4.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSDTIANNIrfyqptasneevqqameqaglakfiatlpqglqtrvgeagrgISGGQAQRIMLARAfLVQQRH 492
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARA-LYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 493 ILIFDEPTAHLDIETEYALKKTMVQLFEHHL-VLFATHRLHWLEQMDYVLVLDNGKI 548
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGAtRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
333-559 |
5.98e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.42 E-value: 5.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdqvnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDqwQQQFT 412
Cdd:COG3840 2 LRLDDLTYRYGDF-----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRF-----YQPTASN-EEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARA 485
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLglrpgLKLTAEQrAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 486 fLVQQRHILIFDEPTAHLDIeteyALKKTMVQLF-----EHHL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLL 558
Cdd:COG3840 144 -LVRKRPILLLDEPFSALDP----ALRQEMLDLVdelcrERGLtVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALL 218
|
.
gi 2468565974 559 Q 559
Cdd:COG3840 219 D 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
334-552 |
8.39e-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: 129.48 E-value: 8.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 334 TIQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTY 413
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 414 LPqkpylfsdtiannirfyqptasneevqQAMEQAGLAKFiatlpqglqtrvgeAGRGI---SGGQAQRIMLARAfLVQQ 490
Cdd:cd03214 78 VP---------------------------QALELLGLAHL--------------ADRPFnelSGGERQRVLLARA-LAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 491 RHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRL-HWLEQMDYVLVLDNGKIAEQG 552
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
333-562 |
1.16e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.98 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLphlaqDQWQQQFT 412
Cdd:COG1121 7 IELENLTVSYGG---RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYL---F----SDTIA----NNIRFYQP--TASNEEVQQAMEQAGLAKFiatlpqgLQTRVGEagrgISGGQAQR 479
Cdd:COG1121 79 YVPQRAEVdwdFpitvRDVVLmgryGRRGLFRRpsRADREAVDEALERVGLEDL-------ADRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 480 IMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQM-DYVLVLDNGKIAEqGPVKQL 557
Cdd:COG1121 148 VLLARA-LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYfDRVLLLNRGLVAH-GPPEEV 225
|
....*
gi 2468565974 558 LQKQH 562
Cdd:COG1121 226 LTPEN 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
333-548 |
8.39e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 126.36 E-value: 8.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQlPHLAQDQWQQQFT 412
Cdd:cd03230 1 IEVRNLSKRYGKK--TA-LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD-IKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRFyqptasneevqqameqaglakfiatlpqglqtrvgeagrgiSGGQAQRIMLARAFLVQQR 491
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 492 hILIFDEPTAHLDIETEYALKKTMVQL-FEHHLVLFATHRLHWLEQM-DYVLVLDNGKI 548
Cdd:cd03230 116 -LLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
335-547 |
8.51e-34 |
|
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: 127.58 E-value: 8.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYL 414
Cdd:cd03225 2 LKNLSFSYPDGARPA-LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 415 PQKP--YLFSDTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAf 486
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFglenlgLPEEEIEERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGV- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 487 LVQQRHILIFDEPTAHLDIETEYALKKTMVQLF-EHHLVLFATHRLHWL-EQMDYVLVLDNGK 547
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
86-558 |
2.38e-33 |
|
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: 136.19 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 86 TEDLRQKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIpwiLLVYIFWQNLTSGIVLVLVFP 165
Cdd:TIGR01271 957 SKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLI---VLGAIFVVSVLQPYIFIAAIP 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 166 IIILFMIILGYAAKDKASSQYAEYVVLS---NHFLDALRGLTTLKMLGlSKEYTHNIYQVSENYRKKT----LSTLR--- 235
Cdd:TIGR01271 1034 VAVIFIMLRAYFLRTSQQLKQLESEARSpifSHLITSLKGLWTIRAFG-RQSYFETLFHKALNLHTANwflyLSTLRwfq 1112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 236 --IAILSTFALDWFTTLSIAI-------LAVFLGLAlMNGTLPLYPALVT------LILAPEYFLPLRDFASDYHATLNG 300
Cdd:TIGR01271 1113 mrIDIIFVFFFIAVTFIAIGTnqdgegeVGIILTLA-MNILSTLQWAVNSsidvdgLMRSVSRVFKFIDLPQEEPRPSGG 1191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 301 KNAFQQTLD-ILAIPTVTDrtllpafTWNEQSRLTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLE 379
Cdd:TIGR01271 1192 GGKYQLSTVlVIENPHAQK-------CWPSGGQMDVQGLTAKYTEAGRAV-LQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 380 ALSGfVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQpTASNEEVQQAMEQAGLAKFIATLPQ 459
Cdd:TIGR01271 1264 ALLR-LLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYE-QWSDEEIWKVAEEVGLKSVIEQFPD 1341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 460 GLQTRVGEAGRGISGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDY 539
Cdd:TIGR01271 1342 KLDFVLVDGGYVLSNGHKQLMCLARSILSKAK-ILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQ 1420
|
490
....*....|....*....
gi 2468565974 540 VLVLDNGKIAEQGPVKQLL 558
Cdd:TIGR01271 1421 FLVIEGSSVKQYDSIQKLL 1439
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
327-552 |
3.35e-33 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 125.99 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 327 WNEQSRLTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQ 406
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPV-LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 407 WQQQFTYLPQKPYLFSDTIANNIRFYQpTASNEEVQQAMeqaglakfiatlpqglqtRVGEAGRGISGGQAQRIMLARAf 486
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARA- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 487 LVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQG 552
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
334-547 |
4.45e-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: 123.89 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 334 TIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTY 413
Cdd:cd00267 1 EIENLSFRYGG---RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 414 LPQkpylfsdtiannirfyqptasneevqqameqaglakfiatlpqglqtrvgeagrgISGGQAQRIMLARAfLVQQRHI 493
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARA-LLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 494 LIFDEPTAHLDIETEYALKKTMVQLFEHHL-VLFATHRLHWLEQ-MDYVLVLDNGK 547
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRtVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-568 |
7.24e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 134.72 E-value: 7.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 17 KMLAGLTVLqafMILFQAIFLAKVLVLS-------WQRKGLSQL---GWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTT 86
Cdd:PLN03232 906 KAVGGLWVV---MILLVCYLTTEVLRVSsstwlsiWTDQSTPKSyspGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAA 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 87 EDLRQKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMiipWILLVYIFWQNLTSGIVLVLVFPI 166
Cdd:PLN03232 983 KRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQL---WQLLSTFALIGTVSTISLWAIMPL 1059
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 167 IILFMIILGYAAKDKASSQYAEYVVLS---NHFLDALRGLTTLK-------MLGLSKEYTHN-----IYQVSEN----YR 227
Cdd:PLN03232 1060 LILFYAAYLYYQSTSREVRRLDSVTRSpiyAQFGEALNGLSSIRaykaydrMAKINGKSMDNnirftLANTSSNrwltIR 1139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 228 KKTLSTLRIAILSTFA-LDWFTTLSIAILAVFLGLALMngtlplYPALVTLILAPeyflPLRDfASDYHATLNGKNAFQQ 306
Cdd:PLN03232 1140 LETLGGVMIWLTATFAvLRNGNAENQAGFASTMGLLLS------YTLNITTLLSG----VLRQ-ASKAENSLNSVERVGN 1208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 307 TLDILAIPTVTDRTLLPAFTWNEQSRLTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVI 386
Cdd:PLN03232 1209 YIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPV-LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE 1287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 387 PQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQpTASNEEVQQAMEQAGLAKFIATLPQGLQTRVG 466
Cdd:PLN03232 1288 LEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALERAHIKDVIDRNPFGLDAEVS 1366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 467 EAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNG 546
Cdd:PLN03232 1367 EGGENFSVGQRQLLSLARA-LLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSG 1445
|
570 580
....*....|....*....|..
gi 2468565974 547 KIAEQGPVKQLLQKQHGPFFEL 568
Cdd:PLN03232 1446 QVLEYDSPQELLSRDTSAFFRM 1467
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-559 |
1.43e-32 |
|
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: 131.18 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGfVIPQ----TGNIQLNGHQLPHLAQDQWQ 408
Cdd:COG1123 5 LEVRDLSVRYPGGDVPA-VDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHggriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 QQFTYLPQKPY--LFSDTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRI 480
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQIAEalenlgLSRAEARARVLELLEAVGLERRLDRYPHQL-----------SGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 481 MLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:COG1123 152 AIAMA-LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEI 230
|
..
gi 2468565974 558 LQ 559
Cdd:COG1123 231 LA 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
332-547 |
2.50e-31 |
|
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: 120.66 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 332 RLTIQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLpHLAQDQWQQQF 411
Cdd:COG4133 2 MLEAENLSCRRGER---LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSD-TIANNIRFYQ----PTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAF 486
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 487 LvQQRHILIFDEPTAHLDIETeyalKKTMVQLFEHHL-----VLFATHRLHWLEQmDYVLVLDNGK 547
Cdd:COG4133 147 L-SPAPLWLLDEPFTALDAAG----VALLAELIAAHLarggaVLLTTHQPLELAA-ARVLDLGDFK 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
333-557 |
7.74e-31 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 119.98 E-value: 7.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFV-----IPQTGNIQLNGHQLPHLAQD-- 405
Cdd:cd03260 1 IELRDLNVYYGD--KHA-LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 406 QWQQQFTYLPQKPYLFSDTIANNIRF---YQPTASNEEVQQAMEQAgLAKfiATLPQGLQTRVgeAGRGISGGQAQRIML 482
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYglrLHGIKLKEELDERVEEA-LRK--AALWDEVKDRL--HALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 483 ARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:cd03260 153 ARALANEPE-VLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
332-565 |
1.00e-30 |
|
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: 120.78 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 332 RLTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQF 411
Cdd:cd03288 19 EIKIHDLCVRYENNLKPV-LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSDTIANNIRfYQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFlVQQR 491
Cdd:cd03288 98 SIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF-VRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 492 HILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQHGPF 565
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
333-552 |
1.10e-30 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 119.53 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQ---WQ 408
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkiRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 QQFTYLPQKPY-----LFS--DTIANNIRFYQPTASNEE----VQQAMEQAGLAKFIAT-LPQGLqtrvgeagrgiSGGQ 476
Cdd:cd03257 82 KEIQMVFQDPMsslnpRMTigEQIAEPLRIHGKLSKKEArkeaVLLLLVGVGLPEEVLNrYPHEL-----------SGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 477 AQRIMLARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLF-EHHL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQG 552
Cdd:cd03257 151 RQRVAIARALALNPK-LLIADEPTSALDVSVQAQILDLLKKLQeELGLtLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
335-562 |
2.48e-30 |
|
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: 118.76 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQ---QF 411
Cdd:cd03261 3 LRGLTKSFGG---RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSD-TIANNIRF--YQPTASNEE-----VQQAMEQAGlakfiatLPQGLQTRVGEagrgISGGQAQRIMLA 483
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFplREHTRLSEEeireiVLEKLEAVG-------LRGAEDLYPAE----LSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 484 RAfLVQQRHILIFDEPTAHLD-IETEY------ALKKTMvqlfeHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVK 555
Cdd:cd03261 149 RA-LALDPELLLYDEPTAGLDpIASGViddlirSLKKEL-----GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPE 222
|
....*..
gi 2468565974 556 QLLQKQH 562
Cdd:cd03261 223 ELRASDD 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
304-562 |
2.51e-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: 124.63 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 304 FQQTLDILAIPTVTDRTLLPAFTWNEQSR-LTIQHLNFQYDDTMDQVN--LKDLNLTLQGYERVAIIGQSGAGKSTLLEA 380
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPlLEVRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 381 LSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT---YLPQKPY--LF-SDTIANNIRF-------YQPTASNEEVQQAMEQ 447
Cdd:COG1123 311 LLGLLRPTSGSILFDGKDLTKLSRRSLRELRRrvqMVFQDPYssLNpRMTVGDIIAEplrlhglLSRAERRERVAELLER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 448 AGL-AKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQRhILIFDEPTAHLDieteYALKKTMVQLF-----EH 521
Cdd:COG1123 391 VGLpPDLADRYPHEL-----------SGGQRQRVAIARALALEPK-LLILDEPTSALD----VSVQAQILNLLrdlqrEL 454
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2468565974 522 HL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQK-QH 562
Cdd:COG1123 455 GLtYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFANpQH 498
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
333-559 |
4.83e-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: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQF 411
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYL-----FS--DTIANNIRFYQPTASNEEVQQAMEQAGLakfiatlPQGLQTRVGEAgrgISGGQAQRIMLAR 484
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRIHGLPDREERIAELLEQVGL-------PPSFLDRYPHQ---LSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 485 AFLVQQRhILIFDEPTAHLDIETeyalKKTMVQLF-----EHHL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:COG1124 152 ALILEPE-LLLLDEPTSALDVSV----QAEILNLLkdlreERGLtYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADL 226
|
..
gi 2468565974 558 LQ 559
Cdd:COG1124 227 LA 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
362-568 |
2.17e-29 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 124.12 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 362 ERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIR-FYQptASNEE 440
Cdd:PTZ00243 1337 EKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDpFLE--ASSAE 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 441 VQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFE 520
Cdd:PTZ00243 1415 VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILMDEATANIDPALDRQIQATVMSAFS 1494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2468565974 521 HHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQHGPFFEL 568
Cdd:PTZ00243 1495 AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSM 1542
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
332-561 |
2.27e-29 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 117.26 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 332 RLTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQtGNIQLNGHQLPHLAQDQWQQQF 411
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAV-LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSDTIANNIRFYQpTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLVQQR 491
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYG-KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 492 hILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:cd03289 159 -ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
333-562 |
2.51e-29 |
|
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: 116.23 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ---Q 409
Cdd:COG1127 6 IEVRNLTKSFGD---RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 410 QFTYLPQKPYLFSD-TIANNIRF---YQPTASNEE----VQQAMEQAGLAKFIATLPqglqtrvGEagrgISGGQAQRIM 481
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFplrEHTDLSEAEirelVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQL-FEHHL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLL 558
Cdd:COG1127 152 LARA-LALDPEILLYDEPTAGLDPITSAVIDELIRELrDELGLtSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELL 230
|
....
gi 2468565974 559 QKQH 562
Cdd:COG1127 231 ASDD 234
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
24-303 |
3.08e-29 |
|
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: 117.25 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 24 VLQAFMILFQAIF---LAKVLVLSWQRKG-LSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLAQVYT 99
Cdd:cd18781 3 LLQWISLLANIAFvfsIANLLQKLLEGKLtTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 100 TGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLVLVFPIIILFMIILGYAAK 179
Cdd:cd18781 83 LGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKIAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 180 DKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWF----TTLSIaIL 255
Cdd:cd18781 163 KLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVayggAALGI-IL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2468565974 256 AVFlglALMNGTLPLYPALVTLILAPEYFLPLRDFASDYHATLNGKNA 303
Cdd:cd18781 242 ALL---QFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAA 286
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
333-554 |
3.62e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 112.18 E-value: 3.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQwqqqf 411
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFS-DTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLAR 484
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALglelqgVPKAEARERAEELLELVGLSGFENAYPHQL-----------SGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 485 AfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHL--VLFATHRLHwlEQM---DYVLVLDN--GKIAEQGPV 554
Cdd:cd03293 145 A-LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGktVLLVTHDID--EAVflaDRVVVLSArpGRIVAEVEV 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
333-551 |
3.70e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 112.44 E-value: 3.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQW---- 407
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 408 QQQFTYLPQKPYLFSD-TIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRI 480
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALplllagVSRKERRERARELLERVGLGDRLDHRPSQL-----------SGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 481 MLARAfLVQQRHILIFDEPTAHLDIETEYALkktMVQLFEHH-----LVLFATHRLHWLEQMDYVLVLDNGKIAEQ 551
Cdd:COG1136 154 AIARA-LVNRPKLILADEPTGNLDSKTGEEV---LELLRELNrelgtTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
333-562 |
7.61e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.52 E-value: 7.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:COG4559 2 LEAENLSVRLGGR--TL-LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYL-FSDTIANNIR------FYQPTASNEEVQQAMEQAGLAKFiatlpqglqtrvgeAGR---GISGGQAQRIML 482
Cdd:COG4559 79 VLPQHSSLaFPFTVEEVVAlgraphGSSAAQDRQIVREALALVGLAHL--------------AGRsyqTLSGGEQQRVQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 483 ARAfLVQ-------QRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFAThrLHWLEQM----DYVLVLDNGKIAEQ 551
Cdd:COG4559 145 ARV-LAQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAV--LHDLNLAaqyaDRILLLHQGRLVAQ 221
|
250
....*....|.
gi 2468565974 552 GPVKQLLQKQH 562
Cdd:COG4559 222 GTPEEVLTDEL 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
332-529 |
3.14e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 110.56 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 332 RLTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDqwqqq 410
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKPYLFS-DTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLA 483
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALglelrgVPKAERRERARELLELVGLAGFEDAYPHQL-----------SGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2468565974 484 RAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATH 529
Cdd:COG1116 151 RA-LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTH 197
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
333-561 |
3.72e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.25 E-value: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:PRK13548 3 LEARNLSVRLGGR--TL-LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYL-FSDTIANNIRF------YQPTASNEEVQQAMEQAGLAKFiatlpqglqtrvgeAGR---GISGGQAQRIML 482
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMgraphgLSRAEDDALVAAALAQVDLAHL--------------AGRdypQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 483 ARAfLVQ------QRHILIFDEPTAHLDieteyalkktmvqLFEHHLVL-----FATHR-------LHWLEQM----DYV 540
Cdd:PRK13548 146 ARV-LAQlwepdgPPRWLLLDEPTSALD-------------LAHQHHVLrlarqLAHERglavivvLHDLNLAaryaDRI 211
|
250 260
....*....|....*....|.
gi 2468565974 541 LVLDNGKIAEQGPVKQLLQKQ 561
Cdd:PRK13548 212 VLLHQGRLVADGTPAEVLTPE 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
113-568 |
5.89e-27 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 116.58 E-value: 5.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 113 IVTNALDGMDEVNNYFNLI---------LSKFMNMMiipW------ILLVYIFWQNLTSGI-----VLVLVFPI-IILFM 171
Cdd:TIGR00957 403 VITNSARKSSTVGEIVNLMsvdaqrfmdLATYINMI---WsaplqvILALYFLWLNLGPSVlagvaVMVLMVPLnAVMAM 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 172 IILGYAAKDKASSQyaEYVVLSNHFLDalrGLTTLKMLGLSKEYTHNIyqvsENYRKKTLSTLR----IAILSTFAldWF 247
Cdd:TIGR00957 480 KTKTYQVAHMKSKD--NRIKLMNEILN---GIKVLKLYAWELAFLDKV----EGIRQEELKVLKksayLHAVGTFT--WV 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 248 TT---LSIAILAV---------------FLGLALMN-GTLPL--YPALVTLILAPEYFLP-LRDFASdyHATLNGKNAFQ 305
Cdd:TIGR00957 549 CTpflVALITFAVyvtvdennildaekaFVSLALFNiLRFPLniLPMVISSIVQASVSLKrLRIFLS--HEELEPDSIER 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 306 QTLDILAIPTVTDRTllPAFTWNEQSRLTIQHLNFQYDDTmdqvnlkdlnltlqgyERVAIIGQSGAGKSTLLEALSGFV 385
Cdd:TIGR00957 627 RTIKPGEGNSITVHN--ATFTWARDLPPTLNGITFSIPEG----------------ALVAVVGQVGCGKSSLLSALLAEM 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 386 IPQTGNIQLNGhqlphlaqdqwqqQFTYLPQKPYLFSDTIANNIRFYQPTASNEeVQQAMEQAGLAKFIATLPQGLQTRV 465
Cdd:TIGR00957 689 DKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKALNEKY-YQQVLEACALLPDLEILPSGDRTEI 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 466 GEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMV---QLFEHHLVLFATHRLHWLEQMDYVLV 542
Cdd:TIGR00957 755 GEKGVNLSGGQKQRVSLARA-VYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpeGVLKNKTRILVTHGISYLPQVDVIIV 833
|
490 500
....*....|....*....|....*.
gi 2468565974 543 LDNGKIAEQGPVKQLLQKQhGPFFEL 568
Cdd:TIGR00957 834 MSGGKISEMGSYQELLQRD-GAFAEF 858
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
353-552 |
8.15e-27 |
|
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: 107.96 E-value: 8.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 353 DLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGhqLPHLAQDQWQQQFTYLPQKPYLFSD-TIANNIRF 431
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRPVSMLFQENNLFAHlTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 432 -YQPTAS-NEEVQQAME----QAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAfLVQQRHILIFDEPTAHLDI 505
Cdd:cd03298 94 gLSPGLKlTAEDRQAIEvalaRVGLAGLEKRLPGEL-----------SGGERQRVALARV-LVRDKPVLLLDEPFAALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 506 eteyALKKTMVQLF------EHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQG 552
Cdd:cd03298 162 ----ALRAEMLDLVldlhaeTKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
351-565 |
9.33e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 115.99 E-value: 9.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIR 430
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 431 FYQpTASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYA 510
Cdd:PLN03130 1335 PFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA-LLRRSKILVLDEATAAVDVRTDAL 1412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 511 LKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQHGPF 565
Cdd:PLN03130 1413 IQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
329-553 |
1.05e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 111.34 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 329 EQSRLTIQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAqdQWQ 408
Cdd:COG3842 2 AMPALELENVSKRYGDV---TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP--PEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 QQFTYLPQKPYLFSD-TIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIM 481
Cdd:COG3842 77 RNVGMVFQDYALFPHlTVAENVAFglrmrgVPKAEIRARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LARAfLVQQRHILIFDEPTAHLDieteYALKKTM-VQLFEHHL-----VLFATHRLHwlEQM---DYVLVLDNGKIAEQG 552
Cdd:COG3842 146 LARA-LAPEPRVLLLDEPLSALD----AKLREEMrEELRRLQRelgitFIYVTHDQE--EALalaDRIAVMNDGRIEQVG 218
|
.
gi 2468565974 553 P 553
Cdd:COG3842 219 T 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
70-545 |
2.48e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 114.74 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 70 LTWIKNRLLDRYATKTTEDLRQKLLAQV-YTTGaaMIAQKGSGNIVTNALD-GMDEVNNYfnlILSKFMNMMIIPWILLV 147
Cdd:PTZ00265 113 LSFISSFCMDVVTTKILKTLKLEFLKSVfYQDG--QFHDNNPGSKLTSDLDfYLEQVNAG---IGTKFITIFTYASAFLG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 148 YIFW---QNLTSGIVLVLVFPIIILFMIILGYAAK-DKASSqyaeyVVLSNHFL----DALRGL----------TTLKML 209
Cdd:PTZ00265 188 LYIWslfKNARLTLCITCVFPLIYICGVICNKKVKiNKKTS-----LLYNNNTMsiieEALVGIrtvvsycgekTILKKF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 210 GLSkEYTHNIYQVSENYrkktLSTLRIAILSTFALD------WFTTLSI----------------AILAVFLGLalmngT 267
Cdd:PTZ00265 263 NLS-EKLYSKYILKANF----MESLHIGMINGFILAsyafgfWYGTRIIisdlsnqqpnndfhggSVISILLGV-----L 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 268 LPLYpaLVTLILA--PEYFLPLRDFASDYHaTLNGKNAFQQTLDILAIPTVtdrtllpaftwneqSRLTIQHLNFQYDDT 345
Cdd:PTZ00265 333 ISMF--MLTIILPniTEYMKSLEATNSLYE-IINRKPLVENNDDGKKLKDI--------------KKIQFKNVRFHYDTR 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 346 MDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLN-GHQLPHLAQDQWQQQFTYLPQKPYLFSDT 424
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNS 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 425 IANNIRF-------------------------------------------YQPTASNE--------------EVQQAMEQ 447
Cdd:PTZ00265 476 IKNNIKYslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmSNTTDSNEliemrknyqtikdsEVVDVSKK 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 448 AGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQL--FEHHLVL 525
Cdd:PTZ00265 556 VLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARA-IIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITI 634
|
570 580
....*....|....*....|
gi 2468565974 526 FATHRLHWLEQMDYVLVLDN 545
Cdd:PTZ00265 635 IIAHRLSTIRYANTIFVLSN 654
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
335-549 |
2.54e-26 |
|
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: 106.85 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLphlaqDQWQQQFTYL 414
Cdd:cd03235 2 VEDLTVSYGG---HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 415 PQK-------PYLFSDTIANNIR-----FYQPTASN-EEVQQAMEQAGLAKFIatlpqglQTRVGEAgrgiSGGQAQRIM 481
Cdd:cd03235 74 PQRrsidrdfPISVRDVVLMGLYghkglFRRLSKADkAKVDEALERVGLSELA-------DRQIGEL----SGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEH-HLVLFATHRLHW-LEQMDYVLVLDNGKIA 549
Cdd:cd03235 143 LARA-LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLvLEYFDRVLLLNRTVVA 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
333-547 |
3.96e-26 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 104.96 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQD--QWQQQ 410
Cdd:cd03229 1 LELKNVSKRYGQ---KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKPYLFSD-TIANNIRFyqptasneevqqameqaglakfiatlpqglqtrvgeagrGISGGQAQRIMLARAfLVQ 489
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIAL---------------------------------------GLSGGQQQRVALARA-LAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 490 QRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQM-DYVLVLDNGK 547
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
333-550 |
4.15e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.29 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQ---WQQ 409
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 410 QFTYLPQKPYLFSD-TIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIML 482
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 483 ARAfLVQQRHILIFDEPTAHLDIETeyALKktMVQLFE--HHL---VLFATHRLHWLEQMDY-VLVLDNGKIAE 550
Cdd:COG2884 149 ARA-LVNRPELLLADEPTGNLDPET--SWE--IMELLEeiNRRgttVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
334-548 |
7.42e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 105.03 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 334 TIQHLNFQYDDTMDQvnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPhlaqdQWQQQFT- 412
Cdd:cd03226 1 RIENISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-----AKERRKSi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 -YLPQKP--YLFSDTIANNIRF--YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAFL 487
Cdd:cd03226 74 gYVMQDVdyQLFTDSVREELLLglKELDAGNEQAETVLKDLDLYALKERHPLSL-----------SGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 488 vQQRHILIFDEPTAHLDieteYALKKTMVQLFEH-----HLVLFATHRLHWLEQM-DYVLVLDNGKI 548
Cdd:cd03226 143 -SGKDLLIFDEPTSGLD----YKNMERVGELIRElaaqgKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
333-552 |
7.71e-26 |
|
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: 105.29 E-value: 7.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAqdQWQQQFT 412
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--PERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRF-----YQPTASNEE-VQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARA 485
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFglklrGVPKAEIRArVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 486 fLVQQRHILIFDEPTAHLDIETEYALKKTMVQLF-EHHL-VLFATHRL-HWLEQMDYVLVLDNGKIAEQG 552
Cdd:cd03259 145 -LAREPSLLLLDEPLSALDAKLREELREELKELQrELGItTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
333-548 |
3.33e-25 |
|
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: 103.72 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ--- 408
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 --------QQFTYLpqkPYLfsdTIANNIR---FYQPTASNEEVQQAM---EQAGLAKFIATLPQGLqtrvgeagrgiSG 474
Cdd:cd03255 81 rrhigfvfQSFNLL---PDL---TALENVElplLLAGVPKKERRERAEellERVGLGDRLNHYPSEL-----------SG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 475 GQAQRIMLARAfLVQQRHILIFDEPTAHLDIETeyalKKTMVQLF------EHHLVLFATHRLHWLEQMDYVLVLDNGKI 548
Cdd:cd03255 144 GQQQRVAIARA-LANDPKIILADEPTGNLDSET----GKEVMELLrelnkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
333-559 |
5.43e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 106.38 E-value: 5.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLphlaqdqwqqqFT 412
Cdd:COG1118 3 IEVRNISKRFGSF--TL-LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-----------FT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLP----------QKPYLFSD-TIANNIRF---YQPTASNEEVQQAMEQ------AGLAKfiaTLPQGLqtrvgeagrgi 472
Cdd:COG1118 69 NLPprerrvgfvfQHYALFPHmTVAENIAFglrVRPPSKAEIRARVEELlelvqlEGLAD---RYPSQL----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 473 SGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFE--HHLVLFATHRLhwLEQM---DYVLVLDNGK 547
Cdd:COG1118 135 SGGQRQRVALARA-LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHDQ--EEALelaDRVVVMNQGR 211
|
250
....*....|..
gi 2468565974 548 IAEQGPVKQLLQ 559
Cdd:COG1118 212 IEQVGTPDEVYD 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
333-558 |
1.04e-24 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 102.66 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGH---QLPHLAQDQWQ 408
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 QQFTYLPQKPYLFSD-TIANNIRF-----YQPTASNEE-VQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIM 481
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIEErVLELLELVGLEDKADAYPAQL-----------SGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LARAfLVQQRHILIFDEPTAHLDIETEYA----LKKTMVQLfehHL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVK 555
Cdd:cd03258 151 IARA-LANNPKVLLCDEATSALDPETTQSilalLRDINREL---GLtIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVE 226
|
...
gi 2468565974 556 QLL 558
Cdd:cd03258 227 EVF 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
144-567 |
3.12e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 107.90 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 144 ILLVYIFWQ----NLTSGIVLVLVFPI---IILFMIIL---GYAAKDKAssqyaeyVVLSNHFLDALrglTTLKMLGLSK 213
Cdd:PLN03130 430 IAMVLLYQQlgvaSLIGSLMLVLMFPIqtfIISKMQKLtkeGLQRTDKR-------IGLMNEVLAAM---DTVKCYAWEN 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 214 EYTHNIYQVsenyRKKTLSTLRIAILSTfALDWFTTLSIAILAVFLGLA---LMNGTLPLYPALVTLILAPEYFLPLRDF 290
Cdd:PLN03130 500 SFQSKVQTV----RDDELSWFRKAQLLS-AFNSFILNSIPVLVTVVSFGvftLLGGDLTPARAFTSLSLFAVLRFPLFML 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 291 ASDYHATLNGKNAFQQTLDILAiptVTDRTLLPAFTWN-EQSRLTIQHLNFQYDDTMDQVNLKDLNLTLQGYERVAIIGQ 369
Cdd:PLN03130 575 PNLITQAVNANVSLKRLEELLL---AEERVLLPNPPLEpGLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGS 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 370 SGAGKSTLLEALSGFVIPQT-GNIQLNGhqlphlaqdqwqqQFTYLPQKPYLFSDTIANNIRFYQPTASnEEVQQAMEQA 448
Cdd:PLN03130 652 TGEGKTSLISAMLGELPPRSdASVVIRG-------------TVAYVPQVSWIFNATVRDNILFGSPFDP-ERYERAIDVT 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 449 GLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLD-----------IETEYAlKKTMVq 517
Cdd:PLN03130 718 ALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARA-VYSNSDVYIFDDPLSALDahvgrqvfdkcIKDELR-GKTRV- 794
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2468565974 518 lfehhlvlFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLqkQHGPFFE 567
Cdd:PLN03130 795 --------LVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS--NNGPLFQ 834
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
328-559 |
3.23e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.40 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 328 NEQSRLTIQHLNFQYDDTmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHlaQDQW 407
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE--ETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 408 Q--QQFTYLPQKP--YLFSDTIANNIRFyqpTASN---------EEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSG 474
Cdd:PRK13635 78 DvrRQVGMVFQNPdnQFVGATVQDDVAF---GLENigvpreemvERVDQALRQVGMEDFLNREPHRL-----------SG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 475 GQAQRIMLArAFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQMDYVLVLDNGKIAEQG 552
Cdd:PRK13635 144 GQKQRVAIA-GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
....*..
gi 2468565974 553 PVKQLLQ 559
Cdd:PRK13635 223 TPEEIFK 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
330-565 |
3.86e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 107.81 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 330 QSRLTIQHLNFQYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGF------------------------- 384
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 385 -----------------------------VIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRFYQPT 435
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 436 ASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTM 515
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA-LLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 516 VQLFEH--HLVLFATHRLHWLEQMDYVLVLDNGK-----IAEQGPVKQLLQKQHGPF 565
Cdd:PTZ00265 1402 VDIKDKadKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVY 1458
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
355-559 |
8.57e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.04 E-value: 8.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 355 NLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHqlPHLAQDQWQQQFTYLPQKPYLFSD-TIANNIRF-Y 432
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRPVSMLFQENNLFSHlTVAQNIGLgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 433 QP-----TASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIet 507
Cdd:PRK10771 97 NPglklnAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARC-LVREQPILLLDEPFSALDP-- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 508 eyALKKTMVQLF-----EHHLVLFATHrlHWLEQMDYV----LVLDNGKIAEQGPVKQLLQ 559
Cdd:PRK10771 163 --ALRQEMLTLVsqvcqERQLTLLMVS--HSLEDAARIaprsLVVADGRIAWDGPTDELLS 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
200-557 |
9.31e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 106.60 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 200 LRGLTTLKMLGLSKEYTHNIYQVsenyRKKTLSTLRIAILsTFALDWFTTLSIAI---LAVFLGLALMNGTLPLYPALVT 276
Cdd:PLN03232 486 LASMDTVKCYAWEKSFESRIQGI----RNEELSWFRKAQL-LSAFNSFILNSIPVvvtLVSFGVFVLLGGDLTPARAFTS 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 277 LILAPEYFLPLRDFASDYHATLNGKNAFQQTLDILaipTVTDRTLLPAFTWNEQS-RLTIQHLNFQYDDTMDQVNLKDLN 355
Cdd:PLN03232 561 LSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELL---LSEERILAQNPPLQPGApAISIKNGYFSWDSKTSKPTLSDIN 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 356 LTLQGYERVAIIGQSGAGKSTLLEALSGFVIP-QTGNIQLNGhqlphlaqdqwqqQFTYLPQKPYLFSDTIANNIRF--- 431
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRG-------------SVAYVPQVSWIFNATVRENILFgsd 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 432 YQPtasnEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLvQQRHILIFDEPTAHLDIETEY-A 510
Cdd:PLN03232 705 FES----ERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVY-SNSDIYIFDDPLSALDAHVAHqV 779
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2468565974 511 LKKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQL 557
Cdd:PLN03232 780 FDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
333-558 |
1.17e-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: 99.68 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ---- 408
Cdd:COG1126 2 IEIENLHKSFGDL--EV-LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlrrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 -----QQFTylpqkpyLFSD-TIANNIRfYQPT----ASNEEV-QQAME---QAGLAKFIATLPQGLqtrvgeagrgiSG 474
Cdd:COG1126 79 vgmvfQQFN-------LFPHlTVLENVT-LAPIkvkkMSKAEAeERAMElleRVGLADKADAYPAQL-----------SG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 475 GQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHL-VLFATHrlhwleQM-------DYVLVLDNG 546
Cdd:COG1126 140 GQQQRVAIARA-LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMtMVVVTH------EMgfarevaDRVVFMDGG 212
|
250
....*....|..
gi 2468565974 547 KIAEQGPVKQLL 558
Cdd:COG1126 213 RIVEEGPPEEFF 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
351-560 |
1.68e-23 |
|
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: 99.33 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDqwQQQFTYLPQKPYLFSD-TIANNI 429
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 430 ------RFYQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQRhILIFDEPTAHL 503
Cdd:cd03299 93 ayglkkRKVDKKEIERKVLEIAEMLGIDHLLNRKPETL-----------SGGEQQRVAIARALVVNPK-ILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 504 DIETEYALKKtMVQLFEHHLVLFATHRLHWLEQM----DYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:cd03299 161 DVRTKEKLRE-ELKKIRKEFGVTVLHVTHDFEEAwalaDKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
333-559 |
1.73e-23 |
|
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: 99.05 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ-F 411
Cdd:cd03224 1 LEVENLNAGYGKS--QI-LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSD-TIANNIRFYQPTASNEEVQQAMEQAgLAKFiatlPQgLQTRVGEAGRGISGGQAQriMLA--RAfLV 488
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV-YELF----PR-LKERRKQLAGTLSGGEQQ--MLAiaRA-LM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 489 QQRHILIFDEPTAHL---------DIETEYALKKTMVQLFEHHlVLFAthrlhwLEQMDYVLVLDNGKIAEQGPVKQLLQ 559
Cdd:cd03224 149 SRPKLLLLDEPSEGLapkiveeifEAIRELRDEGVTILLVEQN-ARFA------LEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
292-556 |
1.75e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.50 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 292 SDYHATLNGKNAFQQTLDILAIPTVTDRTLLPAftwnEQSRLTIQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSG 371
Cdd:COG4178 326 AEWRATVDRLAGFEEALEAADALPEAASRIETS----EDGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSG 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 372 AGKSTLLEALSGFVIPQTGNIqlnghQLPHLAqdqwqqQFTYLPQKPYLFSDTIANNIRFYQPTA--SNEEVQQAMEQAG 449
Cdd:COG4178 400 SGKSTLLRAIAGLWPYGSGRI-----ARPAGA------RVLFLPQRPYLPLGTLREALLYPATAEafSDAELREALEAVG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 450 LAKFIatlpqglqTRVGEA---GRGISGGQAQRIMLARAFLvQQRHILIFDEPTAHLDIETEYAlkktMVQLFEHHL--- 523
Cdd:COG4178 469 LGHLA--------ERLDEEadwDQVLSLGEQQRLAFARLLL-HKPDWLFLDEATSALDEENEAA----LYQLLREELpgt 535
|
250 260 270
....*....|....*....|....*....|....*....
gi 2468565974 524 -VLFATHR-----LHwleqmDYVLVLDNGKIAEQGPVKQ 556
Cdd:COG4178 536 tVISVGHRstlaaFH-----DRVLELTGDGSWQLLPAEA 569
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
333-543 |
1.87e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSDTIANNIRF-YQptASNEEVQQAMEQAGLAKFiaTLPQG-LQTRVGEagrgISGGQAQRIMLAR--AFLV 488
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFpWQ--IRNQQPDPAIFLDDLERF--ALPDTiLTKNIAE----LSGGEKQRISLIRnlQFMP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 489 QqrhILIFDEPTAHLDIETeyalkKTMVQLFEHHL-------VLFATHRLHWLEQMDYVLVL 543
Cdd:PRK10247 157 K---VLLLDEITSALDESN-----KHNVNEIIHRYvreqniaVLWVTHDKDEINHADKVITL 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
351-546 |
7.97e-23 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 97.02 E-value: 7.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNG--HQLPHLAQDQWQQQFT--YLPQKPYLFSDTIA 426
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNknESEPSFEATRSRNRYSvaYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NNIRFYQPTaSNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIE 506
Cdd:cd03290 97 ENITFGSPF-NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA-LYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2468565974 507 -TEYALKKTMVQLF--EHHLVLFATHRLHWLEQMDYVLVLDNG 546
Cdd:cd03290 175 lSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
333-550 |
9.85e-23 |
|
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: 97.12 E-value: 9.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQW---- 407
Cdd:COG4181 9 IELRGLTKTVGTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 408 -------QQQFTYLPqkpylfSDTIANNIRFYQPTASNEEVQQAMEQAgLAKFiatlpqGLQTRVGEAGRGISGGQAQRI 480
Cdd:COG4181 89 arhvgfvFQSFQLLP------TLTALENVMLPLELAGRRDARARARAL-LERV------GLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 481 MLARAFLVQQRhILIFDEPTAHLDIETeyalKKTMVQL-FEHH------LVLfATHRLHWLEQMDYVLVLDNGKIAE 550
Cdd:COG4181 156 ALARAFATEPA-ILFADEPTGNLDAAT----GEQIIDLlFELNrergttLVL-VTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
351-552 |
2.04e-22 |
|
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: 95.80 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQ---TGNIQLNGHQlphLAQDQWQQQFTYLPQKPYLFSD-TIA 426
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQP---RKPDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NNIRFYQ----PTASNEEVQQAMEQAGLAKFIAtlpqglQTRVGEAG-RGISGGQAQRIMLARAFLVQQRhILIFDEPTA 501
Cdd:cd03234 100 ETLTYTAilrlPRKSSDAIRKKRVEDVLLRDLA------LTRIGGNLvKGISGGERRRVSIAVQLLWDPK-VLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 502 HLDIETEYALKKTMVQLF-EHHLVLFATH--RLHWLEQMDYVLVLDNGKIAEQG 552
Cdd:cd03234 173 GLDSFTALNLVSTLSQLArRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
333-548 |
2.80e-22 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 95.29 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ---- 408
Cdd:cd03262 1 IEIKNLHKSFGDF--HV-LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 -----QQFTYLPQKpylfsdTIANNIRFYQPTA---SNEEVQ----QAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQ 476
Cdd:cd03262 78 vgmvfQQFNLFPHL------TVLENITLAPIKVkgmSKAEAEeralELLEKVGLADKADAYPAQL-----------SGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 477 AQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHL-VLFATHRLHW-LEQMDYVLVLDNGKI 548
Cdd:cd03262 141 QQRVAIARA-LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
353-558 |
3.11e-22 |
|
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: 98.25 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 353 DLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLphlaQDQWQQQFT--------YLPQKPYLFSD- 423
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL----QDSARGIFLpphrrrigYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 424 TIANNIRFYQPTASNEEVQQAMEQA----GLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQRhILIFDEP 499
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRISFDEVvellGIGHLLDRRPATL-----------SGGERQRVAIGRALLSSPR-LLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 500 TAHLDieteYALKKTMVQLFE---HHL---VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLL 558
Cdd:COG4148 161 LAALD----LARKAEILPYLErlrDELdipILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
333-552 |
3.29e-22 |
|
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: 94.95 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQG--YervAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQdQWQQQ 410
Cdd:cd03264 1 LQLENLTKRYGK---KRALDGVSLTLGPgmY---GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKP--------YLFSDTIA--NNIRfyqPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRI 480
Cdd:cd03264 74 IGYLPQEFgvypnftvREFLDYIAwlKGIP---SKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 481 MLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQG 552
Cdd:cd03264 140 GIAQA-LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
328-576 |
5.42e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.83 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 328 NEQSRLTIQHLNFQYDDtMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQW 407
Cdd:PRK13632 3 NKSVMIKVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 408 QQQFTYLPQKP--YLFSDTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQR 479
Cdd:PRK13632 82 RKKIGIIFQNPdnQFIGATVEDDIAFglenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 480 IMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFE--HHLVLFATHRLHWLEQMDYVLVLDNGKIAEQG-PV-- 554
Cdd:PRK13632 151 VAIASV-LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGkPKei 229
|
250 260
....*....|....*....|....*...
gi 2468565974 555 ---KQLLQ--KQHGPF-FELTSHMRGVN 576
Cdd:PRK13632 230 lnnKEILEkaKIDSPFiYKLSKKLKGID 257
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
333-550 |
7.90e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 7.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLnGHQLphlaqdqwqqQFT 412
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLF--SDTIANNIRFYQPTASNEEVQQAMEQAGLAkfiatlPQGLQTRVGEagrgISGGQAQRIMLARAFLvQQ 490
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLGRFLFS------GDDAFKPVGV----LSGGEKARLALAKLLL-SP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 491 RHILIFDEPTAHLDIET----EYALKK---TmvqlfehhlVLFATHRLHWLEQM-DYVLVLDNGKIAE 550
Cdd:COG0488 451 PNVLLLDEPTNHLDIETlealEEALDDfpgT---------VLLVSHDRYFLDRVaTRILEFEDGGVRE 509
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
333-570 |
9.06e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.46 E-value: 9.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDD-TMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQL----NGHQLPHLAQDQ 406
Cdd:PRK13631 22 LRVKNLYCVFDEkQENELVaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 407 WQQQ------------FTYLPQKP--YLFSDTIANNIRFyQPTASNEEVQQAMEQAglAKFIATLpqGLQTRVGEAGR-G 471
Cdd:PRK13631 102 NPYSkkiknfkelrrrVSMVFQFPeyQLFKDTIEKDIMF-GPVALGVKKSEAKKLA--KFYLNKM--GLDDSYLERSPfG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 472 ISGGQAQRIMLArAFLVQQRHILIFDEPTAHLDIETEyalkKTMVQLF-----EHHLVLFATHRL-HWLEQMDYVLVLDN 545
Cdd:PRK13631 177 LSGGQKRRVAIA-GILAIQPEILIFDEPTAGLDPKGE----HEMMQLIldakaNNKTVFVITHTMeHVLEVADEVIVMDK 251
|
250 260
....*....|....*....|....*
gi 2468565974 546 GKIAEQGPVKQLLQKQHgpFFELTS 570
Cdd:PRK13631 252 GKILKTGTPYEIFTDQH--IINSTS 274
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
333-558 |
1.26e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.30 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ--- 408
Cdd:COG1135 2 IELENLSKTFPTKGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 -------QQFTYLPQKpylfsdTIANNIRFyqptasneevqqAMEQAGLAKfiatlpQGLQTRVGE-------AGRG--- 471
Cdd:COG1135 82 rkigmifQHFNLLSSR------TVAENVAL------------PLEIAGVPK------AEIRKRVAEllelvglSDKAday 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 472 ---ISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYA----LKK-------TmvqlfehhlVLFATHrlhwleQM 537
Cdd:COG1135 138 psqLSGGQKQRVGIARA-LANNPKVLLCDEATSALDPETTRSildlLKDinrelglT---------IVLITH------EM 201
|
250 260
....*....|....*....|....*...
gi 2468565974 538 -------DYVLVLDNGKIAEQGPVKQLL 558
Cdd:COG1135 202 dvvrricDRVAVLENGRIVEQGPVLDVF 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
333-558 |
2.48e-21 |
|
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: 93.61 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGN-IQLNGHQL---------PH- 401
Cdd:COG1119 4 LELRNVTVRRGGK--TI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRggedvwelrKRi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 402 -LAQDQWQQQFTylpqkPYL---------FSDTIAnniRFYQPTASNEE-VQQAMEQAGLAKFIATLPQGLqtrvgeagr 470
Cdd:COG1119 81 gLVSPALQLRFP-----RDEtvldvvlsgFFDSIG---LYREPTDEQRErARELLELLGLAHLADRPFGTL--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 471 giSGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHL--VLFATHRLH-WLEQMDYVLVLDNGK 547
Cdd:COG1119 144 --SQGEQRRVLIARA-LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAptLVLVTHHVEeIPPGITHVLLLKDGR 220
|
250
....*....|.
gi 2468565974 548 IAEQGPVKQLL 558
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
351-559 |
2.83e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.23 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQL--PHLAQDQWQQQFTYLPQKPYLFSDTIA-N 427
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFPHLTAlE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 428 NIRFyQPT----ASNEEV-QQAMEQagLAKFiatlpqGLQTRVGEAGRGISGGQAQRIMLARAFLVQQRhILIFDEPTAH 502
Cdd:PRK09493 97 NVMF-GPLrvrgASKEEAeKQAREL--LAKV------GLAERAHHYPSELSGGQQQRVAIARALAVKPK-LMLFDEPTSA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 503 LDIETEYALKKTMVQLFEHHLVL-FATHRLHWLEQMDYVLV-LDNGKIAEQGPVKQLLQ 559
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEEGMTMvIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLIK 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
333-552 |
4.17e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.77 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:PRK11231 3 LRTENLTVGYGT---KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPyLFSDTIA------------NNIRFYQPTASNEEVQQAMEQAGLAKFIatlpqglQTRVGEagrgISGGQAQRI 480
Cdd:PRK11231 80 LLPQHH-LTPEGITvrelvaygrspwLSLWGRLSAEDNARVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 481 MLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFAThrLHWLEQM----DYVLVLDNGKIAEQG 552
Cdd:PRK11231 148 FLAMV-LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTV--LHDLNQAsrycDHLVVLANGHVMAQG 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
351-562 |
5.41e-21 |
|
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: 96.68 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGfVIPQTGNIQLNGHQLPHLAQDQWQQ-----Q--FtylpQKPY---- 419
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPlrrrmQvvF----QDPFgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 420 ---LFSDTIANNIRFYQPTASNEE----VQQAMEQAGLAkfiatlPQGLQTRVGEagrgISGGQAQRIMLARAfLVQQRH 492
Cdd:COG4172 377 prmTVGQIIAEGLRVHGPGLSAAErrarVAEALEEVGLD------PAARHRYPHE----FSGGQRQRIAIARA-LILEPK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 493 ILIFDEPTAHLDIeteyALKKTMVQLF-----EHHLV-LFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQK-QH 562
Cdd:COG4172 446 LLVLDEPTSALDV----SVQAQILDLLrdlqrEHGLAyLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFDApQH 519
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-548 |
1.04e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHqlphlaqdqwqQQFTYL 414
Cdd:COG0488 1 LENLSKSFGG---RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 415 PQKPYLFSD-TIANNI---------------RFYQPTASNE-------EVQQAMEQAGL----AKfIATLPQGL------ 461
Cdd:COG0488 67 PQEPPLDDDlTVLDTVldgdaelraleaeleELEAKLAEPDedlerlaELQEEFEALGGweaeAR-AEEILSGLgfpeed 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 462 -QTRVGEagrgISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETeyalkktmVQLFEHHL------VLFATHRLHWL 534
Cdd:COG0488 146 lDRPVSE----LSGGWRRRVALARA-LLSEPDLLLLDEPTNHLDLES--------IEWLEEFLknypgtVLVVSHDRYFL 212
|
250
....*....|....*
gi 2468565974 535 EQM-DYVLVLDNGKI 548
Cdd:COG0488 213 DRVaTRILELDRGKL 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
351-548 |
1.17e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 90.54 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ----------QQFTYLPQKpyl 420
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrrkigvvfQDFRLLPDR--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 421 fsdTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAfLVQQRHIL 494
Cdd:cd03292 94 ---NVYENVAFalevtgVPPREIRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVAIARA-IVNSPTIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 495 IFDEPTAHLDIETEYALkktmVQLFEH-----HLVLFATHRLHWLEQMDY-VLVLDNGKI 548
Cdd:cd03292 159 IADEPTGNLDPDTTWEI----MNLLKKinkagTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
351-552 |
1.80e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 89.53 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQ--TGNIQLNGHQLPhlaQDQWQQQFTYLPQKPYLFsdtiann 428
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLD---KRSFRKIIGYVPQDDILH------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 429 irfyqPTASneeVQQAMEqaglakFIATLpqglqtrvgeagRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETE 508
Cdd:cd03213 95 -----PTLT---VRETLM------FAAKL------------RGLSGGERKRVSIALE-LVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2468565974 509 YALKKTMVQL-FEHHLVLFATHRLHWL--EQMDYVLVLDNGKIAEQG 552
Cdd:cd03213 148 LQVMSLLRRLaDTGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
333-557 |
2.04e-20 |
|
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: 89.87 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLpHLAQDQWQQQFT 412
Cdd:cd03263 1 LQIRNLTKTYKKGTKPA-VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRFYQP------TASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARA 485
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFYARlkglpkSEIKEEVELLLRVLGLTDKANKRARTL-----------SGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 486 fLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:cd03263 148 -LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQEL 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
348-552 |
2.26e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 96.00 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 348 QVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIqlnghqlphlaqdqW-QQQFTYLPQKPYLFSDTIA 426
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WaERSIAYVPQQAWIMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NNIRFYQPTASnEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDie 506
Cdd:PTZ00243 739 GNILFFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARA-VYANRDVYLLDDPLSALD-- 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 507 tEYALKKTMVQLFEHHL-----VLfATHRLHWLEQMDYVLVLDNGKIAEQG 552
Cdd:PTZ00243 815 -AHVGERVVEECFLGALagktrVL-ATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
347-558 |
2.93e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.19 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 347 DQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLP---HLAQDQWQ-----QQFTYLPQKP 418
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarSLSQQKGLirqlrQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 419 YLFSD-TIANNIrFYQPTASNEEVQQAMEQAGlakfiatlpQGLQTRVGEAG------RGISGGQAQRIMLARAFLVQQR 491
Cdd:PRK11264 95 NLFPHrTVLENI-IEGPVIVKGEPKEEATARA---------RELLAKVGLAGketsypRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 492 HILiFDEPTAHLDIETEYALKKTMVQLF-EHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLL 558
Cdd:PRK11264 165 VIL-FDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALF 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
347-558 |
3.08e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.98 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 347 DQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIA 426
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NNI----------RFYQPTASNEE-VQQAMEQAGLAKFiatlpqglqtrvgeAGRGI---SGGQAQRIMLARAfLVQQRH 492
Cdd:PRK09536 95 RQVvemgrtphrsRFDTWTETDRAaVERAMERTGVAQF--------------ADRPVtslSGGERQRVLLARA-LAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 493 ILIFDEPTAHLDIETE---YALKKTMVQlfEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLL 558
Cdd:PRK09536 160 VLLLDEPTASLDINHQvrtLELVRRLVD--DGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
351-557 |
3.30e-20 |
|
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: 89.93 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNG---HQLPHLAQDQWQQQFTYLPQKPYLFSD-TIA 426
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdiNKLKGKALRQLRRQIGMIFQQFNLIERlSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NNI--------RFYQPTASN---EEVQQA---MEQAGLAKFIAtlpqglqTRVGEagrgISGGQAQRIMLARAfLVQQRH 492
Cdd:cd03256 97 ENVlsgrlgrrSTWRSLFGLfpkEEKQRAlaaLERVGLLDKAY-------QRADQ----LSGGQQQRVAIARA-LMQQPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 493 ILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHW-LEQMDYVLVLDNGKIAEQGPVKQL 557
Cdd:cd03256 165 LILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
351-557 |
4.31e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.58 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYL-PQKPYLFSD-TIANN 428
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLvPQEPLLFPNlSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 429 IRFYQPtaSNEEVQQAMEQaglakFIATLPQGLQTRVGEAGRGISGGQAQRIMLArafLVQQRHILIFDEPTAHLD-IET 507
Cdd:PRK15439 107 ILFGLP--KRQASMQKMKQ-----LLAALGCQLDLDSSAGSLEVADRQIVEILRG---LMRDSRILILDEPTASLTpAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 508 EYALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:PRK15439 177 ERLFSRIRELLAQGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
351-549 |
5.38e-20 |
|
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: 87.10 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGhqlphlaqdqwqqqftylpqKPYLFSDTiannir 430
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFASP------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 431 fyqptasneevqQAMEQAGlakfIATLPQglqtrvgeagrgISGGQAQRIMLARAFLVQQRhILIFDEPTAHLDI-ETEy 509
Cdd:cd03216 70 ------------RDARRAG----IAMVYQ------------LSVGERQMVEIARALARNAR-LLILDEPTAALTPaEVE- 119
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2468565974 510 ALKKTMVQLFEHHL-VLFATHRLHWLEQM-DYVLVLDNGKIA 549
Cdd:cd03216 120 RLFKVIRRLRAQGVaVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
351-562 |
5.63e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.51 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFvIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQK-PYLFSDTIANNI 429
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 430 RFYQP-TASNEEVQQAM----EQAGLAKFiatLPQGLQTrvgeagrgISGGQAQRIMLARAFLvqQRH--------ILIF 496
Cdd:COG4138 91 ALHQPaGASSEAVEQLLaqlaEALGLEDK---LSRPLTQ--------LSGGEWQRVRLAAVLL--QVWptinpegqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 497 DEPTAHLDIETEYALKKTMVQLFEHHL-VLFATHRL-HWLEQMDYVLVLDNGKIAEQGPVKQLLQKQH 562
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQQGItVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
333-547 |
1.23e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 85.58 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHqlphlaqdqwqQQFT 412
Cdd:cd03221 1 IELENLSKTYGG---KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQkpylfsdtiannirfyqptasneevqqameqaglakfiatlpqglqtrvgeagrgISGGQAQRIMLARAFLvQQRH 492
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLL-ENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 493 ILIFDEPTAHLDIETEYALKKTMVQLfeHHLVLFATHRLHWLEQM-DYVLVLDNGK 547
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
328-557 |
1.57e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 88.56 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 328 NEQSRLTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGF--VIPQ---TGNIQLNGHQLPHL 402
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDK--QA-LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 403 AQDQWQ--QQFTYLPQKPYLFSDTIANNIRF-------YQPTASNEEVQQAMEQAGL---AKfiatlpqglqTRVGEAGR 470
Cdd:COG1117 84 DVDVVElrRRVGMVFQKPNPFPKSIYDNVAYglrlhgiKSKSELDEIVEESLRKAALwdeVK----------DRLKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 471 GISGGQAQRIMLARAFLVQQRhILIFDEPTAHLD-IETEyALKKTMVQLFEHHLVLFATHRLHwleQM----DYVLVLDN 545
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPE-VLLMDEPTSALDpISTA-KIEELILELKKDYTIVIVTHNMQ---QAarvsDYTAFFYL 228
|
250
....*....|..
gi 2468565974 546 GKIAEQGPVKQL 557
Cdd:COG1117 229 GELVEFGPTEQI 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
351-565 |
1.89e-19 |
|
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: 87.78 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYlpQKPYLFSD-TIANNI 429
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF--QHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 430 RF---YQPTASN-------EEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQRhILIFDEP 499
Cdd:cd03296 96 AFglrVKPRSERppeaeirAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVALARALAVEPK-VLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 500 TAHLDIETEYALKKTMVQLFE--HHLVLFATH-RLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQHGPF 565
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
351-550 |
3.82e-19 |
|
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: 86.72 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ-----FtylpQKPYLFSD-T 424
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigrtF----QIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 425 IANNIR----------------FYQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAfLV 488
Cdd:cd03219 92 VLENVMvaaqartgsglllaraRREEREARERAEELLERVGLADLADRPAGEL-----------SYGQQRRLEIARA-LA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 489 QQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHL-VLFATHRLHWLEQM-DYVLVLDNG-KIAE 550
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLaDRVTVLDQGrVIAE 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
333-553 |
4.06e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.24 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ---- 408
Cdd:PRK09452 15 VELRGISKSFDGK--EV-ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHvntv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 -QQFTYLPQKpylfsdTIANNIRF---YQPTASNE---EVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIM 481
Cdd:PRK09452 92 fQSYALFPHM------TVFENVAFglrMQKTPAAEitpRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LARAfLVQQRHILIFDEPTAHLDieteYALKKTMvQLFEHHL-------VLFATH-RLHWLEQMDYVLVLDNGKIAEQGP 553
Cdd:PRK09452 155 IARA-VVNKPKVLLLDESLSALD----YKLRKQM-QNELKALqrklgitFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
333-552 |
4.26e-19 |
|
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: 86.27 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNG---HQLPHLAqdqwQ 408
Cdd:cd03266 2 ITADALTKRFRDVKKTVQaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvVKEPAEA----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 QQFTYLPQKPYLFSD-TIANNIRFY------QPTASNEEVQQAMEQAGLAKFiatlpqgLQTRVGeagrGISGGQAQRIM 481
Cdd:cd03266 78 RRLGFVSDSTGLYDRlTARENLEYFaglyglKGDELTARLEELADRLGMEEL-------LDRRVG----GFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 482 LARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQM-DYVLVLDNGKIAEQG 552
Cdd:cd03266 147 IARA-LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-569 |
6.83e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 330 QSRLTIQHLNFQYDDT--MDQVNLKDLNLTLqgyerVAIIGQSGAGKSTLLEALSGFV--IPQ---TGNIQLNGHQLPHL 402
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVevLDGVNLEIPDNTI-----TALMGPSGSGKSTLLRVFNRLIelYPEarvSGEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 403 AQDQWQQQFTYLPQKP------YLFsDTIANNIRFYQPTASNEEVQQAMEQAgLAKfiATLPQGLQTRVGEAGRGISGGQ 476
Cdd:PRK14247 76 DVIELRRRVQMVFQIPnpipnlSIF-ENVALGLKLNRLVKSKKELQERVRWA-LEK--AQLWDEVKDRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 477 AQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVK 555
Cdd:PRK14247 152 QQRLCIARA-LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTR 230
|
250
....*....|....
gi 2468565974 556 QLLQKqhgPFFELT 569
Cdd:PRK14247 231 EVFTN---PRHELT 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
351-529 |
8.72e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 8.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQ--LPHLAqdqwqQQFTYL----PQKPYLfsdT 424
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDidDPDVA-----EACHYLghrnAMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 425 IANNIRFYQPTASNEE--VQQAMEQAGLAKfIATLPqglqtrvgeaGRGISGGQAQRIMLARaFLVQQRHILIFDEPTAH 502
Cdd:PRK13539 90 VAENLEFWAAFLGGEEldIAAALEAVGLAP-LAHLP----------FGYLSAGQKRRVALAR-LLVSNRPIWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|..
gi 2468565974 503 LDIETEYALKktmvQLFEHHL-----VLFATH 529
Cdd:PRK13539 158 LDAAAVALFA----ELIRAHLaqggiVIAATH 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
351-557 |
1.46e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQL----PHLAQDQW----QQQFTYLPQkpyLfs 422
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsPRDAQAAGiaiiHQELNLVPN---L-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 423 dTIANNI---------RFYQPTASNEEVQQAMEQAGLakfiaTLPqgLQTRVGEagrgISGGQAQRIMLARAfLVQQRHI 493
Cdd:COG1129 95 -SVAENIflgreprrgGLIDWRAMRRRARELLARLGL-----DID--PDTPVGD----LSVAQQQLVEIARA-LSRDARV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 494 LIFDEPTAHL-DIETEyalkktmvQLFE--HHL------VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:COG1129 162 LILDEPTASLtEREVE--------RLFRiiRRLkaqgvaIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAEL 227
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
18-551 |
1.48e-18 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 89.25 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 18 MLAGLTVLQAFMILFQAIFLAkvlvlSWQRKGLsqLGWLAGAFFLAFLGRHGltwikNRLLDRYAT-KTTEDLRQKLLAQ 96
Cdd:TIGR01194 28 LAGGLAIIALLASINNAIHEE-----NFLGQGS--LFSFGGLCLLALLFRIG-----ADIFPAYAGmHIIANLRIALCEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 97 VYTTGAAMIAQKGSGNIVTNALDGMDEVNNyFNLILSKFMNMMIIPWILLVYIFWQNltsgivlVLVFPIIILFMIIlGY 176
Cdd:TIGR01194 96 ILGAPIEEIDRRGAHNLIPLLTHDIDQINA-FLFIFPPIAIALAIFFFCIAYLAYLS-------VPMFAITISAIII-GT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 177 AAKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFT---TLSIA 253
Cdd:TIGR01194 167 AAQLLAFMGGFKFFHAARDEEDAFNEHTHAIAFGAKELKIHGIRRLSFAHGAIQESANNIADLHIIEILIFIaaeNFGQL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 254 ILAVFLGLALMngTLPLYP-----ALVTLILAPEYFL-PLRDFASDYHATLNGKNAFQQTLDI---LAIP------TVTD 318
Cdd:TIGR01194 247 LFFLLIGCALF--AAAMFAsidaaAISAFVLALLYIKgPLEMLVSALPILAQAQIACQRLADFgerFNEPepelelSDAD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 319 RTLL--PAFTWNeQSRLTIQHLNFQYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNG 396
Cdd:TIGR01194 325 NVLLlaHDKSVD-SIELKDVHMNPKAPEGSEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 397 HQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNIRfyqPTASNEEVQQAMEQAGLAKFIATLPQGLQTRVgeagrGISGGQ 476
Cdd:TIGR01194 404 AAVSADSRDDYRDLFSAIFADFHLFDDLIGPDEG---EHASLDNAQQYLQRLEIADKVKIEDGGFSTTT-----ALSTGQ 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 477 AQRIMLARAFLvQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQMDYVLVLDNGKIAEQ 551
Cdd:TIGR01194 476 QKRLALICAWL-EDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQgkTIIIISHDDQYFELADQIIKLAAGCIVKD 551
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
335-571 |
3.73e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLpHLAQDQWQQQFTYL 414
Cdd:PRK11124 5 LNGINCFYGAH--QA-LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 415 PQK-----------PYLfsdTIANNIrFYQPT-----ASNEEVQQAME---QAGLAKFIATLPQGLqtrvgeagrgiSGG 475
Cdd:PRK11124 81 RRNvgmvfqqynlwPHL---TVQQNL-IEAPCrvlglSKDQALARAEKlleRLRLKPYADRFPLHL-----------SGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 476 QAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLV-LFATHRLHWLEQM-DYVLVLDNGKIAEQGP 553
Cdd:PRK11124 146 QQQRVAIARA-LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITqVIVTHEVEVARKTaSRVVYMENGHIVEQGD 224
|
250
....*....|....*...
gi 2468565974 554 VKQLLQKQHGPFFELTSH 571
Cdd:PRK11124 225 ASCFTQPQTEAFKNYLSH 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-558 |
4.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDTMDQvnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYL 414
Cdd:PRK13644 4 LENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 415 ----PQKPYLfSDTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLAr 484
Cdd:PRK13644 82 vfqnPETQFV-GRTVEEDLAFgpenlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTL-----------SGGQGQCVALA- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 485 AFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLL 558
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
353-562 |
4.63e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 85.49 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 353 DLNLTL-QGyERVAIIGQSGAGKSTLLEALSGFVIPQ---TGNIQLNGHQLPHLAQDQWQQ----QFTYLPQKPY----- 419
Cdd:COG0444 23 GVSFDVrRG-ETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDPMtslnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 420 LFS--DTIANNIRFYQP---TASNEEVQQAMEQAGL---AKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQR 491
Cdd:COG0444 102 VMTvgDQIAEPLRIHGGlskAEARERAIELLERVGLpdpERRLDRYPHEL-----------SGGMRQRVMIARALALEPK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 492 hILIFDEPTAHLDIETEyalkKTMVQLF-----EHHL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQK-QH 562
Cdd:COG0444 171 -LLIADEPTTALDVTIQ----AQILNLLkdlqrELGLaILFITHDLGVVAEIaDRVAVMYAGRIVEEGPVEELFENpRH 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
351-557 |
5.27e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGfVIPQTGNIQLNGHQLPHLAQdqwQQQFTYLPQKPYLFSD------- 423
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLR-LINSQGEIWFDGQPLHNLNR---RQLLPVRHRIQVVFQDpnsslnp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 424 ------TIANNIRFYQPTAS----NEEVQQAMEQAGLAkfiatlPQGLQTRVGEagrgISGGQAQRIMLARAfLVQQRHI 493
Cdd:PRK15134 378 rlnvlqIIEEGLRVHQPTLSaaqrEQQVIAVMEEVGLD------PETRHRYPAE----FSGGQRQRIAIARA-LILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 494 LIFDEPTAHLDIETE---YALKKTMVQlfEHHLV-LFATHRLHWLEQMDY-VLVLDNGKIAEQGPVKQL 557
Cdd:PRK15134 447 IILDEPTSSLDKTVQaqiLALLKSLQQ--KHQLAyLFISHDLHVVRALCHqVIVLRQGEVVEQGDCERV 513
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
365-558 |
7.62e-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: 83.33 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 365 AIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQK-----PYLFSDTIA-NNIRFY-----Q 433
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVEQDsdtavPLTVRDVVAlGRIPHRslwagD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 434 PTASNEEVQQAMEQAGLAKFiatlpqglqtrvgeAGRG---ISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYA 510
Cdd:TIGR03873 111 SPHDAAVVDRALARTELSHL--------------ADRDmstLSGGERQRVHVARA-LAQEPKLLLLDEPTNHLDVRAQLE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2468565974 511 LKKTMVQLFEHHL-VLFATHRL-HWLEQMDYVLVLDNGKIAEQGPVKQLL 558
Cdd:TIGR03873 176 TLALVRELAATGVtVVAALHDLnLAASYCDHVVVLDGGRVVAAGPPREVL 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
351-561 |
1.21e-17 |
|
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: 87.27 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGhqlphlaqdqwqqQFTYLPQKPYLFSDTIANNIR 430
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 431 FyqpTASNEEVQ--QAMEQAGLAKFIATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETE 508
Cdd:TIGR01271 509 F---GLSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARA-VYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 509 YAL-KKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:TIGR01271 585 KEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
19-308 |
1.33e-17 |
|
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: 83.37 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 19 LAGLTVLQAFMILFQAIFLAKVLVLSWQRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLAQVY 98
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 99 TTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLVLVFPIIILFMIILG--- 175
Cdd:cd07346 84 RLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRrri 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 176 YAAKDKASSQYAEyvvLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTLSIAIL 255
Cdd:cd07346 164 RKASREVRESLAE---LSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 256 AVFLGLALMNGTLPLyPALVT-LILAPEYFLPLRDFASDYhatlngkNAFQQTL 308
Cdd:cd07346 241 LLYGGYLVLQGSLTI-GELVAfLAYLGMLFGPIQRLANLY-------NQLQQAL 286
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
331-557 |
1.54e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 84.35 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 331 SRLTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAqdqwqqq 410
Cdd:COG3839 2 ASLELENVSKSYGGV--EA-LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 ftylPQKP---YLFSD-------TIANNIRFY-----QPTAS-NEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSG 474
Cdd:COG3839 72 ----PKDRniaMVFQSyalyphmTVYENIAFPlklrkVPKAEiDRRVREAAELLGLEDLLDRKPKQL-----------SG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 475 GQAQRIMLARAfLVQQRHILIFDEPTAHLDieteYALKKTM-VQLFEHHL-----VLFATHRLHwlEQM---DYVLVLDN 545
Cdd:COG3839 137 GQRQRVALGRA-LVREPKVFLLDEPLSNLD----AKLRVEMrAEIKRLHRrlgttTIYVTHDQV--EAMtlaDRIAVMND 209
|
250
....*....|..
gi 2468565974 546 GKIAEQGPVKQL 557
Cdd:COG3839 210 GRIQQVGTPEEL 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
353-552 |
1.62e-17 |
|
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: 81.57 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 353 DLNLTLQGyERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLphlaQDQWQQQFT--------YLPQKPYLFSD- 423
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL----FDSRKKINLppqqrkigLVFQQYALFPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 424 TIANNIRFYQPTASNEEVQQAMEQAgLAKFiatlpqGLQTRVGEAGRGISGGQAQRIMLARAFLVQQRhILIFDEPTAHL 503
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVDEL-LDLL------GLDHLLNRYPAQLSGGEKQRVALARALAAQPE-LLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 504 DIETEYALKKTMVQLFEH-HL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQG 552
Cdd:cd03297 163 DRALRLQLLPELKQIKKNlNIpVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
351-569 |
1.78e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.53 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPylfSDTIANNIR 430
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 431 FYQ-------------PTASNEEVQQAMEQAGLakfiatlpqgLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFD 497
Cdd:PRK15112 106 ISQildfplrlntdlePEQREKQIIETLRQVGL----------LPDHASYYPHMLAPGQKQRLGLARA-LILRPKVIIAD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 498 EPTAHLDIETEYALKKTMVQLFEHHLV--LFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQkqhGPFFELT 569
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVLA---SPLHELT 246
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
333-567 |
2.13e-17 |
|
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: 81.96 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVNlkDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFT 412
Cdd:cd03295 1 IEFENVTKRYGGGKKAVN--NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRF------YQPTASNEEVQQAMEQAGL--AKFIATLPQGLqtrvgeagrgiSGGQAQRIMLA 483
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALvpkllkWPKEKIRERADELLALVGLdpAEFADRYPHEL-----------SGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 484 RAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFE--HHLVLFATH------RLhwleqMDYVLVLDNGKIAEQGPVK 555
Cdd:cd03295 148 RA-LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHdideafRL-----ADRIAIMKNGEIVQVGTPD 221
|
250
....*....|..
gi 2468565974 556 QLLQKQHGPFFE 567
Cdd:cd03295 222 EILRSPANDFVA 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
336-557 |
2.38e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.54 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 336 QHLNFQYDDTMDQvnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLP 415
Cdd:PRK13652 7 RDLCYSYSGSKEA--LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 416 QKP--YLFSDTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLArAFL 487
Cdd:PRK13652 85 QNPddQIFSPTVEQDIAFgpinlgLDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIA-GVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 488 VQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
351-546 |
2.50e-17 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 82.60 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGhqlphlaqdqwqqQFTYLPQKPYLFSDTIANNIR 430
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 431 F---YQPTASNEEVQQAMEQAGLAKFiatlPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIET 507
Cdd:cd03291 120 FgvsYDEYRYKSVVKACQLEEDITKF----PEKDNTVLGEGGITLSGGQRARISLARA-VYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2468565974 508 EYAL-KKTMVQLFEHHLVLFATHRLHWLEQMDYVLVLDNG 546
Cdd:cd03291 195 EKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
333-558 |
2.51e-17 |
|
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: 81.57 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQ-WQQQF 411
Cdd:COG0410 4 LEVENLHAGYGGI--HV-LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSD-TIANNIRF-YQPTASNEEVQQAMEQAgLAKFiatlPQgLQTRVGEAGRGISGGQAQriMLA--RAfL 487
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLLgAYARRDRAEVRADLERV-YELF----PR-LKERRRQRAGTLSGGEQQ--MLAigRA-L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 488 VQQRHILIFDEPTAHL------DIETeyALKK------TMVqLFEHHLVlFAthrlhwLEQMDYVLVLDNGKIAEQGPVK 555
Cdd:COG0410 152 MSRPKLLLLDEPSLGLapliveEIFE--IIRRlnregvTIL-LVEQNAR-FA------LEIADRAYVLERGRIVLEGTAA 221
|
...
gi 2468565974 556 QLL 558
Cdd:COG0410 222 ELL 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
335-571 |
3.44e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLpHLAQDQWQQQFTYL 414
Cdd:COG4161 5 LKNINCFYGSH--QA-LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 415 PQK-----------PYLfsdTIANN-----IRFYQPT--ASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQ 476
Cdd:COG4161 81 RQKvgmvfqqynlwPHL---TVMENlieapCKVLGLSkeQAREKAMKLLARLRLTDKADRFPLHL-----------SGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 477 AQRIMLARAFLVQQRhILIFDEPTAHLD--IETEYA-----LKKT-MVQLFEHHLVLFAThrlhwlEQMDYVLVLDNGKI 548
Cdd:COG4161 147 QQRVAIARALMMEPQ-VLLFDEPTAALDpeITAQVVeiireLSQTgITQVIVTHEVEFAR------KVASQVVYMEKGRI 219
|
250 260
....*....|....*....|...
gi 2468565974 549 AEQGPVKQLLQKQHGPFFELTSH 571
Cdd:COG4161 220 IEQGDASHFTQPQTEAFAHYLSH 242
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
333-567 |
4.65e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.77 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGN---IQLNGHQLPhlAQDQW-- 407
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPA-LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLT--AKTVWdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 408 QQQFTYLPQKP--YLFSDTIANNIRF--YQPTASNEE----VQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQR 479
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAFglENRAVPRPEmikiVRDVLADVGMLDYIDSEPANL-----------SGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 480 IMLARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLF-EHHLVLFA-THRLHWLEQMDYVLVLDNGKIAEQG-PV-- 554
Cdd:PRK13640 152 VAIAGILAVEPK-IIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISiTHDIDEANMADQVLVLDDGKLLAQGsPVei 230
|
250
....*....|....*...
gi 2468565974 555 --KQLLQKQHG---PFFE 567
Cdd:PRK13640 231 fsKVEMLKEIGldiPFVY 248
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
333-552 |
5.66e-17 |
|
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: 80.36 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLaqDQWQQQFT 412
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARA 485
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFglrlkkLPKAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 486 fLVQQRHILIFDEPTAHLDieteYALKKTM-VQLFEHH-----LVLFATHRLHwlEQM---DYVLVLDNGKIAEQG 552
Cdd:cd03300 145 -LVNEPKVLLLDEPLGALD----LKLRKDMqLELKRLQkelgiTFVFVTHDQE--EALtmsDRIAVMNKGKIQQIG 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
353-529 |
7.21e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.46 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 353 DLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLaQDQWQQQFTYLPQKPYLFSD-TIANNIRF 431
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQDLLYLGHQPGIKTElTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 432 YQP---TASNEEVQQAMEQAGLAKF----IATLPQGLQTRVGeagrgisggqaqrimLARAFLVqQRHILIFDEP-TAhL 503
Cdd:PRK13538 98 YQRlhgPGDDEALWEALAQVGLAGFedvpVRQLSAGQQRRVA---------------LARLWLT-RAPLWILDEPfTA-I 160
|
170 180 190
....*....|....*....|....*....|....
gi 2468565974 504 DieteyalKK---TMVQLFEHHL-----VLFATH 529
Cdd:PRK13538 161 D-------KQgvaRLEALLAQHAeqggmVILTTH 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
354-529 |
9.31e-17 |
|
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: 79.07 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 354 LNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLpHLAQDQWQQQFTYLPQKPYLFSD-TIANNIRFY 432
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTlSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 433 QPTASNEEVQQAMEQAGLAKF----IATLpqglqtrvgeagrgiSGGQAQRIMLARaFLVQQRHILIFDEPTAHLDIETE 508
Cdd:cd03231 98 HADHSDEQVEEALARVGLNGFedrpVAQL---------------SAGQQRRVALAR-LLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....*.
gi 2468565974 509 YALKKTMVQlfehHL-----VLFATH 529
Cdd:cd03231 162 ARFAEAMAG----HCarggmVVLTTH 183
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
51-550 |
1.08e-16 |
|
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: 83.31 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 51 SQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNL 130
Cdd:COG4615 45 AALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 131 ILSKFMNMMIIpwIL-LVYIFWqnlTSGIVLVLVFpIIILFMIILGYAAKDKASSQYA----EYVVLSNHFLDALRGLtt 205
Cdd:COG4615 125 LPELLQSVALV--LGcLAYLAW---LSPPLFLLTL-VLLGLGVAGYRLLVRRARRHLRrareAEDRLFKHFRALLEGF-- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 206 lKMLGLSKE-----YTHNIYQVSENYRKKTLSTLRIAILstfALDWFTTLSIAILAVFLGLALMNGTLPlyPALVTLILA 280
Cdd:COG4615 197 -KELKLNRRrrrafFDEDLQPTAERYRDLRIRADTIFAL---ANNWGNLLFFALIGLILFLLPALGWAD--PAVLSGFVL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 281 PEYFL--PLRDFASDYHATLNGKNAFQQTLDI-LAIPT-VTDRTLLPAFTWNEQ-SRLTIQHLNFQYDDTMDQVN--LKD 353
Cdd:COG4615 271 VLLFLrgPLSQLVGALPTLSRANVALRKIEELeLALAAaEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDEGftLGP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 354 LNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIAnnirfYQ 433
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRLLG-----LD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 434 PTASNEEVQQAMEQAGLAKfiatlpqglQTRVgEAGR----GISGGQAQRIMLARAFLvQQRHILIFDEPTAHLDIE--- 506
Cdd:COG4615 426 GEADPARARELLERLELDH---------KVSV-EDGRfsttDLSQGQRKRLALLVALL-EDRPILVFDEWAADQDPEfrr 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 507 ---TEY--ALK---KTmvqlfehhlVLFATHRLHWLEQMDYVLVLDNGKIAE 550
Cdd:COG4615 495 vfyTELlpELKargKT---------VIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
351-548 |
1.11e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIqLNGHQLPHLAQDQWQQQFT---YLPQKpylfsdTIAN 427
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMFQdarLLPWK------KVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 428 NIRFYQPTASNEEVQQAMEQAGLAKfiatlpqglqtRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIET 507
Cdd:PRK11247 101 NVGLGLKGQWRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARA-LIHRPGLLLLDEPLGALDALT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2468565974 508 EYALKKTMVQLFEHH--LVLFATHRLHWLEQM-DYVLVLDNGKI 548
Cdd:PRK11247 169 RIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
333-560 |
1.27e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.45 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNF--QYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQlphLAQDQWQQQ 410
Cdd:PRK13634 3 ITFQKVEHryQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV---ITAGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQK-------P--YLFSDTIANNIRFyQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRvgeAGRGISGGQAQRIM 481
Cdd:PRK13634 80 LKPLRKKvgivfqfPehQLFEETVEKDICF-GPMNFGVSEEDAKQKAREMIELVGLPEELLAR---SPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LArAFLVQQRHILIFDEPTAHLDIETeyalKKTMVQLF-----EHHL-VLFATHrlhwleQM-------DYVLVLDNGKI 548
Cdd:PRK13634 156 IA-GVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFyklhkEKGLtTVLVTH------SMedaaryaDQIVVMHKGTV 224
|
250
....*....|..
gi 2468565974 549 AEQGPVKQLLQK 560
Cdd:PRK13634 225 FLQGTPREIFAD 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
329-561 |
1.35e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.28 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 329 EQSRLTIQHLNFQYDDTMDQvnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQD--Q 406
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 407 WQQQFTYLPQKP--YLFSDTIANNIRF------YQPTASNEEVQQAMEQAGLAKfiatlpqgLQTRVGEAgrgISGGQAQ 478
Cdd:PRK13636 80 LRESVGMVFQDPdnQLFSASVYQDVSFgavnlkLPEDEVRKRVDNALKRTGIEH--------LKDKPTHC---LSFGQKK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 479 RIMLArAFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLE-QMDYVLVLDNGKIAEQGPVK 555
Cdd:PRK13636 149 RVAIA-GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPK 227
|
....*.
gi 2468565974 556 QLLQKQ 561
Cdd:PRK13636 228 EVFAEK 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
352-558 |
1.52e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 352 KDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQKPYLFSDTIANNI-- 429
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELva 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 430 --RF-YQP--TASNEEVQQAMEQAGLAKFIATLP-QGLQTrvgeagrgISGGQAQRIMLARAfLVQQRHILIFDEPTAHL 503
Cdd:PRK10253 104 rgRYpHQPlfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMV-LAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 504 DIETEYALKKTMVQL-FEHHLVLFAThrLHWLEQ----MDYVLVLDNGKIAEQGPVKQLL 558
Cdd:PRK10253 175 DISHQIDLLELLSELnREKGYTLAAV--LHDLNQacryASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
333-557 |
1.66e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.43 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALS--GFVIPQ---TGNIQLNGHQL--PHLAQD 405
Cdd:PRK14239 6 LQVSDLSVYYNK---KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIysPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 406 QWQQQFTYLPQKPYLFSDTIANNIRF---YQPTASNEEVQQAMEQAGLAkfiATLPQGLQTRVGEAGRGISGGQAQRIML 482
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFPMSIYENVVYglrLKGIKDKQVLDEAVEKSLKG---ASIWDEVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 483 ARAFLVQQRHILIfDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:PRK14239 160 ARVLATSPKIILL-DEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQM 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-564 |
1.72e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.15 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQwqqqFT 412
Cdd:COG4152 2 LELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR----IG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRF------YQPTASNEEVQQAMEQAGLA----KFIATLpqglqtrvgeagrgiSGGQAQRIM 481
Cdd:COG4152 75 YLPEERGLYPKmKVGEQLVYlarlkgLSKAEAKRRADEWLERLGLGdranKKVEEL---------------SKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LARAFLvqqrH---ILIFDEPTAHLD-IETEyALKKTmvqLFEHH----LVLFATHRLHWLEQM-DYVLVLDNGKIAEQG 552
Cdd:COG4152 140 LIAALL----HdpeLLILDEPFSGLDpVNVE-LLKDV---IRELAakgtTVIFSSHQMELVEELcDRIVIINKGRKVLSG 211
|
250
....*....|..
gi 2468565974 553 PVKQlLQKQHGP 564
Cdd:COG4152 212 SVDE-IRRQFGR 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
351-562 |
1.77e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.73 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQqFTYLPQkpYLFSDTI-ANNI 429
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA-FRRDIQ--MVFQDSIsAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 430 RFY------QP----TASNEEVQQA-----MEQAGLAKFIAT-LPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQRhI 493
Cdd:PRK10419 105 RKTvreiirEPlrhlLSLDKAERLArasemLRAVDLDDSVLDkRPPQL-----------SGGQLQRVCLARALAVEPK-L 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 494 LIFDEPTAHLDIeteyALKKTMVQLFEH------HLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQKQH 562
Cdd:PRK10419 173 LILDEAVSNLDL----VLQAGVIRLLKKlqqqfgTACLFITHDLRLVERFcQRVMVMDNGQIVETQPVGDKLTFSS 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
351-564 |
1.95e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.24 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLpHLAQDQWQQQFTYLPQKPYLFSDTIA---N 427
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI-NLVRDKDGQLKVADKNQLRLLRTRLTmvfQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 428 NIRFYQPTASNEEVQQAMEQA-GLAKFIA-TLPQGLQTRVG--EAGRG-----ISGGQAQRIMLARAfLVQQRHILIFDE 498
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQVlGLSKQEArERAVKYLAKVGidERAQGkypvhLSGGQQQRVSIARA-LAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 499 PTAHLDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQKQHGP 564
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
333-548 |
2.56e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.39 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPhlAQDQW--QQQ 410
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT--EENVWdiRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKP--YLFSDTIANNIRF--------YQPTAsnEEVQQAMEQAGLAKFiatlpqglQTRvgEAGRgISGGQAQRI 480
Cdd:PRK13650 83 IGMVFQNPdnQFVGATVEDDVAFglenkgipHEEMK--ERVNEALELVGMQDF--------KER--EPAR-LSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 481 MLARAflVQQR-HILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQMDYVLVLDNGKI 548
Cdd:PRK13650 150 AIAGA--VAMRpKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
333-553 |
3.01e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.85 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQdQWQQQFT 412
Cdd:PRK13537 8 IDFRNVEKRYGD---KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRFYQPTASNEEVQQAMEQAGLAKFiATLPQGLQTRVGEagrgISGGQAQRIMLARAfLVQQR 491
Cdd:PRK13537 84 VVPQFDNLDPDfTVRENLLVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARA-LVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 492 HILIFDEPTAHLDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQM-DYVLVLDNG-KIAEQGP 553
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERLcDRLCVIEEGrKIAEGAP 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
351-562 |
3.23e-16 |
|
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: 78.69 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQwQQQFTYLPQkpYLFSDT------ 424
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ-RRAFRRDVQ--LVFQDSpsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 425 -------IANNIRFY---QPTASNEEVQQAMEQAGLAKFIA-TLPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQRhI 493
Cdd:TIGR02769 104 rmtvrqiIGEPLRHLtslDESEQKARIAELLDMVGLRSEDAdKLPRQL-----------SGGQLQRINIARALAVKPK-L 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 494 LIFDEPTAHLDIeteyALKKTMVQLFEH------HLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQKQH 562
Cdd:TIGR02769 172 IVLDEAVSNLDM----VLQAVILELLRKlqqafgTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLLSFKH 243
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
333-552 |
3.79e-16 |
|
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: 77.30 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ---- 408
Cdd:cd03301 1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDiamv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 -QQFTYLPQKpylfsdTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPqglqtrvgeagRGISGGQAQRIM 481
Cdd:cd03301 78 fQNYALYPHM------TVYDNIAFglklrkVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 482 LARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHrlHWLEQM---DYVLVLDNGKIAEQG 552
Cdd:cd03301 141 LGRA-IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLgtTTIYVTH--DQVEAMtmaDRIAVMNDGQIQQIG 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
354-558 |
4.26e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.05 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 354 LNLTLQGYERVAIIGQSGAGKSTLLEALSGfVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQK-PYLFSDTIANNIRFY 432
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 433 QPT-ASNEEVQQAMEQ-AGLAKFIATLPQGLQTrvgeagrgISGGQAQRIMLARAFLVQQRHI------LIFDEPTAHLD 504
Cdd:PRK03695 94 QPDkTRTEAVASALNEvAEALGLDDKLGRSVNQ--------LSGGEWQRVRLAAVVLQVWPDInpagqlLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 505 IETEYALKKTMVQLFEHHL-VLFATHRL-HWLEQMDYVLVLDNGKIAEQGPVKQLL 558
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIaVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
335-556 |
4.46e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.94 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDTM--DQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQL--PHLAQDQWQQQ 410
Cdd:PRK13637 5 IENLTHIYMEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKP--YLFSDTIANNIRFyQPT---ASNEE----VQQAMEQAGLAKfiatlpQGLQTRvgeAGRGISGGQAQRIM 481
Cdd:PRK13637 85 VGLVFQYPeyQLFEETIEKDIAF-GPInlgLSEEEienrVKRAMNIVGLDY------EDYKDK---SPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LArAFLVQQRHILIFDEPTAHLDIETE---YALKKTMVQLFEHHLVLFAthrlHWLEQM----DYVLVLDNGKIAEQGPV 554
Cdd:PRK13637 155 IA-GVVAMEPKILILDEPTAGLDPKGRdeiLNKIKELHKEYNMTIILVS----HSMEDVaklaDRIIVMNKGKCELQGTP 229
|
..
gi 2468565974 555 KQ 556
Cdd:PRK13637 230 RE 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
331-529 |
4.49e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 78.37 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 331 SRLTIQHLNFQYD-DTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ- 408
Cdd:COG4525 2 SMLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 -QQFTYLPQKPYLfsDTIANNIRFyQPTASNEEVQQAME---QAGLAKFiatlpqglqtrvgeAGRGI---SGGQAQRIM 481
Cdd:COG4525 82 fQKDALLPWLNVL--DNVAFGLRL-RGVPKAERRARAEEllaLVGLADF--------------ARRRIwqlSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 482 LARAFLVQQRhILIFDEPTAHLDIETeyalKKTMVQLF------EHHLVLFATH 529
Cdd:COG4525 145 IARALAADPR-FLLMDEPFGALDALT----REQMQELLldvwqrTGKGVFLITH 193
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
333-557 |
5.22e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 79.74 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHL-AQDqwqQQF 411
Cdd:PRK10851 3 IEIANIKKSFGRT--QV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLhARD---RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSD-TIANNIRF--------YQPTAS--NEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRI 480
Cdd:PRK10851 77 GFVFQHYALFRHmTVFDNIAFgltvlprrERPNAAaiKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 481 MLARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLFEH--HLVLFATH-RLHWLEQMDYVLVLDNGKIAEQGPVKQL 557
Cdd:PRK10851 146 ALARALAVEPQ-ILLLDEPFGALDAQVRKELRRWLRQLHEElkFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
333-562 |
6.31e-16 |
|
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: 80.88 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLN--FQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKS-TLLEAL----SGFVIPqTGNIQLNGHQLPHLAQD 405
Cdd:COG4172 7 LSVEDLSvaFGQGGGTVEA-VKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHP-SGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 406 QWQQ----QFTYLPQKPY-----LFS--DTIANNIRFYQ---PTASNEEVQQAMEQAGL---AKFIATLPQGLqtrvgea 468
Cdd:COG4172 85 ELRRirgnRIAMIFQEPMtslnpLHTigKQIAEVLRLHRglsGAAARARALELLERVGIpdpERRLDAYPHQL------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 469 grgiSGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETE---YALKKTMVQlfEHHL-VLFATHRLHWLEQM-DYVLVL 543
Cdd:COG4172 158 ----SGGQRQRVMIAMA-LANEPDLLIADEPTTALDVTVQaqiLDLLKDLQR--ELGMaLLLITHDLGVVRRFaDRVAVM 230
|
250 260
....*....|....*....|
gi 2468565974 544 DNGKIAEQGPVKQLL-QKQH 562
Cdd:COG4172 231 RQGEIVEQGPTAELFaAPQH 250
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
333-562 |
7.66e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 77.57 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTM------DQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHlaqdq 406
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 407 wqQQFTYLpqkpylfsdtiANNIR--FYQPTAS---NEEVQQAME-----------QAGLAKFIATLPQ-GL-------- 461
Cdd:COG4167 80 --GDYKYR-----------CKHIRmiFQDPNTSlnpRLNIGQILEeplrlntdltaEEREERIFATLRLvGLlpehanfy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 462 -QTrvgeagrgISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLV--LFATHRLHWLEQM- 537
Cdd:COG4167 147 pHM--------LSSGQKQRVALARA-LILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGIsyIYVSQHLGIVKHIs 217
|
250 260
....*....|....*....|....*.
gi 2468565974 538 DYVLVLDNGKIAEQGPVKQLL-QKQH 562
Cdd:COG4167 218 DKVLVMHQGEVVEYGKTAEVFaNPQH 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
351-548 |
1.02e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.45 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQ---WQQQFTYLPQKPYLFSD-TIA 426
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDrTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NN--IRFYQPTASNEEVQQ----AMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAfLVQQRHILIFDEPT 500
Cdd:PRK10908 98 DNvaIPLIIAGASGDDIRRrvsaALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARA-VVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 501 AHLDieteYALKKTMVQLFEHH-----LVLFATHRLHWLEQMDY-VLVLDNGKI 548
Cdd:PRK10908 166 GNLD----DALSEGILRLFEEFnrvgvTVLMATHDIGLISRRSYrMLTLSDGHL 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
351-552 |
1.05e-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: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLphlaQDQWQQQFTYLPQKPYLFSD-TIANNI 429
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLPEERGLYPKmKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 430 RF------YQPTASNEEVQQAMEQAGLAKFiatlpqgLQTRVGEagrgISGGQAQRIMLARAfLVQQRHILIFDEPTAHL 503
Cdd:cd03269 92 VYlaqlkgLKKEEARRRIDEWLERLELSEY-------ANKRVEE----LSKGNQQKVQFIAA-VIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 504 D-IETEYALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQG 552
Cdd:cd03269 160 DpVNVELLKDVIRELARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
335-561 |
1.15e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.47 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLpHLAQDQW-QQQFTY 413
Cdd:PRK13647 7 VEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NAENEKWvRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 414 LPQKP--YLFSDTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLArA 485
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAFgpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIA-G 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 486 FLVQQRHILIFDEPTAHLDIETEYALKKTMVQLF-EHHLVLFATHRLHW-LEQMDYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
333-504 |
1.34e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.72 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAqdQWQQQFT 412
Cdd:PRK11607 20 LEIRNLTKSFDG---QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRF-----YQPTAS-NEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARA 485
Cdd:PRK11607 95 MMFQSYALFPHmTVEQNIAFglkqdKLPKAEiASRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARS 163
|
170
....*....|....*....
gi 2468565974 486 fLVQQRHILIFDEPTAHLD 504
Cdd:PRK11607 164 -LAKRPKLLLLDEPMGALD 181
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
351-552 |
1.35e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.82 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQ--LNGHQLPHLAQDQWQQQFTYLPQKPY--------- 419
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKEKVLEKLVIQKTRfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 420 ---------------LFSDTIANNIRFyQPTASNEEVQQAMEQAglAKFIAT--LPQGLQTRvgeAGRGISGGQAQRIML 482
Cdd:PRK13651 103 irrrvgvvfqfaeyqLFEQTIEKDIIF-GPVSMGVSKEEAKKRA--AKYIELvgLDESYLQR---SPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 483 ArAFLVQQRHILIFDEPTAHLDIETeyalKKTMVQLFEH-----HLVLFATHRL-HWLEQMDYVLVLDNGKIAEQG 552
Cdd:PRK13651 177 A-GILAMEPDFLVFDEPTAGLDPQG----VKEILEIFDNlnkqgKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDG 247
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
351-560 |
1.67e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.13 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQW----QQQFTYLPQKP--YLFSDT 424
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirpvRKRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 425 IANNIRFyQPTASNEEVQQAMEQAglakFIATLPQGLQTRVGEAGR-GISGGQAQRIMLArAFLVQQRHILIFDEPTAHL 503
Cdd:PRK13646 103 VEREIIF-GPKNFKMNLDEVKNYA----HRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIV-SILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 504 DIETEYALKKTM--VQLFEHHLVLFATHRLHWLEQ-MDYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:PRK13646 177 DPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
334-554 |
3.05e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.15 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 334 TIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ---- 408
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 ------QQFtYLpqkpyLFSDTIANNIRFyqptasneevqqAMEQAGLAK-FIATLPQGLQTRVGEAGRG------ISGG 475
Cdd:PRK11153 83 qigmifQHF-NL-----LSSRTVFDNVAL------------PLELAGTPKaEIKARVTELLELVGLSDKAdrypaqLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 476 QAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYA----LKKTMVQLfehHL-VLFATHrlhwleQM-------DYVLVL 543
Cdd:PRK11153 145 QKQRVAIARA-LASNPKVLLCDEATSALDPATTRSilelLKDINREL---GLtIVLITH------EMdvvkricDRVAVI 214
|
250
....*....|.
gi 2468565974 544 DNGKIAEQGPV 554
Cdd:PRK11153 215 DAGRLVEQGTV 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
337-554 |
3.55e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 337 HLNFQydDTMDQVNLkDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDqwqqqfTYLPq 416
Cdd:PRK11144 3 ELNFK--QQLGDLCL-TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKG------ICLP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 417 kP------YLFSD-------TIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLA 483
Cdd:PRK11144 73 -PekrrigYVFQDarlfphyKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSL-----------SGGEKQRVAIG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 484 RAFLVQQRhILIFDEPTAHLDIEteyalKKTMVQLFEHHL-------VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPV 554
Cdd:PRK11144 141 RALLTAPE-LLLMDEPLASLDLP-----RKRELLPYLERLareinipILYVSHSLDEILRLaDRVVVLEQGKVKAFGPL 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
352-565 |
4.96e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.28 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 352 KDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQ-----QFTYlpQKPyLFS---- 422
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsdiQMIF--QDP-LASlnpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 423 ----DTIANNIRFYQPTASNEEVQQ----AMEQAGLakfiatLPQGLQTRVGEagrgISGGQAQRIMLARAFLVQQRHIl 494
Cdd:PRK15079 115 mtigEIIAEPLRTYHPKLSRQEVKDrvkaMMLKVGL------LPNLINRYPHE----FSGGQCQRIGIARALILEPKLI- 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 495 IFDEPTAHLDIeteyALKKTMVQLF-----EHHLVL-FATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQKQHGPF 565
Cdd:PRK15079 184 ICDEPVSALDV----SIQAQVVNLLqqlqrEMGLSLiFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
351-550 |
5.03e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 75.08 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ-----FtylpQKPYLFSD-T 424
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiartF----QNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 425 IANNIR---------------FYQPTASNEE---VQQAMEQagLAKFiatlpqGLQTRVGEAGRGISGGQAQRIMLARAf 486
Cdd:COG0411 96 VLENVLvaaharlgrgllaalLRLPRARREEreaRERAEEL--LERV------GLADRADEPAGNLSYGQQRRLEIARA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 487 LVQQRHILIFDEPTAHLDIEteyaLKKTMVQLF--------------EHHL-VLFAThrlhwleqMDYVLVLDNG-KIAE 550
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPE----ETEELAELIrrlrdergitilliEHDMdLVMGL--------ADRIVVLDFGrVIAE 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
351-548 |
5.24e-15 |
|
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: 73.24 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ-FTYLP---QKPYLFSD-TI 425
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrKREGLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 426 ANNIrfyqptasneevqqameqaglakfiaTLPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQRhILIFDEPTAHLDI 505
Cdd:cd03215 96 AENI--------------------------ALSSLL-----------SGGNQQKVVLARWLARDPR-VLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2468565974 506 ETEYALKKTMVQLFEH-HLVLFATHRLHWLEQM-DYVLVLDNGKI 548
Cdd:cd03215 138 GAKAEIYRLIRELADAgKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-569 |
8.54e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.70 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 347 DQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLpHLAQDQWQ-------QQFTYLPQKPY 419
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL-YFGKDIFQidaiklrKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 420 LFSD-TIANNIRFyqPTASN-----EEVQQAMEQAgLAKfiATLPQGLQTRVGEAGRGISGGQAQRIMLARAFLVQQRhI 493
Cdd:PRK14246 101 PFPHlSIYDNIAY--PLKSHgikekREIKKIVEEC-LRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPK-V 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 494 LIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQKqhgPFFELT 569
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTS---PKNELT 248
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
330-551 |
8.95e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.66 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 330 QSRLTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ 408
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHELSiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 -----------QQFTYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQA 477
Cdd:PRK10584 84 klrakhvgfvfQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 478 QRIMLARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLFEHH---LVLfATHRLHWLEQMDYVLVLDNGKIAEQ 551
Cdd:PRK10584 153 QRVALARAFNGRPD-VLFADEPTGNLDRQTGDKIADLLFSLNREHgttLIL-VTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
328-531 |
9.19e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.43 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 328 NEQSRLTIQHLNFQYDDTMdqvNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGF--VIPQ---TGNIQLNGHQL--P 400
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFL---AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLyaP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 401 HLAQDQWQQQFTYLPQKPYLFSDTIANNIRF------YQPTAsNEEVQQAMEQAGLAKFIatlpqglQTRVGEAGRGISG 474
Cdd:PRK14243 83 DVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYgaringYKGDM-DELVERSLRQAALWDEV-------KDKLKQSGLSLSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 475 GQAQRIMLARAFLVQQRHILIfDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRL 531
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILM-DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
334-561 |
1.07e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.96 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 334 TIQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTY 413
Cdd:COG4604 3 EIKNVSKRYGGK---VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 414 LPQkpylfsdtiANNI-------------RF-Y---QPTASNEE-VQQAMEQAGLA----KFIATLpqglqtrvgeagrg 471
Cdd:COG4604 80 LRQ---------ENHInsrltvrelvafgRFpYskgRLTAEDREiIDEAIAYLDLEdladRYLDEL-------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 472 iSGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIetEYA-------------LKKTMVqlfehhLVL----FATHrlhwl 534
Cdd:COG4604 137 -SGGQRQRAFIAMV-LAQDTDYVLLDEPLNNLDM--KHSvqmmkllrrladeLGKTVV------IVLhdinFASC----- 201
|
250 260
....*....|....*....|....*..
gi 2468565974 535 eQMDYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:COG4604 202 -YADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
351-564 |
1.10e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.07 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQ----QFTYLPQKPYLFSD-TI 425
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 426 ANNIRF---YQPTASNEEVQQAmeQAGLAKFiatlpqGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAH 502
Cdd:PRK10535 104 AQNVEVpavYAGLERKQRLLRA--QELLQRL------GLEDRVEYQPSQLSGGQQQRVSIARA-LMNGGQVILADEPTGA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 503 LDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQKQHGP 564
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGT 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
349-560 |
1.45e-14 |
|
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: 74.22 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 349 VNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ-----------QQFTYLPQK 417
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRelrrkkismvfQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 418 pylfsdTIANNIRF-----YQPTASNEEV-QQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAfLVQQR 491
Cdd:cd03294 118 ------TVLENVAFglevqGVPRAEREERaAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARA-LAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 492 HILIFDEPTAHLD--IETEyaLKKTMVQLFEHH--LVLFATHRLHwlEQM---DYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:cd03294 180 DILLMDEAFSALDplIRRE--MQDELLRLQAELqkTIVFITHDLD--EALrlgDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
345-548 |
1.53e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.48 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 345 TMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLP----HLAQDQWQQQFTYLPQKP-- 418
Cdd:PRK13641 17 PMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQFPea 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 419 YLFSDTIANNIRFyQPTASNEEVQQAMEQAglAKFIATLpqGLQTRVGEAGR-GISGGQAQRIMLArAFLVQQRHILIFD 497
Cdd:PRK13641 97 QLFENTVLKDVEF-GPKNFGFSEDEAKEKA--LKWLKKV--GLSEDLISKSPfELSGGQMRRVAIA-GVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 498 EPTAHLDIETeyalKKTMVQLF-----EHHLVLFATHRLHWL-EQMDYVLVLDNGKI 548
Cdd:PRK13641 171 EPAAGLDPEG----RKEMMQLFkdyqkAGHTVILVTHNMDDVaEYADDVLVLEHGKL 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
351-556 |
1.80e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQL----PHLAQDQW----QQQFTylpqkpyLFS 422
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsPRDAIALGigmvHQHFM-------LVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 423 D-TIANNI---------RFYQPTASNEEVQQAMEQAGLAkfiatLPqgLQTRVGEagrgISGGQAQRIMLARAfLVQQRH 492
Cdd:COG3845 94 NlTVAENIvlgleptkgGRLDRKAARARIRELSERYGLD-----VD--PDAKVED----LSVGEQQRVEILKA-LYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 493 ILIFDEPTAHL-DIETEyALKKTMVQLF-EHHLVLFATHRLHwlEQM---DYVLVLDNGKIAEQGPVKQ 556
Cdd:COG3845 162 ILILDEPTAVLtPQEAD-ELFEILRRLAaEGKSIIFITHKLR--EVMaiaDRVTVLRRGKVVGTVDTAE 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
353-560 |
1.86e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 74.76 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 353 DLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ-----QQFTYLPQKpylfsdTIAN 427
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDicmvfQSYALFPHM------SLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 428 NIRF---YQPTASNE---EVQQAMEQAGLAkfiatlpqGLQTRVGEAgrgISGGQAQRIMLARAfLVQQRHILIFDEPTA 501
Cdd:PRK11432 98 NVGYglkMLGVPKEErkqRVKEALELVDLA--------GFEDRYVDQ---ISGGQQQRVALARA-LILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 502 HLDIETEYALKKTMVQLFEHHLV--LFATHrlhwlEQM------DYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNItsLYVTH-----DQSeafavsDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
22-287 |
2.37e-14 |
|
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: 73.45 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 22 LTVLQAFMILFQAIFLAKVL--VLSWQRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLAQVYT 99
Cdd:pfam00664 7 LAILSGAISPAFPLVLGRILdvLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 100 TGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLVLVFPIIILFMIILGYAAK 179
Cdd:pfam00664 87 QPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 180 DKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTLSIAILAVFL 259
Cdd:pfam00664 167 KLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFG 246
|
250 260
....*....|....*....|....*...
gi 2468565974 260 GLALMNGTLPLYPALVTLILAPEYFLPL 287
Cdd:pfam00664 247 AYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
351-552 |
3.58e-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: 72.37 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHqLPHLAQDQWQQQFTY-LPQKPYLF-----SDT 424
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVvFGQKTQLWwdlpvIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 425 IANNIRFYQptasneeVQQAMEQAGLAKFIATLPQG--LQTRVgeagRGISGGQAQRIMLARAfLVQQRHILIFDEPTAH 502
Cdd:cd03267 116 FYLLAAIYD-------LPPARFKKRLDELSELLDLEelLDTPV----RQLSLGQRMRAEIAAA-LLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 503 LDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQM-DYVLVLDNGKIAEQG 552
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-548 |
5.07e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.43 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLN--FqYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQ 409
Cdd:COG1101 2 LELKNLSktF-NPGTVNEKRaLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 410 QFTYLPQKPYL---FSDTIANN------------IRFYQPTASNEEVQQAMEQAGLAkfiatLPQGLQTRVGEagrgISG 474
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLGLG-----LENRLDTKVGL----LSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 475 GQAQRIMLARAFLVQQRhILIFDEPTAHLDIET-EYALKKT--MVQlfEHHL-VLFATHRL-HWLEQMDYVLVLDNGKI 548
Cdd:COG1101 152 GQRQALSLLMATLTKPK-LLLLDEHTAALDPKTaALVLELTekIVE--ENNLtTLMVTHNMeQALDYGNRLIMMHEGRI 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
351-544 |
1.28e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGhqlphlaqdqwQQQFTYLPQKPYLFSDTIANNIR 430
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQKLYLDTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 431 FYQ--PTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETE 508
Cdd:PRK09544 89 FLRlrPGTKKEDILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARA-LLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2468565974 509 YALKKTMVQLfEHHL---VLFATHRLHW-LEQMDYVLVLD 544
Cdd:PRK09544 157 VALYDLIDQL-RRELdcaVLMVSHDLHLvMAKTDEVLCLN 195
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
351-551 |
2.05e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQ----DQWQQQFTYLPQKPYLFSD-TI 425
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaELRNQKLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 426 ANNIRF------YQPTASNEEVQQAMEQAGLAKfiatlpqglqtRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEP 499
Cdd:PRK11629 105 LENVAMplligkKKPAEINSRALEMLAAVGLEH-----------RANHRPSELSGGERQRVAIARA-LVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 500 TAHLDIETEYALKKTMVQLFEHHLVLF--ATHRLHWLEQMDYVLVLDNGKIAEQ 551
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFlvVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-569 |
2.33e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFV-----IPQTGNIQLNGHQL------PHLAQDQWQQQFTYLPQKPY 419
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIyspdvdPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 420 L-FSDTIANNIRFYQPTASNEEVQQAMEQAgLAKfiATLPQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDE 498
Cdd:PRK14267 100 LtIYDNVAIGVKLNGLVKSKKELDERVEWA-LKK--AALWDEVKDRLNDYPSNLSGGQRQRLVIARA-LAMKPKILLMDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 499 PTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQKqhgPFFELT 569
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVFEN---PEHELT 244
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
333-529 |
2.77e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.11 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQL--PHLAQDQWQQQ 410
Cdd:PRK11248 2 LQISHLYADYGG---KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKPYLfsDTIANNIRFYQ-PTASNEEVQQAM-EQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAFLV 488
Cdd:PRK11248 79 EGLLPWRNVQ--DNVAFGLQLAGvEKMQRLEIAHQMlKKVGLEGAEKRYIWQL-----------SGGQRQRVGIARALAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2468565974 489 QQRhILIFDEPTAHLDIETEYALKKTMVQLFEH--HLVLFATH 529
Cdd:PRK11248 146 NPQ-LLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
336-560 |
3.01e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.50 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 336 QHLNFQYDDTMDQVN---LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQlPHLAQDQW--QQQ 410
Cdd:PRK13633 8 KNVSYKYESNEESTEklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWdiRNK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKP--YLFSDTIANNIRF------YQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIML 482
Cdd:PRK13633 87 AGMVFQNPdnQIVATIVEEDVAFgpenlgIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 483 ArAFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:PRK13633 156 A-GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
333-552 |
3.67e-13 |
|
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: 68.78 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDqwQQQFT 412
Cdd:cd03268 1 LKTNDLTKTYGK---KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSD-TIANNIRFYQ--PTASNEEVQQAMEQAGLAkfiatlpqglqTRVGEAGRGISGGQAQRIMLARAFLvQ 489
Cdd:cd03268 76 ALIEAPGFYPNlTARENLRLLArlLGIRKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALL-G 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 490 QRHILIFDEPTAHLDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQM-DYVLVLDNGKIAEQG 552
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
333-558 |
3.93e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.12 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPhlAQDQW--QQQ 410
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWnlRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKP--YLFSDTIANNIRFYQPTAS--NEEVQQAMEQAGLAKFIatlpqgLQTRVGEAGRgISGGQAQRIMLArAF 486
Cdd:PRK13642 83 IGMVFQNPdnQFVGATVEDDVAFGMENQGipREEMIKRVDEALLAVNM------LDFKTREPAR-LSGGQKQRVAVA-GI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 487 LVQQRHILIFDEPTAHLDIETEYALKKTMVQLFE--HHLVLFATHRLHWLEQMDYVLVLDNGKIAEQGPVKQLL 558
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
333-552 |
4.05e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.65 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQD--QWQQQ 410
Cdd:PRK13638 2 LATSDLWFRYQD--EPV-LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKP--YLFSDTIANNIRFYQPT--ASNEEVQQAMEQAglakfiATLPQGLQTRvGEAGRGISGGQAQRIMLARAF 486
Cdd:PRK13638 79 VATVFQDPeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEA------LTLVDAQHFR-HQPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 487 LVQQRHILIfDEPTAHLDIETE---YALKKTMVQLFEHhlVLFATHRLHWL-EQMDYVLVLDNGKIAEQG 552
Cdd:PRK13638 152 VLQARYLLL-DEPTAGLDPAGRtqmIAIIRRIVAQGNH--VIISSHDIDLIyEISDAVYVLRQGQILTHG 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
333-557 |
5.01e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 69.72 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQD--QWQQQ 410
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKP--YLFSDTIANNIRF--YQPTASNEEVQ----QAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIML 482
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFgpLNLGLSKEEVEkrvkEALKAVGMEGFENKPPHHL-----------SGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 483 ArAFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHL-VLFATHRLHWLE-QMDYVLVLDNGKIAEQGPVKQL 557
Cdd:PRK13639 149 A-GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGItIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
351-541 |
5.76e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.27 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFV----IPQTgNIQLNGHQLP---HLAQD--QWQQQFTYLPQKPYLF 421
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdkSAGS-HIELLGRTVQregRLARDirKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 422 SD-TIANNI---------------RFYQPtASNEEVQQAMEQAGLAKFIatlpqglQTRVGEagrgISGGQAQRIMLARA 485
Cdd:PRK09984 99 NRlSVLENVligalgstpfwrtcfSWFTR-EQKQRALQALTRVGMVHFA-------HQRVST----LSGGQQQRVAIARA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 486 fLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHrlhwLEQMDYVL 541
Cdd:PRK09984 167 -LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVT----LHQVDYAL 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
333-545 |
6.11e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.79 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLngHQLPHLAqdqwqqqft 412
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--PEGEDLL--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQKPYLFSDTIANNIRFyqptasneevqqameqaglakfiatlPQglqtrvgeaGRGISGGQAQRIMLARAFLVQQRh 492
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY--------------------------PW---------DDVLSGGEQQRLAFARLLLHKPK- 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 493 ILIFDEPTAHLDIETEyalkKTMVQLFEHHL--VLFATHRLHWLEQMDYVLVLDN 545
Cdd:cd03223 112 FVFLDEATSALDEESE----DRLYQLLKELGitVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
351-559 |
6.36e-13 |
|
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: 67.94 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGF--VIPQTGNIQLNGHQLPHLAQDQWQQQFTYL-PQKPYLFSD-TIA 426
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLaFQYPPEIPGvKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NNIRFyqptasneevqqameqaglakfiatlpqglqtrVGEagrGISGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIE 506
Cdd:cd03217 96 DFLRY---------------------------------VNE---GFSGGEKKRNEILQLLLLEPD-LAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 507 TEYALKKTMVQLFEHHL-VLFATHRLHWLEQM--DYVLVLDNGKIAEQGPVKQLLQ 559
Cdd:cd03217 139 ALRLVAEVINKLREEGKsVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKELALE 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
354-548 |
7.42e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.97 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 354 LNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLpHLAQDQWQQQFTYLPQKPYLFSD-TIANNIRFY 432
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 433 QPTA--SNEEVQQAMEqaglakfiATLPQ-GLQTRVGEAGRGISGGQAQRIMLARAFlVQQRHILIFDEPTAHLDIETEY 509
Cdd:TIGR01257 1028 AQLKgrSWEEAQLEME--------AMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAF-VGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2468565974 510 ALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKI 548
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRL 1138
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
351-555 |
8.10e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.76 E-value: 8.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQdqwQQQFTYLPQK-------PYLFSD 423
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ---KNLVAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 424 TIANNiRF------YQPTASNEE-VQQAMEQAGLAKFiatlpqgLQTRVGEagrgISGGQAQRIMLARAfLVQQRHILIF 496
Cdd:PRK15056 100 VVMMG-RYghmgwlRRAKKRDRQiVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARA-IAQQGQVILL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 497 DEPTAHLDIETEYALKKTMVQLF-EHHLVLFATHRLHWL-EQMDYVlVLDNGKIAEQGPVK 555
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVtEFCDYT-VMVKGTVLASGPTE 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
328-565 |
8.41e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.04 E-value: 8.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 328 NEQSRLTIQHLNFQYDDTMDQVN-LKDLNLTLQGYERVAIIGQSGAGKST-------LLEALSGFVIPQTGNIQLNGHQL 399
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIAaVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 400 PHLA-QDQWQQQ------FTYLPQKP-------YLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKfiatLPQGlQTRV 465
Cdd:PRK10261 88 IELSeQSAAQMRhvrgadMAMIFQEPmtslnpvFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVR----IPEA-QTIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 466 GEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIeTEYALKKTMVQLFEHHL---VLFATHRLHWLEQM-DYVL 541
Cdd:PRK10261 163 SRYPHQLSGGMRQRVMIAMA-LSCRPAVLIADEPTTALDV-TIQAQILQLIKVLQKEMsmgVIFITHDMGVVAEIaDRVL 240
|
250 260
....*....|....*....|....
gi 2468565974 542 VLDNGKIAEQGPVKQLLQKQHGPF 565
Cdd:PRK10261 241 VMYQGEAVETGSVEQIFHAPQHPY 264
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
333-562 |
1.04e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSG----FVIPQ----TGNIQLNGHQLPHLAQ 404
Cdd:PRK13547 2 LTADHLHVARRH---RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRgarvTGDVTLNGEPLAAIDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 405 DQWQQQFTYLPQ---KPYLFS-DTIANNIRFYQPTASNEEVQQAMEQAGLAKFIAtlpqGLQTRVGEAGRGISGGQAQRI 480
Cdd:PRK13547 79 PRLARLRAVLPQaaqPAFAFSaREIVLLGRYPHARRAGALTHRDGEIAWQALALA----GATALVGRDVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 481 MLARAF---------LVQQRHILIfDEPTAHLDIETEYALKKTMVQLF-EHHL-VLFATHRLHWLEQ-MDYVLVLDNGKI 548
Cdd:PRK13547 155 QFARVLaqlwpphdaAQPPRYLLL-DEPTAALDLAHQHRLLDTVRRLArDWNLgVLAIVHDPNLAARhADRIAMLADGAI 233
|
250
....*....|....
gi 2468565974 549 AEQGPVKQLLQKQH 562
Cdd:PRK13547 234 VAHGAPADVLTPAH 247
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
351-560 |
1.22e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.80 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNG------------HqlPHLaqdqwqqqftylpqkp 418
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsallelgagfH--PEL---------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 419 ylfsdTIANNIRFYqptA-----SNEEVQQAMEQ----AGLAKFI----ATLPQGLQTRVGEAgrgisggqaqrIMLARA 485
Cdd:COG1134 104 -----TGRENIYLN---GrllglSRKEIDEKFDEivefAELGDFIdqpvKTYSSGMRARLAFA-----------VATAVD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 486 FlvqqrHILIFDEPTAHLDIE-TEYALKKtMVQLFEHH-LVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:COG1134 165 P-----DILLVDEVLAVGDAAfQKKCLAR-IRELRESGrTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
351-504 |
1.27e-12 |
|
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: 67.46 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLN-GHQLPHLAQDQWQQ-------------QF-TYLP 415
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDLAQASPREilalrrrtigyvsQFlRVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 416 QKPYLfsDTIANNIRfyqptASNEEVQQAMEQAG--LAKFiaTLPQGL-----QTrvgeagrgISGGQAQRIMLARAFLV 488
Cdd:COG4778 107 RVSAL--DVVAEPLL-----ERGVDREEARARARelLARL--NLPERLwdlppAT--------FSGGEQQRVNIARGFIA 169
|
170
....*....|....*.
gi 2468565974 489 QQRhILIFDEPTAHLD 504
Cdd:COG4778 170 DPP-LLLLDEPTASLD 184
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
362-572 |
1.54e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.08 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 362 ERVAIIGQSGAGKSTLLEALSGFVIPQT---GNIQLNGHQLphlaqDQWQQQF--TYLPQKPYLF-SDTIANNIRF---- 431
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPI-----DAKEMRAisAYVQQDDLFIpTLTVREHLMFqahl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 432 -----YQPTASNEEVQQAMEQAGLAKfiatlpqGLQTRVGEAGR--GISGGQAQRIMLARAfLVQQRHILIFDEPTAHLD 504
Cdd:TIGR00955 127 rmprrVTKKEKRERVDEVLQALGLRK-------CANTRIGVPGRvkGLSGGERKRLAFASE-LLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 505 IETEYALKKTMVQLFEH-HLVLFATHR--LHWLEQMDYVLVLDNGKIAEQGPVKQLLqkqhgPFFELTSHM 572
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKgKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAV-----PFFSDLGHP 264
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
351-560 |
1.81e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.22 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQ----WQQQFTYLPQKP--YLFSDT 424
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQFPesQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 425 IANNIRFYQPT--ASNEEVQ----QAMEQAGLAK-FIATLPQGLqtrvgeagrgiSGGQAQRIMLArAFLVQQRHILIFD 497
Cdd:PRK13643 102 VLKDVAFGPQNfgIPKEKAEkiaaEKLEMVGLADeFWEKSPFEL-----------SGGQMRRVAIA-GILAMEPEVLVLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 498 EPTAHLDIETeyalKKTMVQLFEH-----HLVLFATHRLHWL-EQMDYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:PRK13643 170 EPTAGLDPKA----RIEMMQLFESihqsgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
351-559 |
2.35e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.51 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQFTYLPQK-PYLFSDTIANNI 429
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 430 ------------RFYQptASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLArAFLVQQRHILIFD 497
Cdd:PRK10575 107 aigrypwhgalgRFGA--ADREKVEEAISLVGLKPLAHRLVDSL-----------SGGERQRAWIA-MLVAQDSRCLLLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 498 EPTAHLDIETE---YALKKTMVQlfEHHLVLFAThrLHWLEQM----DYVLVLDNGKIAEQGPVKQLLQ 559
Cdd:PRK10575 173 EPTSALDIAHQvdvLALVHRLSQ--ERGLTVIAV--LHDINMAarycDYLVALRGGEMIAQGTPAELMR 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
365-557 |
2.73e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.07 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 365 AIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQL---PHLAQDQWQQQFTYLPQKPY-------LFSDTIAnnirfyQP 434
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPYgslnprkKVGQILE------EP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 435 TASN---------EEVQQAMEQAGLakfiatlpqglqtRVGEAGR---GISGGQAQRIMLARAFLVQQRhILIFDEPTAH 502
Cdd:PRK11308 119 LLINtslsaaerrEKALAMMAKVGL-------------RPEHYDRyphMFSGGQRQRIAIARALMLDPD-VVVADEPVSA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 503 LDIETEYALKKTMVQL-FEHHLV-LFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLqQELGLSyVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
347-553 |
2.86e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.32 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 347 DQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQwQQQFTYLPQKPYLFSD-TI 425
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVVPQFDNLDLEfTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 426 ANNI----RFYQptASNEEVQQAMeqAGLAKFiATLPQGLQTRVGEagrgISGGQAQRIMLARAfLVQQRHILIFDEPTA 501
Cdd:PRK13536 132 RENLlvfgRYFG--MSTREIEAVI--PSLLEF-ARLESKADARVSD----LSGGMKRRLTLARA-LINDPQLLILDEPTT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 502 HLDIETEYALKKTMVQLFEH-HLVLFATHRLHWLEQM-DYVLVLDNG-KIAEQGP 553
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARgKTILLTTHFMEEAERLcDRLCVLEAGrKIAEGRP 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
333-573 |
2.87e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.06 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEAL---------SGFVI------PQTGNIQL--- 394
Cdd:TIGR03269 1 IEVKNLTKKFDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptSGRIIyhvalcEKCGYVERpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 395 NGHQLPHLAQDQWQQQFTYL-PQKPYLFSDTIANNIRFYQPTASNEE------VQQAMEQAG------LAKFIATLPQ-G 460
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFWnLSDKLRRRIRKRIAIMLQRTFALYGDdtvldnVLEALEEIGyegkeaVGRAVDLIEMvQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 461 LQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLF-EHHLVLFATHrlHWLEQM-- 537
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQ-LAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTS--HWPEVIed 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 2468565974 538 --DYVLVLDNGKIAEQGPVKQLLQKqhgpFFELTSHMR 573
Cdd:TIGR03269 235 lsDKAIWLENGEIKEEGTPDEVVAV----FMEGVSEVE 268
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
328-562 |
3.41e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.96 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 328 NEQSRLTIQHLN--FQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKS-TLLEAL----SGFVIPQTGNIQLNGHQLP 400
Cdd:PRK15134 1 MTQPLLAIENLSvaFRQQQTVRTV-VNDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFHGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 401 HLAQDQWQQ----QFTYLPQKPyLFSDTIANNI-----------RFYQPTASNEEVQQAMEQAGL---AKFIATLPQGLq 462
Cdd:PRK15134 80 HASEQTLRGvrgnKIAMIFQEP-MVSLNPLHTLekqlyevlslhRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQL- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 463 trvgeagrgiSGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIETE---YALKKTMVQLFEHHLvLFATHRLHWLEQM-D 538
Cdd:PRK15134 158 ----------SGGERQRVMIAMALLTRPE-LLIADEPTTALDVSVQaqiLQLLRELQQELNMGL-LFITHNLSIVRKLaD 225
|
250 260
....*....|....*....|....*
gi 2468565974 539 YVLVLDNGKIAEQGPVKQLL-QKQH 562
Cdd:PRK15134 226 RVAVMQNGRCVEQNRAATLFsAPTH 250
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
333-511 |
5.43e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.38 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIqlnghqlphlaqdQWQQ--Q 410
Cdd:PRK15064 320 LEVENLTKGFDN---GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------------KWSEnaN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKPYL-FSD--TIANNIRFYQPTASNEEVQQAMeqagLAKFIATlpqglQTRVGEAGRGISGGQAQRIMLARafL 487
Cdd:PRK15064 384 IGYYAQDHAYdFENdlTLFDWMSQWRQEGDDEQAVRGT----LGRLLFS-----QDDIKKSVKVLSGGEKGRMLFGK--L 452
|
170 180
....*....|....*....|....*
gi 2468565974 488 VQQRH-ILIFDEPTAHLDIETEYAL 511
Cdd:PRK15064 453 MMQKPnVLVMDEPTNHMDMESIESL 477
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
351-552 |
5.43e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQ-----DQWQQQFTYLPQKP--YLFSD 423
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKkikevKRLRKEIGLVFQFPeyQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 424 TIANNIRFyQPTASNEEVQQAMEQAGLAKFIATLPQGLQTRvgeAGRGISGGQAQRIMLArAFLVQQRHILIFDEPTAHL 503
Cdd:PRK13645 107 TIEKDIAF-GPVNLGENKQEAYKKVPELLKLVQLPEDYVKR---SPFELSGGQKRRVALA-GIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 504 DIETEyalkKTMVQLFEH------HLVLFATHRL-HWLEQMDYVLVLDNGKIAEQG 552
Cdd:PRK13645 182 DPKGE----EDFINLFERlnkeykKRIIMVTHNMdQVLRIADEVIVMHEGKVISIG 233
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
347-548 |
1.23e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.50 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 347 DQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQL-NGHQLPHLAQDQWQqqftylpqkpYLFSDti 425
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLE----------FLRAD-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 426 ANNIRFYQPTASNEEVQQAMEQAGLAKFiatlpQGlqTRVGEAGRGISGGQAQRIMLarAFLVQQR-HILIFDEPTAHLD 504
Cdd:PRK10636 392 ESPLQHLARLAPQELEQKLRDYLGGFGF-----QG--DKVTEETRRFSGGEKARLVL--ALIVWQRpNLLLLDEPTNHLD 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2468565974 505 IETEYALKKTMVQlFEHHLVLfATHRLHWLEQM--DYVLVLDnGKI 548
Cdd:PRK10636 463 LDMRQALTEALID-FEGALVV-VSHDRHLLRSTtdDLYLVHD-GKV 505
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
343-576 |
2.17e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.83 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 343 DDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQ-----------QQF 411
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQr 491
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINP- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 492 HILIFDEPTAHLD--IETEYALKKTMVQLFEHHLVLFATHRLHwlEQM---DYVLVLDNGKIAEQGPVKQLLQKQHGPFf 566
Cdd:PRK10070 184 DILLMDEAFSALDplIRTEMQDELVKLQAKHQRTIVFISHDLD--EAMrigDRIAIMQNGEVVQVGTPDEILNNPANDY- 260
|
250
....*....|
gi 2468565974 567 eLTSHMRGVN 576
Cdd:PRK10070 261 -VRTFFRGVD 269
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
351-559 |
3.25e-11 |
|
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: 63.33 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ-FTYLPQKPYLFSD-TIANN 428
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 429 IR--FYQPTASNEEVQQAMEQAgLAKF-IATLPQGLqtrvgeaGRGISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDI 505
Cdd:cd03218 96 ILavLEIRGLSKKEREEKLEEL-LEEFhITHLRKSK-------ASSLSGGERRRVEIARA-LATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 506 ETEYALKKTMVQLFEHHL-VLFATHRLH-WLEQMDYVLVLDNGKIAEQGPVKQLLQ 559
Cdd:cd03218 167 IAVQDIQKIIKILKDRGIgVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
351-560 |
4.58e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.61 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQD----QWQQQFTYLPQKP--YLFSDT 424
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQIRKKVGLVFQFPesQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 425 IANNIRFYQPT--ASNEEVQQ-AMEQAGLAKFIATLpqglqtrVGEAGRGISGGQAQRIMLArAFLVQQRHILIFDEPTA 501
Cdd:PRK13649 103 VLKDVAFGPQNfgVSQEEAEAlAREKLALVGISESL-------FEKNPFELSGGQMRRVAIA-GILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 502 HLDIETeyalKKTMVQLFE--HHL---VLFATHRLHWL-EQMDYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:PRK13649 175 GLDPKG----RKELMTLFKklHQSgmtIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
342-552 |
5.52e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.28 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 342 YDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQ------WQQQFTYlp 415
Cdd:PRK11000 13 YGDV---VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAErgvgmvFQSYALY-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 416 qkPYLfsdTIANNIRFYQPTA--SNEEVQQAMEQAG----LAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAfLVQ 489
Cdd:PRK11000 88 --PHL---SVAENMSFGLKLAgaKKEEINQRVNQVAevlqLAHLLDRKPKAL-----------SGGQRQRVAIGRT-LVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 490 QRHILIFDEPTAHLDIeteyALKKTM-VQLFEHHLVL-----FATHrlHWLEQM---DYVLVLDNGKIAEQG 552
Cdd:PRK11000 151 EPSVFLLDEPLSNLDA----ALRVQMrIEISRLHKRLgrtmiYVTH--DQVEAMtlaDKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
328-563 |
8.38e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.85 E-value: 8.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 328 NEQSRLTIQHLNFQYDDTmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQW 407
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSD-ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 408 QQQFTYLPQKP--YLFSDTIANNIRFYQPTAS------NEEVQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQR 479
Cdd:PRK13648 82 RKHIGIVFQNPdnQFVGSIVKYDVAFGLENHAvpydemHRRVSEALKQVDMLERADYEPNAL-----------SGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 480 IMLArAFLVQQRHILIFDEPTAHLDIETeyalKKTMVQLF-----EHHLVLFA-THRLHWLEQMDYVLVLDNGKIAEQGP 553
Cdd:PRK13648 151 VAIA-GVLALNPSVIILDEATSMLDPDA----RQNLLDLVrkvksEHNITIISiTHDLSEAMEADHVIVMNKGTVYKEGT 225
|
250
....*....|
gi 2468565974 554 VKQLLQKQHG 563
Cdd:PRK13648 226 PTEIFDHAEE 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
352-549 |
1.53e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 352 KDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLA-QDQWQQQFTYLP---QKPYLFSDT--- 424
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPedrQSSGLYLDApla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 425 ------IANNIRFYQptasneevQQAMEQAGLAKFIATLpqGLQ-TRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFD 497
Cdd:PRK15439 360 wnvcalTHNRRGFWI--------KPARENAVLERYRRAL--NIKfNHAEQAARTLSGGNQQKVLIAKC-LEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 498 EPTAHLDIETE---YALKKTMVQlfEHHLVLFATHRLHWLEQM-DYVLVLDNGKIA 549
Cdd:PRK15439 429 EPTRGVDVSARndiYQLIRSIAA--QNVAVLFISSDLEEIEQMaDRVLVMHQGEIS 482
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
351-507 |
1.58e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGH-QLPHLAQDQ---------------WQQQFTYL 414
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQQDPprnvegtvydfvaegIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 415 PQKPYLfSDTIANnirfyQPTASN----EEVQQAMEQAGLAKFIATLPQGLQ-------TRVGEagrgISGGQAQRIMLA 483
Cdd:PRK11147 99 KRYHDI-SHLVET-----DPSEKNlnelAKLQEQLDHHNLWQLENRINEVLAqlgldpdAALSS----LSGGWLRKAALG 168
|
170 180
....*....|....*....|....
gi 2468565974 484 RAfLVQQRHILIFDEPTAHLDIET 507
Cdd:PRK11147 169 RA-LVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
335-557 |
1.80e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 60.85 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQwQQQFTYL 414
Cdd:cd03265 3 VENLVKKYGDF---EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV-RRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 415 PQKPYLFSD-TIANNI----RFYqpTASNEEVQQAMEQagLAKFIatlpqGLQTRVGEAGRGISGGQAQRIMLARAfLVQ 489
Cdd:cd03265 79 FQDLSVDDElTGWENLyihaRLY--GVPGAERRERIDE--LLDFV-----GLLEAADRLVKTYSGGMRRRLEIARS-LVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 490 QRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-561 |
2.72e-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: 63.03 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 341 QYDDTMDQVN---------LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFvipqtgNIQLNGHQLPhlaqdqwQQQF 411
Cdd:TIGR03719 2 QYIYTMNRVSkvvppkkeiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKDFNGEARP-------QPGI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 T--YLPQKPYL-FSDTIANNI-------------------RFYQPTASNEEVqqAMEQAGLAKFIAT------------- 456
Cdd:TIGR03719 69 KvgYLPQEPQLdPTKTVRENVeegvaeikdaldrfneisaKYAEPDADFDKL--AAEQAELQEIIDAadawdldsqleia 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 457 -----LPQGlQTRVGEagrgISGGQAQRIMLARaFLVQQRHILIFDEPTAHLDIETeyalkktmVQLFEHHL------VL 525
Cdd:TIGR03719 147 mdalrCPPW-DADVTK----LSGGERRRVALCR-LLLSKPDMLLLDEPTNHLDAES--------VAWLERHLqeypgtVV 212
|
250 260 270
....*....|....*....|....*....|....*....
gi 2468565974 526 FATHRLHWLEQM-DYVLVLDNGK-IAEQGPVKQLL-QKQ 561
Cdd:TIGR03719 213 AVTHDRYFLDNVaGWILELDRGRgIPWEGNYSSWLeQKQ 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
362-565 |
3.26e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.95 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 362 ERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQ-----QFTYlpQKPYLFSD---TIANNI---- 429
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrdiQFIF--QDPYASLDprqTVGDSImepl 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 430 ---RFYQPTASNEEVQQAMEQAGLakfiatLPQGLQTRVGEagrgISGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIE 506
Cdd:PRK10261 429 rvhGLLPGKAAAARVAWLLERVGL------LPEHAWRYPHE----FSGGQRQRICIARALALNPK-VIIADEAVSALDVS 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 507 TEYALKKTMVQLFEHHLV--LFATHRLHWLEQMDY-VLVLDNGKIAEQGPVKQLLQKQHGPF 565
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIayLFISHDMAVVERISHrVAVMYLGQIVEIGPRRAVFENPQHPY 559
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-558 |
3.56e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 338 LNFQYDDTMDQVNLKdlnltLQGYERVAIIGQSGAGKSTLLEAL-------SGFviPQTGNIQLNGHQLPHLAQD-QWQQ 409
Cdd:PRK14271 29 LGFAGKTVLDQVSMG-----FPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGY--RYSGDVLLGGRSIFNYRDVlEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 410 QFTYLPQKPYLFSDTIANNI----RFYQPTASNEevQQAMEQAGLAKfiATLPQGLQTRVGEAGRGISGGQAQRIMLARA 485
Cdd:PRK14271 102 RVGMLFQRPNPFPMSIMDNVlagvRAHKLVPRKE--FRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 486 FLVQQRhILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLL 558
Cdd:PRK14271 178 LAVNPE-VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLF 250
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
351-555 |
8.95e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLA-QDQWQQQFTYLPQKPYLFSD-TIANN 428
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 429 IRFYQ-PTASNEEV-----QQAMEQAGLAKFIATLPQGLQTRVGEagrgISGGQAQRIMLARAfLVQQRHILIFDEPTAH 502
Cdd:PRK09700 101 LYIGRhLTKKVCGVniidwREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKT-LMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 503 L-DIETEYaLKKTMVQLF-EHHLVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVK 555
Cdd:PRK09700 176 LtNKEVDY-LFLIMNQLRkEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVS 230
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
333-539 |
1.06e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHlAQDQWQQQFT 412
Cdd:PRK13540 2 LDVIELDFDYHD---QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 413 YLPQK----PYLfsdTIANNIRFYQPTAS-NEEVQQAMEQAGLAKFIaTLPQGLqtrvgeagrgISGGQAQRIMLARAFL 487
Cdd:PRK13540 78 FVGHRsginPYL---TLRENCLYDIHFSPgAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 488 VQQRhILIFDEPTAHLDietEYALKKTMVQLFEHH----LVLFATHRLHWLEQMDY 539
Cdd:PRK13540 144 SKAK-LWLLDEPLVALD---ELSLLTIITKIQEHRakggAVLLTSHQDLPLNKADY 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
351-531 |
1.11e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHqlphlaqdqwQQQFT-------------YlpQK 417
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ----------EMRFAsttaalaagvaiiY--QE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 418 PYLFSD-TIANNIRFYQ-PTAS---NEE--VQQAMEQ-AGLAKFIAtlPqglQTRVGEagrgISGGQAQRIMLARAfLVQ 489
Cdd:PRK11288 88 LHLVPEmTVAENLYLGQlPHKGgivNRRllNYEAREQlEHLGVDID--P---DTPLKY----LSIGQRQMVEIAKA-LAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 490 QRHILIFDEPTAHLDI-ETEyalkktmvQLF--------EHHLVLFATHRL 531
Cdd:PRK11288 158 NARVIAFDEPTSSLSArEIE--------QLFrvirelraEGRVILYVSHRM 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
353-557 |
1.19e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.39 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 353 DLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQW---QQQFTYLPQKPYLFSD-TIANN 428
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTDmNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 429 IRF--YQPTASNEE-----VQQAMEQAGLAKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQRHILiFDEPTA 501
Cdd:PRK11831 105 VAYplREHTQLPAPllhstVMMKLEAVGLRGAAKLMPSEL-----------SGGMARRAALARAIALEPDLIM-FDEPFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 502 HLDIETEYALKKTMVQLfEHHL---VLFATHRL-HWLEQMDYVLVLDNGKIAEQGPVKQL 557
Cdd:PRK11831 173 GQDPITMGVLVKLISEL-NSALgvtCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
321-562 |
1.28e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.28 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 321 LLPAftwneqsrLTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFV-----IPQTGNIQLN 395
Cdd:PRK14258 4 LIPA--------IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 396 GHQL--PHLAQDQWQQQFTYLPQKPYLFSDTIANNIRF------YQPTASNEEVQQAMEQAglakfiATLPQGLQTRVGE 467
Cdd:PRK14258 73 NQNIyeRRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYgvkivgWRPKLEIDDIVESALKD------ADLWDEIKHKIHK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 468 AGRGISGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIETEYALKKTM--VQLFEHHLVLFATHRLHWLEQM-DYVLVLD 544
Cdd:PRK14258 147 SALDLSGGQQQRLCIARALAVKPK-VLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLsDFTAFFK 225
|
250 260
....*....|....*....|...
gi 2468565974 545 N-----GKIAEQGPVKQLLQKQH 562
Cdd:PRK14258 226 GnenriGQLVEFGLTKKIFNSPH 248
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
351-552 |
1.32e-09 |
|
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: 58.70 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAqdqwqqqFTYLPQkPYLfsdTIANNIR 430
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG-------LGGGFN-PEL---TGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 431 FYqptA-----SNEEVQQAMEQ----AGLAKFIatlpqglQTRVgeagRGISGGQAQRIMLARAFLVQQRhILIFDEPTA 501
Cdd:cd03220 107 LN---GrllglSRKEIDEKIDEiiefSELGDFI-------DLPV----KTYSSGMKARLAFAIATALEPD-ILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 502 HLDIeteyALKKTMVQLFEHHL-----VLFATHRLHWLEQM-DYVLVLDNGKIAEQG 552
Cdd:cd03220 172 VGDA----AFQEKCQRRLRELLkqgktVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
332-505 |
1.81e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.04 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 332 RLTIQHLNfqYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ- 410
Cdd:COG3845 257 VLEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKPY---LFSD-TIANNI---RFYQPTASN----------EEVQQAMEQAGLAkfiatlPQGLQTRVgeagRGIS 473
Cdd:COG3845 335 VAYIPEDRLgrgLVPDmSVAENLilgRYRRPPFSRggfldrkairAFAEELIEEFDVR------TPGPDTPA----RSLS 404
|
170 180 190
....*....|....*....|....*....|..
gi 2468565974 474 GGQAQRIMLARAFLvQQRHILIFDEPTAHLDI 505
Cdd:COG3845 405 GGNQQKVILARELS-RDPKLLIAAQPTRGLDV 435
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
353-557 |
1.83e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 59.36 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 353 DLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ-------FtylpQKPY--L--- 420
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrmqmvF----QDPYasLnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 421 --FSDTIA-----NNIRfyQPTASNEEVQQAMEQAGL-AKFIATLPQGLqtrvgeagrgiSGGQAQRIMLARAFLVQQRh 492
Cdd:COG4608 112 mtVGDIIAeplriHGLA--SKAERRERVAELLELVGLrPEHADRYPHEF-----------SGGQRQRIGIARALALNPK- 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 493 ILIFDEPTAHLDIEteyalkktmVQ-----LF-----EHHL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQL 557
Cdd:COG4608 178 LIVCDEPVSALDVS---------IQaqvlnLLedlqdELGLtYLFISHDLSVVRHIsDRVAVMYLGKIVEIAPRDEL 245
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
351-548 |
2.78e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.97 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLphlaqDQWQ------QQFTYLPQKPYLFSD- 423
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-----TDWQtakimrEAVAIVPEGRRVFSRm 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 424 TIANNIRFYQPTASNEEVQQAMEqaglaKFIATLPQGLQTRVGEAGRgISGGQAQRIMLARAFLVQQRhILIFDEPTAHL 503
Cdd:PRK11614 96 TVEENLAMGGFFAERDQFQERIK-----WVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPR-LLLLDEPSLGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2468565974 504 DIETEYALKKTMVQLFEHHLVLFATHR--LHWLEQMDYVLVLDNGKI 548
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHV 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
331-550 |
3.49e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.60 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 331 SRLTIQHLNFQYDDTMDQVnlKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ 410
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSV--GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKPYLFSDTIannirfyqptasNEEVQQAmEQAGLAKFIATLpqGLQTRVGEAGRGI-----SGGQAQRIMLARA 485
Cdd:PRK10522 399 FSAVFTDFHLFDQLL------------GPEGKPA-NPALVEKWLERL--KMAHKLELEDGRIsnlklSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 486 fLVQQRHILIFDEPTAHLDIE-TEYALKKTMVQLFEHHLVLFA-THRLHWLEQMDYVLVLDNGKIAE 550
Cdd:PRK10522 464 -LAEERDILLLDEWAADQDPHfRREFYQVLLPLLQEMGKTIFAiSHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
351-562 |
4.82e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.21 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLA-QDQWQQQFTYLPQKPYLFSD-TIANN 428
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 429 IRFYQPTASNEEVQQAMEQAG--LAKF-IATLPQGLqtrvgeaGRGISGGQAQRIMLARAFLVQQRHILIfDEPTAHLDI 505
Cdd:PRK10895 99 LMAVLQIRDDLSAEQREDRANelMEEFhIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILL-DEPFAGVDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468565974 506 ETEYALKKTMVQLFEHHL-VLFATHRL-HWLEQMDYVLVLDNGKIAEQGPVKQLLQKQH 562
Cdd:PRK10895 171 ISVIDIKRIIEHLRDSGLgVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
353-568 |
5.17e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 353 DLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNI-------------QLNGHQLPHLAQDQWqqqfTYLPQKPy 419
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqlrdlyALSEAERRRLLRTEW----GFVHQHP- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 420 lfSDTI-------AN--------------NIRfyqptasnEEVQQAMEQAGLAkfiatlpqglQTRVGEAGRGISGGQAQ 478
Cdd:PRK11701 99 --RDGLrmqvsagGNigerlmavgarhygDIR--------ATAGDWLERVEID----------AARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 479 RIMLARAFLVQQRhiLIF-DEPTAHLDIETEYALKKTMVQLF-EHHL-VLFATH-----RLhwleQMDYVLVLDNGKIAE 550
Cdd:PRK11701 159 RLQIARNLVTHPR--LVFmDEPTGGLDVSVQARLLDLLRGLVrELGLaVVIVTHdlavaRL----LAHRLLVMKQGRVVE 232
|
250
....*....|....*...
gi 2468565974 551 QGPVKQLLQKQHGPFFEL 568
Cdd:PRK11701 233 SGLTDQVLDDPQHPYTQL 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
351-549 |
6.49e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQL-PHLAQDQWQQQFTYLPQ--KPY-LFSD-TI 425
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrIRSPRDAIRAGIAYVPEdrKGEgLVLDlSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 426 ANNIrfyqpTASNEE-------VQQAMEQAGLAKFIATL---PQGLQTRVGEagrgISGGQAQRIMLARAfLVQQRHILI 495
Cdd:COG1129 348 RENI-----TLASLDrlsrgglLDRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKW-LATDPKVLI 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468565974 496 FDEPTAHLDIETEYALKKTMVQLFEHHL-VLFATHRLHWLEQM-DYVLVLDNGKIA 549
Cdd:COG1129 418 LDEPTRGIDVGAKAEIYRLIRELAAEGKaVIVISSELPELLGLsDRILVMREGRIV 473
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
309-567 |
7.22e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 309 DILAIPTVTDRTLLPAftwneqsRLTIQHLNFQYDDTMDQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALS----GF 384
Cdd:TIGR00956 43 DSDYQPTFPNALLKIL-------TRGFRKLKKFRDTKTFDI-LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 385 VIPQTGNIQLNGHQlPHLAQDQWQQQFTYLPQK----PYL-FSDTIANNIRFYQPTASNEEVQQAMEQAGLAKFIAT--- 456
Cdd:TIGR00956 115 HIGVEGVITYDGIT-PEEIKKHYRGDVVYNAETdvhfPHLtVGETLDFAARCKTPQNRPDGVSREEYAKHIADVYMAtyg 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 457 LPQGLQTRVG-EAGRGISGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIETEY----ALkKTMVQlFEHHLVLFATHRL 531
Cdd:TIGR00956 194 LSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAK-IQCWDNATRGLDSATALefirAL-KTSAN-ILDTTPLVAIYQC 270
|
250 260 270
....*....|....*....|....*....|....*...
gi 2468565974 532 --HWLEQMDYVLVLDNGKIAEQGPVKQLLQkqhgpFFE 567
Cdd:TIGR00956 271 sqDAYELFDKVIVLYEGYQIYFGPADKAKQ-----YFE 303
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-524 |
8.11e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.54 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 355 NLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ---FTYlpQKPYLFSD-TIANNIR 430
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgvvRTF--QHVRLFREmTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 431 FYQPTASNEEV--------------QQAMEQAGlakfiatlpQGLQtRVG-------EAGRgISGGQAQRIMLARAFLVQ 489
Cdd:PRK11300 103 VAQHQQLKTGLfsgllktpafrraeSEALDRAA---------TWLE-RVGllehanrQAGN-LAYGQQRRLEIARCMVTQ 171
|
170 180 190
....*....|....*....|....*....|....*
gi 2468565974 490 QRhILIFDEPTAHLDIETEYALKKTMVQLFEHHLV 524
Cdd:PRK11300 172 PE-ILMLDEPAAGLNPKETKELDELIAELRNEHNV 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
351-560 |
9.60e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.02 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHqlphlaqDQWQQQFTYLP-------QKPYLF-- 421
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-------VPFKRRKEFARrigvvfgQRSQLWwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 422 ---SDTIANNIRFYQptASNEEVQQAMEQaglakFIATLPQG--LQTRVgeagRGISGGQAQRIMLARAFLvqqrH---I 493
Cdd:COG4586 111 lpaIDSFRLLKAIYR--IPDAEYKKRLDE-----LVELLDLGelLDTPV----RQLSLGQRMRCELAAALL----HrpkI 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 494 LIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQK 560
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
335-507 |
1.07e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLnGHQLPHLAQDQWQQQFTyl 414
Cdd:PRK11147 322 MENVNYQIDG---KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAELD-- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 415 PQKpylfsdTIANNIrfyqptasnEEVQQAMEQAG--------LAKFIATlPQGLQTRVgeagRGISGGQAQRIMLARAF 486
Cdd:PRK11147 396 PEK------TVMDNL---------AEGKQEVMVNGrprhvlgyLQDFLFH-PKRAMTPV----KALSGGERNRLLLARLF 455
|
170 180
....*....|....*....|.
gi 2468565974 487 LvQQRHILIFDEPTAHLDIET 507
Cdd:PRK11147 456 L-KPSNLLILDEPTNDLDVET 475
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
349-565 |
1.22e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 349 VNlkDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQ---TGNIQLNGHQLPHLAQDQ------------WQQQFTY 413
Cdd:PRK09473 32 VN--DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKElnklraeqismiFQDPMTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 414 LpqKPYL-FSDTIANNIRFYQPTASNEEVQQAMEQAGLAKfiatLPQGLQtRVGEAGRGISGGQAQRIMLARAFLVQQRh 492
Cdd:PRK09473 110 L--NPYMrVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVK----MPEARK-RMKMYPHEFSGGMRQRVMIAMALLCRPK- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468565974 493 ILIFDEPTAHLDIeTEYALKKTMVQLFEHHL---VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQKQHGPF 565
Cdd:PRK09473 182 LLIADEPTTALDV-TVQAQIMTLLNELKREFntaIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
331-504 |
1.43e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.81 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 331 SRLTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQDQWQQQ 410
Cdd:COG1137 2 MTLEAENLVKSYGKR--TV-VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 -FTYLPQKPYLFSD-TIANNI------RFYQPTASNEEVQQAMEQAGLAKfIATLPqglqtrvgeaGRGISGGQAQRIML 482
Cdd:COG1137 79 gIGYLPQEASIFRKlTVEDNIlavlelRKLSKKEREERLEELLEEFGITH-LRKSK----------AYSLSGGERRRVEI 147
|
170 180
....*....|....*....|..
gi 2468565974 483 ARAFLVQQRHILiFDEPTAHLD 504
Cdd:COG1137 148 ARALATNPKFIL-LDEPFAGVD 168
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
331-559 |
2.09e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 331 SRLTIQHLNFQYDDTMdqvNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQ--------LNGHQLPHL 402
Cdd:PRK10938 2 SSLQISQGTFRLSDTK---TLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqfshitrLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 403 AQDQWQQQFT-YLPQKPYLFSDTIANNIRFYqpTASNEEVQQAMEQAGlakfIATLpqgLQTRVgeagRGISGGQAQRIM 481
Cdd:PRK10938 79 VSDEWQRNNTdMLSPGEDDTGRTTAEIIQDE--VKDPARCEQLAQQFG----ITAL---LDRRF----KYLSTGETRKTL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVL-FATHRLHWL-EQMDYVLVLDNGKIAEQGPVKQLLQ 559
Cdd:PRK10938 146 LCQA-LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLvLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
347-559 |
2.63e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.09 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 347 DQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPqtGNIQLNGHQLphlaqdqwqqqftyLPQKPYLFSD--- 423
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVL--------------LDGKPVAPCAlrg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 424 ----TIANNIRfyqpTASN------EEVQQAMEQAGLAKFIATLPQGLQTrVG--EAGR-------GISGGQAQRIMLAR 484
Cdd:PRK10418 79 rkiaTIMQNPR----SAFNplhtmhTHARETCLALGKPADDATLTAALEA-VGleNAARvlklypfEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 485 AFLVQQRhILIFDEPTAHLDIETE---YALKKTMVQlfEHHL-VLFATHRLHWLEQM-DYVLVLDNGKIAEQGPVKQLLQ 559
Cdd:PRK10418 154 ALLCEAP-FIIADEPTTDLDVVAQariLDLLESIVQ--KRALgMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-543 |
3.66e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 364 VAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQ---LPHLAQDQWQQQFT--------------YLPQKPYLFSDTIA 426
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWdeiLDEFRGSELQNYFTkllegdvkvivkpqYVDLIPKAVKGKVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NNIRFYQPTASNEEVQQAMEQAGLakfiatlpqgLQTRVGEagrgISGGQAQRIMLArAFLVQQRHILIFDEPTAHLDIE 506
Cdd:cd03236 109 ELLKKKDERGKLDELVDQLELRHV----------LDRNIDQ----LSGGELQRVAIA-AALARDADFYFFDEPSSYLDIK 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2468565974 507 TEYALKKTMVQLFEH-HLVLFATHRLHWLEQM-DYVLVL 543
Cdd:cd03236 174 QRLNAARLIRELAEDdNYVLVVEHDLAVLDYLsDYIHCL 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
351-546 |
8.54e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNghqlphLAQDQWQQQftylpqkpylfsDTIANNIr 430
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQFGRE------------ASLIDAI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 431 fyqptASNEEVQQAME---QAGLAKfiatlPQGLQTRVGEagrgISGGQAQRIMLARAfLVQQRHILIFDEPTAHLDIET 507
Cdd:COG2401 107 -----GRKGDFKDAVEllnAVGLSD-----AVLWLRRFKE----LSTGQKFRFRLALL-LAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2468565974 508 EYALKKTMVQLFEHHLV--LFATHR---LHWLeQMDYVLVLDNG 546
Cdd:COG2401 172 AKRVARNLQKLARRAGItlVVATHHydvIDDL-QPDLLIFVGYG 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
354-506 |
9.62e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 354 LNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHqlpHLAQDQWQQQFTYLPQKPYLFSDTIA-NNIRFY 432
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYLGHLPGLKADLSTlENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 433 --------QPTASNeevqqAMEQAGLAKFIATLPqglqtrvgeagRGISGGQAQRIMLARAFLvQQRHILIFDEPTAHLD 504
Cdd:PRK13543 107 cglhgrraKQMPGS-----ALAIVGLAGYEDTLV-----------RQLSAGQKKRLALARLWL-SPAPLWLLDEPYANLD 169
|
..
gi 2468565974 505 IE 506
Cdd:PRK13543 170 LE 171
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
330-546 |
1.18e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 52.25 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 330 QSRLTIQHLNFQYDdtMDQVNLKDLNlTLQGYER----VAIIGQSGAGKSTLLEALSGF----VIpqTGNIQLNGHQLPh 401
Cdd:cd03232 1 GSVLTWKNLNYTVP--VKGGKRQLLN-NISGYVKpgtlTALMGESGAGKTTLLDVLAGRktagVI--TGEILINGRPLD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 402 laqDQWQQQFTYLPQKPYLFsdtiannirfyqptaSNEEVQQAMEqaglakFIATLpqglqtrvgeagRGISGGQAQRIM 481
Cdd:cd03232 75 ---KNFQRSTGYVEQQDVHS---------------PNLTVREALR------FSALL------------RGLSVEQRKRLT 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 482 LARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHLVLFAThrLHW-----LEQMDYVLVLDNG 546
Cdd:cd03232 119 IGVE-LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCT--IHQpsasiFEKFDRLLLLKRG 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
362-547 |
1.26e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.50 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 362 ERVAIIGQSGAGKSTLLEALSGFVIPQ--TGNIQLNGHQLphlaQDQWQQQFTYLPQKPYLFSD-TIANNIRFYQ----P 434
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP----TKQILKRTGFVTQDDILYPHlTVRETLVFCSllrlP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 435 TASNEEVQQAMEQAGLAKFiaTLPQGLQTRVGEAG-RGISGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIETEYALKK 513
Cdd:PLN03211 171 KSLTKQEKILVAESVISEL--GLTKCENTIIGNSFiRGISGGERKRVSIAHEMLINPS-LLILDEPTSGLDATAAYRLVL 247
|
170 180 190
....*....|....*....|....*....|....*..
gi 2468565974 514 TMVQLFEH-HLVLFATHR-LHWLEQM-DYVLVLDNGK 547
Cdd:PLN03211 248 TLGSLAQKgKTIVTSMHQpSSRVYQMfDSVLVLSEGR 284
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
333-561 |
1.42e-07 |
|
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: 54.06 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQ-TGNIQLNGHQLP-HLAQDQWQQQ 410
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQ---KPYLFSDT-IANNI------RFYQPTASNEEVQQ-----AMEQAGLAKFIATLPQGlqtrvgeagrGISGG 475
Cdd:TIGR02633 338 IAMVPEdrkRHGIVPILgVGKNItlsvlkSFCFKMRIDAAAELqiigsAIQRLKVKTASPFLPIG----------RLSGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 476 QAQRIMLARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLFEH--HLVLFATHRLHWLEQMDYVLVLDNGKIAEQGP 553
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPR-VLILDEPTRGVDVGAKYEIYKLINQLAQEgvAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFV 486
|
....*...
gi 2468565974 554 VKQLLQKQ 561
Cdd:TIGR02633 487 NHALTQEQ 494
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
351-547 |
1.62e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGfVIPQ---TGNIQLNGHQL-PHLAQDQWQ-------QQFTYLPQKpy 419
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELqASNIRDTERagiaiihQELALVKEL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 420 lfsdTIANNIrFY--QPT--------ASNEEVQQAMEQAGLAKFIATlpqglqtRVGEAGrgisGGQAQRIMLARAfLVQ 489
Cdd:PRK13549 98 ----SVLENI-FLgnEITpggimdydAMYLRAQKLLAQLKLDINPAT-------PVGNLG----LGQQQLVEIAKA-LNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 490 QRHILIFDEPTAHLdIETEYALKKTMVQLFEHHLV--LFATHRLHWLEQM-DYVLVLDNGK 547
Cdd:PRK13549 161 QARLLILDEPTASL-TESETAVLLDIIRDLKAHGIacIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
314-549 |
1.99e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 314 PTVTDRTLLPAFTWNEQSrltiqhlnFQYDDtmDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNI- 392
Cdd:PLN03073 498 PTPDDRPGPPIISFSDAS--------FGYPG--GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVf 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 393 --------QLNGHQLPHLAqdqwqqqftyLPQKPYLFSdtiannIRFYqPTASNEEVQQAMEQAGLAKFIATlpQGLQTr 464
Cdd:PLN03073 568 rsakvrmaVFSQHHVDGLD----------LSSNPLLYM------MRCF-PGVPEQKLRAHLGSFGVTGNLAL--QPMYT- 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 465 vgeagrgISGGQAQRIMLARaFLVQQRHILIFDEPTAHLDIETEYALKKTMVqLFEHHlVLFATHRLHWLE-QMDYVLVL 543
Cdd:PLN03073 628 -------LSGGQKSRVAFAK-ITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQGG-VLMVSHDEHLISgSVDELWVV 697
|
....*.
gi 2468565974 544 DNGKIA 549
Cdd:PLN03073 698 SEGKVT 703
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
365-546 |
2.00e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 365 AIIGQSGAGKSTLLEALSGFV---IPQTGNIQLNGHQLPHLAQDQW---QQQFTYLPQKpylfsdTIANNIRFY----QP 434
Cdd:TIGR00956 793 ALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGRPLDSSFQRSIgyvQQQDLHLPTS------TVRESLRFSaylrQP 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 435 TA-----SNEEVQQAMEQAGLAKFIATLpqglqtrVGEAGRGISGGQAQRIMLARAfLVQQRHILIF-DEPTAHLDIETE 508
Cdd:TIGR00956 867 KSvskseKMEYVEEVIKLLEMESYADAV-------VGVPGEGLNVEQRKRLTIGVE-LVAKPKLLLFlDEPTSGLDSQTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2468565974 509 YALKKTMVQLFEHHLVLFAThrLH-----WLEQMDYVLVLDNG 546
Cdd:TIGR00956 939 WSICKLMRKLADHGQAILCT--IHqpsaiLFEEFDRLLLLQKG 979
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
362-552 |
2.07e-07 |
|
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: 52.41 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 362 ERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLphlaqdqwqqqfTYLPQK---------PYLFSDTIANnirFY 432
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYikadyegtvRDLLSSITKD---FY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 433 QPTASNEEVQQAMEqaglakfiatLPQGLQTRVGEagrgISGGQAQRIMLArAFLVQQRHILIFDEPTAHLDIETEYALK 512
Cdd:cd03237 91 THPYFKTEIAKPLQ----------IEQILDREVPE----LSGGELQRVAIA-ACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2468565974 513 KTMVQLFEH---------HLVLFATHrlhwleQMDYVLVLDnGKIAEQG 552
Cdd:cd03237 156 KVIRRFAENnektafvveHDIIMIDY------LADRLIVFE-GEPSVNG 197
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
333-563 |
2.51e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSG---FVIPQtGNIQLNGHQLPHLAQDQWQQ 409
Cdd:PRK09580 2 LSIKDLHVSVEDK---AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredYEVTG-GTVEFKGKDLLELSPEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 410 Q-----FTYLPQKP----YLFSDTIANNIRFYQPtasneevQQAMEQAGLAKFIA------TLPQGLQTRvgEAGRGISG 474
Cdd:PRK09580 78 EgifmaFQYPVEIPgvsnQFFLQTALNAVRSYRG-------QEPLDRFDFQDLMEekiallKMPEDLLTR--SVNVGFSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 475 GQAQR-IMLARAFLvqQRHILIFDEPTAHLDIETEYALKKTMVQLF-EHHLVLFATHRLHWLE--QMDYVLVLDNGKIAE 550
Cdd:PRK09580 149 GEKKRnDILQMAVL--EPELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVK 226
|
250
....*....|....*.
gi 2468565974 551 QGP---VKQLLQKQHG 563
Cdd:PRK09580 227 SGDftlVKQLEEQGYG 242
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
347-511 |
1.50e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.09 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 347 DQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLnGHQLpHLAqdqwqqqftYLPQkpylFSDTIA 426
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-KLA---------YVDQ----SRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NNIRFYqptasnEEVQQAMEQAGLAKFiaTLP------------QGLQTRVGEagrgISGGQAQRIMLARAfLVQQRHIL 494
Cdd:TIGR03719 399 PNKTVW------EEISGGLDIIKLGKR--EIPsrayvgrfnfkgSDQQKKVGQ----LSGGERNRVHLAKT-LKSGGNVL 465
|
170
....*....|....*..
gi 2468565974 495 IFDEPTAHLDIETEYAL 511
Cdd:TIGR03719 466 LLDEPTNDLDVETLRAL 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
357-515 |
1.59e-06 |
|
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: 50.94 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 357 TLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLnghqlphlaqdqwQQQFTYLPQkpYL---FSDTIANNIRfyq 433
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-------------DLKISYKPQ--YIspdYDGTVEEFLR--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 434 pTASNEEVQQAMEQAGLAKfiatlPQGL----QTRVGEagrgISGGQAQRIMLArAFLVQQRHILIFDEPTAHLDIETEY 509
Cdd:COG1245 424 -SANTDDFGSSYYKTEIIK-----PLGLekllDKNVKD----LSGGELQRVAIA-ACLSRDADLYLLDEPSAHLDVEQRL 492
|
....*.
gi 2468565974 510 ALKKTM 515
Cdd:COG1245 493 AVAKAI 498
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
362-515 |
2.32e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 362 ERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQlnghqlphlaqdqWQQQFTYLPQkpYLFSDT----------IANNIR- 430
Cdd:PRK13409 366 EVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-------------PELKISYKPQ--YIKPDYdgtvedllrsITDDLGs 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 431 -FYQPtasneEVQQAMEqaglakfiatLPQGLQTRVGEagrgISGGQAQRIMLArAFLVQQRHILIFDEPTAHLDIETEY 509
Cdd:PRK13409 431 sYYKS-----EIIKPLQ----------LERLLDKNVKD----LSGGELQRVAIA-ACLSRDADLYLLDEPSAHLDVEQRL 490
|
....*.
gi 2468565974 510 ALKKTM 515
Cdd:PRK13409 491 AVAKAI 496
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
359-565 |
3.51e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 359 QGyERVAIIGQSGAGKSTLLEALSGFV-IP---QTGNIQLNGHQLPHLAQDQWQQ----QFTYLPQKP-------YLFSD 423
Cdd:PRK11022 32 QG-EVVGIVGESGSGKSVSSLAIMGLIdYPgrvMAEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPmtslnpcYTVGF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 424 TIANNIRFYQPTASNEEVQQAMEqaglakfiatlpqgLQTRVG---EAGR------GISGGQAQRIMLARAFLVQQRhIL 494
Cdd:PRK11022 111 QIMEAIKVHQGGNKKTRRQRAID--------------LLNQVGipdPASRldvyphQLSGGMSQRVMIAMAIACRPK-LL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 495 IFDEPTAHLDIETEYALKKTMVQL--FEHHLVLFATHRLHWL-EQMDYVLVLDNGKIAEQGPVKQLLQKQHGPF 565
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
364-523 |
3.86e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 364 VAIIGQSGAGKSTLLEALSGFVIPQTGNIQlnghqlphlAQDQWQ---------QQFTYlpqkpylFSDTIANNIR-FYQ 433
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYE---------EEPSWDevlkrfrgtELQNY-------FKKLYNGEIKvVHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 434 PtasneevqQAMEQaglakfiatLPQGLQTRVGEA-----GRGI---------------------SGGQAQRIMLARAfL 487
Cdd:PRK13409 166 P--------QYVDL---------IPKVFKGKVRELlkkvdERGKldevverlglenildrdiselSGGELQRVAIAAA-L 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2468565974 488 VQQRHILIFDEPTAHLDIET---------EYALKKTMVqLFEHHL 523
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIRQrlnvarlirELAEGKYVL-VVEHDL 271
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-529 |
4.78e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 341 QYDDTMDQVN---------LKDLNLT-LQGyERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLnghqlphlaqdqwQQQ 410
Cdd:PRK11819 4 QYIYTMNRVSkvvppkkqiLKDISLSfFPG-AKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-------------APG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FT--YLPQKPYL-------------FSDTIA-----NNI--RFYQPTASNEEVqqAMEQAGLAKFIAT------------ 456
Cdd:PRK11819 70 IKvgYLPQEPQLdpektvrenveegVAEVKAaldrfNEIyaAYAEPDADFDAL--AAEQGELQEIIDAadawdldsqlei 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 457 ------LPQGlQTRVGEagrgISGGQAQRIMLARaFLVQQRHILIFDEPTAHLDIETeyalkktmVQLFEHHL------V 524
Cdd:PRK11819 148 amdalrCPPW-DAKVTK----LSGGERRRVALCR-LLLEKPDMLLLDEPTNHLDAES--------VAWLEQFLhdypgtV 213
|
....*
gi 2468565974 525 LFATH 529
Cdd:PRK11819 214 VAVTH 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
355-558 |
6.79e-06 |
|
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: 49.03 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 355 NLTLQGYER--VAIIGQSGAGKSTLLEALSGFVIPQTGNIQLnghqlphLAQDQW---------------------QQQF 411
Cdd:TIGR03269 302 NVSLEVKEGeiFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV-------RVGDEWvdmtkpgpdgrgrakryigilHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQKPYLFSDTIANNIRFYQPTASNEEVQqAMEQAGLA--KFIATLPQGLQTrvgeagrgISGGQAQRIMLARAfLVQ 489
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGLELPDELARMKAVI-TLKMVGFDeeKAEEILDKYPDE--------LSEGERHRVALAQV-LIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468565974 490 QRHILIFDEPTAHLDIETEYALKKTMVQLFE--HHLVLFATHrlhwleQMDYVL-------VLDNGKIAEQGPVKQLL 558
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSH------DMDFVLdvcdraaLMRDGKIVKIGDPEEIV 516
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
353-561 |
1.55e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 353 DLNLTLQGYERVAIIGQSGAGKSTLLEALSGfVIP--QTGNIQLNGHQLP-HLAQDQWQQQFTYLPQ--KPY-LFSD--- 423
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPVKiRNPQQAIAQGIAMVPEdrKRDgIVPVmgv 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 424 ----TIANNIRFYQPTASNEevqqAMEQAGLAKFIATLPqgLQTRVGEAGRG-ISGGQAQRIMLARAFLVQQRhILIFDE 498
Cdd:PRK13549 359 gkniTLAALDRFTGGSRIDD----AAELKTILESIQRLK--VKTASPELAIArLSGGNQQKAVLAKCLLLNPK-ILILDE 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 499 PTAHLDIETEYALKKTMVQLFEHHL-VLFATHRL-HWLEQMDYVLVLDNGKIAEQGPVKQLLQKQ 561
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQGVaIIVISSELpEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ 496
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
47-268 |
2.07e-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: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 47 RKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLAQVYTTGAAMIAQKGSGNIVTNALDgMDEVNN 126
Cdd:cd18570 35 SGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 127 YF-NLILSKFMNM-MIIpwILLVYIFWQNLTSGIVLVLVFPIIILFMIILGYAAKDKASSQYAEYVVLSNHFLDALRGLT 204
Cdd:cd18570 114 AIsSTTISLFLDLlMVI--ISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468565974 205 TLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTLSIAILAVFLGLALMNGTL 268
Cdd:cd18570 192 TIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQL 255
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
364-505 |
2.10e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 364 VAIIGQSGAGKSTLLEALSGFVIPQTGNIQ-----------LNGHQLphlaqdqwqqqFTYlpqkpylFSDTIANNIRF- 431
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRGTEL-----------QDY-------FKKLANGEIKVa 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 432 -------YQPTASNEEVQQAMEQA---GLAKFIATLpQGLQTRVGEAGRGISGGQAQRIMLARAfLVQQRHILIFDEPTA 501
Cdd:COG1245 164 hkpqyvdLIPKVFKGTVRELLEKVderGKLDELAEK-LGLENILDRDISELSGGELQRVAIAAA-LLRDADFYFFDEPSS 241
|
....
gi 2468565974 502 HLDI 505
Cdd:COG1245 242 YLDI 245
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
333-552 |
2.39e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.17 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNFQYDDTmdQVnLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGF----VIpqTGNIQLNGHQLPHLAQDQWQ 408
Cdd:CHL00131 8 LEIKNLHASVNEN--EI-LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaykIL--EGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 QQFTYLP-QKPYlfsdTIA--NNIRFYQPTASNEEVQQAMEQAGLAKFIATL----------PQGLQTRVGEagrGISGG 475
Cdd:CHL00131 83 HLGIFLAfQYPI----EIPgvSNADFLRLAYNSKRKFQGLPELDPLEFLEIIneklklvgmdPSFLSRNVNE---GFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 476 QAQR-IMLARAFLVQQRHILifDEPTAHLDIEteyALK-------KTMVQlfEHHLVLFaTHRLHWLEQM--DYVLVLDN 545
Cdd:CHL00131 156 EKKRnEILQMALLDSELAIL--DETDSGLDID---ALKiiaeginKLMTS--ENSIILI-THYQRLLDYIkpDYVHVMQN 227
|
....*..
gi 2468565974 546 GKIAEQG 552
Cdd:CHL00131 228 GKIIKTG 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
333-549 |
2.97e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 333 LTIQHLNfqyddTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLP-HLAQDQWQQQF 411
Cdd:PRK10982 251 LEVRNLT-----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANEAINHGF 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 412 TYLPQK----------PYLFSDTIANNIRFYQPTA--SNEEVQQAMEQAGLAKFIATlpQGLQTRVGEagrgISGGQAQR 479
Cdd:PRK10982 326 ALVTEErrstgiyaylDIGFNSLISNIRNYKNKVGllDNSRMKSDTQWVIDSMRVKT--PGHRTQIGS----LSGGNQQK 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 480 IMLARaFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQMDYVLVLDNGKIA 549
Cdd:PRK10982 400 VIIGR-WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDkgIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
363-507 |
4.36e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 363 RVAIIGQSGAGKSTLLEALSGFVIPQTGNIQL-NGHQLPHLAQDQWQ-QQFTYLpqkpylfsDTI-----------ANNI 429
Cdd:PRK15064 29 RYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQFAfEEFTVL--------DTVimghtelwevkQERD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 430 RFY-QPTASNEEvqqAMEQAGL-AKFIATLPQGLQTRVGE--AGRGISGGQAQ------------RIMLARAfLVQQRHI 493
Cdd:PRK15064 101 RIYaLPEMSEED---GMKVADLeVKFAEMDGYTAEARAGEllLGVGIPEEQHYglmsevapgwklRVLLAQA-LFSNPDI 176
|
170
....*....|....
gi 2468565974 494 LIFDEPTAHLDIET 507
Cdd:PRK15064 177 LLLDEPTNNLDINT 190
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
351-503 |
4.87e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGfVIPQ---TGNIQLNG-------------------HQlpHLAqdqwq 408
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGevcrfkdirdsealgiviiHQ--ELA----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 409 qqftylpQKPYLfsdTIANNIRFYQPTAS------NEEVQQAMEQagLAKFiatlpqGL----QTRVGEAGRgisgGQAQ 478
Cdd:NF040905 89 -------LIPYL---SIAENIFLGNERAKrgvidwNETNRRAREL--LAKV------GLdespDTLVTDIGV----GKQQ 146
|
170 180
....*....|....*....|....*
gi 2468565974 479 RIMLARAfLVQQRHILIFDEPTAHL 503
Cdd:NF040905 147 LVEIAKA-LSKDVKLLILDEPTAAL 170
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
347-550 |
5.48e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 347 DQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPhlaqdqwqqqftylPQKPYlfsDTIA 426
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--------------PRSPL---DAVK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NNIRFYQPT------------ASNEEVQQAMEQAGLAKFIATLPQGLQTRVGEAGRG---------------ISGGQAQR 479
Cdd:PRK09700 338 KGMAYITESrrdngffpnfsiAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQREllalkchsvnqniteLSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 480 IMLARaFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEH-HLVLFATHRL-HWLEQMDYVLVLDNGKIAE 550
Cdd:PRK09700 418 VLISK-WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
362-521 |
5.73e-05 |
|
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: 44.10 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 362 ERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLphlaqdqwqqqfTYLPQKPYLfsdtiannirfyqptasneev 441
Cdd:cd03222 26 EVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP------------VYKPQYIDL--------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 442 qqameqaglakfiatlpqglqtrvgeagrgiSGGQAQRIMLArAFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEH 521
Cdd:cd03222 73 -------------------------------SGGELQRVAIA-AALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
303-504 |
6.57e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 303 AFQQTLDILAIPTVTD---RTLLPAftwnEQSRLTIQHLNFQYDDtmdQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLE 379
Cdd:PRK10938 232 AHSEQLEGVQLPEPDEpsaRHALPA----NEPRIVLNNGVVSYND---RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 380 ALSGfVIPQ--TGNIQLNGHQLPHlAQDQW--QQQFTYLPQK---PYLFSDTIAN--------NIRFYQ--PTASNEEVQ 442
Cdd:PRK10938 305 LITG-DHPQgySNDLTLFGRRRGS-GETIWdiKKHIGYVSSSlhlDYRVSTSVRNvilsgffdSIGIYQavSDRQQKLAQ 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468565974 443 QAMEQAGLAKFIATLPqglqtrvgeaGRGISGGQaQRIML-ARAfLVQQRHILIFDEPTAHLD 504
Cdd:PRK10938 383 QWLDILGIDKRTADAP----------FHSLSWGQ-QRLALiVRA-LVKHPTLLILDEPLQGLD 433
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
362-537 |
1.00e-04 |
|
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: 42.75 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 362 ERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQlnghqlphlaqdqwqqqftylpqkpYLFSDTIANNIRFyqptasneev 441
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------YIDGEDILEEVLD---------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 442 qqameqaglakfiatlpQGLQTRVGEAGRGISGGQAQRIMLARAFLVQQRhILIFDEPTAHLDIETEYALKKTMVQLFEH 521
Cdd:smart00382 48 -----------------QLLLIIVGGKKASGSGELRLRLALALARKLKPD-VLILDEITSLLDAEQEALLLLLEELRLLL 109
|
170 180
....*....|....*....|...
gi 2468565974 522 HL-------VLFATHRLHWLEQM 537
Cdd:smart00382 110 LLkseknltVILTTNDEKDLGPA 132
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
51-291 |
1.12e-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: 44.48 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 51 SQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLAQVYTTGAAMIAQKGSGNIV------TNALDGMdeV 124
Cdd:cd18565 51 GQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMsvlnndVNQLERF--L 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 125 NNYFNLILSKFMNMMIIpWILLVYIFWQnLTsgIVLVLVFPIIILFMIILG------YAAKDKASSQyaeyvvLSNHFLD 198
Cdd:cd18565 129 DDGANSIIRVVVTVLGI-GAILFYLNWQ-LA--LVALLPVPLIIAGTYWFQrrieprYRAVREAVGD------LNARLEN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 199 ALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALdWFTTLsIAILAVFL--GLALMNGTLPLYP---- 272
Cdd:cd18565 199 NLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVI-RLVAG-AGFVATFVvgGYWVLDGPPLFTGtltv 276
|
250 260
....*....|....*....|.
gi 2468565974 273 -ALVTLILAPEYFL-PLRDFA 291
Cdd:cd18565 277 gTLVTFLFYTQRLLwPLTRLG 297
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
475-565 |
1.54e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 475 GQAQRIMLARAfLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH--LVLFATHRLHWLEQM-DYVLVLDNGKIAEQ 551
Cdd:PRK15093 162 GECQKVMIAIA-LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWaDKINVLYCGQTVET 240
|
90
....*....|....
gi 2468565974 552 GPVKQLLQKQHGPF 565
Cdd:PRK15093 241 APSKELVTTPHHPY 254
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
15-270 |
1.65e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 43.65 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 15 LFKMLAGLTVLQAFMILFQAIFLAKVLVLSWQRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLL 94
Cdd:cd18563 4 GFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 95 AQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMN--MMIIpwILLVYIFWQNLTSGIVLVLVFPIIILFMI 172
Cdd:cd18563 84 EHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTniLMII--GIGVVLFSLNWKLALLVLIPVPLVVWGSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 173 ILGYAAKDKASSQYAEYVVLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTLSI 252
Cdd:cd18563 162 FFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGT 241
|
250
....*....|....*...
gi 2468565974 253 AILAVFLGLALMNGTLPL 270
Cdd:cd18563 242 LIVWYFGGRQVLSGTMTL 259
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
335-560 |
2.03e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 335 IQHLNFQYDDTmdqVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQ-LNG---------HQLPHLAq 404
Cdd:NF033858 4 LEGVSHRYGKT---VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGdmadarhrrAVCPRIA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 405 dqwqqqftYLPQK------PYLfsdTIANNIRFY-----QPTASNEE-VQQAMEQAGLAKFiATLPqglqtrvgeAGRgI 472
Cdd:NF033858 80 --------YMPQGlgknlyPTL---SVFENLDFFgrlfgQDAAERRRrIDELLRATGLAPF-ADRP---------AGK-L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 473 SGGQAQRIMLARAfLVQQRHILIFDEPTAHLD----------IETEYALKKTMVqlfehhlVLFATHRLHWLEQMDYVLV 542
Cdd:NF033858 138 SGGMKQKLGLCCA-LIHDPDLLILDEPTTGVDplsrrqfwelIDRIRAERPGMS-------VLVATAYMEEAERFDWLVA 209
|
250
....*....|....*...
gi 2468565974 543 LDNGKIAEQGPVKQLLQK 560
Cdd:NF033858 210 MDAGRVLATGTPAELLAR 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
351-567 |
3.95e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQ---TGNIQLNGHQLPHLAQdqwQQQFTYLPQKP-YLFSDTIA 426
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVP---RKTSAYISQNDvHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 427 NNIRF-------------YQPTASNEEVQQAMEQAGLAKFI-ATLPQGLQ-------------------TRVG-EAGRGI 472
Cdd:PLN03140 258 ETLDFsarcqgvgtrydlLSELARREKDAGIFPEAEVDLFMkATAMEGVKsslitdytlkilgldickdTIVGdEMIRGI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 473 SGGQAQRIMLARaFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH----LVLFATHRLHWLEQMDYVLVLDNGKI 548
Cdd:PLN03140 338 SGGQKKRVTTGE-MIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTeatvLMSLLQPAPETFDLFDDIILLSEGQI 416
|
250
....*....|....*....
gi 2468565974 549 AEQGPVKQLLQkqhgpFFE 567
Cdd:PLN03140 417 VYQGPRDHILE-----FFE 430
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
363-399 |
4.76e-04 |
|
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: 39.91 E-value: 4.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2468565974 363 RVAIIGQSGAGKSTLLEALSGFVI-----------PQTGNIQLNGHQL 399
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAivsdypgttrdPNEGRLELKGKQI 48
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
331-529 |
4.96e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.68 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 331 SRLTIQhlNFQyddtmdqvNLKDLNLTLQGyERVAIIGQSGAGKSTLLEALSGFvipqtgniqLNGHQLPHLAQDQWQQQ 410
Cdd:COG3593 4 EKIKIK--NFR--------SIKDLSIELSD-DLTVLVGENNSGKSSILEALRLL---------LGPSSSRKFDEEDFYLG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 411 FTYLPQKPYL---FSDTIANNIRFYQPTASNEEVQQAME--QAGLAKFIATLPQGLQTRVGEAGRG-------------- 471
Cdd:COG3593 64 DDPDLPEIEIeltFGSLLSRLLRLLLKEEDKEELEEALEelNEELKEALKALNELLSEYLKELLDGldlelelsldeled 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 472 --------ISGGQA----------QRIM-------LARAFLVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHHL-VL 525
Cdd:COG3593 144 llkslslrIEDGKElpldrlgsgfQRLIllallsaLAELKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVI 223
|
....
gi 2468565974 526 FATH 529
Cdd:COG3593 224 ITTH 227
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
348-513 |
5.06e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 348 QVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIqlnghQLPHLAQDQWQQQFTYLPQKPYLfsDTIAN 427
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSY-----TFPGNWQLAWVNQETPALPQPAL--EYVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 428 NIRFYQPTASneEVQQAMEQA---------GLAKFI---------ATLPQGL---QTRVGEAGRGISGGQAQRIMLARAf 486
Cdd:PRK10636 87 GDREYRQLEA--QLHDANERNdghaiatihGKLDAIdawtirsraASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQA- 163
|
170 180
....*....|....*....|....*..
gi 2468565974 487 LVQQRHILIFDEPTAHLDIETEYALKK 513
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEK 190
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
50-270 |
6.44e-04 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 42.02 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 50 LSQLGWLAGAFFLAFLG-RHGLTWIKNRLLDRYATKTTEDLRQKLLAQVYTTGAAMIAQKGSGNIVTNALDGMDEVNNYf 128
Cdd:cd18554 41 VYKLFTIIGIMFFIFLIlRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDF- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 129 nlILSKFMNM---MIIPWILLVYIFWQNLTSGIVLVLVFPIIILFMIILGYAAKDKASSQYAEYVVLSNHFLDALRGLTT 205
Cdd:cd18554 120 --ITTGLMNIwldMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSV 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 206 LKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTLSIAILAVFLGLALMNGTLPL 270
Cdd:cd18554 198 IKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTV 262
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
471-531 |
1.02e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 1.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 471 GISGGQAQRIMLARAF---LVQQRHILIFDEPTAHLDIETEYALKKTMVQLFEHH-LVLFATHRL 531
Cdd:cd03227 77 QLSGGEKELSALALILalaSLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLP 141
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
19-268 |
1.25e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 40.93 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 19 LAGLTVLQAFMILFQAIFLAKVL--VLSWQRKGLSQLGWLAGAFFLAFLGRHGLTWIKNRLLDRYATKttedLRQKLLAQ 96
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLIsyLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMR----VRSALSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 97 VY----TTGAAMIAQKGSGNIVT---NALDGMDEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLVLVFPIIIL 169
Cdd:cd18579 78 IYrkalRLSSSARQETSTGEIVNlmsVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 170 FMIILGyaakdKASSQYAEY----VVLSNHFLDALRgltTLKMLGLSKEYTHNIyqvsENYRKKTLSTLRIA--ILSTFA 243
Cdd:cd18579 158 LAKLIS-----KLRKKLMKAtderVKLTNEILSGIK---VIKLYAWEKPFLKRI----EELRKKELKALRKFgyLRALNS 225
|
250 260
....*....|....*....|....*
gi 2468565974 244 LDWFTTLSIAILAVFLGLALMNGTL 268
Cdd:cd18579 226 FLFFSTPVLVSLATFATYVLLGNPL 250
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
358-392 |
1.48e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 1.48e-03
10 20 30
....*....|....*....|....*....|....*
gi 2468565974 358 LQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNI 392
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
447-543 |
1.49e-03 |
|
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: 40.68 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 447 QAGLAKFIATLPQ-GLQ-TRVGEAGRGISGGQAQRIMLARAFLVQQRH--ILIFDEPTAHLDIETEYALKKTMVQLFEH- 521
Cdd:cd03271 143 IPKIARKLQTLCDvGLGyIKLGQPATTLSGGEAQRIKLAKELSKRSTGktLYILDEPTTGLHFHDVKKLLEVLQRLVDKg 222
|
90 100
....*....|....*....|..
gi 2468565974 522 HLVLFATHRLHWLEQMDYVLVL 543
Cdd:cd03271 223 NTVVVIEHNLDVIKCADWIIDL 244
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
461-563 |
1.93e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.87 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 461 LQTRVGEAGRGISGGQAQRIMLArAFLVQQRHILIFDEPTAHLDIETEYAL---KKTMVQlfEHHLVLFATHRLHWLEQM 537
Cdd:NF000106 134 LTEAAGRAAAKYSGGMRRRLDLA-ASMIGRPAVLYLDEPTTGLDPRTRNEVwdeVRSMVR--DGATVLLTTQYMEEAEQL 210
|
90 100
....*....|....*....|....*..
gi 2468565974 538 DYVL-VLDNGKIAEQGPVKQLLQKQHG 563
Cdd:NF000106 211 AHELtVIDRGRVIADGKVDELKTKVGG 237
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
22-279 |
3.18e-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: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 22 LTVLQAFMILFQAIFLAKVLvlSWQRKGLSQLGWLAgAFFLAFLGRHGLTWIKNRLLDRYATKTTEDLRQKLLAQVYTTG 101
Cdd:cd18551 7 LSLLGTAASLAQPLLVKNLI--DALSAGGSSGGLLA-LLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 102 AAMIAQKGSGNIVTNALDGMDEVNNYFNLILSKFMN---MMIIPWILLVYIFWQnLTsgIVLVLVFPIIILFMIILGYAA 178
Cdd:cd18551 84 VSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTgvlTVVGAVVLMFLLDWV-LT--LVTLAVVPLAFLIILPLGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 179 KdKASSQYAEYV-VLSNHFLDALRGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRI-AILSTFALdwfTTLSIAILA 256
Cdd:cd18551 161 R-KASKRAQDALgELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIeALIGPLMG---LAVQLALLV 236
|
250 260
....*....|....*....|....*
gi 2468565974 257 VFL--GLALMNGTLPLyPALVTLIL 279
Cdd:cd18551 237 VLGvgGARVASGALTV-GTLVAFLL 260
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
364-392 |
3.36e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.30 E-value: 3.36e-03
10 20
....*....|....*....|....*....
gi 2468565974 364 VAIIGQSGAGKSTLLEALSGFVIPQTGNI 392
Cdd:cd01854 88 SVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
472-543 |
3.62e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 3.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468565974 472 ISGGQAQRIMLARAFLVQQRH--ILIFDEPTAHLDIETEYALKKTMVQL-FEHHLVLFATHRLHWLEQMDYVLVL 543
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPSKKptLYVLDEPTTGLHTHDIKALIYVLQSLtHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
363-397 |
3.73e-03 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 38.24 E-value: 3.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2468565974 363 RVAIIGQSGAGKSTLLEALSGF----V--IPQT------GNIQLNGH 397
Cdd:cd04164 5 KVVIAGKPNVGKSSLLNALAGRdraiVsdIAGTtrdvieEEIDLGGI 51
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
122-280 |
3.82e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 39.39 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 122 DEVNNYFNLILSKFMNMMIIPWILLVYIFWQNLTSGIVLVLVFPIIILFMIILGYAAKDKASSQYAEYVV-LSNHFLDAL 200
Cdd:cd18585 103 DTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLGKKIGQQLVQLRAeLRTELVDGL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 201 RGLTTLKMLGLSKEYTHNIYQVSENYRKKTLSTLRIAILSTFALDWFTTLSIAILAVFLGLALMNGTL--PLYPALVTLI 278
Cdd:cd18585 183 QGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALdgALLAMLVFAV 262
|
..
gi 2468565974 279 LA 280
Cdd:cd18585 263 LA 264
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
333-404 |
4.89e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 4.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468565974 333 LTIQHLNFqyddTMDQVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNGHQLPHLAQ 404
Cdd:PRK13541 2 LSLHQLQF----NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK 69
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
460-543 |
5.37e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 460 GLQ-TRVGEAGRGISGGQAQRIMLARAFL--VQQRHILIFDEPTAHLDIETeyaLKKTM--VQLFEH--HLVLFATHRLH 532
Cdd:TIGR00630 817 GLGyIRLGQPATTLSGGEAQRIKLAKELSkrSTGRTLYILDEPTTGLHFDD---IKKLLevLQRLVDkgNTVVVIEHNLD 893
|
90
....*....|.
gi 2468565974 533 WLEQMDYVLVL 543
Cdd:TIGR00630 894 VIKTADYIIDL 904
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
461-505 |
5.99e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 5.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2468565974 461 LQTRvgeAGRGISGGQAQRIMLARAFLVQQrHILIFDEPTAHLDI 505
Cdd:PLN03073 337 MQVK---ATKTFSGGWRMRIALARALFIEP-DLLLLDEPTNHLDL 377
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
351-396 |
6.02e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.33 E-value: 6.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2468565974 351 LKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGFVIPQTGNIQLNG 396
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG 59
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
350-552 |
6.11e-03 |
|
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: 38.07 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 350 NLKDLNLTLQGYERVAIIGQSGAGKSTLLEAlsgfVIPQTGNIQLNGhqlphlaqdqwqqqftyLPQKPYlfsdtianni 429
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE----GLYASGKARLIS-----------------FLPKFS---------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 430 rfYQPTASNEEVQqAMEQAGLAKFiaTLPQGLQTrvgeagrgISGGQAQRIMLARAFLVQQRHIL-IFDEPTAHLDIETE 508
Cdd:cd03238 59 --RNKLIFIDQLQ-FLIDVGLGYL--TLGQKLST--------LSGGELQRVKLASELFSEPPGTLfILDEPSTGLHQQDI 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2468565974 509 YALKKTMVQLF-EHHLVLFATHRLHWLEQMDYVLVL------DNGKIAEQG 552
Cdd:cd03238 126 NQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
348-511 |
6.28e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 39.35 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 348 QVNLKDLNLTLQGYERVAIIGQSGAGKSTLLEALSGfVIPQTGniqlnghqlPHLAQDQWQQQFtYLPQKPYLFSDTIAN 427
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYG---------GRLTKPAKGKLF-YVPQRPYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468565974 428 NIRFyqPTASNEEVQQAMEQAGLAKFIATLPQG--LQTRVG-EAGRG----ISGGQAQRIMLARAFLVQQRHIlIFDEPT 500
Cdd:TIGR00954 534 QIIY--PDSSEDMKRRGLSDKDLEQILDNVQLThiLEREGGwSAVQDwmdvLSGGEKQRIAMARLFYHKPQFA-ILDECT 610
|
170
....*....|.
gi 2468565974 501 AHLDIETEYAL 511
Cdd:TIGR00954 611 SAVSVDVEGYM 621
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
473-506 |
7.33e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 7.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2468565974 473 SGGQAQRIMLARaFLV---QQRHILIFDEPTAHL---DIE 506
Cdd:COG0178 828 SGGEAQRVKLAS-ELSkrsTGKTLYILDEPTTGLhfhDIR 866
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
347-383 |
9.84e-03 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 38.17 E-value: 9.84e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2468565974 347 DQVNLKDLNLTLQGyERVAIIGQSGAGKSTLLEALSG 383
Cdd:COG1162 153 TGEGLDELRELLKG-KTSVLVGQSGVGKSTLINALLP 188
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