|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-527 |
5.48e-155 |
|
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: 454.60 E-value: 5.48e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 2 KKLTTILFQYKIFPVLMFLVSTGLGILVITQNILIADFLAKIIRHQ--FQGLWIVLFILLGVLLLRATVQFLNQWLGDTL 79
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGapLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 80 AFKVKHMLRQRVIYK--------NNGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIML 151
Cdd:COG4988 86 AARVKRRLRRRLLEKllalgpawLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 152 ITAPFIPLFYIIFGLKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSG 231
Cdd:COG4988 166 VTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 232 LMLEFISMLGIGLVALEATLSLvVFHNIDFKTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASDVVFEFLEQPN----Y 307
Cdd:COG4988 246 AVLEFFASLSIALVAVYIGFRL-LGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEpaapA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 308 NNEFLlkyEENQKPFIQLTDISFRYDDsDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRD 387
Cdd:COG4988 325 GTAPL---PAAGPPSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 388 L----------NIGILSQQPYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMR 456
Cdd:COG4988 401 LsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQ 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 457 RIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIA 527
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVE 551
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-512 |
2.64e-115 |
|
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: 351.59 E-value: 2.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 19 FLVSTGL-----GILVITQNILIADFLAKIIR--HQFQGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKVKHMLRQRV 91
Cdd:TIGR02857 4 ALALLALlgvlgALLIIAQAWLLARVVDGLISagEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 92 IYK--------NNGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYII 163
Cdd:TIGR02857 84 LEAvaalgprwLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 164 FGLKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFISMLGIG 243
Cdd:TIGR02857 164 IGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 244 LVALEATLSLvVFHNIDFKTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASDVVFEFLE---QPNYNNEFLLkyeENQK 320
Cdd:TIGR02857 244 LVAVYIGFRL-LAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDaapRPLAGKAPVT---AAPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDSDRlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NI 390
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadadadswrdQI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPD 469
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446659814 470 LVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIR 512
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-527 |
1.82e-91 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 291.30 E-value: 1.82e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 1 MKKLTTILFQYK---IFPVLMFLVSTGLGILVItqnILIADFLAKIIRHQ-FQGLWIVLFILLGVLLLRATVQFLNQWLG 76
Cdd:COG1132 9 LRRLLRYLRPYRgllILALLLLLLSALLELLLP---LLLGRIIDALLAGGdLSALLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 77 DTLAFKVKHMLRQRVIYK---------NNgHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTA 147
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHllrlplsffDR-RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 148 LIMLITAPFIPLFYIIFGLKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSA 227
Cdd:COG1132 165 LIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 228 FLSGLMLEFISMLGIGLVALEATLsLVVFHNIDFKTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASDVVFEFLEQPNy 307
Cdd:COG1132 245 ALFFPLMELLGNLGLALVLLVGGL-LVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 308 nnefLLKYEENQKPF------IQLTDISFRYDDsDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI 381
Cdd:COG1132 323 ----EIPDPPGAVPLppvrgeIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 382 S---TNQRDL-------NIGILSQQPYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEML 450
Cdd:COG1132 398 LidgVDIRDLtleslrrQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNL 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 451 SGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIA 527
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-526 |
4.20e-85 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 275.19 E-value: 4.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 26 GILVITQNILIADFLAKII-----RHQFQGLWIVLFILLGVlllRATVQFLNQWLGDTLAFKVKHMLRQRVIYK------ 94
Cdd:PRK11174 35 GLLLIAQAWLLATILQALIienipREALLPPFILLILLFVL---RALLAWLRERVGFKAGQHIRQQIRQQVLDKlqqlgp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 95 --NNGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIFGLKTRDES 172
Cdd:PRK11174 112 awIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTAPLIPLFMALVGMGAADAN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 173 KDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFISMLGIGLVAleatls 252
Cdd:PRK11174 192 RRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASISIALVA------ 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 253 lVVF-----HNIDFKTAAIAI---------ILAPEFYNAIKDLGQAFHTGKQSEGASDVVFEFLEQPnynnefLLKYEEN 318
Cdd:PRK11174 266 -VYFgfsylGELNFGHYGTGVtlfagffvlILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETP------LAHPQQG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 319 QKPFIQLTDISFRYDD------SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGV--YQptiGTISTNQ---RD 387
Cdd:PRK11174 339 EKELASNDPVTIEAEDleilspDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGielRE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 388 LN-------IGILSQQPYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIE 459
Cdd:PRK11174 416 LDpeswrkhLSWVGQNPQLPHGTLRDNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLA 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 460 LCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
20-296 |
4.95e-79 |
|
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: 249.63 E-value: 4.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 20 LVSTGLGILVITQNILIADFLAKII--RHQFQGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKVKHMLRQRVIYK--- 94
Cdd:cd18584 3 LLGLLAALLIIAQAWLLARIIAGVFleGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARlla 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 95 -----NNGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIFGLKTR 169
Cdd:cd18584 83 lgpalLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKAAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 170 DESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFISMLGIGLVALEA 249
Cdd:cd18584 163 AASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAVYI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446659814 250 TLSLvVFHNIDFKTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASD 296
Cdd:cd18584 243 GFRL-LGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAE 288
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-528 |
1.38e-76 |
|
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: 255.53 E-value: 1.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 16 VLMFLVSTGLGILV--ITQNILiaDFLakIIRHQFQGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKV---------K 84
Cdd:COG2274 162 LLASLLINLLALATplFTQVVI--DRV--LPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIdlrlssrffR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 85 HMLRQRVIYKNNGHPiGEQMTILTENiDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIF 164
Cdd:COG2274 238 HLLRLPLSFFESRSV-GDLASRFRDV-ESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLF 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 165 GLKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFISMLG-IG 243
Cdd:COG2274 316 QPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLAtVA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 244 LVALEATLslVVFHNIdfkT--AAIAI-ILAPEFYNAIKDLGQAFHTGKQSEGASDVVFEFLEQP--NYNNEFLLKYEEn 318
Cdd:COG2274 396 LLWLGAYL--VIDGQL---TlgQLIAFnILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPpeREEGRSKLSLPR- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 319 QKPFIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------- 388
Cdd:COG2274 470 LKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLrqidpaslrr 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 NIGILSQQPYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMK 467
Cdd:COG2274 550 QIGVVLQDVFLFSGTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRN 629
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 468 PDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIAD 528
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
101-527 |
4.58e-73 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 242.75 E-value: 4.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 101 GEQMTILTENIDGLAPFY-KSYLPqVFKSMMVPLIIIIAMFFIHFNTALI----MLITAPFIPLFyiiFGLKTRDESKDQ 175
Cdd:COG4987 112 GDLLNRLVADVDALDNLYlRVLLP-LLVALLVILAAVAFLAFFSPALALVlalgLLLAGLLLPLL---AARLGRRAGRRL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 176 MTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFISMLGIGLVALEAtLSLVV 255
Cdd:COG4987 188 AAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLA-APLVA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 256 FHNIDFkTAAIAIILAP----EfynAIKDLGQAFHTGKQSEGASDVVFEFLEQPNYNNEFLLKYEENQKPFIQLTDISFR 331
Cdd:COG4987 267 AGALSG-PLLALLVLAAlalfE---ALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 332 YDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGILSQQPYIFS 401
Cdd:COG4987 343 YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLrdldeddlrrRIAVVPQRPHLFD 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 402 ASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGL 480
Cdd:COG4987 423 TTLRENLRLARpDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446659814 481 DIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIA 527
Cdd:COG4987 503 DAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
323-524 |
2.77e-57 |
|
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: 188.75 E-value: 2.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGI 392
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENItmfkdienntieevldevglldkvqsftkgintiigeggemLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446659814 473 FDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGR 524
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
129-527 |
1.75e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 182.33 E-value: 1.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 129 MMVPLIIIIAMF----FIHFNTAL----IMLITAPFIP-LFYIIfGLKTrdeSKDQMTYLNQFSQRFLNIAKGLVTLKLF 199
Cdd:PRK11160 141 LVAALVVILVLTiglsFFDLTLALtlggILLLLLLLLPlLFYRL-GKKP---GQDLTHLRAQYRVQLTEWLQGQAELTLF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 200 N-------RTEQTEKHIYDDSTQFRTLT-----MRILRSAFLSGLMLeFISMLGIGLVAL-EATLSLVVFhnidfktAAI 266
Cdd:PRK11160 217 GaedryrqQLEQTEQQWLAAQRRQANLTglsqaLMILANGLTVVLML-WLAAGGVGGNAQpGALIALFVF-------AAL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 267 AI--ILAPefynaikdLGQAF-HTGkQSEGASDVVFEFLEQP-----NYNNEFllkyeENQKPFIQLTDISFRYDDSDRL 338
Cdd:PRK11160 289 AAfeALMP--------VAGAFqHLG-QVIASARRINEITEQKpevtfPTTSTA-----AADQVSLTLNNVSFTYPDQPQP 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGILSQQPYIFSASIKENI 408
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdyseaalrqaISVVSQRVHLFSATLRDNL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 409 TMFK-DIENNTIEEVLDEVGLLDKVQSfTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHM 487
Cdd:PRK11160 435 LLAApNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQ 513
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446659814 488 IQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIA 527
Cdd:PRK11160 514 ILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
323-526 |
2.47e-49 |
|
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: 170.10 E-value: 2.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGI 392
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLV 471
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 472 IFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
323-528 |
6.84e-48 |
|
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: 165.84 E-value: 6.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI---STNQRDL-------NIGI 392
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldGTDIRQLdpadlrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLV 471
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 472 IFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIAD 528
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
323-526 |
1.82e-46 |
|
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: 162.71 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDD-SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIS---TNQRDLN-------IG 391
Cdd:cd03249 1 IEFKNVSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgVDIRDLNlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQPYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDL 470
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKpDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 471 VIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
323-529 |
3.16e-45 |
|
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: 158.81 E-value: 3.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGI 392
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiglhdlrsrISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 473 FDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIADD 529
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
322-526 |
4.08e-45 |
|
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: 158.54 E-value: 4.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 322 FIQLTDISFRYDdSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IG 391
Cdd:cd03254 2 EIEFENVNFSYD-EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdisrkslrsmIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQPYIFSASIKENITMFKDIENNT-IEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDL 470
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEeVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 471 VIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKII 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
86-525 |
4.67e-45 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 169.13 E-value: 4.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 86 MLRQRVIYKNNgHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIFG 165
Cdd:TIGR00958 244 LLRQDLGFFDE-NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFG 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 166 LKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMR--ILRSAF-----LSGlMLEFIS 238
Cdd:TIGR00958 323 KRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRkaLAYAGYlwttsVLG-MLIQVL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 239 MLGIG--LVaLEATLS---LVVFhnidfktaaiaIILAPEFYNAIKDLGQAFHTGKQSEGASDVVFEFLE-QPNYNNEFL 312
Cdd:TIGR00958 402 VLYYGgqLV-LTGKVSsgnLVSF-----------LLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDrKPNIPLTGT 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 313 LKYEeNQKPFIQLTDISFRY-DDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--- 388
Cdd:TIGR00958 470 LAPL-NLEGLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvqy 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 -------NIGILSQQPYIFSASIKENITM-FKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIEL 460
Cdd:TIGR00958 549 dhhylhrQVALVGQEPVLFSGSVRENIAYgLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAI 628
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 461 CRLLVMKPDLVIFDEPATGLDIQTEHMIQNvlFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
322-528 |
4.19e-44 |
|
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: 166.19 E-value: 4.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 322 FIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIS---TNQRDL-------NIG 391
Cdd:TIGR03375 463 EIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLldgVDIRQIdpadlrrNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQPYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDL 470
Cdd:TIGR03375 543 YVPQDPRLFYGTLRDNIALGApYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPI 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 471 VIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIAD 528
Cdd:TIGR03375 623 LLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVAD 680
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
101-507 |
5.34e-42 |
|
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: 157.91 E-value: 5.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 101 GEQMTILTENIDGLAPFY-KSYLPQVfKSMMVPLIIIIAMFFIHFNTALI----MLITAPFIPLfyiIFGLKTRDESKDQ 175
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYvRVIVPAG-VALVVGAAAVAAIAVLSVPAALIlaagLLLAGFVAPL---VSLRAARAAEQAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 176 MTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSglmlEFISMLGIGLVALEATL---S 252
Cdd:TIGR02868 186 ARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG----AALTLLAAGLAVLGALWaggP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 253 LVVFHNIDFKTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASDVVFEFLEQPNYNNEFLL---KYEENQKPFIQLTDIS 329
Cdd:TIGR02868 262 AVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSApaaGAVGLGKPTLELRDLS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 330 FRYDDSDRlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGILSQQPYI 399
Cdd:TIGR02868 342 AGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSsldqdevrrrVSVCAQDAHL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 FSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPAT 478
Cdd:TIGR02868 421 FDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
410 420
....*....|....*....|....*....
gi 446659814 479 GLDIQTEHMIQNVLFQHFKDTTMIVIAHR 507
Cdd:TIGR02868 501 HLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
323-525 |
2.86e-41 |
|
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: 148.39 E-value: 2.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDD-SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IG 391
Cdd:cd03248 12 VKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyehkylhskVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQPYIFSASIKENITM-FKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDL 470
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYgLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 471 VIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
323-530 |
3.73e-40 |
|
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: 145.71 E-value: 3.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGI 392
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaladpawlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFKD-IENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLV 471
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 472 IFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIADDR 530
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGS 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
323-526 |
5.37e-40 |
|
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: 145.07 E-value: 5.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGI 392
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIrevtldslrrAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLV 471
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 472 IFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
323-528 |
1.82e-39 |
|
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: 141.68 E-value: 1.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN---------IGIL 393
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQPYIFSASIKENItmfkdienntieevldevglldkvqsftkgintiigegGEMLSGGQMRRIELCRLLVMKPDLVIF 473
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 474 DEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIAD 528
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
99-511 |
2.69e-39 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 151.41 E-value: 2.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 99 PIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIFGLKTRDESKDQMTY 178
Cdd:PRK10790 120 PVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAY 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 179 LNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRsafLSGLMLE-----FISMLGIGLVALeatlsl 253
Cdd:PRK10790 200 LADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLR---LDGFLLRpllslFSALILCGLLML------ 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 254 vvfhnidFKTAAIAIILAPEFYNAIKDLGQAFH-----TGKQSEGASDVV-----FEFLEQPNYnnefllKYEENQKPF- 322
Cdd:PRK10790 271 -------FGFSASGTIEVGVLYAFISYLGRLNEplielTTQQSMLQQAVVagervFELMDGPRQ------QYGNDDRPLq 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 ---IQLTDISFRYDDsDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------N 389
Cdd:PRK10790 338 sgrIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslshsvlrqG 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 IGILSQQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPD 469
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQ 496
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446659814 470 LVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTI 511
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI 538
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
309-527 |
5.82e-39 |
|
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: 149.90 E-value: 5.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 309 NEFLLKYEENQKP--------FIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGT 380
Cdd:COG4618 309 NELLAAVPAEPERmplprpkgRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 381 ISTNQRDL----------NIGILSQQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEML 450
Cdd:COG4618 389 VRLDGADLsqwdreelgrHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 451 SGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHFKD--TTMIVIAHRDNTIRHLQRRLYIENGRLIA 527
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKArgATVVVITHRPSLLAAVDKLLVLRDGRVQA 546
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
323-529 |
3.91e-38 |
|
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: 139.78 E-value: 3.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGI 392
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkknlrelrrkVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQP--YIFSASIKENItMF---------KDIENNtIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIELC 461
Cdd:COG1122 80 VFQNPddQLFAPTVEEDV-AFgpenlglprEEIRER-VEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 462 RLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQ-HFKDTTMIVIAHR-DNTIRHLQRRLYIENGRLIADD 529
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDlDLVAELADRVIVLDDGRIVADG 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-528 |
4.44e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 140.22 E-value: 4.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-----IGILSQ 395
Cdd:COG1121 5 PAIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRrarrrIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 396 QPYI---FSASIKENITM-----------FKDIENNTIEEVLDEVGLLDKvqsftkgINTIIGEggemLSGGQMRRIELC 461
Cdd:COG1121 83 RAEVdwdFPITVRDVVLMgrygrrglfrrPSRADREAVDEALERVGLEDL-------ADRPIGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 462 RLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHFKD--TTMIVIAHRDNTIR-HLQRRLYIeNGRLIAD 528
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRRegKTILVVTHDLGAVReYFDRVLLL-NRGLVAH 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
323-524 |
4.72e-38 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 138.76 E-value: 4.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDR---LVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRdlnIGILSQQPYI 399
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---IAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 FSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATG 479
Cdd:cd03250 78 QNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446659814 480 LDIQTE-HMIQNVLFQHFKDT-TMIVIAHRDNTIRHLQRRLYIENGR 524
Cdd:cd03250 158 VDAHVGrHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
324-524 |
5.15e-38 |
|
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: 138.75 E-value: 5.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 324 QLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGIL 393
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTklslkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQP--YIFSASIKE-------NITMFKDIENNTIEEVLDEVGLLDKVQSFTkgintiigeggEMLSGGQMRRIELCRLL 464
Cdd:cd03225 81 FQNPddQFFGPTVEEevafgleNLGLPEEEIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446659814 465 VMKPDLVIFDEPATGLDIQTEHMIQNVLFQ-HFKDTTMIVIAHRDNTIRHL-QRRLYIENGR 524
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
323-525 |
1.50e-37 |
|
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: 136.19 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGI 392
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENItmfkdienntieevldevglldkvqsftkgintiigeggemLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 473 FDEPATGLDIQTEHMIQNVLfQHFK--DTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAI-AALKaaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
323-526 |
2.30e-37 |
|
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: 146.81 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGI 392
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLaiadpawlrrQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFKdiENNTIEEVLDEV---GLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPD 469
Cdd:TIGR01846 536 VLQENVLFSRSIRDNIALCN--PGAPFEHVIHAAklaGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPR 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 470 LVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIA 670
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
320-530 |
7.82e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 136.33 E-value: 7.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 320 KPFIQLTDISFRYDDSDRLV--LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--------- 388
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 -----NIGILSQQPYIF-SASIKENITM------FKDIENNT-IEEVLDEVGLLDKVQSFtkgintiIGEggemLSGGQM 455
Cdd:COG1136 82 rlrrrHIGFVFQFFNLLpELTALENVALplllagVSRKERRErARELLERVGLGDRLDHR-------PSQ----LSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 456 RRIELCRLLVMKPDLVIFDEPaTG-LDIQTEHMIQNVLFQHFKD--TTMIVIAHRDNTIRHLQRRLYIENGRLIADDR 530
Cdd:COG1136 151 QRVAIARALVNRPKLILADEP-TGnLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
323-526 |
1.95e-36 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 143.94 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGI 392
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLagldvqavrrQLGV 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:TIGR03797 532 VLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILL 611
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446659814 473 FDEPATGLDIQTEHMIQNVLFQhfKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:TIGR03797 612 FDEATSALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGRVV 663
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
323-526 |
2.24e-36 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 142.79 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIS---TNQRDL-------NIGI 392
Cdd:PRK13657 335 VEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgTDIRTVtraslrrNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFKdiENNTIEEVLDEVGL---LDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPD 469
Cdd:PRK13657 414 VFQDAGLFNRSIEDNIRVGR--PDATDEEMRAAAERaqaHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 470 LVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-531 |
4.16e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL-------------N 389
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkrreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 IGILSQ-QPYIFSASIKENItMF---------KDIENNtIEEVLDEVGLLDKVQSFTkgintiigeggEMLSGGQMRRIE 459
Cdd:COG2884 81 IGVVFQdFRLLPDRTVYENV-ALplrvtgksrKEIRRR-VREVLDLVGLSDKAKALP-----------HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 460 LCRLLVMKPDLVIFDEPaTG-LDIQTEHMIQNvLFQHFKDT-TMIVIA-HRDNTIRHLQRR-LYIENGRLIADDRN 531
Cdd:COG2884 148 IARALVNRPELLLADEP-TGnLDPETSWEIME-LLEEINRRgTTVLIAtHDLELVDRMPKRvLELEDGRLVRDEAR 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
323-525 |
4.30e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.01 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGI 392
Cdd:COG4619 1 LELEGLSFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSampppewrrqVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENIT---MFKDIENN--TIEEVLDEVGL----LDK-VQSftkgintiigeggemLSGGQMRRIELCR 462
Cdd:COG4619 79 VPQEPALWGGTVRDNLPfpfQLRERKFDreRALELLERLGLppdiLDKpVER---------------LSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 463 LLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHF--KDTTMIVIAHRDNTIRHL-QRRLYIENGRL 525
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
323-529 |
7.31e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.26 E-value: 7.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------NIGIL 393
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVardpaevrrRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQPYIFSA-SIKENITMF-------KDIENNTIEEVLDEVGLLDKvqsftkgINTIIGEggemLSGGQMRRIELCRLLV 465
Cdd:COG1131 79 PQEPALYPDlTVRENLRFFarlyglpRKEARERIDELLELFGLTDA-------ADRKVGT----LSGGMKQRLGLALALL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 466 MKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKD-TTMIVIAHRDNTIRHLQRRL-YIENGRLIADD 529
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVaIIDKGRIVADG 213
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
322-526 |
1.05e-33 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 135.84 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 322 FIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IG 391
Cdd:TIGR03796 477 YVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREeiprevlansVA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQPYIFSASIKENITMFKD-IENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDL 470
Cdd:TIGR03796 557 MVDQDIFLFEGTVRDNLTLWDPtIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSI 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 471 VIFDEPATGLDIQTEHMIQNVLFQhfKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:TIGR03796 637 LILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVV 690
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
137-526 |
2.45e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 133.99 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 137 IAMFFIHFNTALIMLITAPFIPLFYIIFGLKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNrTEQTEKHIYDD-STQ 215
Cdd:PRK11176 158 IMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFG-GQEVETKRFDKvSNR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 216 FRTLTMRILRSAFLSGLMLEFISMLGIGLVALEATLSLVvfhnIDFKTA-AIAIILAPEF-----YNAIKDLGQAFHTGK 289
Cdd:PRK11176 237 MRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSV----MDTLTAgTITVVFSSMIalmrpLKSLTNVNAQFQRGM 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 290 qseGASDVVFEFLEQPNYNNEFllKYE-ENQKPFIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTH 368
Cdd:PRK11176 313 ---AACQTLFAILDLEQEKDEG--KRViERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIAN 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 369 LIAGVYQPTIGTISTNQRDL----------NIGILSQQPYIFSASIKENITMFKD--IENNTIEEVLDEVGLLDKVQSFT 436
Cdd:PRK11176 388 LLTRFYDIDEGEILLDGHDLrdytlaslrnQVALVSQNVHLFNDTIANNIAYARTeqYSREQIEEAARMAYAMDFINKMD 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 437 KGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQR 516
Cdd:PRK11176 468 NGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADE 547
|
410
....*....|
gi 446659814 517 RLYIENGRLI 526
Cdd:PRK11176 548 ILVVEDGEIV 557
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
340-476 |
7.36e-33 |
|
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: 122.76 E-value: 7.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGILSQQPYIFSA-SIKENI 408
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 409 -------TMFKDIENNTIEEVLDEVGLLDKvqsftkgINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEP 476
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
323-525 |
7.97e-33 |
|
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: 124.91 E-value: 7.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDR--LVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL------------ 388
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 --NIGILSQQPY-IFSASIKENITM-------FKDIENNTIEEVLDEVGLLDKvqsftkgINTIIGEggemLSGGQMRRI 458
Cdd:cd03255 81 rrHIGFVFQSFNlLPDLTALENVELplllagvPKKERRERAEELLERVGLGDR-------LNHYPSE----LSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 459 ELCRLLVMKPDLVIFDEPaTG-LDIQTEHMIQNVLFQ--HFKDTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:cd03255 150 AIARALANDPKIILADEP-TGnLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
324-529 |
1.33e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 124.18 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 324 QLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL-----NIGILSQQPY 398
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLekerkRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 399 I---FSASIKENITM-----------FKDIENNTIEEVLDEVGLLDKvqsftkgINTIIGEggemLSGGQMRRIELCRLL 464
Cdd:cd03235 79 IdrdFPISVRDVVLMglyghkglfrrLSKADKAKVDEALERVGLSEL-------ADRQIGE----LSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 465 VMKPDLVIFDEPATGLDIQTEHMIQNVLFQ-HFKDTTMIVIAHRDNTI-RHLQRRLYIeNGRLIADD 529
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVlEYFDRVLLL-NRTVVASG 213
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
22-296 |
5.80e-32 |
|
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: 124.70 E-value: 5.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 22 STGLGILVITQNILIADFLAKIIRHQFQGLWI-----VLFILLGVLLLRATVQFLNQWLGDTLAFKVKHMLRQRVIYK-- 94
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWedimpPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 95 ------NNGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIFGLKT 168
Cdd:cd18561 81 klgpgyLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 169 RDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFISMLGIGLVALE 248
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446659814 249 ATLSLVVfHNIDFKTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASD 296
Cdd:cd18561 241 GALRVLG-GQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAAD 287
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
319-528 |
5.86e-32 |
|
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: 123.17 E-value: 5.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 319 QKPFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------- 389
Cdd:COG1127 2 SEPMIEVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglsekelye 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 ----IGILSQQPYIFSA-SIKENI----TMFKDIENNTIEE----VLDEVGLLDKVQSFTkgintiiGEggemLSGGQMR 456
Cdd:COG1127 80 lrrrIGMLFQGGALFDSlTVFENVafplREHTDLSEAEIRElvleKLELVGLPGAADKMP-------SE----LSGGMRK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 457 RIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNvLFQHFKD---TTMIVIAHRDNTIRHLQRRLY-IENGRLIAD 528
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDE-LIRELRDelgLTSVVVTHDLDSAFAIADRVAvLADGKIIAE 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
309-525 |
7.86e-32 |
|
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: 129.00 E-value: 7.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 309 NEFLLKYEENQKPF--------IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGT 380
Cdd:TIGR01842 295 NELLANYPSRDPAMplpepeghLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 381 ISTNQRDLN----------IGILSQQPYIFSASIKENITMFKD-IENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEM 449
Cdd:TIGR01842 375 VRLDGADLKqwdretfgkhIGYLPQDVELFPGTVAENIARFGEnADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGAT 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 450 LSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHFK--DTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAI-KALKarGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
327-526 |
3.27e-31 |
|
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: 127.63 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 327 DISFRYDdSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGILSQQ 396
Cdd:COG5265 362 NVSFGYD-PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRdvtqaslraaIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 397 PYIFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDE 475
Cdd:COG5265 441 TVLFNDTIAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446659814 476 PATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
323-527 |
4.48e-31 |
|
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: 120.68 E-value: 4.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL-------------N 389
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglseaelyrlrrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 IGILSQQPYIFSA-SIKENI--------TMFKDIENNTIEEVLDEVGLLDKVQSFTkgintiiGEggemLSGGQMRRIEL 460
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafplrehtRLSEEEIREIVLEKLEAVGLRGAEDLYP-------AE----LSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 461 CRLLVMKPDLVIFDEPATGLDIQTEHMIQNvLFQHFKDT---TMIVIAHRDNTIRHLQRRLY-IENGRLIA 527
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDD-LIRSLKKElglTSIMVTHDLDTAFAIADRIAvLYDGKIVA 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
319-506 |
4.87e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.35 E-value: 4.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 319 QKPFIQLTDISFRY--DDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTN-----QRDLNIG 391
Cdd:COG1116 4 AAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQPYIFS-ASIKENIT-------MFKDIENNTIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIELCRL 463
Cdd:COG1116 84 VVFQEPALLPwLTVLDNVAlglelrgVPKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446659814 464 LVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDT--TMIVIAH 506
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTH 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
321-516 |
8.53e-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: 118.74 E-value: 8.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------NIG 391
Cdd:COG4133 1 MMLEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdaredyrrRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQPYIFSA-SIKENITMF-----KDIENNTIEEVLDEVGLldkvqsfTKGINTIIGeggeMLSGGQMRRIELCRLLV 465
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFWaalygLRADREAIDEALEAVGL-------AGLADLPVR----QLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446659814 466 MKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIA-HRDNTIRHLQR 516
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARV 199
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
323-506 |
1.25e-30 |
|
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: 118.73 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDR--LVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-----IGILSQ 395
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTgpgpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 396 QPYIFS-ASIKENIT-------MFKDIENNTIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIELCRLLVMK 467
Cdd:cd03293 81 QDALLPwLTVLDNVAlglelqgVPKAEARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARALAVD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446659814 468 PDLVIFDEPATGLDIQTEHMIQNVLFQHFKDT--TMIVIAH 506
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTH 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
323-529 |
6.97e-30 |
|
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: 117.65 E-value: 6.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------NIGIL 393
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQPYIFSA-SIKENITMF------KDIENN-TIEEVLDEVGLLDKvqsftkgINTIIGEggemLSGGQMRRIELCRLLV 465
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFaelyglFDEELKkRIEELIELLGLEEF-------LDRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 466 MKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIA-HRDNTIRHLQRRLYI-ENGRLIADD 529
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEALCDRVVIlHKGKVVAQG 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
133-528 |
8.15e-30 |
|
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: 124.08 E-value: 8.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 133 LIIIIAMFFIHFNTALIMLITAPfIPLFYIIFGLKTRDESK---DQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHI 209
Cdd:TIGR01193 282 ILVIVGLFLVRQNMLLFLLSLLS-IPVYAVIIILFKRTFNKlnhDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKI 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 210 YDDSTQFRTLTMRILRSAFLSGLmLEFISMLGIGLVALEATLSLVVFHNIDFKTAAIAIILAPEFYNAIKDLGQAFHTGK 289
Cdd:TIGR01193 361 DSEFGDYLNKSFKYQKADQGQQA-IKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 290 QSEGASDVVFE-FLEQPNYNNEFLLKYEENQKPFIQLTDISFRYDDSDRlVLNDLNLEIFKGDQIALVGPSGAGKSTLTH 368
Cdd:TIGR01193 440 AARVANNRLNEvYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAK 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 369 LIAGVYQPTIGTISTNQRDLN----------IGILSQQPYIFSASIKENITMFKDiENNTIEEVLDEVGLL---DKVQSF 435
Cdd:TIGR01193 519 LLVGFFQARSGEILLNGFSLKdidrhtlrqfINYLPQEPYIFSGSILENLLLGAK-ENVSQDEIWAACEIAeikDDIENM 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 436 TKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEH-MIQNVLFqhFKDTTMIVIAHRDNTIRHL 514
Cdd:TIGR01193 598 PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKkIVNNLLN--LQDKTIIFVAHRLSVAKQS 675
|
410
....*....|....
gi 446659814 515 QRRLYIENGRLIAD 528
Cdd:TIGR01193 676 DKIIVLDHGKIIEQ 689
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
324-524 |
1.97e-29 |
|
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: 113.49 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 324 QLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNqrdlnigilsqqpyifsas 403
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 404 ikenitmFKDIENNTIEEVLDEVGLLDkvQsftkgintiigeggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQ 483
Cdd:cd00267 60 -------GKDIAKLPLEELRRRIGYVP--Q----------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446659814 484 TEHMIQNVLFQHFKD-TTMIVIAHRDNTIRHLQRRLY-IENGR 524
Cdd:cd00267 115 SRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIvLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-528 |
1.30e-28 |
|
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: 114.13 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRL--VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NI 390
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrrrrkafrrRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPYifsAS----------IKE--NITMFKDIENnTIEEVLDEVGL----LDKVqsftkgintiigegGEMLSGGQ 454
Cdd:COG1124 82 QMVFQDPY---ASlhprhtvdriLAEplRIHGLPDREE-RIAELLEQVGLppsfLDRY--------------PHQLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 455 MRRIELCRLLVMKPDLVIFDEPATGLD--IQTEhmIQNVL--FQHFKDTTMIVIAHRDNTIRHL-QRRLYIENGRLIAD 528
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDvsVQAE--ILNLLkdLREERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEE 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
325-526 |
1.62e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.93 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 325 LTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTnQRDLNIGILSQQPYIFS-AS 403
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLRIGYLPQEPPLDDdLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 404 IKENITM-----------FKDIENNT----------------------------IEEVLDEVGLldKVQSFTKGINTiig 444
Cdd:COG0488 78 VLDTVLDgdaelraleaeLEELEAKLaepdedlerlaelqeefealggweaearAEEILSGLGF--PEEDLDRPVSE--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 445 eggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQT----EHMIQNvlFQHfkdtTMIVIAH-R---DNTIRHLqr 516
Cdd:COG0488 153 -----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKN--YPG----TVLVVSHdRyflDRVATRI-- 219
|
250
....*....|
gi 446659814 517 rLYIENGRLI 526
Cdd:COG0488 220 -LELDRGKLT 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
316-528 |
2.89e-27 |
|
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: 115.39 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 316 EENQKPFIQLTDISFRYD---DSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---- 388
Cdd:COG1123 254 AAAAEPLLEVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtkls 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 ---------NIGILSQQPYifsASIKENITMFKDIE--------------NNTIEEVLDEVGLLDKVqsftkgINTIIGE 445
Cdd:COG1123 334 rrslrelrrRVQMVFQDPY---SSLNPRMTVGDIIAeplrlhgllsraerRERVAELLERVGLPPDL------ADRYPHE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 446 ggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNvLFQHFKD---TTMIVIAHRDNTIRHLQRRLYI-E 521
Cdd:COG1123 405 ----LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILN-LLRDLQRelgLTYLFISHDLAVVRYIADRVAVmY 479
|
....*..
gi 446659814 522 NGRLIAD 528
Cdd:COG1123 480 DGRIVED 486
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
323-526 |
4.40e-27 |
|
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: 109.19 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVY-----QPTIGTISTNQRDLN-------- 389
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYdldvdvle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 ----IGILSQQPYIFSASIKENITM--------FKDIENNTIEEVLDEVGLLDKVQSFTKGINtiigeggemLSGGQMRR 457
Cdd:cd03260 79 lrrrVGMVFQKPNPFPGSIYDNVAYglrlhgikLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446659814 458 IELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHrdN---TIRHLQRRLYIENGRLI 526
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH--NmqqAARVADRTAFLLNGRLV 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
321-528 |
6.72e-27 |
|
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: 109.40 E-value: 6.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIG-TIS--------TNQRDL--N 389
Cdd:COG1119 2 PLLELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgerrggEDVWELrkR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 IGILS---QQPYIFSASIKE--------NITMFK---DIENNTIEEVLDEVGLLDKvqsftkgINTIIGEggemLSGGQM 455
Cdd:COG1119 80 IGLVSpalQLRFPRDETVLDvvlsgffdSIGLYReptDEQRERARELLELLGLAHL-------ADRPFGT----LSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 456 RRIELCRLLVMKPDLVIFDEPATGLDI-QTEHMIQ--NVLFQHfKDTTMIVIAHRDNTI-RHLQRRLYIENGRLIAD 528
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLgARELLLAllDKLAAE-GAPTLVLVTHHVEEIpPGITHVLLLKDGRVVAA 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
120-523 |
7.06e-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: 115.81 E-value: 7.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 120 SYLPQVFKSMMVPLIIII-AMFFIHFNTALIMLITAP------FIPLFYIIFG--LKtRDESKDQMTYLNQFSQRFLnia 190
Cdd:TIGR00957 1077 SMIPPVIKMFMGSLFNVIgALIVILLATPIAAVIIPPlgllyfFVQRFYVASSrqLK-RLESVSRSPVYSHFNETLL--- 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 191 kGLVTLKLFNRTEQTEkHIYD---DSTQfRTLTMRILRSAFLSgLMLEFIsmlGIGLVALEATLSLVVFHNIDFKTAAIA 267
Cdd:TIGR00957 1153 -GVSVIRAFEEQERFI-HQSDlkvDENQ-KAYYPSIVANRWLA-VRLECV---GNCIVLFAALFAVISRHSLSAGLVGLS 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 268 IILAPEFYNAIKDLGQAfhtgkQSEGASDVV-FEFL-EQPNYNNEFLLKYEENQKPF-------IQLTDISFRYDDSDRL 338
Cdd:TIGR00957 1226 VSYSLQVTFYLNWLVRM-----SSEMETNIVaVERLkEYSETEKEAPWQIQETAPPSgwpprgrVEFRNYCLRYREDLDL 1300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTH-------------LIAGVyqpTIGTISTNQRDLNIGILSQQPYIFSASIK 405
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLglfrinesaegeiIIDGL---NIAKIGLHDLRFKITIIPQDPVLFSGSLR 1377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 406 ENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTE 485
Cdd:TIGR00957 1378 MNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
410 420 430
....*....|....*....|....*....|....*...
gi 446659814 486 HMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENG 523
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKG 1495
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
328-526 |
1.88e-26 |
|
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: 107.21 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 328 ISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-------------IGILS 394
Cdd:cd03257 9 VSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrrlrkirrkeIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPY-----------IFSASIKENITMFKD-IENNTIEEVLDEVGLLDKVqsftkgINTIIGEggemLSGGQMRRIELCR 462
Cdd:cd03257 89 QDPMsslnprmtigeQIAEPLRIHGKLSKKeARKEAVLLLLVGVGLPEEV------LNRYPHE----LSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 463 LLVMKPDLVIFDEPATGLDIQTEHMIQNvLFQHFKD---TTMIVIAHRDNTIRHLQRRLYI-ENGRLI 526
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILD-LLKKLQEelgLTLLFITHDLGVVAKIADRVAVmYAGKIV 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
323-506 |
2.14e-26 |
|
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: 106.85 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN------------I 390
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkninelrqkV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPYIFS-ASIKENIT--------MFKDIENNTIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIELC 461
Cdd:cd03262 79 GMVFQQFNLFPhLTVLENITlapikvkgMSKAEAEERALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446659814 462 RLLVMKPDLVIFDEPATGLDIQtehMIQNVLfQHFKD-----TTMIVIAH 506
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPE---LVGEVL-DVMKDlaeegMTMVVVTH 193
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
321-494 |
2.25e-26 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 107.84 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDsDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------- 389
Cdd:COG3638 1 PMLELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalrgralrrlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 --IGILSQQPYIFS-ASIKENI---------------TMFKDIENNTIEEVLDEVGLLDKVQSFTkgintiigeggEMLS 451
Cdd:COG3638 80 rrIGMIFQQFNLVPrLSVLTNVlagrlgrtstwrsllGLFPPEDRERALEALERVGLADKAYQRA-----------DQLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446659814 452 GGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQ 494
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRR 191
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
323-530 |
3.89e-26 |
|
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: 105.96 E-value: 3.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGI 392
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStipledlrssLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFKDIENNTIEEVLDevglldkvqsftkgintiIGEGGEMLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 473 FDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIADDR 530
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
324-528 |
5.44e-26 |
|
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: 104.44 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 324 QLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGIL 393
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAslspkelarkIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQqpyifsasikenitmfkdienntieeVLDEVGLLDKVQsftKGINTiigeggemLSGGQMRRIELCRLLVMKPDLVIF 473
Cdd:cd03214 79 PQ--------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 474 DEPATGLDIQTEHMIQNVLFQHFKDTTMIVIA--HRDN-TIRHLQRRLYIENGRLIAD 528
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMvlHDLNlAARYADRVILLKDGRIVAQ 179
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
319-506 |
9.12e-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: 108.26 E-value: 9.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 319 QKPFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--------NI 390
Cdd:COG3842 2 AMPALELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekrNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQ----PYIfsaSIKENIT---MFKDIENNTI----EEVLDEVGLLDKVQSFtkgintiIGEggemLSGGQMRRIE 459
Cdd:COG3842 80 GMVFQDyalfPHL---TVAENVAfglRMRGVPKAEIrarvAELLELVGLEGLADRY-------PHQ----LSGGQQQRVA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446659814 460 LCRLLVMKPDLVIFDEPATGLDIQT-EHMiQNVLFQHFKD--TTMIVIAH 506
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLrEEM-REELRRLQRElgITFIYVTH 194
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
323-506 |
1.06e-25 |
|
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: 104.91 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--------NIGILS 394
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVtgvpperrNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIF-SASIKENI-------TMFKDIENNTIEEVLDEVGLLDKVQSFTkgintiigeggEMLSGGQMRRIELCRLLVM 466
Cdd:cd03259 79 QDYALFpHLTVAENIafglklrGVPKAEIRARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446659814 467 KPDLVIFDEPATGLDIQT-EHMIQNVL-FQHFKDTTMIVIAH 506
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTH 189
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
323-525 |
1.48e-25 |
|
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: 103.25 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------NIGIL 393
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkkepeevkrRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQPYIFsasikenitmfkdiENNTIEEVLDevglldkvqsftkgintiigeggemLSGGQMRRIELCRLLVMKPDLVIF 473
Cdd:cd03230 79 PEEPSLY--------------ENLTVRENLK-------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446659814 474 DEPATGLDIQTEHMIQNVLFQH-FKDTTMIVIAHRDNTIRHL-QRRLYIENGRL 525
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
323-524 |
1.50e-25 |
|
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: 103.42 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIGILSQQPyifsa 402
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 sIKENITM-FKDIENNTIEEVLDEVGLLdkvqsftkgintiigeggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLD 481
Cdd:cd03229 74 -LRRRIGMvFQDFALFPHLTVLENIALG--------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446659814 482 IQTEHMIQNVLFQHFKD--TTMIVIAHR-DNTIRHLQRRLYIENGR 524
Cdd:cd03229 133 PITRREVRALLKSLQAQlgITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
317-529 |
2.11e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 111.22 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 317 ENQKP--------FIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL 388
Cdd:PLN03232 1221 ENNRPvsgwpsrgSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 N----------IGILSQQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRI 458
Cdd:PLN03232 1301 AkfgltdlrrvLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLL 1380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 459 ELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIADD 529
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
323-540 |
2.13e-25 |
|
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: 105.38 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGI 392
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISklplhtlrsrLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:cd03288 100 ILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 473 FDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIADDRNISVNITENG 540
Cdd:cd03288 180 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDG 247
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
323-529 |
2.28e-25 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 105.61 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDS---DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN---------- 389
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkklkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 ---IGILSQQP--YIFSASIKENItMF---------KDIENnTIEEVLDEVGLLDKV--QS-FTkgintiigeggemLSG 452
Cdd:TIGR04521 81 rkkVGLVFQFPehQLFEETVYKDI-AFgpknlglseEEAEE-RVKEALELVGLDEEYleRSpFE-------------LSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 453 GQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHR-DNTIRHLQRRLYIENGRLIADD 529
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFkrLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIVLDG 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
321-530 |
3.73e-25 |
|
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: 103.67 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDSD-RL-VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------- 388
Cdd:COG4181 7 PIIELRGLTKTVGTGAgELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 ----NIGILSQQ-PYIFSASIKENITM------FKDIEnNTIEEVLDEVGLLDKVQSFTKGintiigeggemLSGGQMRR 457
Cdd:COG4181 87 lrarHVGFVFQSfQLLPTLTALENVMLplelagRRDAR-ARARALLERVGLGHRLDHYPAQ-----------LSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 458 IELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKD--TTMIVIAHRDNTIRHLQRRLYIENGRLIADDR 530
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
323-518 |
4.17e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.13 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDlNIGILSQQPYIFSA 402
Cdd:COG4178 363 LALEDLTLRTPD-GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-RVLFLPQRPYLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 SIKENIT---MFKDIENNTIEEVLDEVGL------LDKVQSFTKgintiigeggeMLSGGQMRRIELCRLLVMKPDLVIF 473
Cdd:COG4178 441 TLREALLypaTAEAFSDAELREALEAVGLghlaerLDEEADWDQ-----------VLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446659814 474 DEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRL 518
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
327-506 |
4.37e-25 |
|
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: 102.72 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 327 DISFRYDDSdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-------IGILSQQP-- 397
Cdd:cd03226 4 NISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKakerrksIGYVMQDVdy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 398 YIFSASIKENITMFKDI---ENNTIEEVLDEVGLLDKV----QSftkgintiigeggemLSGGQMRRIELCRLLVMKPDL 470
Cdd:cd03226 83 QLFTDSVREELLLGLKEldaGNEQAETVLKDLDLYALKerhpLS---------------LSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446659814 471 VIFDEPATGLDiqTEHMiQNV--LFQHFK--DTTMIVIAH 506
Cdd:cd03226 148 LIFDEPTSGLD--YKNM-ERVgeLIRELAaqGKAVIVITH 184
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
339-528 |
6.81e-25 |
|
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: 103.29 E-value: 6.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------NIGILS--QQPYIFSA-SIKE 406
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglppheiaRLGIGRtfQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 407 NITM--------------FKDIE---NNTIEEVLDEVGLLDKvqsftkgINTIIGEggemLSGGQMRRIELCRLLVMKPD 469
Cdd:cd03219 95 NVMVaaqartgsglllarARREEreaRERAEELLERVGLADL-------ADRPAGE----LSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 470 LVIFDEPATGLDIQ-TEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLY-IENGRLIAD 528
Cdd:cd03219 164 LLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSLADRVTvLDQGRVIAE 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
323-528 |
8.19e-25 |
|
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: 103.58 E-value: 8.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGI 392
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYI-FSASIKENITM--------F-----KDIEnnTIEEVLDEVGLLDKVQsftKGINTiigeggemLSGGQMRRI 458
Cdd:COG1120 80 VPQEPPApFGLTVRELVALgryphlglFgrpsaEDRE--AVEEALERTGLEHLAD---RPVDE--------LSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446659814 459 ELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHrD-N-TIRHLQRRLYIENGRLIAD 528
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLH-DlNlAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
323-525 |
1.22e-24 |
|
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: 101.72 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDdSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN------------- 389
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgraipylrrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 IGILSQQ-PYIFSASIKENItMF---------KDIeNNTIEEVLDEVGLLDKVQSFTKGintiigeggemLSGGQMRRIE 459
Cdd:cd03292 80 IGVVFQDfRLLPDRNVYENV-AFalevtgvppREI-RKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 460 LCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTI--RHLQRRLYIENGRL 525
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvdTTRHRVIALERGKL 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
323-529 |
1.63e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 108.67 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGI 392
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIskfglmdlrkVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:PLN03130 1318 IPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 473 FDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIADD 529
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFD 1454
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
320-528 |
2.01e-24 |
|
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: 106.53 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 320 KPFIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTI---GTISTNQRDL-------- 388
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLlelsealr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 --NIGILSQQPY--IFSASIKENITMFKDIENNTIEEVLDEV-GLLDKVqsftkGINTIIGEGGEMLSGGQMRRIELCRL 463
Cdd:COG1123 82 grRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVlELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 464 LVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHRDNTIRHL-QRRLYIENGRLIAD 528
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVED 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
320-526 |
2.50e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 320 KPFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRdLNIGILSQQpyi 399
Cdd:COG0488 313 KKVLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET-VKIGYFDQH--- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 fSASIKENITMFKDI----ENNTIEEVLDEVGLL----DKVQSFTKgintiigeggeMLSGGQMRRIELCRLLVMKPDLV 471
Cdd:COG0488 387 -QEELDPDKTVLDELrdgaPGGTEQEVRGYLGRFlfsgDDAFKPVG-----------VLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 472 IFDEPATGLDIQTEHMIQNVLfQHFkDTTMIVIAHrDntiRHL-----QRRLYIENGRLI 526
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEAL-DDF-PGTVLLVSH-D---RYFldrvaTRILEFEDGGVR 508
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
323-492 |
4.70e-24 |
|
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: 100.27 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------NIGIL 393
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtdrkaarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQPYIFSA-SIKENITMF-------KDIENNTIEEVLDEVGLLDKvqsftkgINTIIGEggemLSGGQMRRIELCRLLV 465
Cdd:cd03263 81 PQFDALFDElTVREHLRFYarlkglpKSEIKEEVELLLRVLGLTDK-------ANKRART----LSGGMKRKLSLAIALI 149
|
170 180
....*....|....*....|....*..
gi 446659814 466 MKPDLVIFDEPATGLDIQTEHMIQNVL 492
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLI 176
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
339-527 |
4.96e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 100.87 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--------NIGILSQQPYIFSasikeNITM 410
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItnlppekrDISYVPQNYALFP-----HMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 411 FKDIENNTIEEVLDEVGLLDKVQSFTK--GINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMI 488
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446659814 489 QNVL--FQHFKDTTMIVIAHRDNTIRHLQRRLYI-ENGRLIA 527
Cdd:cd03299 169 REELkkIRKEFGVTVLHVTHDFEEAWALADKVAImLNGKLIQ 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
323-506 |
5.03e-24 |
|
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: 99.96 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGdQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN---------IGIL 393
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkqpqklrrrIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQPYIFSasikeNITMF---------KDIENNT----IEEVLDEVGLLDKVqsfTKGINTiigeggemLSGGQMRRIEL 460
Cdd:cd03264 78 PQEFGVYP-----NFTVRefldyiawlKGIPSKEvkarVDEVLELVNLGDRA---KKKIGS--------LSGGMRRRVGI 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446659814 461 CRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAH 506
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
323-542 |
5.57e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 107.04 E-value: 5.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDD-SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI----STNQRDLN-------I 390
Cdd:PTZ00265 383 IQFKNVRFHYDTrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindSHNLKDINlkwwrskI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPYIFSASIKENITM----FKDIEN-------------------------------------------------N 417
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKYslysLKDLEAlsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 418 TIE--EVLD---EVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL 492
Cdd:PTZ00265 543 TIKdsEVVDvskKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 493 --FQHFKDTTMIVIAHRDNTIRHLQRRLYI---ENGRLIADDRNISVNITENGDD 542
Cdd:PTZ00265 623 nnLKGNENRITIIIAHRLSTIRYANTIFVLsnrERGSTVDVDIIGEDPTKDNKEN 677
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
329-507 |
5.93e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 105.56 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 329 SFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGILSQQPY 398
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqldswrsRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 399 IFSASIKENITMFK-DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPA 477
Cdd:PRK10789 400 LFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190
....*....|....*....|....*....|
gi 446659814 478 TGLDIQTEHMIQNVLFQHFKDTTMIVIAHR 507
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHR 509
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
323-526 |
1.84e-23 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 99.19 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLV--LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL------------ 388
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgkelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 -NIGILSQQPYIFSA-SIKENIT-------MFKDIENNTIEEVLDEVGLLDKVQSFTkgintiigeggEMLSGGQMRRIE 459
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVAlpleiagVPKAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 460 LCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDT--TMIVIAHRDNTIRHL-QRRLYIENGRLI 526
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRIcDRVAVMEKGEVV 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
318-527 |
2.21e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 99.68 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI--------STNQRDL- 388
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitisKENLKEIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 -NIGILSQQP---YIfSASIKENITMfkDIENN---------TIEEVLDEVG---LLDKVQSFtkgintiigeggemLSG 452
Cdd:PRK13632 83 kKIGIIFQNPdnqFI-GATVEDDIAF--GLENKkvppkkmkdIIDDLAKKVGmedYLDKEPQN--------------LSG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 453 GQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIA 527
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIA 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
323-506 |
6.52e-23 |
|
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: 94.82 E-value: 6.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRdLNIGILSQqpyifsa 402
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-VKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 sikenitmfkdienntieevldevglldkvqsftkgintiigeggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDI 482
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180
....*....|....*....|....
gi 446659814 483 QTEHMIQNVLfQHFKDtTMIVIAH 506
Cdd:cd03221 104 ESIEALEEAL-KEYPG-TVILVSH 125
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
323-528 |
1.44e-22 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 96.48 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN------------- 389
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgkalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 IGILSQQPYIFS-ASIKENI---------------TMFKDIENNTIEEVLDEVGLLDKvqsftkgINTIIGEggemLSGG 453
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVlsgrlgrrstwrslfGLFPKEEKQRALAALERVGLLDK-------AYQRADQ----LSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 454 QMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLF---QHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIAD 528
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKrinREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
339-528 |
2.02e-22 |
|
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: 96.65 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------------------------- 389
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglpphriarlgiartfqnprlfpeltvle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 ---IGILSQQPYIFSASIKENITMFKDIENNT--IEEVLDEVGLLDKvqsftkgINTIIGEggemLSGGQMRRIELCRLL 464
Cdd:COG0411 99 nvlVAAHARLGRGLLAALLRLPRARREEREARerAEELLERVGLADR-------ADEPAGN----LSYGQQRRLEIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 465 VMKPDLVIFDEPATGLDIQ-TEHMIQnvLFQHFKD---TTMIVIAHRDNTIRHLQRRLY-IENGRLIAD 528
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEeTEELAE--LIRRLRDergITILLIEHDMDLVMGLADRIVvLDFGRVIAE 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
323-528 |
3.76e-22 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 94.87 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRlvlnDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIGILSQQPyiFSA 402
Cdd:cd03298 1 VRLDKIRFSYGEQPM----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 SIKENiTMFK--DIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEM------LSGGQMRRIELCRLLVMKPDLVIFD 474
Cdd:cd03298 75 LFQEN-NLFAhlTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEkrlpgeLSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 475 EPATGLDIQTEHMIQNVLFQHFKDT--TMIVIAHRDNTIRHLQRRL-YIENGRLIAD 528
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRVvFLDNGRIAAQ 210
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
16-296 |
5.42e-22 |
|
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: 96.07 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 16 VLMFLVSTGLGILVItqnILIADFLAKIIRHQF--QGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKVKHMLRQRVIY 93
Cdd:cd18781 2 VLLQWISLLANIAFV---FSIANLLQKLLEGKLttASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 94 K--------NNGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIFG 165
Cdd:cd18781 79 KllrlgpsyQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 166 LKTRdesKDQMTYLNQFSQ---RFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFI----S 238
Cdd:cd18781 159 KIAK---KLLSKYWGSYTDlgdSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVayggA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 239 MLGIGLvaleaTLSLVVFHNIDFKTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASD 296
Cdd:cd18781 236 ALGIIL-----ALLQFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASD 288
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
340-529 |
5.66e-22 |
|
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: 94.28 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEI---FKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------------IGILSQQPYIFS- 401
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsrkkinlppqqrkIGLVFQQYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 402 ASIKENITM-FKDIENNTIEEVLDEVglldkVQSFtkGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGL 480
Cdd:cd03297 90 LNVRENLAFgLKRKRNREDRISVDEL-----LDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446659814 481 DIQTEHMIQNVL---FQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIADD 529
Cdd:cd03297 163 DRALRLQLLPELkqiKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
331-512 |
6.78e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 6.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 331 RYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIsTNQRDLNIGILSQQ---PYIFSASIKEN 407
Cdd:NF040873 1 GYGG--RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-RRAGGARVAYVPQRsevPDSLPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 408 ITM--FKDI---------ENNTIEEVLDEVGL--LDKVQsftkgintiIGEggemLSGGQMRRIELCRLLVMKPDLVIFD 474
Cdd:NF040873 78 VAMgrWARRglwrrltrdDRAAVDDALERVGLadLAGRQ---------LGE----LSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 446659814 475 EPATGLDIQT-EHMIQNVLFQHFKDTTMIVIAHRDNTIR 512
Cdd:NF040873 145 EPTTGLDAESrERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
336-540 |
7.24e-22 |
|
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: 93.36 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGV--YQPTIGTI----------STNQR-DLNIGILSQQPYifsa 402
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEIlfkgeditdlPPEERaRLGIFLAFQYPP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 sikenitmfkdiennTIEEVldevglldKVQSFTKGINtiigEGgemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDI 482
Cdd:cd03217 88 ---------------EIPGV--------KNADFLRYVN----EG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446659814 483 QTEHMIQNVLFQ-HFKDTTMIVIAHRDNTIRHLQ--RRLYIENGRLIAD-DRNISVNITENG 540
Cdd:cd03217 138 DALRLVAEVINKlREEGKSVLIITHYQRLLDYIKpdRVHVLYDGRIVKSgDKELALEIEKKG 199
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
337-498 |
1.31e-21 |
|
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: 93.76 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 337 RLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRD-----------LNIGILSQQPYIF-SASI 404
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarLGIGYLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 405 KENITMF-------KDIENNTIEEVLDEVglldkvqsftkGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPA 477
Cdd:cd03218 93 EENILAVleirglsKKEREEKLEELLEEF-----------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180
....*....|....*....|.
gi 446659814 478 TGLDIQTEHMIQNVLfQHFKD 498
Cdd:cd03218 162 AGVDPIAVQDIQKII-KILKD 181
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
323-531 |
1.33e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 94.00 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGT-----ISTNQRDLNI------- 390
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVDErlirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPYIF-SASIKENItMF---------KDIENNTIEEVLDEVGLLDKVQSFTkgintiigegGEmLSGGQMRRIEL 460
Cdd:PRK09493 80 GMVFQQFYLFpHLTALENV-MFgplrvrgasKEEAEKQARELLAKVGLAERAHHYP----------SE-LSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446659814 461 CRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHFKD--TTMIVIAHRDNTIRHLQRRL-YIENGRlIADDRN 531
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVM-QDLAEegMTMVIVTHEIGFAEKVASRLiFIDKGR-IAEDGD 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-508 |
1.46e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.76 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIG-------TISTNQRDL-----NI 390
Cdd:PRK13639 2 LETRDLKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGevlikgePIKYDKKSLlevrkTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQP--YIFSASIKE-------NITMFKDIENNTIEEVLDEVGLldkvqsftkgintiigEGGE-----MLSGGQMR 456
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEdvafgplNLGLSKEEVEKRVKEALKAVGM----------------EGFEnkpphHLSGGQKK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446659814 457 RIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRD 508
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
337-508 |
1.51e-21 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 92.56 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 337 RLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------NIGILSQQPYIFSA-SIKE 406
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfqrdsiarGLLYLGHAPGIKTTlSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 407 NITMFKDI-ENNTIEEVLDEVGLldkvqsftKGINTIIGEggeMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTE 485
Cdd:cd03231 93 NLRFWHADhSDEQVEEALARVGL--------NGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....
gi 446659814 486 HMIQNVLFQHFKDTTMIVIA-HRD 508
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTtHQD 185
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
323-530 |
1.73e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 93.28 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdrLVLNdLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------IGILS 394
Cdd:COG3840 2 LRLDDLTYRYGD---FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTalppaerpVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIFSA-SIKENITM-------FKDIENNTIEEVLDEVGLLDKVQSFTkgintiigeggEMLSGGQMRRIELCRLLVM 466
Cdd:COG3840 78 QENNLFPHlTVAQNIGLglrpglkLTAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 467 KPDLVIFDEPATGLDI-QTEHMIQNVLFQHfKDT--TMIVIAHRDNTIRHL-QRRLYIENGRLIADDR 530
Cdd:COG3840 147 KRPILLLDEPFSALDPaLRQEMLDLVDELC-RERglTVLMVTHDPEDAARIaDRVLLVADGRIAADGP 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
323-529 |
2.59e-21 |
|
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: 92.43 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSdrLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------NIGIL 393
Cdd:cd03265 1 IEVENLVKKYGDF--EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvreprevrrRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQPYIFSA-SIKENITMFKDIEN-------NTIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIELCRLLV 465
Cdd:cd03265 79 FQDLSVDDElTGWENLYIHARLYGvpgaerrERIDELLDFVGLLEAADRLVK-----------TYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 466 MKPDLVIFDEPATGLDIQT-EHM---IQNVLFQHfkDTTMIVIAHRDNTIRHLQRRL-YIENGRLIADD 529
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTrAHVweyIEKLKEEF--GMTILLTTHYMEEAEQLCDRVaIIDHGRIIAEG 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
323-502 |
2.98e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.14 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------IGILS 394
Cdd:COG3839 4 LELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdlppkdrnIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIF-SASIKENIT-------MFKDIENNTIEEVLDEVGLLDKVQSFTKGintiigeggemLSGGQMRRIELCRLLVM 466
Cdd:COG3839 82 QSYALYpHMTVYENIAfplklrkVPKAEIDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRVALGRALVR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446659814 467 KPDLVIFDEPATGLD----IQTEHMIQNvLFQHFKdTTMI 502
Cdd:COG3839 151 EPKVFLLDEPLSNLDaklrVEMRAEIKR-LHRRLG-TTTI 188
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
339-516 |
4.05e-21 |
|
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: 93.38 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRdlnIGILSQQPYIFSASIKENITMFKDIENNT 418
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR---ISFSSQFSWIMPGTIKENIIFGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 419 IEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMI-QNVLFQHFK 497
Cdd:cd03291 129 YKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMA 208
|
170
....*....|....*....
gi 446659814 498 DTTMIVIAhrdNTIRHLQR 516
Cdd:cd03291 209 NKTRILVT---SKMEHLKK 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
323-525 |
5.77e-21 |
|
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: 93.00 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHL------------IAGVyqpTIGTISTNQRDLNI 390
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAflrllntegdiqIDGV---SWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDL 470
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 471 VIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
323-506 |
6.00e-21 |
|
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: 91.16 E-value: 6.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------IGILS 394
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdlppkdrdIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QqpyifSASIKENITMFKDIE-----NNTIEEVLDEvglldKVQSFTK--GINTIIGEGGEMLSGGQMRRIELCRLLVMK 467
Cdd:cd03301 79 Q-----NYALYPHMTVYDNIAfglklRKVPKDEIDE-----RVREVAEllQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446659814 468 PDLVIFDEPATGLD--IQTEHMIQNVLFQHFKDTTMIVIAH 506
Cdd:cd03301 149 PKVFLMDEPLSNLDakLRVQMRAELKRLQQRLGTTTIYVTH 189
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
340-529 |
6.20e-21 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 93.22 E-value: 6.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------NIGILSQQPYIFSA-SIKENIT 409
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvreprkvrrSIGIVPQYASVDEDlTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 410 MF-------KDIENNTIEEVLDEVGLLDKVQSFTKGintiigeggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDI 482
Cdd:TIGR01188 89 MMgrlyglpKDEAEERAEELLELFELGEAADRPVGT-----------YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446659814 483 QTEHMIQNvLFQHFK--DTTMIVIAHRDNTIRHLQRRL-YIENGRLIADD 529
Cdd:TIGR01188 158 RTRRAIWD-YIRALKeeGVTILLTTHYMEEADKLCDRIaIIDHGRIIAEG 206
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
336-542 |
6.40e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.05 E-value: 6.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAG--VYQPTIGTISTNQRDL---------NIGI-LS-QQP----- 397
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDIlelspderaRAGIfLAfQYPveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 398 --------YIFSASIKENITMFKDIEnnTIEEVLDEVGLlDKvqSFTK-GINtiigEGgemLSGGQMRRIELCRLLVMKP 468
Cdd:COG0396 92 vsvsnflrTALNARRGEELSAREFLK--LLKEKMKELGL-DE--DFLDrYVN----EG---FSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 469 DLVIFDEPATGLDIQT-EHMIQNVLFQHFKDTTMIVIAHrdntirhlQRRL--YIE--------NGRLIA-DDRNISVNI 536
Cdd:COG0396 160 KLAILDETDSGLDIDAlRIVAEGVNKLRSPDRGILIITH--------YQRIldYIKpdfvhvlvDGRIVKsGGKELALEL 231
|
....*.
gi 446659814 537 TENGDD 542
Cdd:COG0396 232 EEEGYD 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
320-526 |
7.51e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.15 E-value: 7.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 320 KPFIQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLI--AGVYQPTI---GTISTNQRDL------ 388
Cdd:PRK14239 3 EPILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVtitGSIVYNGHNIysprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 ------NIGILSQQPYIFSASIKENITMFKDIENNTIEEVLDEVglldkVQSFTKG------INTIIGEGGEMLSGGQMR 456
Cdd:PRK14239 81 tvdlrkEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEA-----VEKSLKGasiwdeVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 457 RIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHR-DNTIRHLQRRLYIENGRLI 526
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSmQQASRISDRTGFFLDGDLI 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
323-526 |
4.45e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGT--ISTNQRDL------------ 388
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlnIAGNHFDFsktpsdkairel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 --NIGILSQQ----PYIfsaSIKENIT--------MFKDIENNTIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQ 454
Cdd:PRK11124 81 rrNVGMVFQQynlwPHL---TVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 455 MRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHFKDT--TMIVIAHRDNTIRHLQRR-LYIENGRLI 526
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSII-RELAETgiTQVIVTHEVEVARKTASRvVYMENGHIV 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-530 |
5.93e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIST------NQRDL---NIGIL 393
Cdd:PRK13536 42 IDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpARARLaraRIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQPYI-FSASIKENITMFK---DIENNTIEEVLDEvgLLDKVQSFTKGiNTIIGEggemLSGGQMRRIELCRLLVMKPD 469
Cdd:PRK13536 120 PQFDNLdLEFTVRENLLVFGryfGMSTREIEAVIPS--LLEFARLESKA-DARVSD----LSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446659814 470 LVIFDEPATGLDIQTEHMIQNVLFQHF-KDTTMIVIAHRDNTIRHLQRRL-YIENGRLIADDR 530
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLCDRLcVLEAGRKIAEGR 255
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
323-506 |
6.79e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 88.90 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI-------STNQRDLN-----I 390
Cdd:COG1126 2 IEIENLHKSFGD--LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTItvdgedlTDSKKDINklrrkV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPYIFS-ASIKENIT--------MFKDIENNTIEEVLDEVGLLDKVQSFTkgintiigeggEMLSGGQMRRIELC 461
Cdd:COG1126 80 GMVFQQFNLFPhLTVLENVTlapikvkkMSKAEAEERAMELLERVGLADKADAYP-----------AQLSGGQQQRVAIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446659814 462 RLLVMKPDLVIFDEPATGLDIQtehMIQNVLfqhfkDT---------TMIVIAH 506
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPE---LVGEVL-----DVmrdlakegmTMVVVTH 194
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
325-525 |
1.14e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.58 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 325 LTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLnigilsqqpyifsASI 404
Cdd:PRK11247 15 LNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-------------AEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 405 KENI-TMFKD---------IEN----------NTIEEVLDEVGLLDKVqsftkgintiiGEGGEMLSGGQMRRIELCRLL 464
Cdd:PRK11247 80 REDTrLMFQDarllpwkkvIDNvglglkgqwrDAALQALAAVGLADRA-----------NEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 465 VMKPDLVIFDEPATGLD----IQTEHMIQNVLFQH-FkdTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHgF--TVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
339-516 |
1.23e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 93.44 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRdlnIGILSQQPYIFSASIKENITMFKDIENNT 418
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR---ISFSPQTSWIMPGTIKDNIIFGLSYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 419 IEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMI-QNVLFQHFK 497
Cdd:TIGR01271 518 YTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMS 597
|
170
....*....|....*....
gi 446659814 498 DTTMIVIAHRdntIRHLQR 516
Cdd:TIGR01271 598 NKTRILVTSK---LEHLKK 613
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
318-527 |
1.26e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.92 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-------- 389
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeetvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 --IGILSQQP-YIFSASIKENITMFKdIENNTI---------EEVLDEVGLldkvQSFTKgintiigEGGEMLSGGQMRR 457
Cdd:PRK13635 81 rqVGMVFQNPdNQFVGATVQDDVAFG-LENIGVpreemvervDQALRQVGM----EDFLN-------REPHRLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446659814 458 IELCRLLVMKPDLVIFDEPATGLD-IQTEHMIQNVlfQHFKD---TTMIVIAHRDNTIRHLQRRLYIENGRLIA 527
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDpRGRREVLETV--RQLKEqkgITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
336-511 |
1.34e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIGIL-SQQPYIF-------SASIKEN 407
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaEACHYLGhrnamkpALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 408 ITMFKDIENNT---IEEVLDEVGLLDkvqsftkgintIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQT 484
Cdd:PRK13539 94 LEFWAAFLGGEeldIAAALEAVGLAP-----------LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....*...
gi 446659814 485 EHMIQNVLFQHFKDTTMIVIA-HRDNTI 511
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAAtHIPLGL 190
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
323-526 |
1.40e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGT--ISTNQRDL------------ 388
Cdd:COG4161 3 IQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlnIAGHQFDFsqkpsekairll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 --NIGILSQQ----PYIfsaSIKENIT--------MFKDIENNTIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQ 454
Cdd:COG4161 81 rqKVGMVFQQynlwPHL---TVMENLIeapckvlgLSKEQAREKAMKLLARLRLTDKADRFPL-----------HLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 455 MRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHFKDT--TMIVIAHRDNTIRHLQRR-LYIENGRLI 526
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEII-RELSQTgiTQVIVTHEVEFARKVASQvVYMEKGRII 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-543 |
1.57e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIS---------TNQRDLNIG 391
Cdd:PRK13537 6 APIDFRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsrARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQ----QPyifSASIKENITMFK---DIENNTIEEVLDevGLLDkvqsFTKGINTIIGEGGEmLSGGQMRRIELCRLL 464
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLVFGryfGLSAAAARALVP--PLLE----FAKLENKADAKVGE-LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 465 VMKPDLVIFDEPATGLDIQTEHMIQNVLFQHF-KDTTMIVIAHRDNTIRHLQRRL-YIENGRLIAD-------DRNISVN 535
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERLCDRLcVIEEGRKIAEgaphaliESEIGCD 233
|
....*....
gi 446659814 536 ITE-NGDDL 543
Cdd:PRK13537 234 VIEiYGPDP 242
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
330-529 |
1.71e-19 |
|
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: 87.77 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 330 FRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTN------QRD---LNIGIL--SQQPY 398
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglvpwkRRKkflRRIGVVfgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 399 IFSASIKENITMFKDIEN-------NTIEEVLDevgLLDkvqsftkgINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLV 471
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDlpparfkKRLDELSE---LLD--------LEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 472 IFDEPATGLDIQTEHMIQNVLFQHFKD--TTMIVIAHRDNTIRHLQRR-LYIENGRLIADD 529
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALARRvLVIDKGRLLYDG 236
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
319-481 |
1.86e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.78 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 319 QKPFIQLTDISFRYDDSdrLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI----------STNQRDl 388
Cdd:PRK11432 3 QKNFVVLKNITKRFGSN--TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthrSIQQRD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 nIGILSQQPYIFS-ASIKENI----TMF---KDIENNTIEEVLDEVGLLDKVQSFTKGIntiigeggemlSGGQMRRIEL 460
Cdd:PRK11432 80 -ICMVFQSYALFPhMSLGENVgyglKMLgvpKEERKQRVKEALELVDLAGFEDRYVDQI-----------SGGQQQRVAL 147
|
170 180
....*....|....*....|.
gi 446659814 461 CRLLVMKPDLVIFDEPATGLD 481
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLD 168
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
327-521 |
1.89e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 92.67 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 327 DISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLT----HLIAGVYQPTIGTISTNQRDLN-----IGILSQQP 397
Cdd:TIGR01271 1222 GLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTEGEIQIDGVSWNSVTLQtwrkaFGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 398 YIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPA 477
Cdd:TIGR01271 1302 FIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446659814 478 TGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIE 521
Cdd:TIGR01271 1382 AHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIE 1425
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
339-508 |
3.33e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 85.55 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN------------IGILSQQP--YIFSASI 404
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrkgllerrqrVGLVFQDPddQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 405 KENIT---MFKDIENNTIEEVLDEVglLDKVqsftkGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLD 481
Cdd:TIGR01166 87 DQDVAfgpLNLGLSEAEVERRVREA--LTAV-----GASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*..
gi 446659814 482 IQTEHMIQNVLFQHFKDTTMIVIAHRD 508
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
132-506 |
3.80e-19 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 91.55 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 132 PLIIIIAMFFIHFNTALIMLITAPF----IPLFYIIfGLKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFnrteQTEK 207
Cdd:TIGR00957 442 PLQVILALYFLWLNLGPSVLAGVAVmvlmVPLNAVM-AMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLY----AWEL 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 208 HIYDDSTQFRTLTMRILR-SAFLSGLMlEFISMLGIGLVALeATLSLVVF---HNI-DFKTAAIAIILAPEFYNAIKDLG 282
Cdd:TIGR00957 517 AFLDKVEGIRQEELKVLKkSAYLHAVG-TFTWVCTPFLVAL-ITFAVYVTvdeNNIlDAEKAFVSLALFNILRFPLNILP 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 283 QAFHTGKQSEGASDVVFEFLEQPNYNNEFLLK--YEENQKPFIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSG 360
Cdd:TIGR00957 595 MVISSIVQASVSLKRLRIFLSHEELEPDSIERrtIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVG 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 361 AGKSTLTHLIAGVYQPTIGTISTNQrdlNIGILSQQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGIN 440
Cdd:TIGR00957 675 CGKSSLLSALLAEMDKVEGHVHMKG---SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDR 751
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 441 TIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQT-EHMIQNVLFQH--FKDTTMIVIAH 506
Cdd:TIGR00957 752 TEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIFEHVIGPEgvLKNKTRILVTH 820
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
323-481 |
9.19e-19 |
|
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: 84.96 E-value: 9.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------IGILS 394
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkniealrrIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIFSA-SIKENITMF---KDIENNTIEEVLDEVGLLD----KVQSFTKGintiigeggemlsggqMR-RIELCRLLV 465
Cdd:cd03268 79 EAPGFYPNlTARENLRLLarlLGIRKKRIDEVLDVVGLKDsakkKVKGFSLG----------------MKqRLGIALALL 142
|
170
....*....|....*.
gi 446659814 466 MKPDLVIFDEPATGLD 481
Cdd:cd03268 143 GNPDLLILDEPTNGLD 158
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
323-487 |
1.22e-18 |
|
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: 84.98 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSdrLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--------NIGILS 394
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItnlpphkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIFS-ASIKENIT-------MFKDIENNTIEEVLDEVGLLDKVQSFTkgintiigeggEMLSGGQMRRIELCRLLVM 466
Cdd:cd03300 79 QNYALFPhLTVFENIAfglrlkkLPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVN 147
|
170 180
....*....|....*....|..
gi 446659814 467 KPDLVIFDEPATGLDIQ-TEHM 487
Cdd:cd03300 148 EPKVLLLDEPLGALDLKlRKDM 169
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
316-506 |
2.03e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.19 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 316 EENQKPFIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI--------STNQRD 387
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 388 L--NIGILSQQP-YIFSASIKENITMFkDIENNT---------IEEVLDEVGLLDKVQSFTKGintiigeggemLSGGQM 455
Cdd:PRK13648 81 LrkHIGIVFQNPdNQFVGSIVKYDVAF-GLENHAvpydemhrrVSEALKQVDMLERADYEPNA-----------LSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446659814 456 RRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAH 506
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVrkVKSEHNITIISITH 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
323-483 |
2.24e-18 |
|
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: 84.31 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSdrLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI--------STNQRDLNIGILS 394
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIFS-ASIKENIT----MFKDIENNTIEEVLDEV-GLLDKVQsftkgINTIIGEGGEMLSGGQMRRIELCRLLVMKP 468
Cdd:cd03296 81 QHYALFRhMTVFDNVAfglrVKPRSERPPEAEIRAKVhELLKLVQ-----LDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170
....*....|....*
gi 446659814 469 DLVIFDEPATGLDIQ 483
Cdd:cd03296 156 KVLLLDEPFGALDAK 170
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
323-506 |
2.30e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.46 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDS---DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIS---------TNQRDL-- 388
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervitagKKNKKLkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 ---NIGILSQQP--YIFSASIKENIT-------MFKDIENNTIEEVLDEVGLLDKVQS---FTkgintiigeggemLSGG 453
Cdd:PRK13634 83 lrkKVGIVFQFPehQLFEETVEKDICfgpmnfgVSEEDAKQKAREMIELVGLPEELLArspFE-------------LSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 454 QMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQ--HFKDTTMIVIAH 506
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTH 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-528 |
2.40e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 82.48 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSdrLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIgilsqqpyifsA 402
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF-----------A 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 SIKEnitmfkdienntieevldevglldkvqSFTKGINTIigeggEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDI 482
Cdd:cd03216 68 SPRD---------------------------ARRAGIAMV-----YQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446659814 483 Q-TEHmiqnvLFQHFKD-----TTMIVIAHRDNTIRHLQRRLYI-ENGRLIAD 528
Cdd:cd03216 116 AeVER-----LFKVIRRlraqgVAVIFISHRLDEVFEIADRVTVlRDGRVVGT 163
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
313-529 |
2.53e-18 |
|
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: 84.12 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 313 LKYEENQKPFIQLTD---ISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQR--- 386
Cdd:cd03220 8 KSYPTYKGGSSSLKKlgiLGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvss 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 387 --DLNIGIlsqQPyifSASIKENITM---FKDIENNTIEEVLDEvglldkVQSFTKgintiIGEGGEM----LSGGQMRR 457
Cdd:cd03220 88 llGLGGGF---NP---ELTGRENIYLngrLLGLSRKEIDEKIDE------IIEFSE-----LGDFIDLpvktYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 458 IELCRLLVMKPDLVIFDEP-ATGlDIQTEHMIQNVLFQHFKDTTMIVIA-HRDNTIRHL-QRRLYIENGRLIADD 529
Cdd:cd03220 151 LAFAIATALEPDILLIDEVlAVG-DAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
323-527 |
2.72e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.17 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGI 392
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaenekwvrskVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQP--YIFSASIKE-------NITMFKDIENNTIEEVLDEVGLLDkvqsftkgintIIGEGGEMLSGGQMRRIELCRL 463
Cdd:PRK13647 84 VFQDPddQVFSSTVWDdvafgpvNMGLDKDEVERRVEEALKAVRMWD-----------FRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 464 LVMKPDLVIFDEPATGLDIQTEHMIQNVLFQ-HFKDTTMIVIAHR-DNTIRHLQRRLYIENGRLIA 527
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDvDLAAEWADQVIVLKEGRVLA 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
318-526 |
3.10e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 84.32 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTL-------THLIAGVYqpTIGTISTNQRDLN- 389
Cdd:COG1117 7 TLEPKIEVRNLNVYYGD--KQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrmNDLIPGAR--VEGEILLDGEDIYd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 -----------IGILSQQPYIFSASIKENITM--------FKDIENNTIEEVLDEVGLLDKV-----QSFTKgintiige 445
Cdd:COG1117 83 pdvdvvelrrrVGMVFQKPNPFPKSIYDNVAYglrlhgikSKSELDEIVEESLRKAALWDEVkdrlkKSALG-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 446 ggemLSGGQMRRieLC--RLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRdntirhLQ--RRL--- 518
Cdd:COG1117 155 ----LSGGQQQR--LCiaRALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHN------MQqaARVsdy 222
|
250
....*....|
gi 446659814 519 --YIENGRLI 526
Cdd:COG1117 223 taFFYLGELV 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
323-513 |
3.31e-18 |
|
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: 83.53 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDdSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN------------- 389
Cdd:cd03290 1 VQVTNGYFSWG-SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESepsfeatrsrnry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 -IGILSQQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKP 468
Cdd:cd03290 80 sVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446659814 469 DLVIFDEPATGLDIQ-TEHMIQNVLFQHFKDT--TMIVIAHRDNTIRH 513
Cdd:cd03290 160 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDDkrTLVLVTHKLQYLPH 207
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
323-483 |
4.38e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.58 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL---------NIGIL 393
Cdd:COG1118 3 IEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlpprerRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQPyifsA-----SIKENI-------TMFKDIENNTIEEVLDEVGL--LDKV---QsftkgintiigeggemLSGGQMR 456
Cdd:COG1118 81 FQHY----AlfphmTVAENIafglrvrPPSKAEIRARVEELLELVQLegLADRypsQ----------------LSGGQRQ 140
|
170 180
....*....|....*....|....*..
gi 446659814 457 RIELCRLLVMKPDLVIFDEPATGLDIQ 483
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAK 167
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
323-528 |
4.51e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.48 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDdsdRLVLNdLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------IGILS 394
Cdd:PRK10771 2 LKLTDITWLYH---HLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTttppsrrpVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIFS-ASIKENITM-------FKDIENNTIEEVLDEVGLLDKVQSFTkgintiiGEggemLSGGQMRRIELCRLLVM 466
Cdd:PRK10771 78 QENNLFShLTVAQNIGLglnpglkLNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 467 KPDLVIFDEPATGLDIQTEHMIQNVLFQ--HFKDTTMIVIAHR-DNTIRHLQRRLYIENGRLIAD 528
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVSQvcQERQLTLLMVSHSlEDAARIAPRSLVVADGRIAWD 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
323-526 |
8.38e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 84.74 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLV--LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL------------ 388
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalserelraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 -NIGILSQQPYIFSA-SIKENItMF---------KDIEnNTIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRR 457
Cdd:COG1135 82 rKIGMIFQHFNLLSSrTVAENV-ALpleiagvpkAEIR-KRVAELLELVGLSDKADAYPS-----------QLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 458 IELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfqhfKD------TTMIVIAHRDNTIRHL-QRRLYIENGRLI 526
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLL----KDinrelgLTIVLITHEMDVVRRIcDRVAVLENGRIV 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
318-525 |
1.04e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.56 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRYDDSDRL--VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI-----STNQ----- 385
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqPMSKlssaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 386 ----RDLNIGILSQQPYI---FSASikENITMFKDI-------ENNTIEEVLDEVGLLDKVQSFTkgintiigeggEMLS 451
Cdd:PRK11629 81 kaelRNQKLGFIYQFHHLlpdFTAL--ENVAMPLLIgkkkpaeINSRALEMLAAVGLEHRANHRP-----------SELS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 452 GGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
323-529 |
1.08e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 83.31 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQP--------TIGTISTNQRDL-----N 389
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITLTAKTVwdireK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 IGILSQQP--YIFSASIKENITMfkDIEN---------NTIEEVLDEVGLLDKVQSFTKGintiigeggemLSGGQMRRI 458
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAF--GLENravprpemiKIVRDVLADVGMLDYIDSEPAN-----------LSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446659814 459 ELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDT--TMIVIAHRDNTIRHLQRRLYIENGRLIADD 529
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
323-526 |
1.20e-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: 82.35 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVlNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------NIGI 392
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFS-ASIKENITMFKDIEN---NTIEEVLDE----VGLldkvqsftkGINTIIGEGGEMLSGGQMRRIELCRLL 464
Cdd:cd03295 80 VIQQIGLFPhMTVEENIALVPKLLKwpkEKIRERADEllalVGL---------DPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 465 VMKPDLVIFDEPATGLDIQTEHMIQNvLFQHFKDT---TMIVIAHR-DNTIRHLQRRLYIENGRLI 526
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQE-EFKRLQQElgkTIVFVTHDiDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
336-506 |
1.24e-17 |
|
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: 86.14 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTiSTNQRDLNIGILSQQPYI-FSASIKENITM---- 410
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-ARPQPGIKVGYLPQEPQLdPTKTVRENVEEgvae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 411 -------FKDIENNTIEEVLDEVGLLDKVqsfTKGINTIIGEGG-------EM----------------LSGGQMRRIEL 460
Cdd:TIGR03719 96 ikdaldrFNEISAKYAEPDADFDKLAAEQ---AELQEIIDAADAwdldsqlEIamdalrcppwdadvtkLSGGERRRVAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446659814 461 CRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHFKDtTMIVIAH 506
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
337-481 |
1.45e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 337 RLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRD-----------LNIGILSQQPYIF-SASI 404
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmhkrarLGIGYLPQEASIFrKLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 405 KENITMF-------KDIENNTIEEVLDEVGLlDKVQSfTKGIntiigeggeMLSGGQMRRIELCRLLVMKPDLVIFDEPA 477
Cdd:COG1137 96 EDNILAVlelrklsKKEREERLEELLEEFGI-THLRK-SKAY---------SLSGGERRRVEIARALATNPKFILLDEPF 164
|
....
gi 446659814 478 TGLD 481
Cdd:COG1137 165 AGVD 168
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
323-525 |
1.67e-17 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 81.45 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDIsfRYDDSDRLVLNDLNLEifKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------IGILS 394
Cdd:TIGR01277 1 LALDKV--RYEYEHLPMEFDLNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTglapyqrpVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIFS-ASIKENITM-------FKDIENNTIEEVLDEVGLLDKVQSFTkgintiigeggEMLSGGQMRRIELCRLLVM 466
Cdd:TIGR01277 77 QENNLFAhLTVRQNIGLglhpglkLNAEQQEKVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446659814 467 KPDLVIFDEPATGLD-IQTEHMIQNV--LFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:TIGR01277 146 PNPILLLDEPFSALDpLLREEMLALVkqLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
321-529 |
2.40e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.74 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------I 390
Cdd:PRK13548 1 AMLEARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspaelarrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPYI-FSASIKENITM-------FKDIENNTIEEVLDEVGLLD-KVQSFTKgintiigeggemLSGGQMRRIELC 461
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMgraphglSRAEDDALVAAALAQVDLAHlAGRDYPQ------------LSGGEQQRVQLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 462 RLLV------MKPDLVIFDEPATGLDIQTEHMIQNVLFQ--HFKDTTMIVIAHRDN-TIRHLQRRLYIENGRLIADD 529
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQlaHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
321-523 |
3.13e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 85.80 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYD-DSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPtIGTISTNQRDlNIGILSQQPYI 399
Cdd:PLN03232 613 PAISIKNGYFSWDsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-AETSSVVIRG-SVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 FSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATG 479
Cdd:PLN03232 691 FNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446659814 480 LDIQTEHMIQNVLFQH-FKDTTMIVIAHRDNTIRHLQRRLYIENG 523
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDeLKGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
335-529 |
3.82e-17 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 80.81 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 335 SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL-------------NIGILSQQ-PYIF 400
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgkklrklrrRIGMIFQHyNLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 401 SASIKENITM---------------FKDIENNTIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIELCRLLV 465
Cdd:TIGR02315 93 RLTVLENVLHgrlgykptwrsllgrFSEEDKERALSALERVGLADKAYQRAD-----------QLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 466 MKPDLVIFDEPATGLDIQTEHMIQNVLF---QHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIADD 529
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKrinKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
336-481 |
4.63e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.83 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTI---GTISTNQRDLN--------IGILSQQPYIFS-AS 403
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTalpaeqrrIGILFQDDLLFPhLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 404 IKENI------TMFKDIENNTIEEVLDEVGLLDKvqsFTKGINTiigeggemLSGGQMRRIELCRLLVMKPDLVIFDEPA 477
Cdd:COG4136 93 VGENLafalppTIGRAQRRARVEQALEEAGLAGF---ADRDPAT--------LSGGQRARVALLRALLAEPRALLLDEPF 161
|
....
gi 446659814 478 TGLD 481
Cdd:COG4136 162 SKLD 165
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
337-527 |
5.70e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 337 RLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-----------IGILSQQPYIFSA-SI 404
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhararrgIGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 405 KENITMFKDIENN-TIEEVLDEVGLLdkVQSFTkgINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQ 483
Cdd:PRK10895 96 YDNLMAVLQIRDDlSAEQREDRANEL--MEEFH--IEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446659814 484 TEHMIQNVLfQHFKDTTMIVIAHRDN---TIRHLQRRLYIENGRLIA 527
Cdd:PRK10895 172 SVIDIKRII-EHLRDSGLGVLITDHNvreTLAVCERAYIVSQGHLIA 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
323-527 |
6.38e-17 |
|
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: 79.63 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIGILSQQPYI--- 399
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 ----FSASIKENITMFKDIENNTIEEVLDEVG-LLDKVqsftkGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFD 474
Cdd:cd03269 79 rglyPKMKVIDQLVYLAQLKGLKKEEARRRIDeWLERL-----ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 475 EPATGLD-IQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHL-QRRLYIENGRLIA 527
Cdd:cd03269 154 EPFSGLDpVNVELLKDVIRELARAGKTVILSTHQMELVEELcDRVLLLNKGRAVL 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
321-481 |
7.15e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.58 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------IGI 392
Cdd:PRK11607 18 PLLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLShvppyqrpINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFS-ASIKENIT-------MFKDIENNTIEEVLDEVglldKVQSFTKgintiigEGGEMLSGGQMRRIELCRLL 464
Cdd:PRK11607 96 MFQSYALFPhMTVEQNIAfglkqdkLPKAEIASRVNEMLGLV----HMQEFAK-------RKPHQLSGGQRQRVALARSL 164
|
170
....*....|....*..
gi 446659814 465 VMKPDLVIFDEPATGLD 481
Cdd:PRK11607 165 AKRPKLLLLDEPMGALD 181
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
323-532 |
7.28e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.05 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL------------NI 390
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglmklreSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQP--YIFSASIkenitmFKDIENNTIEEVLDEVGLLDKVQSFTK--GINTIIGEGGEMLSGGQMRRIELCRLLVM 466
Cdd:PRK13636 85 GMVFQDPdnQLFSASV------YQDVSFGAVNLKLPEDEVRKRVDNALKrtGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 467 KPDLVIFDEPATGLDIQTEHMIQNVLFQHFK--DTTMIVIAHRDNTIrhlqrRLYIENGRLIADDRNI 532
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIV-----PLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
340-529 |
1.09e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.64 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI------------STNQRDL--NIGILSQQPyifSASIK 405
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhitpetgNKNLKKLrkKVSLVFQFP---EAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 406 ENiTMFKDIE-------------NNTIEEVLDEVGLLDKVqsftkgintiIGEGGEMLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:PRK13641 100 EN-TVLKDVEfgpknfgfsedeaKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446659814 473 FDEPATGLDIQTEHMiqnvLFQHFKDT-----TMIVIAHR-DNTIRHLQRRLYIENGRLIADD 529
Cdd:PRK13641 169 LDEPAAGLDPEGRKE----MMQLFKDYqkaghTVILVTHNmDDVAEYADDVLVLEHGKLIKHA 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
319-520 |
1.19e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.92 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 319 QKPFIQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------I 390
Cdd:PRK09452 11 LSPLVELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvpaenrhV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPYIFS-ASIKENI--------TMFKDIENNtIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIELC 461
Cdd:PRK09452 89 NTVFQSYALFPhMTVFENVafglrmqkTPAAEITPR-VMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 462 RLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfqhfkdttmiviahrdntiRHLQRRLYI 520
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNEL-------------------KALQRKLGI 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
340-527 |
1.23e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.55 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNqrDLNIGILSQQPYIFSASIKENItMFKDIENNTI 419
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKQKEIKPVRKKVGV-VFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 420 EE-VLDEVGLLDKVQSFTKG-INTIIGEGGEM--------------LSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQ 483
Cdd:PRK13643 99 EEtVLKDVAFGPQNFGIPKEkAEKIAAEKLEMvgladefwekspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446659814 484 TE-HMIQnvLFQHFKDT--TMIVIAHRDNTIRHLQRRLY-IENGRLIA 527
Cdd:PRK13643 179 ARiEMMQ--LFESIHQSgqTVVLVTHLMDDVADYADYVYlLEKGHIIS 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
323-506 |
1.43e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSdrLVLNDLNLEIFKGDQIALVGPSGAGKSTL-------THLIAG-------------VYQPTIGTIS 382
Cdd:PRK14243 11 LRTENLNVYYGSF--LAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnrlNDLIPGfrvegkvtfhgknLYAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 383 TNQRdlnIGILSQQPYIFSASIKENITM------FKDIENNTIEEVLDEVGLLDKVQSFTKgintiigEGGEMLSGGQMR 456
Cdd:PRK14243 89 VRRR---IGMVFQKPNPFPKSIYDNIAYgaringYKGDMDELVERSLRQAALWDEVKDKLK-------QSGLSLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446659814 457 RIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAH 506
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
323-528 |
1.56e-16 |
|
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: 78.56 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLV--LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI-------STNQRD--LNIG 391
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgfdvVKEPAEarRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQPYIFS-ASIKENITMFKD---IENNTIEEVLDEV-GLLDkvqsftkgINTIIGEGGEMLSGGQMRRIELCRLLVM 466
Cdd:cd03266 82 FVSDSTGLYDrLTARENLEYFAGlygLKGDELTARLEELaDRLG--------MEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 467 KPDLVIFDEPATGLDIQTEHMIQNVLfQHFKD--TTMIVIAHRDNTIRHL-QRRLYIENGRLIAD 528
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFI-RQLRAlgKCILFSTHIMQEVERLcDRVVVLHRGRVVYE 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
323-511 |
1.70e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.82 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDS---DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN---------- 389
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 ----IGILSQQP--YIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKginTIIGEGGEMLSGGQMRRIELCRL 463
Cdd:PRK13646 83 vrkrIGMVFQFPesQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSR---DVMSQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446659814 464 LVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHRDNTI 511
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEV 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
323-528 |
2.11e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.13 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRL---VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIGILSQQPYI 399
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 FSASIKENITMFKDIENntIEEVLDEVGLL---DKVQSFTKGINTIIGEGG------------------EM--------- 449
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKK--IKEIRRRVGVVfqfAEYQLFEQTIEKDIIFGPvsmgvskeeakkraakyiELvgldesylq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 450 -----LSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQ-HFKDTTMIVIAHR-DNTIRHLQRRLYIEN 522
Cdd:PRK13651 161 rspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDlDNVLEWTKRTIFFKD 240
|
....*.
gi 446659814 523 GRLIAD 528
Cdd:PRK13651 241 GKIIKD 246
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
323-522 |
2.63e-16 |
|
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: 76.42 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFrYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDlNIGILSQQPYIFSA 402
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-DLLFLPQRPYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 SIKEnitmfkdienntieevldevglldkvqsftkginTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDI 482
Cdd:cd03223 79 TLRE----------------------------------QLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446659814 483 QTEHMIQNVLFQHFkdTTMIVIAHRDNTIRHLQRRLYIEN 522
Cdd:cd03223 125 ESEDRLYQLLKELG--ITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
339-483 |
2.76e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.51 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTN--------QRDLNIGILSQQPYIFS-ASIKENI- 408
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvsrlhARDRKVGFVFQHYALFRhMTVFDNIa 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 409 ---TMFKDIENNTIEEVLDEVG-LLDKVQsftkgINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQ 483
Cdd:PRK10851 97 fglTVLPRRERPNAAAIKAKVTqLLEMVQ-----LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
321-506 |
4.11e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.54 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQ-----PTIGTI-----STNQRDLNI 390
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVeffnqNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQ-------PYIFSASIKENITMFKDIE--------NNTIEEVLDEVGLLDKVQSftkgintIIGEGGEMLSGGQM 455
Cdd:PRK14258 84 NRLRRQvsmvhpkPNLFPMSVYDNVAYGVKIVgwrpkleiDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 456 RRIELCRLLVMKPDLVIFDEPATGLD----IQTEHMIQNVLFQhfKDTTMIVIAH 506
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSH 209
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
342-527 |
4.40e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 79.77 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 342 DLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------------IGILSQQPYIFS-ASIKE 406
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrkgiflppekrrIGYVFQEARLFPhLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 407 NITM---FKDIENNTI--EEVLDevgLLdkvqsftkGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLD 481
Cdd:TIGR02142 95 NLRYgmkRARPSERRIsfERVIE---LL--------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446659814 482 IQTEHMI----QNvLFQHFkDTTMIVIAHRDNTIRHLQRRLYI-ENGRLIA 527
Cdd:TIGR02142 164 DPRKYEIlpylER-LHAEF-GIPILYVSHSLQEVLRLADRVVVlEDGRVAA 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
323-530 |
5.23e-16 |
|
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: 77.09 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-----------IG 391
Cdd:cd03224 1 LEVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglppheraragIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQPYIF-SASIKENITM-----FKDIENNTIEEVLDEVGLLDKVQSftkgintiiGEGGEmLSGGQMRRIELCRLLV 465
Cdd:cd03224 79 YVPEGRRIFpELTVEENLLLgayarRRAKRKARLERVYELFPRLKERRK---------QLAGT-LSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 466 MKPDLVIFDEPATGLDIQTEHMIQNVLfQHFKD--TTMIVIAHRDNTIRHLQRRLYI-ENGRLIADDR 530
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAI-RELRDegVTILLVEQNARFALEIADRAYVlERGRVVLEGT 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
339-528 |
6.72e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.80 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL-------------NIGILSQQPyiFSA--- 402
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnraqrkafrrDIQMVFQDS--ISAvnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 --SIKENI--------TMFKDIENNTIEEVLDEVGLLDKVQSFTKGintiigeggeMLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:PRK10419 105 rkTVREIIreplrhllSLDKAERLARASEMLRAVDLDDSVLDKRPP----------QLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 473 FDEPATGLDI--QTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHL-QRRLYIENGRLIAD 528
Cdd:PRK10419 175 LDEAVSNLDLvlQAGVIRLLKKLQQQFGTACLFITHDLRLVERFcQRVMVMDNGQIVET 233
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
16-245 |
7.34e-16 |
|
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: 78.36 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 16 VLMFLVSTGLGILV--ITQnILIADFlakIIRHQFQGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKVKHMLRQRViY 93
Cdd:cd07346 5 LLLLLLATALGLALplLTK-LLIDDV---IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 94 KN---------NGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIF 164
Cdd:cd07346 80 RHlqrlslsffDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 165 GLKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFISMLGIGL 244
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
.
gi 446659814 245 V 245
Cdd:cd07346 240 V 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
292-537 |
7.90e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 80.23 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 292 EGASD-VVFEFLEQ---PNYNNEFLLKyeenqKPFIQLTDISFRYDDSDRLVL---NDLNLEIFKGDQIALVGPSGAGKS 364
Cdd:TIGR03269 250 EGTPDeVVAVFMEGvseVEKECEVEVG-----EPIIKVRNVSKRYISVDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKT 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 365 TLTHLIAGVYQPTIGTIS----------TNQRDLN-------IGILSQQPYIFS-ASIKENITMFKDIenntieEVLDEV 426
Cdd:TIGR03269 325 TLSKIIAGVLEPTSGEVNvrvgdewvdmTKPGPDGrgrakryIGILHQEYDLYPhRTVLDNLTEAIGL------ELPDEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 427 GLLD-----KVQSFT-KGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKD-- 498
Cdd:TIGR03269 399 ARMKavitlKMVGFDeEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEme 478
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446659814 499 TTMIVIAHRDNTIRHL-QRRLYIENGRL--IADDRNISVNIT 537
Cdd:TIGR03269 479 QTFIIVSHDMDFVLDVcDRAALMRDGKIvkIGDPEEIVEELT 520
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
340-504 |
8.03e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.48 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGvYQPT----IGTISTN-----------------QRDLNIGILSQQPY 398
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKgvkgSGSVLLNgmpidakemraisayvqQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 399 -IFSASIKENITMFKDIENNTIEEVLDEVGLLdkvqsftKGINTIIGEGGEM--LSGGQMRRIELCRLLVMKPDLVIFDE 475
Cdd:TIGR00955 120 lMFQAHLRMPRRVTKKEKRERVDEVLQALGLR-------KCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180
....*....|....*....|....*....
gi 446659814 476 PATGLDIQTEHMIQNVLfQHFKDTTMIVI 504
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVL-KGLAQKGKTII 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
339-526 |
8.76e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.10 E-value: 8.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIGI-LSQQP-----------YIFsasikE 406
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARsLSQQKglirqlrqhvgFVF-----Q 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 407 NITMF--KDIENNTIE------------------EVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIELCRLLVM 466
Cdd:PRK11264 93 NFNLFphRTVLENIIEgpvivkgepkeeatararELLAKVGLAGKETSYPR-----------RLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446659814 467 KPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDT-TMIVIAHRDNTIRHL-QRRLYIENGRLI 526
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIV 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
323-506 |
1.07e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 77.21 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYD--DSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQR-----DLNIGILSQ 395
Cdd:COG4525 4 LTVRHVSVRYPggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 396 Q----PYIfsaSIKENIT-------MFKDIENNTIEEVLDEVGLLDKVQSFtkgintiIGEggemLSGGQMRRIELCRLL 464
Cdd:COG4525 84 KdallPWL---NVLDNVAfglrlrgVPKAERRARAEELLALVGLADFARRR-------IWQ----LSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446659814 465 VMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDT--TMIVIAH 506
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITH 193
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
340-506 |
1.28e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 76.35 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL------------NIGILsqqPYIfsaSIKEN 407
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpdrmvvfqNYSLL---PWL---TVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 408 I---------TMFKDIENNTIEEVLDEVGLldkvqsfTKGINTIIGEggemLSGGQMRRIELCRLLVMKPDLVIFDEPAT 478
Cdd:TIGR01184 75 IalavdrvlpDLSKSERRAIVEEHIALVGL-------TEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190
....*....|....*....|....*....|
gi 446659814 479 GLDIQTEHMIQNVLFQHFKDT--TMIVIAH 506
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHrvTVLMVTH 173
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-506 |
1.76e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 77.40 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLV--LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTI---GTISTNQRDL--------- 388
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLlklsekelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 -----NIGILSQQPYifSA---------SIKENITMFKDIENNT----IEEVLDEVGLLDKVQsftkgintIIGEGGEML 450
Cdd:COG0444 82 kirgrEIQMIFQDPM--TSlnpvmtvgdQIAEPLRIHGGLSKAEarerAIELLERVGLPDPER--------RLDRYPHEL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 451 SGGQMRRIELCRLLVMKPDLVIFDEPATGLD--IQTEhmIQNVL--FQHFKDTTMIVIAH 506
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDvtIQAQ--ILNLLkdLQRELGLAILFITH 209
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
323-504 |
1.97e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.01 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDS---DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL----------- 388
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkvklsdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 -NIGILSQQP--YIFSAsikeniTMFKDIE-------------NNTIEEVLDEVGL-----LDKvQSFTkgintiigegg 447
Cdd:PRK13637 83 kKVGLVFQYPeyQLFEE------TIEKDIAfgpinlglseeeiENRVKRAMNIVGLdyedyKDK-SPFE----------- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 448 emLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVI 504
Cdd:PRK13637 145 --LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTII 199
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
323-482 |
2.05e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 76.31 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGI 392
Cdd:COG4559 2 LEAENLSVRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawspwelarrRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYI-FSASIKENITM-------FKDIENNTIEEVLDEVGLLDKVQ-SFTkgintiigeggeMLSGGQMRRIELCRL 463
Cdd:COG4559 80 LPQHSSLaFPFTVEEVVALgraphgsSAAQDRQIVREALALVGLAHLAGrSYQ------------TLSGGEQQRVQLARV 147
|
170 180
....*....|....*....|....*.
gi 446659814 464 LV-------MKPDLVIFDEPATGLDI 482
Cdd:COG4559 148 LAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
341-517 |
2.19e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.44 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 341 NDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL-------------NIGILSQQPYifsASIKEN 407
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkddewravrsDIQMIFQDPL---ASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 408 IT---------------MFKDIENNTIEEVLDEVGLLDKVqsftkgINTIIGEggemLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:PRK15079 115 MTigeiiaeplrtyhpkLSRQEVKDRVKAMMLKVGLLPNL------INRYPHE----FSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446659814 473 FDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHRDNTIRHLQRR 517
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLqqLQREMGLSLIFIAHDLAVVKHISDR 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
320-507 |
2.38e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 320 KPFIQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI----------STNQ-RDL 388
Cdd:COG1129 2 EPLLEMRGISKSF--GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIlldgepvrfrSPRDaQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 NIGILSQQPYIFSA-SIKENITMFKDIENNTI----------EEVLDEVGL-LDkvqsftkgINTIIGEggemLSGGQMR 456
Cdd:COG1129 80 GIAIIHQELNLVPNlSVAENIFLGREPRRGGLidwramrrraRELLARLGLdID--------PDTPVGD----LSVAQQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 457 RIELCRLLVMKPDLVIFDEPATGLdiqTEHMIQNvLFQ---HFKD--TTMIVIAHR 507
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASL---TEREVER-LFRiirRLKAqgVAIIYISHR 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
327-523 |
3.31e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.05 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 327 DISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDlnIG------------ILS 394
Cdd:PTZ00243 1313 GVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE--IGayglrelrrqfsMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMK-PDLVIF 473
Cdd:PTZ00243 1391 QDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILM 1470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446659814 474 DEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENG 523
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
321-482 |
5.11e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRdLNIGILSQQPYIf 400
Cdd:PRK09544 3 SLVSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-LRIGYVPQKLYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 401 SASIKENITMFKDIENNTIEEvlDEVGLLDKVQSftkgiNTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGL 480
Cdd:PRK09544 79 DTTLPLTVNRFLRLRPGTKKE--DILPALKRVQA-----GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
..
gi 446659814 481 DI 482
Cdd:PRK09544 152 DV 153
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
331-520 |
5.22e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 331 RYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIGIlsqqpyifSASIKENITM 410
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR--------EASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 411 FKDIenNTIEEVLDEVGLLDkVQSFTKGINTiigeggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQT----EH 486
Cdd:COG2401 109 KGDF--KDAVELLNAVGLSD-AVLWLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTakrvAR 177
|
170 180 190
....*....|....*....|....*....|....
gi 446659814 487 MIQNVLFQHfkDTTMIVIAHRDNTIRHLQRRLYI 520
Cdd:COG2401 178 NLQKLARRA--GITLVVATHHYDVIDDLQPDLLI 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
340-514 |
5.39e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 76.31 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL-------------NIGILSQQPYifsASIKE 406
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsgrelrplrrRMQMVFQDPY---ASLNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 407 NITMfKDI-----ENNTI---EEVLDEVG-LLDKVqsftkGINTiigeggE-------MLSGGQMRRIELCRLLVMKPDL 470
Cdd:COG4608 111 RMTV-GDIiaeplRIHGLaskAERRERVAeLLELV-----GLRP------EhadryphEFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446659814 471 VIFDEPATGLD--IQTEhmIQNVL--FQHFKDTTMIVIAHRDNTIRHL 514
Cdd:COG4608 179 IVCDEPVSALDvsIQAQ--VLNLLedLQDELGLTYLFISHDLSVVRHI 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
318-513 |
9.98e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.59 E-value: 9.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--------- 388
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIstlkpeiyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 -NIGILSQQPYIFSASIKENITMFKDIENNTIEEV-----LDEVGLLDKVqsFTKGINTiigeggemLSGGQMRRIELCR 462
Cdd:PRK10247 81 qQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAiflddLERFALPDTI--LTKNIAE--------LSGGEKQRISLIR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446659814 463 LLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVI--AHRDNTIRH 513
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINH 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
331-525 |
1.06e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.51 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 331 RYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQrdlNIGILSQQPYIFSASIKENITM 410
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER---SIAYVPQQAWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 411 FKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQT-EHMIQ 489
Cdd:PTZ00243 744 FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVE 823
|
170 180 190
....*....|....*....|....*....|....*.
gi 446659814 490 NVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:PTZ00243 824 ECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
336-481 |
1.21e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 76.70 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTiSTNQRDLNIGILSQQPYI-FSASIKENI------ 408
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-ARPAPGIKVGYLPQEPQLdPEKTVRENVeegvae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 409 -----TMFKDIENNTIEEVLDEVGLLD---KVQsftkginTIIGEGG--------EM----------------LSGGQMR 456
Cdd:PRK11819 98 vkaalDRFNEIYAAYAEPDADFDALAAeqgELQ-------EIIDAADawdldsqlEIamdalrcppwdakvtkLSGGERR 170
|
170 180
....*....|....*....|....*
gi 446659814 457 RIELCRLLVMKPDLVIFDEPATGLD 481
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
318-528 |
1.31e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.87 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNiGILSQQp 397
Cdd:PRK11300 1 MSQPLLSVSGLMMRF--GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-GLPGHQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 398 yIFSASIK---ENITMFKD---IEN---------NT-------------------IEEV---LDEVGLLDKVQSftkgin 440
Cdd:PRK11300 77 -IARMGVVrtfQHVRLFREmtvIENllvaqhqqlKTglfsgllktpafrraeseaLDRAatwLERVGLLEHANR------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 441 tiigEGGEmLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNV---LFQHFkDTTMIVIAHRDNTIRHLQRR 517
Cdd:PRK11300 150 ----QAGN-LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELiaeLRNEH-NVTVLLIEHDMKLVMGISDR 223
|
250
....*....|..
gi 446659814 518 LY-IENGRLIAD 528
Cdd:PRK11300 224 IYvVNQGTPLAN 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
384-512 |
1.92e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.61 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 384 NQRDLN--IGILSQQPYIFSASIKENITMFKdiENNTIEEV--LDEVGLLDK-VQSFTKGINTIIGEGGEMLSGGQMRRI 458
Cdd:PTZ00265 1290 NLKDLRnlFSIVSQEPMLFNMSIYENIKFGK--EDATREDVkrACKFAAIDEfIESLPNKYDTNVGPYGKSLSGGQKQRI 1367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 459 ELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHRDNTIR 512
Cdd:PTZ00265 1368 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIK 1423
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
339-529 |
2.05e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQR-----DLNIGIlsqQPyifSASIKENITM--- 410
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallELGAGF---HP---ELTGRENIYLngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 411 ---FKDIEnntIEEVLDEV----GL---LD-KVQSFTKGintiigeggeMLSggqmrrielcRL-----LVMKPDLVIFD 474
Cdd:COG1134 115 llgLSRKE---IDEKFDEIvefaELgdfIDqPVKTYSSG----------MRA----------RLafavaTAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 475 EP-ATGlDIQtehmiqnvlFQH--------FKD--TTMIVIAHRDNTIRHL-QRRLYIENGRLIADD 529
Cdd:COG1134 172 EVlAVG-DAA---------FQKkclarireLREsgRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDG 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
323-514 |
2.05e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.46 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNI-----GILSQQP 397
Cdd:PRK10619 6 LNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdGQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 398 YIFSASIKENITM---------FKDIENNTIEEVLDEVGLlDKVQSFTKGINTI----IGEGGEM-----LSGGQMRRIE 459
Cdd:PRK10619 84 KNQLRLLRTRLTMvfqhfnlwsHMTVLENVMEAPIQVLGL-SKQEARERAVKYLakvgIDERAQGkypvhLSGGQQQRVS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 460 LCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKD-TTMIVIAHRDNTIRHL 514
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHV 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
321-481 |
2.10e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.70 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYD-DSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRdlNIGILSQQPYI 399
Cdd:PLN03130 613 PAISIKNGYFSWDsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRG--TVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 FSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATG 479
Cdd:PLN03130 691 FNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
..
gi 446659814 480 LD 481
Cdd:PLN03130 771 LD 772
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
336-515 |
2.75e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTN------QRD------LNIGILsqqpyifsAS 403
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgepirrQRDeyhqdlLYLGHQ--------PG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 404 IK------ENITMF----KDIENNTIEEVLDEVGLldkvqsftkgintiigEGGEM-----LSGGQMRRIELCRLLVMKP 468
Cdd:PRK13538 85 IKteltalENLRFYqrlhGPGDDEALWEALAQVGL----------------AGFEDvpvrqLSAGQQRRVALARLWLTRA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446659814 469 DLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIA-HRD-----NTIRHLQ 515
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTtHQDlpvasDKVRKLR 201
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
337-525 |
3.82e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.83 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 337 RLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-------------IGILSQQPYIF-SA 402
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrevpflrrqIGMIFQDHHLLmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 SIKENITMFKDIENNTIEEV-------LDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIELCRLLVMKPDLVIFDE 475
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIrrrvsaaLDKVGLLDKAKNFPI-----------QLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446659814 476 PATGLDIQTEHMIQNvLFQHFK--DTTMIVIAHRDNTI-RHLQRRLYIENGRL 525
Cdd:PRK10908 164 PTGNLDDALSEGILR-LFEEFNrvGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
323-526 |
4.79e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.47 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDS---DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNqrDLNIGILSQQPYI 399
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVD--DTLITSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 fsASIKENITM-FKDIENNTIEE-VLDEVGLldKVQSFtkGIN------------TIIGEGGEM-------LSGGQMRRI 458
Cdd:PRK13649 81 --KQIRKKVGLvFQFPESQLFEEtVLKDVAF--GPQNF--GVSqeeaealareklALVGISESLfeknpfeLSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446659814 459 ELCRLLVMKPDLVIFDEPATGLDIQ--TEHMiqnVLFQ--HFKDTTMIVIAHRDNTIRHLQRRLYI-ENGRLI 526
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKgrKELM---TLFKklHQSGMTIVLVTHLMDDVANYADFVYVlEKGKLV 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
330-492 |
5.03e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 71.53 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 330 FRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQP---TIGTISTNQRDLN-------IGILSQQPYI 399
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKpdqfqkcVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 FSA-SIKENIT---MFK--DIENNTIEEVLDEVGLLDKVqsftkGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIF 473
Cdd:cd03234 93 LPGlTVRETLTytaILRlpRKSSDAIRKKRVEDVLLRDL-----ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170
....*....|....*....
gi 446659814 474 DEPATGLDIQTEHMIQNVL 492
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTL 186
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
323-527 |
5.08e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.80 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISfrydDSDRLVlnDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTiGTISTNQRDLNI----------GI 392
Cdd:COG4138 1 LQLNDVA----VAGRLG--PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDwsaaelarhrAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQ-------P---YI-FSASIKENITMFKDiennTIEEVLDEVGLLDKvqsFTKGINTiigeggemLSGGQMRRIELC 461
Cdd:COG4138 74 LSQQqsppfamPvfqYLaLHQPAGASSEAVEQ----LLAQLAEALGLEDK---LSRPLTQ--------LSGGEWQRVRLA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 462 R-LLVMKPD------LVIFDEPATGLDIQTEHMIQNVLfQHFKDT--TMIVIAHRDN-TIRHLQRRLYIENGRLIA 527
Cdd:COG4138 139 AvLLQVWPTinpegqLLLLDEPMNSLDVAQQAALDRLL-RELCQQgiTVVMSSHDLNhTLRHADRVWLLKQGKLVA 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
323-528 |
7.61e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.06 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN------IGILsqq 396
Cdd:COG4152 2 LELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpedrrrIGYL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 397 P-----YIfSASIKENITMF--------KDIENNtIEEVLDEVGLLD----KVQSftkgintiigeggemLSGGQMRRIE 459
Cdd:COG4152 77 PeerglYP-KMKVGEQLVYLarlkglskAEAKRR-ADEWLERLGLGDrankKVEE---------------LSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 460 LCRLLVMKPDLVIFDEPATGLD-IQTEHMIQNVLFQHFKDTTMIVIAHR-DNTIRHLQRRLYIENGRLIAD 528
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDpVNVELLKDVIRELAAKGTTVIFSSHQmELVEELCDRIVIINKGRKVLS 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
340-526 |
8.06e-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: 71.91 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------------IGILSQQPYIF-SASI 404
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsrkelrelrrkkISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 405 KENIT-------MFKDIENNTIEEVLDEVGLLDKVQSFtkgintiIGEggemLSGGQMRRIELCRLLVMKPDLVIFDEPA 477
Cdd:cd03294 120 LENVAfglevqgVPRAEREERAAEALELVGLEGWEHKY-------PDE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446659814 478 TGLD--IQTEhmIQNVLFQHFKDT--TMIVIAHR-DNTIRHLQRRLYIENGRLI 526
Cdd:cd03294 189 SALDplIRRE--MQDELLRLQAELqkTIVFITHDlDEALRLGDRIAIMKDGRLV 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
323-526 |
1.10e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.56 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-----------IG 391
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfsklqgirklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQP--YIFSASIKENITM------FKDIE-NNTIEEVLDEVGLlDKVQSFTKgintiigeggEMLSGGQMRRIELCR 462
Cdd:PRK13644 81 IVFQNPetQFVGRTVEEDLAFgpenlcLPPIEiRKRVDRALAEIGL-EKYRHRSP----------KTLSGGQGQCVALAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 463 LLVMKPDLVIFDEPATGLDIQT-EHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-527 |
1.36e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.37 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDdSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI--------STNQRDLN--IGI 392
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitKENIREVRkfVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQP--YIFSASIKEnitmfkDIENNTIEEVLDEVGLLDKVQSFTK--GINTIIGEGGEMLSGGQMRRIELCRLLVMKP 468
Cdd:PRK13652 83 VFQNPddQIFSPTVEQ------DIAFGPINLGLDEETVAHRVSSALHmlGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446659814 469 DLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVI--AHRDNTIRHLQRRLYI-ENGRLIA 527
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEMADYIYVmDKGRIVA 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
323-498 |
1.61e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.89 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSD----RLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI------STNQRDL---- 388
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldTSDEENLwdir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 -NIGILSQQP--YIFSASIKENITMFKD---IENNTIEEVLDEVglLDKVqsftkGINTIIGEGGEMLSGGQMRRIELCR 462
Cdd:PRK13633 85 nKAGMVFQNPdnQIVATIVEEDVAFGPEnlgIPPEEIRERVDES--LKKV-----GMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446659814 463 LLVMKPDLVIFDEPATGLD-------------IQTEHMIQNVLFQHFKD 498
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDpsgrrevvntikeLNKKYGITIILITHYME 206
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
339-521 |
1.94e-13 |
|
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: 72.86 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYqPTIGTISTNQRDLNIGILSQQPYIFSASIKENIT-------MF 411
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIypdssedMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 412 -KDIENNTIEEVLDEVGLLDKVQSftKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEhmiqN 490
Cdd:TIGR00954 546 rRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----G 619
|
170 180 190
....*....|....*....|....*....|...
gi 446659814 491 VLFQHFKDT--TMIVIAHRDNTIRHLQRRLYIE 521
Cdd:TIGR00954 620 YMYRLCREFgiTLFSVSHRKSLWKYHEYLLYMD 652
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
355-529 |
2.12e-13 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 71.37 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 355 LVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------IGILSQQPYIFS-ASIKENITM---FKDIENNTIEEV 422
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTnvpphlrhINMVFQSYALFPhMTVEENVAFglkMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 423 LDEVglLDKVQSFTKGINTIIgeggeMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTT 500
Cdd:TIGR01187 81 VLEA--LRLVQLEEFADRKPH-----QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELktIQEQLGIT 153
|
170 180 190
....*....|....*....|....*....|
gi 446659814 501 MIVIAHRDNTIRHLQRRLYI-ENGRLIADD 529
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAImRKGKIAQIG 183
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-526 |
2.28e-13 |
|
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: 68.73 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 335 SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAG--VYQPTIGTISTNQRDLnigilsqQPYIFSASI----KENI 408
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL-------DKRSFRKIIgyvpQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 409 TmfkdIENNTIEEVLDEVGLLdkvqsftKGIntiigeggemlSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMI 488
Cdd:cd03213 93 L----HPTLTVRETLMFAAKL-------RGL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446659814 489 QnVLFQHFKDT--TMIVIAH--RDNTIRHLQRRLYIENGRLI 526
Cdd:cd03213 151 M-SLLRRLADTgrTIICSIHqpSSEIFELFDKLLLLSQGRVI 191
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
323-526 |
2.48e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.37 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLV--LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL------------ 388
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsekelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 -NIGILSQQPYIFSA-SIKENITMFKDIEN-------NTIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIE 459
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVFDNVALPLELAGtpkaeikARVTELLELVGLSDKADRYPA-----------QLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446659814 460 LCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfqhfKDT------TMIVIAHRDNTIRHLQRRL-YIENGRLI 526
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELL----KDInrelglTIVLITHEMDVVKRICDRVaVIDAGRLV 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
323-506 |
2.52e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.18 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRydDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRdlNIGILSQQ------ 396
Cdd:PRK11831 8 VDMRGVSFT--RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE--NIPAMSRSrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 397 ---PYIF-SASIKENITMFKDI-----ENNTIEEVLDEVGLLDKVQSFtkGINtiiGEGGEM---LSGGQMRRIELCRLL 464
Cdd:PRK11831 84 krmSMLFqSGALFTDMNVFDNVayplrEHTQLPAPLLHSTVMMKLEAV--GLR---GAAKLMpseLSGGMARRAALARAI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446659814 465 VMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAH 506
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSH 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
336-481 |
2.96e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.60 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPT--IGTISTNQRDLN------IGILSQ-----------Q 396
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTkqilkrTGFVTQddilyphltvrE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 397 PYIFSASIKENITMFKDIENNTIEEVLDEVGLldkvqsfTKGINTIIGEGG-EMLSGGQMRRIELCRLLVMKPDLVIFDE 475
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELGL-------TKCENTIIGNSFiRGISGGERKRVSIAHEMLINPSLLILDE 232
|
....*.
gi 446659814 476 PATGLD 481
Cdd:PLN03211 233 PTSGLD 238
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
84-278 |
3.14e-13 |
|
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: 69.98 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 84 KHMLRQRVIYKNNgHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYII 163
Cdd:pfam00664 82 KKILRQPMSFFDT-NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 164 FGLKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFISMLGIG 243
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
170 180 190
....*....|....*....|....*....|....*
gi 446659814 244 LVALEATlSLVVFHNIDFKTAAIAIILAPEFYNAI 278
Cdd:pfam00664 241 LALWFGA-YLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-506 |
3.72e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.49 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 335 SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTL----THLI----------------AGVYQPTIGTISTNQRdlnIGILS 394
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtfNRLLelneearvegevrlfgRNIYSPDVDPIEVRRE---VGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIFS-ASIKENITM---------FKDIENNTIEEVLDEVGLLDKVQSFTKgintiigEGGEMLSGGQMRRIELCRLL 464
Cdd:PRK14267 92 QYPNPFPhLTIYDNVAIgvklnglvkSKKELDERVEWALKKAALWDEVKDRLN-------DYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446659814 465 VMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAH 506
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
298-494 |
3.83e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 72.20 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 298 VFEFLEQPNYNNEFLLKYEENQKPFIQLTDISFRYDDSDRLVLNdLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPT 377
Cdd:PLN03073 484 VDAVVNDPDYKFEFPTPDDRPGPPIISFSDASFGYPGGPLLFKN-LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 378 IGTISTNQRdLNIGILSQQpYIFSASIKENITM-----FKDIENNTIEEVLDEVGLLDK--VQSFTkgintiigeggeML 450
Cdd:PLN03073 563 SGTVFRSAK-VRMAVFSQH-HVDGLDLSSNPLLymmrcFPGVPEQKLRAHLGSFGVTGNlaLQPMY------------TL 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446659814 451 SGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQ-TEHMIQN-VLFQ 494
Cdd:PLN03073 629 SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDaVEALIQGlVLFQ 674
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
318-507 |
6.02e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.21 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRYDDsdrLVLND-LNLEIFKGdQI-ALVGPSGAGKSTLTHLIAGVYQPTIGTI----------STNQ 385
Cdd:COG3845 1 MMPPALELRGITKRFGG---VVANDdVSLTVRPG-EIhALLGENGAGKSTLMKILYGLYQPDSGEIlidgkpvrirSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 386 -RDLNIGILSQQPYIFSA-SIKENITM--------FKDIE--NNTIEEVLDEVGL-LDkvqsftkgINTIIGEggemLSG 452
Cdd:COG3845 77 aIALGIGMVHQHFMLVPNlTVAENIVLgleptkggRLDRKaaRARIRELSERYGLdVD--------PDAKVED----LSV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 453 GQMRRIELCRLLVMKPDLVIFDEPATGLDIQ-TEHmiqnvLFQHFKD-----TTMIVIAHR 507
Cdd:COG3845 145 GEQQRVEILKALYRGARILILDEPTAVLTPQeADE-----LFEILRRlaaegKSIIFITHK 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
300-525 |
1.17e-12 |
|
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: 71.20 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 300 EFLEQPNY----NNEFLLKYEENQKPFIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQ 375
Cdd:TIGR01257 902 EEMEDPEHpegiNDSFFERELPGLVPGVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 376 PTIGTISTNQRDL---------NIGILSQQPYIF-SASIKENITMFKDIENNTIEEV-LDEVGLLDKVqsftkGINTIIG 444
Cdd:TIGR01257 982 PTSGTVLVGGKDIetnldavrqSLGMCPQHNILFhHLTVAEHILFYAQLKGRSWEEAqLEMEAMLEDT-----GLHHKRN 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 445 EGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRL-YIENG 523
Cdd:TIGR01257 1057 EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIaIISQG 1136
|
..
gi 446659814 524 RL 525
Cdd:TIGR01257 1137 RL 1138
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
323-506 |
1.28e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.80 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-----IGILSQQ- 396
Cdd:PRK11248 2 LQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaeRGVVFQNe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 397 ---PYifsASIKENIT-------MFKDIENNTIEEVLDEVGLldkvqsftkgintiigEGGE-----MLSGGQMRRIELC 461
Cdd:PRK11248 80 gllPW---RNVQDNVAfglqlagVEKMQRLEIAHQMLKKVGL----------------EGAEkryiwQLSGGQRQRVGIA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446659814 462 RLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDT--TMIVIAH 506
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITH 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
318-517 |
1.36e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRD---------- 387
Cdd:PRK09700 1 MATPYISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhklaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 388 -LNIGILSQQ-PYIFSASIKENITM---------------FKDIENNTiEEVLDEVGLldKVQsftkgINTIIGEggemL 450
Cdd:PRK09700 79 qLGIGIIYQElSVIDELTVLENLYIgrhltkkvcgvniidWREMRVRA-AMMLLRVGL--KVD-----LDEKVAN----L 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 451 SGGQMRRIELCRLLVMKPDLVIFDEPATGL-DIQTEHMIQnVLFQHFKDTTMIV-IAHRDNTIRHLQRR 517
Cdd:PRK09700 147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLFL-IMNQLRKEGTAIVyISHKLAEIRRICDR 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
321-480 |
2.36e-12 |
|
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: 66.54 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDlnigILSQQPY-- 398
Cdd:COG0410 2 PMLEVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED----ITGLPPHri 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 399 -------------IFSA-SIKENITM--FKDIENNTIEEVLDEVglldkVQSFtkginTIIGE-----GGEmLSGGQMRR 457
Cdd:COG0410 76 arlgigyvpegrrIFPSlTVEENLLLgaYARRDRAEVRADLERV-----YELF-----PRLKErrrqrAGT-LSGGEQQM 144
|
170 180
....*....|....*....|...
gi 446659814 458 IELCRLLVMKPDLVIFDEPATGL 480
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGL 167
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
325-508 |
2.39e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.13 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 325 LTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIGILS-QQPYIF--- 400
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTyQKQLCFvgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 401 SASIKENITM----FKDIENNTIEEVLDEVGLLDKVQSFtkgINTIIGeggeMLSGGQMRRIELCRLLVMKPDLVIFDEP 476
Cdd:PRK13540 82 RSGINPYLTLrencLYDIHFSPGAVGITELCRLFSLEHL---IDYPCG----LLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 446659814 477 ATGLDIQTEHMIQNVLFQHFKDTTMIVI-AHRD 508
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLtSHQD 187
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
339-525 |
2.93e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--------------NIGILSQQ-PYIFSAS 403
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeearaklrakHVGFVFQSfMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 404 IKENITM----FKDIENNTIE---EVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIELCRLLVMKPDLVIFDEP 476
Cdd:PRK10584 105 ALENVELpallRGESSRQSRNgakALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446659814 477 ATGLDIQTEHMIQNVLFQHFKD--TTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
323-525 |
3.14e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIGILSQQPYIFSA 402
Cdd:PRK10522 323 LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 sIKENITMF--------KDIENNTIEEVLDEVGLLDKVQSftkgintiigEGGEM----LSGGQMRRIELCRLLVMKPDL 470
Cdd:PRK10522 402 -VFTDFHLFdqllgpegKPANPALVEKWLERLKMAHKLEL----------EDGRIsnlkLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 471 VIFDEPATGLDIQTEHMIQNVLFQHFKDT--TMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMgkTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-526 |
3.26e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.61 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 335 SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLI---AGVYQPTI---GTISTNQRDL----------NIGILSQQPY 398
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKIkvdGKVLYFGKDIfqidaiklrkEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 399 IFS-ASIKENITM------FKDIE--NNTIEEVLDEVGLLDKVQSFtkgintiIGEGGEMLSGGQMRRIELCRLLVMKPD 469
Cdd:PRK14246 101 PFPhLSIYDNIAYplkshgIKEKReiKKIVEECLRKVGLWKEVYDR-------LNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 470 LVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIAHRDNTIRHLQRRL-YIENGRLI 526
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVaFLYNGELV 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
323-481 |
4.49e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.75 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSdrLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------IGILS 394
Cdd:PRK11000 4 VTLRNVTKAYGDV--VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNdvppaergVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQ----PYIfsaSIKENITmF---------KDIEN--NTIEEVLDEVGLLDKVQsftkgintiigeggEMLSGGQMRRIE 459
Cdd:PRK11000 82 QSyalyPHL---SVAENMS-FglklagakkEEINQrvNQVAEVLQLAHLLDRKP--------------KALSGGQRQRVA 143
|
170 180
....*....|....*....|..
gi 446659814 460 LCRLLVMKPDLVIFDEPATGLD 481
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLD 165
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
321-505 |
6.57e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.56 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------I 390
Cdd:PRK09536 2 PMIDVSDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalsaraasrrV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPYI-FSASIKENITM-----------FKDIENNTIEEVLDEVGLLDKV-QSFTKgintiigeggemLSGGQMRR 457
Cdd:PRK09536 80 ASVPQDTSLsFEFDVRQVVEMgrtphrsrfdtWTETDRAAVERAMERTGVAQFAdRPVTS------------LSGGERQR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446659814 458 IELCRLLVMKPDLVIFDEPATGLDIQteHMIQNV-LFQHFKDTTMIVIA 505
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDIN--HQVRTLeLVRRLVDDGKTAVA 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
343-527 |
7.10e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 343 LNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYqPTIGTISTNQRDLNI----------GILSQQ-PYIFSASIKENITMF 411
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaelarhrAYLSQQqTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 412 ------KDIENNTIEEVLDEVGLLDKVqsfTKGINTiigeggemLSGGQMRRIELCR-LLVMKPD------LVIFDEPAT 478
Cdd:PRK03695 94 qpdktrTEAVASALNEVAEALGLDDKL---GRSVNQ--------LSGGEWQRVRLAAvVLQVWPDinpagqLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 479 GLDI-QtehmiQNVLFQHFKD-----TTMIVIAHRDN-TIRHLQRRLYIENGRLIA 527
Cdd:PRK03695 163 SLDVaQ-----QAALDRLLSElcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKLLA 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
289-484 |
7.34e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.60 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 289 KQSEGASDVVFEFleqPNYNNEFLLKYEENQKPFIqLTDISF--RYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTL 366
Cdd:TIGR00956 730 GEVLGSTDLTDES---DDVNDEKDMEKESGEDIFH-WRNLTYevKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTL 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 367 THLIAGvyQPTIGTISTNQRDLN-----------IGILSQQ-----------PYIFSASIKENITMFKDIENNTIEEVLD 424
Cdd:TIGR00956 806 LNVLAE--RVTTGVITGGDRLVNgrpldssfqrsIGYVQQQdlhlptstvreSLRFSAYLRQPKSVSKSEKMEYVEEVIK 883
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 425 EVGLLDKVQSftkgintIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIF-DEPATGLDIQT 484
Cdd:TIGR00956 884 LLEMESYADA-------VVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQT 937
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
324-527 |
8.23e-12 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 64.85 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 324 QLTDISFRYDDSdrLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-----------IGI 392
Cdd:TIGR03410 2 EVSNLNVYYGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITklppheraragIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 393 LSQQPYIFSA-SIKENITM----FKDIENNTIEEVLDEVGLLDKVQSftkgintiiGEGGEmLSGGQMRRIELCRLLVMK 467
Cdd:TIGR03410 80 VPQGREIFPRlTVEENLLTglaaLPRRSRKIPDEIYELFPVLKEMLG---------RRGGD-LSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 468 PDLVIFDEPATGldiqtehmIQNVLFQHFKDTTMIVIAHRDNTI----------RHLQRRLY-IENGRLIA 527
Cdd:TIGR03410 150 PKLLLLDEPTEG--------IQPSIIKDIGRVIRRLRAEGGMAIllveqyldfaRELADRYYvMERGRVVA 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
323-526 |
8.83e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.52 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGV--YQPTIGTISTN----QRDLNIGILSQ- 395
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcEKCGYVERPSKv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 396 -QP--------------------YIFSASIKENITMFKD----------IENntIEEVLDEVG------------LLDKV 432
Cdd:TIGR03269 79 gEPcpvcggtlepeevdfwnlsdKLRRRIRKRIAIMLQRtfalygddtvLDN--VLEALEEIGyegkeavgravdLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 433 QsFTKGINTIIGEggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDT--TMIVIAHRDNT 510
Cdd:TIGR03269 157 Q-LSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250
....*....|....*..
gi 446659814 511 IRHL-QRRLYIENGRLI 526
Cdd:TIGR03269 232 IEDLsDKAIWLENGEIK 248
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
13-245 |
8.89e-12 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 65.87 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 13 IFPVLMFLVSTGLGIL--VITQNIlIADFLAKIiRHQFQGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKV------- 83
Cdd:cd18544 2 ILALLLLLLATALELLgpLLIKRA-IDDYIVPG-QGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIiydlrrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 84 --KHMLRQRVIYKNNgHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFY 161
Cdd:cd18544 80 lfSHIQRLPLSFFDR-TPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 162 IIFGLKTRD---ESKDQMTYLNQFSQRFLNiakGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFIS 238
Cdd:cd18544 159 YLFRKKSRKayrEVREKLSRLNAFLQESIS---GMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLS 235
|
....*..
gi 446659814 239 MLGIGLV 245
Cdd:cd18544 236 SLALALV 242
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
324-511 |
1.51e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 324 QLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRdLNIGILSQQpyifsas 403
Cdd:PRK11147 321 EMENVNYQIDG--KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-LEVAYFDQH------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 404 iKENITMFKDIENNTIE---EVldEVG-----LLDKVQSF---TKGINTIIgeggEMLSGGQMRRIELCRLLvMKP-DLV 471
Cdd:PRK11147 391 -RAELDPEKTVMDNLAEgkqEV--MVNgrprhVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLF-LKPsNLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446659814 472 IFDEPATGLDIQT----EHMIQNvlfqhFKDTTMIVIAHR---DNTI 511
Cdd:PRK11147 463 ILDEPTNDLDVETlellEELLDS-----YQGTVLLVSHDRqfvDNTV 504
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
340-529 |
1.74e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL-------------NIGILSQQPY-------- 398
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpeaqkllrqKIQIVFQNPYgslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 399 ---IFSASIKENITMFKDIENNTIEEVLDEVGLldKVQSFtkgintiiGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDE 475
Cdd:PRK11308 111 vgqILEEPLLINTSLSAAERREKALAMMAKVGL--RPEHY--------DRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 476 PATGLDIQTEHMIQNVLF---QHFKdTTMIVIAHRDNTIRHlqrrlyiengrlIADD 529
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMdlqQELG-LSYVFISHDLSVVEH------------IADE 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
323-511 |
2.09e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLnlEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGT-ISTNQRdlnIGILS--QQPYI 399
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLPSL--TLNAGDSWAFVGANGSGKSALARALAGELPLLSGErQSQFSH---ITRLSfeQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 FSASIKENIT-MFKDIENNT----IEEVLDEVGLLDKVQSFTK--GINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVI 472
Cdd:PRK10938 79 VSDEWQRNNTdMLSPGEDDTgrttAEIIQDEVKDPARCEQLAQqfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446659814 473 FDEPATGLDIQTEHMIQNVLFQ-HFKDTTMIVIAHRDNTI 511
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEI 198
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
336-528 |
2.84e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.88 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGILSQQPYifsasIK 405
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlssrqlarrLALLPQHHL-----TP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 406 ENITMFKDIE-----NNTIEEVL--DEVGLLDKVQSFTkGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPAT 478
Cdd:PRK11231 89 EGITVRELVAygrspWLSLWGRLsaEDNARVNQAMEQT-RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 479 GLDI--QTEHMiqnVLFQHFKDT--TMIVIAHRDN-TIRHLQRRLYIENGRLIAD 528
Cdd:PRK11231 168 YLDInhQVELM---RLMRELNTQgkTVVTVLHDLNqASRYCDHLVVLANGHVMAQ 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
323-528 |
3.47e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.96 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYD-DSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IG 391
Cdd:PRK13642 5 LEVENLVFKYEkESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaenvwnlrrkIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQP--YIFSASIKENITMfkDIENNTI--EEvldevgLLDKVQSFTKGINTIIGEGGE--MLSGGQMRRIELCRLLV 465
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAF--GMENQGIprEE------MIKRVDEALLAVNMLDFKTREpaRLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 466 MKPDLVIFDEPATGLDIQTEHMIQNVLFQhFKDT---TMIVIAHRDNTIRHLQRRLYIENGRLIAD 528
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
323-399 |
3.91e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.56 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGI 392
Cdd:COG4604 2 IEIKNVSKRYGG--KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAttpsrelakrLAI 79
|
....*..
gi 446659814 393 LSQQPYI 399
Cdd:COG4604 80 LRQENHI 86
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
336-526 |
4.92e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAG--VYQPTIGTISTNQRDL---------NIGILSQQPYIFSASI 404
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESIldlepeeraHLGIFLAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 405 KENITMFKDIENNT-----------------IEEVLDEVGLldkVQSFtkgINTIIGEGgemLSGGQMRRIELCRLLVMK 467
Cdd:CHL00131 99 VSNADFLRLAYNSKrkfqglpeldplefleiINEKLKLVGM---DPSF---LSRNVNEG---FSGGEKKRNEILQMALLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 468 PDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIahrdntIRHLQRRL-YI--------ENGRLI 526
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMTSENSIIL------ITHYQRLLdYIkpdyvhvmQNGKII 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
323-525 |
5.42e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.60 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYD-DSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IG 391
Cdd:PRK13650 5 IEVKNLTFKYKeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeenvwdirhkIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQP--YIFSASIKENITMfkDIEN---------NTIEEVLDEVGLLD-KVQSFTKgintiigeggemLSGGQMRRIE 459
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAF--GLENkgipheemkERVNEALELVGMQDfKEREPAR------------LSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446659814 460 LCRLLVMKPDLVIFDEPATGLD-------IQTehmIQNVLFQHfkDTTMIVIAHRDNTIRHLQRRLYIENGRL 525
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDpegrlelIKT---IKGIRDDY--QMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-506 |
9.01e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 62.24 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTL----THLIAGVYQPTI-GTISTNQRDL----------NIGILSQQPY-IFSA 402
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLlrvfNRLIELYPEARVsGEVYLDGQDIfkmdvielrrRVQMVFQIPNpIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 SIKENITMFKDIEN--NTIEEVLDEVG-LLDKVQSFTKGINTIIGEGGEmLSGGQMRRIELCRLLVMKPDLVIFDEPATG 479
Cdd:PRK14247 98 SIFENVALGLKLNRlvKSKKELQERVRwALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180
....*....|....*....|....*..
gi 446659814 480 LDIQTEHMIQNVLFQHFKDTTMIVIAH 506
Cdd:PRK14247 177 LDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
321-520 |
1.38e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.04 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTnQRDLNIGILSQQPYIF 400
Cdd:PRK10636 311 PLLKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLGYFAQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 401 SASIKENITMFKDIENNTIEEVL-DEVGLL----DKVQSFTkgintiigeggEMLSGGQMRRIELCRLLVMKPDLVIFDE 475
Cdd:PRK10636 388 LRADESPLQHLARLAPQELEQKLrDYLGGFgfqgDKVTEET-----------RRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446659814 476 PATGLDIQTEHMIQNVLFQHfkDTTMIVIAHRDNTIRHLQRRLYI 520
Cdd:PRK10636 457 PTNHLDLDMRQALTEALIDF--EGALVVVSHDRHLLRSTTDDLYL 499
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
314-506 |
2.49e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.79 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 314 KYEENQ-KPFIQLTDISFRyddsdrlvlndlnleiFKGDQI-ALVGPSGAGKSTLTHLIAGVYQPTIGTISTnqRDLNIG 391
Cdd:PRK13631 30 VFDEKQeNELVALNNISYT----------------FEKNKIyFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ----ILSQQPYIFSASIK------ENITM---------FKDiennTIEE--VLDEVGL-LDKVQSFTKGINTIIGEGGEM 449
Cdd:PRK13631 92 dkknNHELITNPYSKKIKnfkelrRRVSMvfqfpeyqlFKD----TIEKdiMFGPVALgVKKSEAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 450 ---------LSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEH-MIQNVLFQHFKDTTMIVIAH 506
Cdd:PRK13631 168 sylerspfgLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITH 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
340-529 |
2.85e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRD---------LNIGIL----SQqpYIFSASIKE 406
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrrkefaRRIGVVfgqrSQ--LWWDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 407 NITMFK---DIENNTIEEVLDE-VGLLDkVQSFtkgINTIIGEggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDI 482
Cdd:COG4586 116 SFRLLKaiyRIPDAEYKKRLDElVELLD-LGEL---LDTPVRQ----LSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446659814 483 QTEHMIQNVL--FQHFKDTTMIVIAHRDNTIRHLQRRLY-IENGRLIADD 529
Cdd:COG4586 188 VSKEAIREFLkeYNRERGTTILLTSHDMDDIEALCDRVIvIDHGRIIYDG 237
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
317-481 |
2.97e-10 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 60.97 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 317 ENQKPFIQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIS-------------- 382
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLE--VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRvggeeirlkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 383 ----TNQRDL-----NIGILSQQPYIFS-ASIKENIT--------MFKDIENNTIEEVLDEVGLLDKVQSFTKgintiig 444
Cdd:COG4598 81 elvpADRRQLqrirtRLGMVFQSFNLWShMTVLENVIeapvhvlgRPKAEAIERAEALLAKVGLADKRDAYPA------- 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 446659814 445 eggeMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLD 481
Cdd:COG4598 154 ----HLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
323-484 |
4.97e-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: 61.87 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQrDLNIGILSQQpyifsa 402
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-TVKLAYVDQS------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 siKENItmfkDIENNTIEEVLDevGlLDKVQSFTKGINT--IIG----EGGE------MLSGGQMRRIELCRLLVMKPDL 470
Cdd:TIGR03719 394 --RDAL----DPNKTVWEEISG--G-LDIIKLGKREIPSraYVGrfnfKGSDqqkkvgQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|....
gi 446659814 471 VIFDEPATGLDIQT 484
Cdd:TIGR03719 465 LLLDEPTNDLDVET 478
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
335-482 |
6.08e-10 |
|
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: 58.60 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 335 SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIgilsqqpYIFSASIKENITMFKdi 414
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR-------RSPRDAIRAGIAYVP-- 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 415 enntiEEVLDEvGLldkVQSFTKGINTIIGEggeMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDI 482
Cdd:cd03215 82 -----EDRKRE-GL---VLDLSVAENIALSS---LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
323-518 |
7.02e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.63 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDdSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------IGILS 394
Cdd:PRK11650 4 LKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNelepadrdIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQ----PYIfsaSIKENItmfkdienntieevldEVGLldKVQSFTKG-INTIIGEGGEM-------------LSGGQMR 456
Cdd:PRK11650 83 QNyalyPHM---SVRENM----------------AYGL--KIRGMPKAeIEERVAEAARIleleplldrkpreLSGGQRQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 457 RIELCRLLVMKPDLVIFDEPATGLD----IQtehmiqnvlfqhfkdttMIViahrdnTIRHLQRRL 518
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDaklrVQ-----------------MRL------EIQRLHRRL 184
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
335-518 |
9.85e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 9.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 335 SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQrDLNIGILSQQP----------YIfSASI 404
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIVARLQQDPprnvegtvydFV-AEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 405 KENITMFK-------DIENNTIEEVLDEvglLDKVQS---------FTKGINTI---IGEGGEM----LSGGQMRRIELC 461
Cdd:PRK11147 92 EEQAEYLKryhdishLVETDPSEKNLNE---LAKLQEqldhhnlwqLENRINEVlaqLGLDPDAalssLSGGWLRKAALG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 462 RLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHFKDtTMIVIAHRDNTIRHLQRRL 518
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNMATRI 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-481 |
1.17e-09 |
|
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: 60.11 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 354 ALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--------------NIGILSQQPYIFS-ASIKENIT-----MFKD 413
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargiflpphrrRIGYVFQEARLFPhLSVRGNLLygrkrAPRA 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 414 IENNTIEEVLDEVG---LLDkvqsftKGINTiigeggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLD 481
Cdd:COG4148 109 ERRISFDEVVELLGighLLD------RRPAT--------LSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
321-528 |
1.24e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.89 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDSDRL--VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGT-------ISTNQRDL--- 388
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdVATLDADAlaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 ----NIGILSQQPYIFS-ASIKENI---TMFKDIENNT----IEEVLDEVGLLDKVqSFTKGintiigeggeMLSGGQMR 456
Cdd:PRK10535 83 lrreHFGFIFQRYHLLShLTAAQNVevpAVYAGLERKQrllrAQELLQRLGLEDRV-EYQPS----------QLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446659814 457 RIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQ-HFKDTTMIVIAHRDNTIRHLQRRLYIENGRLIAD 528
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
337-488 |
1.26e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.94 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 337 RLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGILSQQPYIFSA---S 403
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykrakyIGRVFQDPMMGTApsmT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 404 IKENITM----------FKDIENNTIEEVLDEV-----GLLDKvqsftkgINTIIGeggeMLSGGQmrRIELCrlLVM-- 466
Cdd:COG1101 99 IEENLALayrrgkrrglRRGLTKKRRELFRELLatlglGLENR-------LDTKVG----LLSGGQ--RQALS--LLMat 163
|
170 180
....*....|....*....|....
gi 446659814 467 --KPDLVIFDEPATGLDIQTEHMI 488
Cdd:COG1101 164 ltKPKLLLLDEHTAALDPKTAALV 187
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
13-245 |
1.40e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 59.37 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 13 IFPVLMFLVSTGLGILV--ITQNILiaDFLakIIRHQFQGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKVKHMLRQR 90
Cdd:cd18542 2 LLAILALLLATALNLLIplLIRRII--DSV--IGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 91 vIYKN---------NGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFY 161
Cdd:cd18542 78 -LYDHlqrlsfsfhDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 162 IIFGLKTR---DESKDQMTYLNQFSQRflNIAkGLVTLKLFNRtEQTEKHIYDD-STQFRTLTMRI--LRSAFLSglMLE 235
Cdd:cd18542 157 YVFFKKVRpafEEIREQEGELNTVLQE--NLT-GVRVVKAFAR-EDYEIEKFDKeNEEYRDLNIKLakLLAKYWP--LMD 230
|
250
....*....|
gi 446659814 236 FISMLGIGLV 245
Cdd:cd18542 231 FLSGLQIVLV 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
323-524 |
1.57e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKST-------LTHLIAGVY----------------QPTIG 379
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVYpsgdirfhgesllhasEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 380 TISTNQrdlnIGILSQQPYIfSASIKENIT------------MFKDIENNTIEEVLDEVGLLDKVQSftkgintiIGEGG 447
Cdd:PRK15134 88 GVRGNK----IAMIFQEPMV-SLNPLHTLEkqlyevlslhrgMRREAARGEILNCLDRVGIRQAAKR--------LTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 448 EMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHRDNTIRHLQRRLYI-ENGR 524
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVmQNGR 234
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
313-503 |
1.95e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 313 LKYEENQKPF---IQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI--STNQrd 387
Cdd:PRK15064 307 IRFEQDKKLHrnaLEVENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENA-- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 388 lNIGILSQQPyifSASIKENITMFKDIENNTIEEVLDEV--GLLDKVQsFTkgiNTIIGEGGEMLSGGQMRRIELCRLLV 465
Cdd:PRK15064 383 -NIGYYAQDH---AYDFENDLTLFDWMSQWRQEGDDEQAvrGTLGRLL-FS---QDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190
....*....|....*....|....*....|....*...
gi 446659814 466 MKPDLVIFDEPATGLDIQTEHMIQNVLfQHFKDTTMIV 503
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMAL-EKYEGTLIFV 491
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
319-506 |
2.07e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.74 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 319 QKPFIQLTDISFRYDDSdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-------IG 391
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqalqknlVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 392 ILSQQPYI---FSASIKENITM-----------FKDIENNTIEEVLDEVGLLDKVQSftkgintIIGEggemLSGGQMRR 457
Cdd:PRK15056 82 YVPQSEEVdwsFPVLVEDVVMMgryghmgwlrrAKKRDRQIVTAALARVDMVEFRHR-------QIGE----LSGGQKKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446659814 458 IELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHFKDT--TMIVIAH 506
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL-RELRDEgkTMLVSTH 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
323-481 |
2.25e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI--------STNQRDlnigilS 394
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdmaDARHRR------A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 QQPYIfsA--------------SIKENITMF-------KDIENNTIEEVLDEVGLldkvQSFT-----Kgintiigegge 448
Cdd:NF033858 74 VCPRI--AympqglgknlyptlSVFENLDFFgrlfgqdAAERRRRIDELLRATGL----APFAdrpagK----------- 136
|
170 180 190
....*....|....*....|....*....|...
gi 446659814 449 mLSGGQMRRIELCRLLVMKPDLVIFDEPATGLD 481
Cdd:NF033858 137 -LSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
321-481 |
2.31e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 321 PFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYqP------------------TIGTIS 382
Cdd:PRK10938 259 PRIVLNNGVVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PqgysndltlfgrrrgsgeTIWDIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 383 TnqrdlNIGILSQQ---PYIFSASIKENItmfkdienntIEEVLDEVGLL----DKVQSFTKGINTIIGEGGEM------ 449
Cdd:PRK10938 336 K-----HIGYVSSSlhlDYRVSTSVRNVI----------LSGFFDSIGIYqavsDRQQKLAQQWLDILGIDKRTadapfh 400
|
170 180 190
....*....|....*....|....*....|...
gi 446659814 450 -LSGGQMRRIELCRLLVMKPDLVIFDEPATGLD 481
Cdd:PRK10938 401 sLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
312-518 |
2.34e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 312 LLKYEENQKPFIQLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQR----- 386
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 387 ------DLNIGILSQQPYIF-SASIKENItMFKDIENNTIEEVLDEvglldKVQSFTKGINTIIGEGGEMLSGGQMrrIE 459
Cdd:PRK15439 79 tpakahQLGIYLVPQEPLLFpNLSVKENI-LFGLPKRQASMQKMKQ-----LLAALGCQLDLDSSAGSLEVADRQI--VE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 460 LCRLLVMKPDLVIFDEPATGLD-IQTEHmiqnvLFQHF-----KDTTMIVIAHRDNTIRHLQRRL 518
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTpAETER-----LFSRIrellaQGVGIVFISHKLPEIRQLADRI 210
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
319-529 |
2.77e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.58 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 319 QKPFIQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN--------- 389
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqtakimr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 --IGILSQQPYIFS-ASIKENITM---FKDIE--NNTIEEVLDevglldkvqSFTKGINTIIGEGGEMlSGGQMRRIELC 461
Cdd:PRK11614 80 eaVAIVPEGRRVFSrMTVEENLAMggfFAERDqfQERIKWVYE---------LFPRLHERRIQRAGTM-SGGEQQMLAIG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 462 RLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKD-TTMIVIAHRDNTIRHLQRRLYI-ENGRLIADD 529
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVlENGHVVLED 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
340-528 |
2.92e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.10 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTL----THLIAGVYQP---------TIGTISTNQRDLNIGiLSQQPYIFSA---- 402
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITGDKSAgshiellgrTVQREGRLARDIRKS-RANTGYIFQQfnlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 ---SIKENITM---------------FKDIENNTIEEVLDEVGLldkVQSFTKGINTiigeggemLSGGQMRRIELCRLL 464
Cdd:PRK09984 99 nrlSVLENVLIgalgstpfwrtcfswFTREQKQRALQALTRVGM---VHFAHQRVST--------LSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446659814 465 VMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHR-DNTIRHLQRRLYIENGRLIAD 528
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQvDYALRYCERIVALRQGHVFYD 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
326-481 |
4.44e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.71 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 326 TDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNI---GILS-------- 394
Cdd:PRK13638 5 SDLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrGLLAlrqqvatv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 395 -QQP--YIFSASIKENITM-FKDI---ENNTIEEVLDEVGLLDkVQSFTKgintiigEGGEMLSGGQMRRIELCRLLVMK 467
Cdd:PRK13638 83 fQDPeqQIFYTDIDSDIAFsLRNLgvpEAEITRRVDEALTLVD-AQHFRH-------QPIQCLSHGQKKRVAIAGALVLQ 154
|
170
....*....|....
gi 446659814 468 PDLVIFDEPATGLD 481
Cdd:PRK13638 155 ARYLLLDEPTAGLD 168
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-523 |
6.17e-09 |
|
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: 56.65 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 346 EIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDlnigiLSQQP-YI---FSASIKEnitMFKDIENNTIEE 421
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----VSYKPqYIkadYEGTVRD---LLSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 422 VLDEVGLLDKVQsftkgINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDT 499
Cdd:cd03237 93 PYFKTEIAKPLQ-----IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIrrFAENNEK 167
|
170 180
....*....|....*....|....
gi 446659814 500 TMIVIAHRDNTIRHLQRRLYIENG 523
Cdd:cd03237 168 TAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
353-494 |
7.19e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 353 IALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIG----------ILSQQP-----------YIFSASIKENITMF 411
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdysyrsqrirMIFQDPstslnprqrisQILDFPLRLNTDLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 412 KDIENNTIEEVLDEVGLLDKVQSFTKgintiigeggEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNV 491
Cdd:PRK15112 122 PEQREKQIIETLRQVGLLPDHASYYP----------HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINL 191
|
...
gi 446659814 492 LFQ 494
Cdd:PRK15112 192 MLE 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
340-483 |
7.45e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.16 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVyQPTIGTISTNQRDLN-------------IGILSQQPYifsAS--- 403
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDglsrralrplrrrMQVVFQDPF---GSlsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 404 -------IKE-----NITMFKDIENNTIEEVLDEVGLLdkvqsftkgintiigegGEML-------SGGQMRRIELCRLL 464
Cdd:COG4172 378 rmtvgqiIAEglrvhGPGLSAAERRARVAEALEEVGLD-----------------PAARhryphefSGGQRQRIAIARAL 440
|
170 180
....*....|....*....|.
gi 446659814 465 VMKPDLVIFDEPATGLD--IQ 483
Cdd:COG4172 441 ILEPKLLVLDEPTSALDvsVQ 461
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
309-506 |
7.78e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 309 NEFLLKY--EENQKpfIQLTDISF------RYDDSDRLV--------LNDLNL-----EIFKGDQIALVGPSGAGKSTLT 367
Cdd:PRK13409 305 NEYLKGYlpEENMR--IRPEPIEFeerpprDESERETLVeypdltkkLGDFSLeveggEIYEGEVIGIVGPNGIGKTTFA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 368 HLIAGVYQPTIGTISTNQRdlnigiLSQQP-YI---FSASIKENITMFKDIENNTI--EEVLDEVGlLDKVqsFTKGINT 441
Cdd:PRK13409 383 KLLAGVLKPDEGEVDPELK------ISYKPqYIkpdYDGTVEDLLRSITDDLGSSYykSEIIKPLQ-LERL--LDKNVKD 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 442 iigeggemLSGGQMRR--IELCrlLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHF---KDTTMIVIAH 506
Cdd:PRK13409 454 --------LSGGELQRvaIAAC--LSRDADLYLLDEPSAHLDVEQRLAVAKAI-RRIaeeREATALVVDH 512
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-528 |
2.43e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.49 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 354 ALVGPSGAGKSTLTHLIAGVYQPTIGTIST-----------NQRDL-----NIGILSQQPYIFSASIKENI----TMFKD 413
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSgdvllggrsifNYRDVlefrrRVGMLFQRPNPFPMSIMDNVlagvRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 414 IENNTIEEV----LDEVGLLDKVQSFtkgintiIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQ 489
Cdd:PRK14271 131 VPRKEFRGVaqarLTEVGLWDAVKDR-------LSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446659814 490 NVLFQHFKDTTMIVIAHR-DNTIRHLQRRLYIENGRLIAD 528
Cdd:PRK14271 204 EFIRSLADRLTVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
339-528 |
2.95e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI----------STNQRDLNIGILSQqpyifsasikeNI 408
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyASKEVARRIGLLAQ-----------NA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 409 TMFKDIennTIEEVL-----------------DEVGLLDKVQSftKGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLV 471
Cdd:PRK10253 91 TTPGDI---TVQELVargryphqplftrwrkeDEEAVTKAMQA--TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 472 IFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHRDN-TIRHLQRRLYIENGRLIAD 528
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLseLNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQ 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
335-492 |
4.82e-08 |
|
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: 53.40 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 335 SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGvyQPTIGTISTN------QRDLNIGILS---QQPYIFSASIk 405
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITGEilingrPLDKNFQRSTgyvEQQDVHSPNL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 406 enitmfkdiennTIEEVLDEVGLLdkvqsftKGintiigeggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTE 485
Cdd:cd03232 95 ------------TVREALRFSALL-------RG-----------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
....*..
gi 446659814 486 HMIQNVL 492
Cdd:cd03232 145 YNIVRFL 151
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
314-381 |
5.57e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 5.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 314 KYEENQKPFIQLTDISFRYDDSD-RLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI 381
Cdd:PRK13545 13 KYKMYNKPFDKLKDLFFRSKDGEyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
317-506 |
6.02e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.73 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 317 ENQKPFIQLTD--ISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTiGTIS------------ 382
Cdd:PRK09473 7 QQADALLDVKDlrVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIGgsatfngreiln 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 383 TNQRDLN------IGILSQ------QPYI-FSASIKENITMFKDIENNtiEEVLDEVGLLDKVQ--SFTKGINTIIGEgg 447
Cdd:PRK09473 86 LPEKELNklraeqISMIFQdpmtslNPYMrVGEQLMEVLMLHKGMSKA--EAFEESVRMLDAVKmpEARKRMKMYPHE-- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446659814 448 emLSGGQMRRIELCRLLVMKPDLVIFDEPATGLD--IQTEHM-IQNVLFQHFkDTTMIVIAH 506
Cdd:PRK09473 162 --FSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtVQAQIMtLLNELKREF-NTAIIMITH 220
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
318-497 |
6.25e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRYDDSDrlVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI-------STNQRDLNI 390
Cdd:PRK13543 7 TAPPLLAAHALAFSRNEEP--VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDRSRFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 391 GILSQQPyifsaSIKENITMFKDIE----------NNTIEEVLDEVGLLDKVQSFTKgintiigeggeMLSGGQMRRIEL 460
Cdd:PRK13543 85 AYLGHLP-----GLKADLSTLENLHflcglhgrraKQMPGSALAIVGLAGYEDTLVR-----------QLSAGQKKRLAL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 446659814 461 CRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFK 497
Cdd:PRK13543 149 ARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLR 185
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
339-381 |
6.94e-08 |
|
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: 53.21 E-value: 6.94e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTI 381
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI 68
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
323-526 |
1.51e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.09 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 323 IQLTDISFRYDDSDRL---VLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVY-----QPTIG--TISTNQRDLN--- 389
Cdd:PRK13645 7 IILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGdyAIPANLKKIKevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 -----IGILSQQP--YIFSASIKENITMFKDIENNTIEEVLDEV-GLLDKVQSFTKGINTIIGEggemLSGGQMRRIELC 461
Cdd:PRK13645 87 rlrkeIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVpELLKLVQLPEDYVKRSPFE----LSGGQKRRVALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 462 RLLVMKPDLVIFDEPATGLDIQTEHMIQNV---LFQHFKDTTMIVIAHRDNTIRHLQRRLYIENGRLI 526
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
353-524 |
1.61e-07 |
|
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: 50.83 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 353 IALVGPSGAGKSTLTHLIAGVYQPTIGTIstnqrdlnigilsqqpyifsasikenitMFKDIENNTIEEVLDEvglldkv 432
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGV----------------------------IYIDGEDILEEVLDQL------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 433 qsftkgINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQ-------NVLFQHFKDTTMIVIA 505
Cdd:smart00382 50 ------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLLLKSEKNLTVILTT 123
|
170 180
....*....|....*....|....*
gi 446659814 506 HR------DNTIRHLQRRLYIENGR 524
Cdd:smart00382 124 NDekdlgpALLRRRFDRRIVLLLIL 148
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-482 |
1.68e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 52.62 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 320 KPFIQLTDISFRYDDsdRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDlnigilSQQPYI 399
Cdd:PRK11701 4 QPLLSVRGLTKLYGP--RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD------GQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 400 FSASIKENITMFKD----IENN-------------TIEEVLDEVGL-------------LDKVQsftkgINTI-IGEGGE 448
Cdd:PRK11701 76 YALSEAERRRLLRTewgfVHQHprdglrmqvsaggNIGERLMAVGArhygdiratagdwLERVE-----IDAArIDDLPT 150
|
170 180 190
....*....|....*....|....*....|....
gi 446659814 449 MLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDI 482
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
335-482 |
2.10e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.48 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 335 SDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNI---------------------GIL 393
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdairagiayvpedrkgeGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQpyifsaSIKENITM--FKDI----------ENNTIEEVLDEVGLldKvqsfTKGINTIIGEggemLSGGQMRRIELC 461
Cdd:COG1129 343 LDL------SIRENITLasLDRLsrgglldrrrERALAEEYIKRLRI--K----TPSPEQPVGN----LSGGNQQKVVLA 406
|
170 180
....*....|....*....|.
gi 446659814 462 RLLVMKPDLVIFDEPATGLDI 482
Cdd:COG1129 407 KWLATDPKVLILDEPTRGIDV 427
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
354-530 |
2.85e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.57 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 354 ALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--------------NIGILSQQPYIFSA-SIKENIT--------- 409
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekgiclppekrRIGYVFQDARLFPHyKVRGNLRygmaksmva 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 410 MFKDIenntieevldeVGLLdkvqsftkGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDI--QTEHM 487
Cdd:PRK11144 108 QFDKI-----------VALL--------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprKRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446659814 488 --IQNvLFQHFKdTTMIVIAHRDNTIRHL-QRRLYIENGRLIADDR 530
Cdd:PRK11144 169 pyLER-LAREIN-IPILYVSHSLDEILRLaDRVVVLEQGKVKAFGP 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
338-526 |
3.98e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 52.34 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 338 LVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL--------------NIGILSQQPYIFS-A 402
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisdaelrevrrkKIAMVFQSFALMPhM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 SIKENITMFKDIENNTIEE-------VLDEVGLLDKVQSFTkgintiigeggEMLSGGQMRRIELCRLLVMKPDLVIFDE 475
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEErrekaldALRQVGLENYAHSYP-----------DELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446659814 476 PATGLD--IQTEHMIQNVLFQHFKDTTMIVIAHR-DNTIRHLQRRLYIENGRLI 526
Cdd:PRK10070 191 AFSALDplIRTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVV 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
339-514 |
4.37e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 339 VLNDLNLEIFKGDQIALVGPSGAGKST----LTHLIAgvyqpTIGTISTNQRDLN-------------IGILSQQPYifs 401
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHnlnrrqllpvrhrIQVVFQDPN--- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 402 ASIKENITMFKDIE---------------NNTIEEVLDEVGLLDKVQSFTKGintiigeggeMLSGGQMRRIELCRLLVM 466
Cdd:PRK15134 373 SSLNPRLNVLQIIEeglrvhqptlsaaqrEQQVIAVMEEVGLDPETRHRYPA----------EFSGGQRQRIAIARALIL 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446659814 467 KPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAHRDNTIRHL 514
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLksLQQKHQLAYLFISHDLHVVRAL 492
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
323-382 |
4.75e-07 |
|
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: 52.49 E-value: 4.75e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446659814 323 IQLTDISFRY---DDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIS 382
Cdd:COG4615 328 LELRGVTYRYpgeDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL 390
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
13-247 |
4.81e-07 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 51.64 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 13 IFPVLMFLVSTGLGIL--VITQNI--LIADFLAKIIRHQFQGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKVKHMLR 88
Cdd:cd18547 2 ILVIILAIISTLLSVLgpYLLGKAidLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 89 QRVIYKNN--------GHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLF 160
Cdd:cd18547 82 KDLFEKLQrlplsyfdTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 161 YIIFGLKTRDESKDQMTY---LNQFSQRFLNiakGLVTLKLFNRTEQTEKhiyddstQFRTLTMRILRSA----FLSGLM 233
Cdd:cd18547 162 TKFIAKRSQKYFRKQQKAlgeLNGYIEEMIS---GQKVVKAFNREEEAIE-------EFDEINEELYKASfkaqFYSGLL 231
|
250
....*....|....*..
gi 446659814 234 ---LEFISMLGIGLVAL 247
Cdd:cd18547 232 mpiMNFINNLGYVLVAV 248
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
336-490 |
5.30e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGV--YQPTIGTISTNQRDL-----------NIGILSQQP----- 397
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLlelspedrageGIFMAFQYPveipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 398 ---YIFSASIKENITMFKDIE-------NNTIEEvldEVGLLDKVQS-FTKGINtiIGeggemLSGGQMRRIELCRLLVM 466
Cdd:PRK09580 93 vsnQFFLQTALNAVRSYRGQEpldrfdfQDLMEE---KIALLKMPEDlLTRSVN--VG-----FSGGEKKRNDILQMAVL 162
|
170 180
....*....|....*....|....
gi 446659814 467 KPDLVIFDEPATGLDIQTEHMIQN 490
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVAD 186
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
340-530 |
5.51e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.66 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTlTHLIAGVYQPTIG-------TISTNQRDLNIGILSQQPYIF----SASIKENI 408
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGrrpwrf*TWCANRRALRRTIG*HRPVR*grreSFSGRENL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 409 TMFK---DIENNTIEEVLDEvgLLDKVqSFTKGIntiiGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTE 485
Cdd:NF000106 108 YMIGr*lDLSRKDARARADE--LLERF-SLTEAA----GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446659814 486 HMIQNVLFQHFKD--TTMIVIAHRDNTIRHLQRRLYIENGRLIADDR 530
Cdd:NF000106 181 NEVWDEVRSMVRDgaTVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
16-245 |
7.06e-07 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 50.88 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 16 VLMFLVS-TGLGILVITQNILIADFLAKiirhQFQGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKVKHMLRQRvIYK 94
Cdd:cd18552 6 LGMILVAaTTAALAWLLKPLLDDIFVEK----DLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND-LFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 95 N---------NGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIFG 165
Cdd:cd18552 81 KllrlplsffDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 166 LKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFISMLGIGLV 245
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
334-515 |
7.38e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 334 DSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTnqRDLNIGILsQQPYI----FSASIKENIT 409
Cdd:PRK13541 10 NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNI-AKPYCtyigHNLGLKLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 410 MFKDIEnnTIEEVLDEVGLLDKVQSFTKgINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQ 489
Cdd:PRK13541 87 VFENLK--FWSEIYNSAETLYAAIHYFK-LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170 180
....*....|....*....|....*..
gi 446659814 490 NVLFQHFKDTTMIVIA-HRDNTIRHLQ 515
Cdd:PRK13541 164 NLIVMKANSGGIVLLSsHLESSIKSAQ 190
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
340-485 |
8.53e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN-----------IGILSQQ-PYIFSASIKEN 407
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqeagIGIIHQElNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 408 ITMFKDIEN--NTIE--EVLDEVGLLDKVQSFTKGINTIIGEggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGL-DI 482
Cdd:PRK10762 100 IFLGREFVNrfGRIDwkKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDT 175
|
...
gi 446659814 483 QTE 485
Cdd:PRK10762 176 ETE 178
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
324-527 |
1.52e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 324 QLTDISFRYddSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN----------IGIL 393
Cdd:PRK10575 13 ALRNVSFRV--PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswsskafarkVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 394 SQQ-PYIFSASIKENITM-----------FKDIENNTIEEVLDEVGLLDKVQSFTkgintiigeggEMLSGGQMRRIELC 461
Cdd:PRK10575 91 PQQlPAAEGMTVRELVAIgrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLV-----------DSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 462 RLLVMKPDLVIFDEPATGLDI--QTE--HMIQNVlfQHFKDTTMIVIAHRDN-TIRHLQRRLYIENGRLIA 527
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIahQVDvlALVHRL--SQERGLTVIAVLHDINmAARYCDYLVALRGGEMIA 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
318-520 |
1.69e-06 |
|
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: 51.17 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIG-------TISTNQRDL-- 388
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagkSILTNISDVhq 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 NIGILSQqpyiFSA-----SIKENITMFKDIENNTIEEVldevgllDKVQSF---TKGINTIIGEGGEMLSGGQMRRIEL 460
Cdd:TIGR01257 2013 NMGYCPQ----FDAiddllTGREHLYLYARLRGVPAEEI-------EKVANWsiqSLGLSLYADRLAGTYSGGNKRKLST 2081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 461 CRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVI-AHRDNTIRHLQRRLYI 520
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLtSHSMEECEALCTRLAI 2142
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
13-245 |
1.73e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 49.84 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 13 IFPVLMFLVSTGLGILVITQNILIADfLAKIIRHQFQGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKVKHMLRQRVI 92
Cdd:cd18778 2 ILTLLCALLSTLLGLVPPWLIRELVD-LVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 93 ---------YKNNgHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYII 163
Cdd:cd18778 81 dklqrlslrYFDD-RQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 164 FGLKTR---DESKDQMTYLNQFSQRflNIAkGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILR-SAFLSGLMlEFISM 239
Cdd:cd18778 160 YSKKVRpryRKVREALGELNALLQD--NLS-GIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKlWAIFHPLM-EFLTS 235
|
....*.
gi 446659814 240 LGIGLV 245
Cdd:cd18778 236 LGTVLV 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
328-483 |
1.80e-06 |
|
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: 50.45 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 328 ISFRYDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKS-----TLTHLIAGVYQPTiGTISTNQRDLnigilsqqpyiFSA 402
Cdd:COG4172 14 VAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalsILRLLPDPAAHPS-GSILFDGQDL-----------LGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 403 SIKE-------NITM-FKD----------IENNTIE------------------EVLDEVGLLD---KVQSFTkgintii 443
Cdd:COG4172 82 SERElrrirgnRIAMiFQEpmtslnplhtIGKQIAEvlrlhrglsgaaararalELLERVGIPDperRLDAYP------- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446659814 444 geggEMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLD--IQ 483
Cdd:COG4172 155 ----HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtVQ 192
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
83-243 |
3.21e-06 |
|
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: 48.97 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 83 VKHMLRQRVIYKNNgHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYI 162
Cdd:cd18551 76 WRRLLRLPVSFFDR-RRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIIL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 163 IFGLKTRDESKDQMTYLNQFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILR-SAFLS-----GLMLEF 236
Cdd:cd18551 155 PLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKiEALIGplmglAVQLAL 234
|
....*..
gi 446659814 237 ISMLGIG 243
Cdd:cd18551 235 LVVLGVG 241
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
337-528 |
3.40e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 337 RLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTI--------GTISTNQRDLNI----------GILSQ--Q 396
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAidaprlarlrAVLPQaaQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 397 PyIFSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEGGEMLSGGQMRRIELCRLL---------VMK 467
Cdd:PRK13547 94 P-AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446659814 468 PDLVIFDEPATGLDIQTEHMIQNVLFQHFKDTTMIVIA--HRDN-TIRHLQRRLYIENGRLIAD 528
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNlAARHADRIAMLADGAIVAH 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
320-482 |
5.44e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 320 KPFIQLTDISFRyDDSDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIS------TNQ-----RDL 388
Cdd:COG3845 255 EVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRldgediTGLsprerRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 389 NIGILSQQPY----IFSASIKENITM---------------FKDIENNTieevldevglLDKVQSF---TKGINTIIGeg 446
Cdd:COG3845 334 GVAYIPEDRLgrglVPDMSVAENLILgryrrppfsrggfldRKAIRAFA----------EELIEEFdvrTPGPDTPAR-- 401
|
170 180 190
....*....|....*....|....*....|....*.
gi 446659814 447 geMLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDI 482
Cdd:COG3845 402 --SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
336-484 |
6.86e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 336 DRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIStnqrdlnIGILSQQPYI--FSASIKENITMFkd 413
Cdd:PRK11819 336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-------IGETVKLAYVdqSRDALDPNKTVW-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 414 ienntiEEV---LDEVGLLDK-------VQSFT-KGI--NTIIGeggeMLSGGQMRRIELCRLLVMKPDLVIFDEPATGL 480
Cdd:PRK11819 407 ------EEIsggLDIIKVGNReipsrayVGRFNfKGGdqQKKVG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
....
gi 446659814 481 DIQT 484
Cdd:PRK11819 477 DVET 480
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
340-384 |
7.97e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 7.97e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTN 384
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
346-506 |
1.61e-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: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 346 EIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRdlnigiLSQQP-YI---FSASIKENI--TMFKDIENNTI 419
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK------ISYKPqYIspdYDGTVEEFLrsANTDDFGSSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 420 E-EVLDEVGlLDKVqsFTKGINTiigeggemLSGGQMRR--IELCrlLVMKPDLVIFDEPATGLDIQTEHMIQNVLfQHF 496
Cdd:COG1245 436 KtEIIKPLG-LEKL--LDKNVKD--------LSGGELQRvaIAAC--LSRDADLYLLDEPSAHLDVEQRLAVAKAI-RRF 501
|
170
....*....|...
gi 446659814 497 ---KDTTMIVIAH 506
Cdd:COG1245 502 aenRGKTAMVVDH 514
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
337-517 |
2.46e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 337 RLVLNDLNLEIFKGDQIALVGPSGAGKSTL-----THLIAG---------VYQPTIG-TISTNQRDLN------------ 389
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFlrymaMHAIDGipkncqilhVEQEVVGdDTTALQCVLNtdiertqlleee 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 390 IGILSQQPYI------FSASIKENITMFKDIENNTIEEVLDEVGLLDKVQSFTKGINTIIGEG--GEM-------LSGGQ 454
Cdd:PLN03073 270 AQLVAQQRELefetetGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSftPEMqvkatktFSGGW 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 455 MRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQHFKdtTMIVIAH-RD--NT----IRHLQRR 517
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSHaREflNTvvtdILHLHGQ 417
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
354-481 |
2.79e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 354 ALVGPSGAGKSTLTHLIAG-----------------VYQPTIGTIS--TNQRDLNI-GILSQQPYIFSASIKENITMFKD 413
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAGrktggyiegdirisgfpKKQETFARISgyCEQNDIHSpQVTVRESLIYSAFLRLPKEVSKE 989
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446659814 414 IENNTIEEVLDEVGLlDKVQSFTKGINTIIGeggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLD 481
Cdd:PLN03140 990 EKMMFVDEVMELVEL-DNLKDAIVGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
340-392 |
2.86e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 2.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIS--------TNQRD-LNIGI 392
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILidgqemrfASTTAaLAAGV 81
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
350-506 |
3.31e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 350 GDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIST--NQRdlnIGILSQQPYIFsasikenitmfkdiENNTieeVLDEVG 427
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdpNER---LGKLRQDQFAF--------------EEFT---VLDTVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 428 L----LDKVQSFTKGI-----------------NTIIGE---------GGEMLSG---------GQMR--------RIEL 460
Cdd:PRK15064 87 MghteLWEVKQERDRIyalpemseedgmkvadlEVKFAEmdgytaearAGELLLGvgipeeqhyGLMSevapgwklRVLL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446659814 461 CRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQhfKDTTMIVIAH 506
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
342-506 |
3.83e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 342 DLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDL-------------NIGILSQQPYifsASIKENI 408
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspgklqalrrDIQFIFQDPY---ASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 409 TMfkdieNNTIEEVLDEVGLLDKvQSFTKGINTIIGEGG----------EMLSGGQMRRIELCRLLVMKPDLVIFDEPAT 478
Cdd:PRK10261 419 TV-----GDSIMEPLRVHGLLPG-KAAAARVAWLLERVGllpehawrypHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190
....*....|....*....|....*....|
gi 446659814 479 GLDIQTEHMIQNVLFQHFKD--TTMIVIAH 506
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDfgIAYLFISH 522
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
349-482 |
4.85e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 349 KGDQIALVGPSGAGKSTLTHLIAGVYQPtigtistnqrdlNIGILSQQPyifsaSIKENI---------TMFKDIENN-- 417
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIP------------NLGDYEEEP-----SWDEVLkrfrgtelqNYFKKLYNGei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 418 ------------------TIEEVL---DEVGLLDKVQSFTkGINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEP 476
Cdd:PRK13409 161 kvvhkpqyvdlipkvfkgKVRELLkkvDERGKLDEVVERL-GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
....*.
gi 446659814 477 ATGLDI 482
Cdd:PRK13409 240 TSYLDI 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
340-528 |
6.29e-05 |
|
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: 45.59 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTI-GTISTNQRDLNIGILSQqpyifsaSIKENITMF-KDIENN 417
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDIRNPAQ-------AIRAGIAMVpEDRKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 418 TIEEVLDeVG---LLDKVQSFTKgiNTIIGEGGEM-----------------------LSGGQMRRIELCRLLVMKPDLV 471
Cdd:TIGR02633 349 GIVPILG-VGkniTLSVLKSFCF--KMRIDAAAELqiigsaiqrlkvktaspflpigrLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 472 IFDEPATGLDIQTEHMIQNVLFQHFKD-TTMIVIAHRDNTIRHLQRR-LYIENGRLIAD 528
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSDRvLVIGEGKLKGD 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
340-511 |
6.81e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYqPTiGTIS------------TNQRD---LNIGILSQQ----PYIf 400
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PH-GTYEgeiifegeelqaSNIRDterAGIAIIHQElalvKEL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 401 saSIKENITMFKDIENNTI----------EEVLDEVGLldkvqsftkGIN--TIIGEggemLSGGQMRRIELCRLLVMKP 468
Cdd:PRK13549 98 --SVLENIFLGNEITPGGImdydamylraQKLLAQLKL---------DINpaTPVGN----LGLGQQQLVEIAKALNKQA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446659814 469 DLVIFDEPATGLdiqTEHMIQnVLFQHFKD-----TTMIVIAHRDNTI 511
Cdd:PRK13549 163 RLLILDEPTASL---TESETA-VLLDIIRDlkahgIACIYISHKLNEV 206
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
340-504 |
7.59e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNI---------GILsqqpYI----------F 400
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdglanGIV----YIsedrkrdglvL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 401 SASIKEN--ITMFKDIENNTI-----EEVLdEVGllDKVQSF---TKGINTIIGeggeMLSGGQMRRIELCRLLVMKPDL 470
Cdd:PRK10762 344 GMSVKENmsLTALRYFSRAGGslkhaDEQQ-AVS--DFIRLFnikTPSMEQAIG----LLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190
....*....|....*....|....*....|....
gi 446659814 471 VIFDEPATGLDIQTEHMIQNvLFQHFKDTTMIVI 504
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQ-LINQFKAEGLSII 449
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
340-513 |
8.52e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.17 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTH--LIAGVYQPTIGTISTNQRDL----------NIGILSqqPYIfsaSIKEn 407
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFdtIYAEGQRRYVESLSAYARQFlgqmdkpdvdSIEGLS--PAI---AIDQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 408 itmfKDIENN------TIEEVLDEVGLLDKVQSFTKGINTIIGEG---------GEMLSGGQMRRIELCRLLVMKPD--L 470
Cdd:cd03270 85 ----KTTSRNprstvgTVTEIYDYLRLLFARVGIRERLGFLVDVGlgyltlsrsAPTLSGGEAQRIRLATQIGSGLTgvL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446659814 471 VIFDEPATGLDIQTEHMIQNVLfQHFKD--TTMIVIAHRDNTIRH 513
Cdd:cd03270 161 YVLDEPSIGLHPRDNDRLIETL-KRLRDlgNTVLVVEHDEDTIRA 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
340-527 |
8.52e-05 |
|
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: 45.20 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVY-------------QPTIGTISTNQRDLNIGILSQQ-PYIFSASIK 405
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgeiywsgSPLKASNIRDTERAGIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 406 ENITMFKDIENNTI-----EEVLDEVGLLDKVQSFTKGINTIIGEGGemlsGGQMRRIELCRLLVMKPDLVIFDEPATGL 480
Cdd:TIGR02633 97 ENIFLGNEITLPGGrmaynAMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446659814 481 diqTEHMIQnVLFQHFKD-----TTMIVIAHRDNTIRHLQRRL-YIENGRLIA 527
Cdd:TIGR02633 173 ---TEKETE-ILLDIIRDlkahgVACVYISHKLNEVKAVCDTIcVIRDGQHVA 221
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
107-241 |
1.10e-04 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. 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.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 44.43 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 107 LTENI-DGLapfyksylpqvfKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIFGLKTRDESK---DQMTYLNQF 182
Cdd:cd18573 115 LTQNLsDGL------------RSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKqvqDALADATKV 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 183 SQ-RFLNIAkglvTLKLFNRtEQTEKHIYDDstQFRTLTMRILRSAFLSGLMLEFISMLG 241
Cdd:cd18573 183 AEeRLSNIR----TVRAFAA-ERKEVERYAK--KVDEVFDLAKKEALASGLFFGSTGFSG 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
318-494 |
1.11e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 318 NQKPFIQLTDISFRyddsDRLVLNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLNIgilsQQP 397
Cdd:PRK09700 261 AHETVFEVRNVTSR----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP----RSP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 398 YI------------------FSA-SIKENITMFKDIENNTIEEVL------DEVGLLDKVQSFTK----GINTIIGEgge 448
Cdd:PRK09700 333 LDavkkgmayitesrrdngfFPNfSIAQNMAISRSLKDGGYKGAMglfhevDEQRTAENQRELLAlkchSVNQNITE--- 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446659814 449 mLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVLFQ 494
Cdd:PRK09700 410 -LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ 454
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
340-512 |
1.84e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYqPTiGTIS---------TNQRDLN------IGILSQQ----PYIf 400
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PH-GSYEgeilfdgevCRFKDIRdsealgIVIIHQElaliPYL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 401 saSIKENITMFKDIENNTI----------EEVLDEVGLLDKVQsftkginTIIGEGGEmlsgGQMRRIELCRLLVMKPDL 470
Cdd:NF040905 94 --SIAENIFLGNERAKRGVidwnetnrraRELLAKVGLDESPD-------TLVTDIGV----GKQQLVEIAKALSKDVKL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446659814 471 VIFDEPATGL-DIQTEHMIQnvLFQHFKD--TTMIVIAHRDNTIR 512
Cdd:NF040905 161 LILDEPTAALnEEDSAALLD--LLLELKAqgITSIIISHKLNEIR 203
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-169 |
3.65e-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: 42.50 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 16 VLMFLVSTGLGiLVIT--QNILIADFLA-KIIRHQFQGLWIVLFILLGVLLLRATVQFLNQWLGDTLAFKVKHMLRQRVi 92
Cdd:cd18563 5 FLLMLLGTALG-LVPPylTKILIDDVLIqLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 93 YKN---------NGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYII 163
Cdd:cd18563 83 YEHlqrlslsffDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYF 162
|
....*.
gi 446659814 164 FGLKTR 169
Cdd:cd18563 163 FWKKIR 168
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
104-245 |
4.32e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 42.48 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 104 MTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIFGLKTR---DESKDQMTYLN 180
Cdd:cd18546 99 MTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSrayRRARERIAAVN 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446659814 181 -QFSQrflNIAkGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRILRSAFLSGLMLEFISMLGIGLV 245
Cdd:cd18546 179 aDLQE---TLA-GIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
346-382 |
4.55e-04 |
|
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: 41.61 E-value: 4.55e-04
10 20 30
....*....|....*....|....*....|....*..
gi 446659814 346 EIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIS 382
Cdd:cd01854 81 ELLKGKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
346-523 |
7.29e-04 |
|
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: 40.63 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 346 EIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIStnqrdlnigilsqqpyifsasikenitmfkdienntieevLDE 425
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE----------------------------------------WDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 426 VGLLDKVQSFTkgintiigeggemLSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIV 503
Cdd:cd03222 61 ITPVYKPQYID-------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIrrLSEEGKKTALV 127
|
170 180
....*....|....*....|
gi 446659814 504 IAHRDNTIRHLQRRLYIENG 523
Cdd:cd03222 128 VEHDLAVLDYLSDRIHVFEG 147
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
84-245 |
7.31e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 41.78 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 84 KHMLRQRVIYkNNGHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYII 163
Cdd:cd18557 77 SSLLRQEIAF-FDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 164 FGLKTRDESK---DQMTYLNQF-SQRFLNIakglVTLKLFNRtEQTEKHIYDDSTQ--FRTLTMRILRSAFLSGLMlEFI 237
Cdd:cd18557 156 YGRYIRKLSKevqDALAKAGQVaEESLSNI----RTVRSFSA-EEKEIRRYSEALDrsYRLARKKALANALFQGIT-SLL 229
|
....*...
gi 446659814 238 SMLGIGLV 245
Cdd:cd18557 230 IYLSLLLV 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
340-504 |
9.77e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTISTNQRDLN---------------------IGILSQQPY 398
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneainhgfalvteerrsTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 399 IFS---ASIKENITMFKDIENNTIEEvlDEVGLLDKVQSFTKGINTIIGEggemLSGGQMRRIELCRLLVMKPDLVIFDE 475
Cdd:PRK10982 344 GFNsliSNIRNYKNKVGLLDNSRMKS--DTQWVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180
....*....|....*....|....*....
gi 446659814 476 PATGLDIQTEHMIQNVLFQHFKDTTMIVI 504
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
450-506 |
1.42e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446659814 450 LSGGQMRRIEL-CRLL--VMKPDLVIFDEPATGLDIQTEHMIQNVLFQ-HFKDTTMIVIAH 506
Cdd:PRK00635 810 LSGGEIQRLKLaYELLapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSlTHQGHTVVIIEH 870
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
450-507 |
1.95e-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: 39.27 E-value: 1.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446659814 450 LSGGQMRRIELC---RLLVMKPD-LVIFDEPATGLDIQTEHMIQNVLFQHF-KDTTMIVIAHR 507
Cdd:cd03227 78 LSGGEKELSALAlilALASLKPRpLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHL 140
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
443-506 |
2.16e-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: 39.91 E-value: 2.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446659814 443 IGEGGEMLSGGQMRRIELCRLLVMK---PDLVIFDEPATGL---DIQteHMIqNVLfQHFKD--TTMIVIAH 506
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVK--KLL-EVL-QRLVDkgNTVVVIEH 230
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
69-256 |
2.99e-03 |
|
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: 39.86 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 69 QFLNQWLGDTLAFKVKH---------MLRQRVIYKNNgHPIGEQMTILTENIDGLAPFYKSYLPQVFKSMMVPLIIIIAM 139
Cdd:cd18565 71 QYLSGVLWRRFAQRVQHdlrtdtydhVQRLDMAFFED-RQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAIL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 140 FFIHFNTALIMLITAPFIPLFYIIFglKTRDESKdqmtYLN------QFSQRFLNIAKGLVTLKLFNRTEQTEKHIYDDS 213
Cdd:cd18565 150 FYLNWQLALVALLPVPLIIAGTYWF--QRRIEPR----YRAvreavgDLNARLENNLSGIAVIKAFTAEDFERERVADAS 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 214 TQFRTLTMR--ILRSAFLSGL----MLEFISMLGIG-------LVALEATLS---LVVF 256
Cdd:cd18565 224 EEYRDANWRaiRLRAAFFPVIrlvaGAGFVATFVVGgywvldgPPLFTGTLTvgtLVTF 282
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
340-480 |
3.52e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTLTHLIAGVYQPTIGTIstnqrdlnigILSQQPYIFSAS---IKENITMFKDiEN 416
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI----------LFQGKEIDFKSSkeaLENGISMVHQ-EL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 417 NTIEE--VLDEVGL-----------LDKVQSFTK------GINTIIGEGGEMLSGGQMRRIELCRLLVMKPDLVIFDEPA 477
Cdd:PRK10982 83 NLVLQrsVMDNMWLgryptkgmfvdQDKMYRDTKaifdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
...
gi 446659814 478 TGL 480
Cdd:PRK10982 163 SSL 165
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
340-512 |
4.00e-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: 38.46 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 340 LNDLNLEIFKGDQIALVGPSGAGKSTL--THLIAGVYQPTIGTISTNQRDLNIgilsqqpyifsasikenitmfkdienn 417
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLvnEGLYASGKARLISFLPKFSRNKLI--------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 418 tieeVLDEVGLLDKVqsftkGINTI-IGEGGEMLSGGQMRRIELCRLLV--MKPDLVIFDEPATGLDIQTEHMIQNVLFQ 494
Cdd:cd03238 64 ----FIDQLQFLIDV-----GLGYLtLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKG 134
|
170
....*....|....*....
gi 446659814 495 HF-KDTTMIVIAHRDNTIR 512
Cdd:cd03238 135 LIdLGNTVILIEHNLDVLS 153
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
450-506 |
4.63e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 4.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446659814 450 LSGGQMRRIELCRLLVMK---PDLVIFDEPATGL---DIQteHMIqNVLfQHFKD--TTMIVIAH 506
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIK--KLL-EVL-QRLVDkgNTVVVIEH 890
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
122-247 |
5.73e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 39.00 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 122 LPQVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFIPLFYIIFGLKTRDESKDQMTYLNQFSqrflNIAK----GLVTLK 197
Cdd:cd18576 114 LAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEAN----TIVEetlqGIRVVK 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446659814 198 LFNRtEQTEKHIYDDSTQfRTLTMRiLRSAFLSGLMLEFISMLGIGLVAL 247
Cdd:cd18576 190 AFTR-EDYEIERYRKALE-RVVKLA-LKRARIRALFSSFIIFLLFGAIVA 236
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
450-506 |
6.14e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 38.95 E-value: 6.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446659814 450 LSGGQMRRIELCRLLVMKPDLVIFDEPATGLDIQTEHMIQNVL--FQHFKDTTMIVIAH 506
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLleLQQKENMALVLITH 212
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
84-245 |
6.90e-03 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 38.55 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 84 KHMLRQRVIYKNNgHPIGEQMTILTENID------GLAPFYksylpqVFKSMMVPLIIIIAMFFIHFNTALIMLITAPFI 157
Cdd:cd18541 81 AHLLTLSPSFYQK-NRTGDLMARATNDLNavrmalGPGILY------LVDALFLGVLVLVMMFTISPKLTLIALLPLPLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446659814 158 PLFYIIFGLKTRDESK---DQMTYLNQFSQRFLNiakGLVTLKLFNRTEQTEKHIYDDSTQFRTLTMRIlrsAFLSGLM- 233
Cdd:cd18541 154 ALLVYRLGKKIHKRFRkvqEAFSDLSDRVQESFS---GIRVIKAFVQEEAEIERFDKLNEEYVEKNLRL---ARVDALFf 227
|
170
....*....|....
gi 446659814 234 --LEFISMLGIGLV 245
Cdd:cd18541 228 plIGLLIGLSFLIV 241
|
|
| |
