|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-577 |
7.74e-112 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 346.00 E-value: 7.74e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 9 TPSIFSAIQKLRELLtREEKIKWLGIVGFALVVSLLEVVTASVIvvfAQVLNDPSVGQKYfqklgitenlspgKTVFYVA 88
Cdd:COG1132 2 SKSPRKLLRRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLL---GRIIDALLAGGDL-------------SALLLLL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 89 IAVGVVYVVKNLIAAAEVFFQNFSIQKMCFEFKNKLLHRYAQADYGFYLTRNSSFGLQVVGSDVEQ---AFSSGMVSLAR 165
Cdd:COG1132 65 LLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAveqFLAHGLPQLVR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 166 SLSegsVFIFLVGMIVYVNPTLVLIIFVIgMTLGLLTSKFLLPKFYYWGQNLQQTGFHTHKNLMQFFHSFKEIVLLGKKE 245
Cdd:COG1132 145 SVV---TLIGALVVLFVIDWRLALIVLLV-LPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 246 SFVKAYQVHSKERSKVQAIQTATNALPRMGIEILFVGLFVLTI---SYLCMGHESPmqmIGLLSGYLYAGFRLMPGLNRI 322
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLlvgGLLVLSGSLT---VGDLVAFILYLLRLFGPLRQL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 323 INDLNALKSVIPSIDRVhQEYIAFES----KSNYVDETSFRFtkSIEFNNVNFKYlNSKKNTLSNINLKINKGESVGIVG 398
Cdd:COG1132 298 ANVLNQLQRALASAERI-FELLDEPPeipdPPGAVPLPPVRG--EIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 399 HTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSfqWHKKIGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVD 474
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDgvdiRDLTLES--LRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 475 SAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMI 554
Cdd:COG1132 452 AAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI 531
|
570 580
....*....|....*....|...
gi 2258881611 555 AHRVSTLKNCDRIFKIENGKLSE 577
Cdd:COG1132 532 AHRLSTIRNADRILVLDDGRIVE 554
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-585 |
1.58e-96 |
|
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: 309.84 E-value: 1.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 14 SAIQKLRELLTREEKIkWLGIVGFALVVSLLEVVTAsvivVFAQVLNDPSVGQKYFQklgitenlspgkTVFYVAIAVGV 93
Cdd:COG2274 142 FGLRWFLRLLRRYRRL-LLQVLLASLLINLLALATP----LFTQVVIDRVLPNQDLS------------TLWVLAIGLLL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 94 VYVVKNLIAAAEVFFQNFSIQKMCFEFKNKLLHRYAQADYGFYLTRNssfglqvVGS------DVE--QAFSSGmvSLAR 165
Cdd:COG2274 205 ALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRS-------VGDlasrfrDVEsiREFLTG--SLLT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 166 SLSEGSVFIFLVGMIVYVNPTLVLIiFVIGMTLGLLTSKFLLPKFYYWGQNLQQTGFHTHKNLMQFFHSFKEIVLLGKKE 245
Cdd:COG2274 276 ALLDLLFVLIFLIVLFFYSPPLALV-VLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAES 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 246 SFV----KAYQVHSKERSKVQAIQTATNALPrMGIEILFVGLFVLTISYLCMGHEspMQMIGLLSGYLYAGfRLMPGLNR 321
Cdd:COG2274 355 RFRrrweNLLAKYLNARFKLRRLSNLLSTLS-GLLQQLATVALLWLGAYLVIDGQ--LTLGQLIAFNILSG-RFLAPVAQ 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 322 IINDLNALKSVIPSIDR---VHQEYIAFESKSNYVDETsfRFTKSIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVG 398
Cdd:COG2274 431 LIGLLQRFQDAKIALERlddILDLPPEREEGRSKLSLP--RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 399 HTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSfqWHKKIGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVD 474
Cdd:COG2274 509 RSGSGKSTLLKLLLGLYEPTSGRILIDgidlRQIDPAS--LRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAAR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 475 SAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMI 554
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
|
570 580 590
....*....|....*....|....*....|..
gi 2258881611 555 AHRVSTLKNCDRIFKIENGKLSEV-RKDSVLA 585
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDgTHEELLA 698
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
363-577 |
7.30e-78 |
|
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: 256.61 E-value: 7.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKkNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSfqWHKK 438
Cdd:COG4988 336 SIELEDVSFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINgvdlSDLDPAS--WRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNP 518
Cdd:COG4988 413 IAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVE 551
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
172-577 |
1.59e-74 |
|
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: 248.14 E-value: 1.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 172 VFIFLVGMIVYVNPTLVLIIFVIGMTLGLLtskflLPKFYY-----WGQNLQQTGFHTHKNLMQFFHSFKEIVLLGKKES 246
Cdd:COG4987 142 VILAAVAFLAFFSPALALVLALGLLLAGLL-----LPLLAArlgrrAGRRLAAARAALRARLTDLLQGAAELAAYGALDR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 247 FVKAYQVHSKERSKVQAIQTATNALpRMGIEILFVGLFVLTIsyLCMGheSPMQMIGLLSGYLYAGFRLMP-----GLNR 321
Cdd:COG4987 217 ALARLDAAEARLAAAQRRLARLSAL-AQALLQLAAGLAVVAV--LWLA--APLVAAGALSGPLLALLVLAAlalfeALAP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 322 IINDLNALKSVIPSIDRV----HQEYIAFESKSNYVDETSFrftkSIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIV 397
Cdd:COG4987 292 LPAAAQHLGRVRAAARRLnellDAPPAVTEPAEPAPAPGGP----SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 398 GHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNsfQWHKKIGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAV 473
Cdd:COG4987 368 GPSGSGKSTLLALLLRFLDPQSGSITLGgvdlRDLDED--DLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 474 DSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIM 553
Cdd:COG4987 446 ERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLL 525
|
410 420
....*....|....*....|....
gi 2258881611 554 IAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:COG4987 526 ITHRLAGLERMDRILVLEDGRIVE 549
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
364-577 |
3.36e-74 |
|
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: 236.74 E-value: 3.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQwhKKI 439
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASLR--RQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPE 519
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 520 VLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
364-577 |
6.93e-74 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 235.97 E-value: 6.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ----YKPNSFQwhKKI 439
Cdd:cd03253 1 IEFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdireVTLDSLR--RAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPE 519
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 520 VLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVE 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
364-577 |
7.37e-72 |
|
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: 230.19 E-value: 7.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDA----QYKPNSfqWHKKI 439
Cdd:cd03254 3 IEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirDISRKS--LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPE 519
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 520 VLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
364-574 |
3.04e-71 |
|
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: 226.50 E-value: 3.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHKKIGY 441
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSINLIDDTVEANIafgcdkidkealdnavdsaqlrqfvnslpnglkttigergirVSGGERQRISIARALYRNPEVL 521
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 522 IFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGK 574
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-592 |
4.69e-69 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 233.84 E-value: 4.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 20 RELLTREEKIKWLGIVgfALVVSLLEVVTASVIVVFAQVLNDPSVGQKYFQKLgitenlspgktvFYVAIAVGVVYVVKN 99
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVL--AGVAMILVAATESTLAALLKPLLDDGFGGRDRSVL------------WWVPLVVIGLAVLRG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 100 LIAAAEVFFQNFSIQKMCFEFKNKLLHRYAQADYGFYLTRNSSFGLQVVGSDVEQAFSSGMVSLARSLSEGSVFIFLVGM 179
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 180 IVYVNPTLVLIIFVIGMTLGLLTSKFLlPKFYYWGQNLQQTGFHTHKNLMQFFHSFKEIVLLGKKESFVKAY-QVHSKER 258
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVS-KRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFdAVSNRNR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 259 SKVQAIQTATNALPRMGIEILFVGL-FVLTISylcmGHESPMQ--MIGLLSGYLYAGFRLMPGLNRIINDLNALKSVIPS 335
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIASLALaVVLFIA----LFQAQAGslTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 336 IDRVhqeyIAFESKSNYVDETSF---RFTKSIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLIL 412
Cdd:TIGR02203 304 AESL----FTLLDSPPEKDTGTRaieRARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 413 GLLRPEKGNVLID----AQYKPNSFQWHkkIGYVAQSINLIDDTVEANIAFG-CDKIDKEALDNAVDSAQLRQFVNSLPN 487
Cdd:TIGR02203 380 RFYEPDSGQILLDghdlADYTLASLRRQ--VALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 488 GLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRI 567
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
570 580 590
....*....|....*....|....*....|..
gi 2258881611 568 FKIENGKLSE-------VRKDSVLAMSHHIGN 592
Cdd:TIGR02203 538 VVMDDGRIVErgthnelLARNGLYAQLHNMQF 569
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
364-578 |
3.51e-67 |
|
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: 218.18 E-value: 3.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNT-LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY-KPNSFQWH-KKIG 440
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDiRDLNLRWLrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEV 520
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 521 LIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSEV 578
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQ 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
363-577 |
2.06e-64 |
|
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: 222.00 E-value: 2.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYlNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ----YKPNSFqwHKK 438
Cdd:COG5265 357 EVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirdVTQASL--RAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNP 518
Cdd:COG5265 434 IGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
363-575 |
3.90e-64 |
|
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: 209.75 E-value: 3.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQWHkk 438
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdiRQLDPADLRRN-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNP 518
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
364-577 |
2.97e-63 |
|
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: 208.11 E-value: 2.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQwhKKI 439
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghdlALADPAWLR--RQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPE 519
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 520 VLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
363-567 |
6.79e-58 |
|
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: 202.52 E-value: 6.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYlNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKP--NSFQWHKKIG 440
Cdd:TIGR02857 321 SLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEV 520
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2258881611 521 LIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRI 567
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRI 526
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
363-577 |
5.36e-57 |
|
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: 190.78 E-value: 5.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNsfQWHKK 438
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvdiSKIGLH--DLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIAFgCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNP 518
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLDP-FGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
363-577 |
2.33e-56 |
|
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: 201.89 E-value: 2.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQwhKK 438
Cdd:TIGR01846 455 AITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDgvdlAIADPAWLR--RQ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNP 518
Cdd:TIGR01846 533 MGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNP 612
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:TIGR01846 613 RILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAE 671
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
364-574 |
2.17e-55 |
|
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: 186.14 E-value: 2.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKY---LNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVlidaqykpnsfQWHKKIG 440
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-----------SVPGSIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQSINLIDDTVEANIAFGcDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEV 520
Cdd:cd03250 70 YVSQEPWIQNGTIRENILFG-KPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 521 LIFDEATSALDSATEKQLMEtiDTIC----DAHTVIMIAHRVSTLKNCDRIFKIENGK 574
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHIFE--NCILglllNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
363-586 |
2.40e-55 |
|
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: 196.51 E-value: 2.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQWHkk 438
Cdd:COG4618 330 RLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDgadlSQWDREELGRH-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIA-FGcdKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRN 517
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIArFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 518 PEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKNCDRIFKIENGKLSEV-RKDSVLAM 586
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFgPRDEVLAR 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
151-577 |
5.52e-55 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 196.01 E-value: 5.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 151 DVEQAFSSGMVSLARSLSEGSVFIFLVGMIVYVNPTLVLIIFVIGMTLGL---LTSKfllpKFYYWGQNLQQTGFHTHKN 227
Cdd:PRK11176 131 DSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIairVVSK----RFRNISKNMQNTMGQVTTS 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 228 LMQFFHSFKEIVLLGKKESFVKAY-QVHSKERSKVQAIQTATNAL-PRMGIEILFVGLFVLTISYLcmghesPMQMIGLL 305
Cdd:PRK11176 207 AEQMLKGHKEVLIFGGQEVETKRFdKVSNRMRQQGMKMVSASSISdPIIQLIASLALAFVLYAASF------PSVMDTLT 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 306 SGYLYAGFRLMPGLNRiinDLNALKSVIPSIDR---VHQEYIAFESKSNYVDETSFRFTKS---IEFNNVNFKYLNSKKN 379
Cdd:PRK11176 281 AGTITVVFSSMIALMR---PLKSLTNVNAQFQRgmaACQTLFAILDLEQEKDEGKRVIERAkgdIEFRNVTFTYPGKEVP 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 380 TLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDA----QYKPNSFQwhKKIGYVAQSINLIDDTVEA 455
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrDYTLASLR--NQVALVSQNVHLFNDTIAN 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 456 NIAFGC-DKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSAT 534
Cdd:PRK11176 436 NIAYARtEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2258881611 535 EKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:PRK11176 516 ERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
359-577 |
8.31e-53 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 190.17 E-value: 8.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 359 RFTKSIEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWH 436
Cdd:PRK13657 330 RVKGAVEFDDVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdiRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 437 KKIGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYR 516
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
364-577 |
6.50e-52 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 187.21 E-value: 6.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlNSKKNT--LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQWHk 437
Cdd:TIGR02204 338 IEFEQVNFAY-PARPDQpaLDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDgvdlRQLDPAELRAR- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 kIGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRN 517
Cdd:TIGR02204 416 -MALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 518 PEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:TIGR02204 495 APILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVA 554
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
365-574 |
2.00e-50 |
|
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: 173.04 E-value: 2.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 365 EFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHKKIGYV 442
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdlTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSIN--LIDDTVEANIAFGC--DKIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRISIARAL 514
Cdd:cd03225 81 FQNPDdqFFGPTVEEEVAFGLenLGLPEEEIEERVEEAlelvGLEGLRDRSPFTL-----------SGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 515 YRNPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKN-CDRIFKIENGK 574
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
364-575 |
5.04e-50 |
|
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: 172.52 E-value: 5.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHKKIGY 441
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKdiTKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSIN--LIDDTVEANIAFGCD--KIDKEALDNAVDSAqLRQFvnslpnGLkTTIGERGI-RVSGGERQRISIARALYR 516
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAFGPEnlGLPREEIRERVEEA-LELV------GL-EHLADRPPhELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTL-KNCDRIFKIENGKL 575
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVaELADRVIVLDDGRI 212
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
364-584 |
1.36e-48 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 180.30 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLN-SKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHKKIG 440
Cdd:TIGR00958 479 IEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEV 520
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 521 LIFDEATSALDSATEKQLMEtiDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSEVRKDSVL 584
Cdd:TIGR00958 639 LILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
364-575 |
4.64e-48 |
|
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: 165.47 E-value: 4.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNsfQWHKKI 439
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDgadiSQWDPN--ELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDDTVEANIafgcdkidkealdnavdsaqlrqfvnslpnglkttigergirVSGGERQRISIARALYRNPE 519
Cdd:cd03246 79 GYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 520 VLIFDEATSALDSATEKQLMETI-DTICDAHTVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
378-577 |
1.83e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 175.03 E-value: 1.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 378 KNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLrPEKGNVLIDAQ--YKPNSFQWHKKIGYVAQSINLIDDTVEA 455
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIelRELDPESWRKHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 456 NIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATE 535
Cdd:PRK11174 442 NVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2258881611 536 KQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:PRK11174 522 QLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
364-577 |
8.03e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.06 E-value: 8.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNT--LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID------------AQYk 429
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdisslserelARL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 430 pnsfqWHKKIGYVAQSINLIDD-TVEANIAFGC------DKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSG 502
Cdd:COG1136 84 -----RRRHIGFVFQFFNLLPElTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRPSQL-----------SG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 503 GERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
364-575 |
9.29e-47 |
|
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: 163.80 E-value: 9.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLN-SKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAqyKP-NSFQ---WHKK 438
Cdd:cd03248 12 VKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG--KPiSQYEhkyLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNP 518
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
364-575 |
9.29e-46 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 162.60 E-value: 9.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQ-WH--KKIG 440
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlWEirKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQsiN----LIDDTVEANIAFGC-------DKIdKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRIS 509
Cdd:TIGR04520 81 MVFQ--NpdnqFVGATVEDDVAFGLenlgvprEEM-RKRVDEALKLVGMEDFRDREPHLL-----------SGGQKQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 510 IARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKI 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
175-557 |
5.18e-45 |
|
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: 167.15 E-value: 5.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 175 FLVGMIVYVNPTLVLIIFVIGMTLGLLTSKFLLPKFYYW-----GQNLQQTGFHTHKNLMQFFHSFKEIVLLGKKESFVK 249
Cdd:TIGR02868 138 LVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRaaraaEQALARLRGELAAQLTDALDGAAELVASGALPAALA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 250 AYQVHSKERSKVQAIQTATNALpRMGIEILFVGLFVLtiSYLCMGheSPMQMIGLLSGYLYAGFRLMP-----GLNRIIN 324
Cdd:TIGR02868 218 QVEEADRELTRAERRAAAATAL-GAALTLLAAGLAVL--GALWAG--GPAVADGRLAPVTLAVLVLLPlaafeAFAALPA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 325 DLNALKSVIPSIDRVhQEYIAFESKSNYV----DETSFRFTKSIEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHT 400
Cdd:TIGR02868 293 AAQQLTRVRAAAERI-VEVLDAAGPVAEGsapaAGAVGLGKPTLELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 401 GSGKSTLIDLILGLLRPEKGNVLIDAqYKPNSF---QWHKKIGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQ 477
Cdd:TIGR02868 371 GSGKSTLLATLAGLLDPLQGEVTLDG-VPVSSLdqdEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVG 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 478 LRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHR 557
Cdd:TIGR02868 450 LADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
283-577 |
8.40e-45 |
|
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: 168.98 E-value: 8.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 283 LFVLTISYLCMGHESPmqmiGLLSGYLYAGFRLMPGLNRIINDLNALKSVIPSIDRVHQeyiAFESKSNYvDETSF---R 359
Cdd:TIGR03797 376 LFAAAISLLGGAGLSL----GSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKP---ILEALPEV-DEAKTdpgK 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 360 FTKSIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHK 437
Cdd:TIGR03797 448 LSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQdlAGLDVQAVRR 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 KIGYVAQSINLIDDTVEANIAFGCDKIDKEALDnAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRN 517
Cdd:TIGR03797 528 QLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWE-AARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRK 606
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 518 PEVLIFDEATSALDSATEKQLMETIDTIcdAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:TIGR03797 607 PRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQ 664
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
172-577 |
9.71e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 167.31 E-value: 9.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 172 VFIFLVGMIVYVNPTLVLIIFVIgmtlgLLTSKFLLPK-FYYWG----QNLQQTGFHTHKNLMQFFHSFKEIVLLGKKES 246
Cdd:PRK11160 147 VILVLTIGLSFFDLTLALTLGGI-----LLLLLLLLPLlFYRLGkkpgQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 247 FVKAYQVHSKERSKVQAIQTATNALPRmGIEILFVGLFVLTISYLCM----GHESPMQMIGLLSGYLYAGFR-LMPglnr 321
Cdd:PRK11160 222 YRQQLEQTEQQWLAAQRRQANLTGLSQ-ALMILANGLTVVLMLWLAAggvgGNAQPGALIALFVFAALAAFEaLMP---- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 322 IINDLNALKSVIPSIDRVHqEYIAFESKSNYVDETSFRFTK-SIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHT 400
Cdd:PRK11160 297 VAGAFQHLGQVIASARRIN-EITEQKPEVTFPTTSTAAADQvSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRT 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 401 GSGKSTLIDLILGLLRPEKGNVLIDAQykpNSFQWHKK-----IGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDS 475
Cdd:PRK11160 376 GCGKSTLLQLLTRAWDPQQGEILLNGQ---PIADYSEAalrqaISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQ 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 476 AQLRQFVNSlPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIA 555
Cdd:PRK11160 453 VGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIT 531
|
410 420
....*....|....*....|..
gi 2258881611 556 HRVSTLKNCDRIFKIENGKLSE 577
Cdd:PRK11160 532 HRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
365-567 |
6.79e-44 |
|
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: 155.77 E-value: 6.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 365 EFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykpNSFQWHKKIGYVAQ 444
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 445 SINLIDD---TVEANIAFGCD----------KIDKEALDNAVDSAQLRQFVNSlpnglktTIGErgirVSGGERQRISIA 511
Cdd:cd03235 76 RRSIDRDfpiSVRDVVLMGLYghkglfrrlsKADKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVLLA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 512 RALYRNPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVST-LKNCDRI 567
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLvLEYFDRV 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
361-584 |
1.33e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.02 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 361 TKSIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAqyKPNSFQWHKkIG 440
Cdd:COG1121 4 MPAIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG--KPPRRARRR-IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQSINLIDD---TVEANIAFGCD----------KIDKEALDNAVDSAQLRQFVNSLpnglkttIGErgirVSGGERQR 507
Cdd:COG1121 79 YVPQRAEVDWDfpiTVRDVVLMGRYgrrglfrrpsRADREAVDEALERVGLEDLADRP-------IGE----LSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 508 ISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTL-KNCDRIFKIENGKLSEVRKDSVL 584
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVrEYFDRVLLLNRGLVAHGPPEEVL 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
364-575 |
4.03e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.43 E-value: 4.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNsfQWHKKI 439
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgkplSAMPPP--EWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDDTVEANIAFGcDKIDKEALDNAVDSAQLRQFvnslpnGLKTTIGERGI-RVSGGERQRISIARALYRNP 518
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFP-FQLRERKFDRERALELLERL------GLPPDILDKPVeRLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAH------RVstlknCDRIFKIENGKL 575
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
363-577 |
1.83e-42 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 161.21 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKKNtLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQwhKK 438
Cdd:TIGR01192 334 AVEFRHITFEFANSSQG-VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDgidiNTVTRESLR--KS 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNP 518
Cdd:TIGR01192 411 IATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:TIGR01192 491 PILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIE 549
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
364-575 |
2.40e-42 |
|
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: 151.49 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNT--LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQW---- 435
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdiSKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 436 HKKIGYVAQSINLIDD-TVEANIAFGC------DKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRI 508
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLllagvpKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 509 SIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDA--HTVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
364-591 |
4.29e-42 |
|
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: 152.99 E-value: 4.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLnskKNT------LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID-----AQYKPNS 432
Cdd:TIGR04521 1 IKLKNVSYIYQ---PGTpfekkaLDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDgrditAKKKKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 433 FQWHKKIGYV-----AQsinLIDDTVEANIAFGCD--KIDKEALDNAVDSAqLRQFvnslpnGLKTTIGERG-IRVSGGE 504
Cdd:TIGR04521 78 KDLRKKVGLVfqfpeHQ---LFEETVYKDIAFGPKnlGLSEEEAEERVKEA-LELV------GLDEEYLERSpFELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 505 RQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDA--HTVIMIAHRVS-TLKNCDRIFKIENGKL------ 575
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkgLTVILVTHSMEdVAEYADRVIVMHKGKIvldgtp 227
|
250
....*....|....*.
gi 2258881611 576 SEVRKDSVLAMSHHIG 591
Cdd:TIGR04521 228 REVFSDVDELEKIGLD 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
364-577 |
1.55e-41 |
|
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: 157.37 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNT---LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID-----AQYKPNSFQW 435
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkdltKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 436 HKKIGYVAQ----SINlIDDTVEANIAFGCD---KIDKEALDNAVDSAqLRQFvnslpnGLKTTIGERGIR-VSGGERQR 507
Cdd:COG1123 341 RRRVQMVFQdpysSLN-PRMTVGDIIAEPLRlhgLLSRAERRERVAEL-LERV------GLPPDLADRYPHeLSGGQRQR 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 508 ISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKLSE 577
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
364-580 |
2.00e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 149.05 E-value: 2.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSF-QWHKK 438
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlSRLKRREIpYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDD-TVEANIAF-----GCD-KIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIA 511
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALplrvtGKSrKEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 512 RALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIA-HRVSTLKNCD-RIFKIENGKLSEVRK 580
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkRVLELEDGRLVRDEA 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
381-528 |
4.36e-41 |
|
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: 145.87 E-value: 4.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHKKIGYVAQSINLIDD-TVEANI 457
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdlTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 458 AFGcdkIDKEALDNAVDSAQLRQFVNSLPNG--LKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATS 528
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
361-575 |
1.27e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 148.60 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 361 TKSIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY--KPNSFQWHKK 438
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITisKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSIN--LIDDTVEANIAFGCD--KID----KEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISI 510
Cdd:PRK13632 85 IGIIFQNPDnqFIGATVEDDIAFGLEnkKVPpkkmKDIIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 511 ARALYRNPEVLIFDEATSALDSATEKQLMETIDTICD--AHTVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
363-577 |
2.37e-40 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 155.26 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAqyKPNSFQWH----KK 438
Cdd:PRK10790 340 RIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG--RPLSSLSHsvlrQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIAFGCDkIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNP 518
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
364-575 |
4.60e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 145.98 E-value: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID-AQYKPNSFQWHKKIGYV 442
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSINLIDD-TVEANIAFGCD--KIDKEALDNAVDSAqLRQFvnSLPNGLKTTIGErgirVSGGERQRISIARALYRNPE 519
Cdd:COG1131 79 PQEPALYPDlTVRENLRFFARlyGLPRKEARERIDEL-LELF--GLTDAADRKVGT----LSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 520 VLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTL-KNCDRIFKIENGKL 575
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAeRLCDRVAIIDKGRI 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
364-577 |
5.12e-40 |
|
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: 145.80 E-value: 5.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNT--LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-----YKPNSFQWH 436
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 437 KKIGYVAQSINLIDD-TVEANIAFG--CDKIDKEALDNAVDsaQLRQFVnslpnGLKTTIGERGIRVSGGERQRISIARA 513
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPleIAGVPKAEIEERVL--ELLELV-----GLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 514 LYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKLSE 577
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
365-574 |
1.14e-39 |
|
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: 142.00 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 365 EFNNVNFKYLNSKknTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY--KPNSFQWHKKIGYV 442
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDiaKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQsinliddtveaniafgcdkidkealdnavdsaqlrqfvnslpnglkttigergirVSGGERQRISIARALYRNPEVLI 522
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 523 FDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRVSTLKN-CDRIFKIENGK 574
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
364-577 |
1.90e-39 |
|
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: 144.19 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYL--NSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ---YKPNSFQ--WH 436
Cdd:cd03257 2 LEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRkiRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 437 KKIGYVAQ----SIN-------LIDDTVEANIafgcdKIDKEALDNAVDSAQLRQ------FVNSLPNGLkttigergir 499
Cdd:cd03257 82 KEIQMVFQdpmsSLNprmtigeQIAEPLRIHG-----KLSKKEARKEAVLLLLVGvglpeeVLNRYPHEL---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 500 vSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKLS 576
Cdd:cd03257 147 -SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
.
gi 2258881611 577 E 577
Cdd:cd03257 226 E 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
365-575 |
1.08e-38 |
|
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: 140.26 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 365 EFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNsfQWHKKIG 440
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDgkdlASLSPK--ELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQSINLIddtveaNIAfgcDKIDKealdnavdsaqlrqFVNSLpnglkttigergirvSGGERQRISIARALYRNPEV 520
Cdd:cd03214 77 YVPQALELL------GLA---HLADR--------------PFNEL---------------SGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 521 LIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVS-TLKNCDRIFKIENGKL 575
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNlAARYADRVILLKDGRI 176
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
364-575 |
2.04e-38 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 142.10 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNsfQWHKKI 439
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlASLSRR--ELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDD-TVEANIAFGC----------DKIDKEALDNAVDSAQLRQF----VNSLpnglkttigergirvSGGE 504
Cdd:COG1120 78 AYVPQEPPAPFGlTVRELVALGRyphlglfgrpSAEDREAVEEALERTGLEHLadrpVDEL---------------SGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 505 RQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAH------RVstlknCDRIFKIENGKL 575
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHdlnlaaRY-----ADRLVLLKDGRI 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
364-577 |
2.04e-38 |
|
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: 139.37 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSfqwHKKI 439
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDgvpvSDLEKAL---SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDDTVEANIafgcdkidkealdnavdsaqlrqfvnslpnglkttigerGIRVSGGERQRISIARALYRNPE 519
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 520 VLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
364-589 |
2.94e-38 |
|
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: 141.48 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVN--FKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHKKI 439
Cdd:COG1124 2 LEVRNLSvsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQ----SIN---LIDDTV-EANIAFGCDKIDK---EALDnAV--DSAQLRQFVNSLpnglkttigergirvSGGERQ 506
Cdd:COG1124 82 QMVFQdpyaSLHprhTVDRILaEPLRIHGLPDREEriaELLE-QVglPPSFLDRYPHQL---------------SGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 507 RISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAH---RVSTLknCDRIFKIENGKLSEVR-K 580
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHdlaVVAHL--CDRVAVMQNGRIVEELtV 223
|
....*....
gi 2258881611 581 DSVLAMSHH 589
Cdd:COG1124 224 ADLLAGPKH 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
370-573 |
6.57e-38 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 147.94 E-value: 6.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 370 NFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSF--QWHKKIGYVAQSIN 447
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 448 LIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEAT 527
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2258881611 528 SALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENG 573
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHG 525
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
364-556 |
7.28e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 140.61 E-value: 7.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNT--LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPnsfqwHKKI 439
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvTGP-----GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQsinliDD------TVEANIAFGCD--KIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQR 507
Cdd:COG1116 83 GVVFQ-----EPallpwlTVLDNVALGLElrGVPKAERRERARELlelvGLAGFEDAYPHQL-----------SGGMRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 508 ISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAH 556
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTH 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
364-556 |
7.97e-38 |
|
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: 139.14 E-value: 7.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNT--LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSfqwHKKIGY 441
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP---GPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSINLID-DTVEANIAFG------CDKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARAL 514
Cdd:cd03293 78 VFQQDALLPwLTVLDNVALGlelqgvPKAEARERAEELLELVGLSGFENAYPHQL-----------SGGMRQRVALARAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2258881611 515 YRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAH 556
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTH 190
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
364-574 |
1.48e-37 |
|
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: 139.24 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSF-QWHKK 438
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdiNKLKGKALrQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDD-TVEANIAFGC--------------DKIDKEALDNAVDSAQLRQFVNSlpnglkttigeRGIRVSGG 503
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRlgrrstwrslfglfPKEEKQRALAALERVGLLDKAYQ-----------RADQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 504 ERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVS-TLKNCDRIFKIENGK 574
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDlAREYADRIVGLKDGR 222
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
46-577 |
2.52e-37 |
|
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: 147.58 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 46 VVTASVIVVFAQVLndpsvGQKYFQKlgITENLSPGK---TVFYVAIAVGVVYVVKNLIAAAEVFFQNFSIQKMCFEFKN 122
Cdd:TIGR01193 161 IVIAAIIVTLISIA-----GSYYLQK--IIDTYIPHKmmgTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIIL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 123 KLLHRYAQADYGFYLTRN-----SSFglqVVGSDVEQAFSSGMVSLARSLSegsvFIFLVGMI-VYVNPTLVLIIFVIGM 196
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRtgeivSRF---TDASSIIDALASTILSLFLDMW----ILVIVGLFlVRQNMLLFLLSLLSIP 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 197 TLGLLTSKFLLPkfyYWGQNLQQ---------------TGFHTHKNLMQFFHSFKEIVLLgkKESFVKAYQVHSKERSKV 261
Cdd:TIGR01193 307 VYAVIIILFKRT---FNKLNHDAmqanavlnssiiedlNGIETIKSLTSEAERYSKIDSE--FGDYLNKSFKYQKADQGQ 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 262 QAIQTATNALprMGIEILFVGLFVLTISYLCMGHespmqmigLLSGYLYAGFRLMPgLNRIINDLNALKSVIPSIDRVHQ 341
Cdd:TIGR01193 382 QAIKAVTKLI--LNVVILWTGAYLVMRGKLTLGQ--------LITFNALLSYFLTP-LENIINLQPKLQAARVANNRLNE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 342 EYI--AFESKSNYVDETSfRFTKSIEFNNVNFKY-LNSkkNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPE 418
Cdd:TIGR01193 451 VYLvdSEFINKKKRTELN-NLNGDIVINDVSYSYgYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 419 KGNVLIDAQYKPN--SFQWHKKIGYVAQSINLIDDTVEANIAFGC-DKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGE 495
Cdd:TIGR01193 528 SGEILLNGFSLKDidRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 496 RGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDaHTVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:TIGR01193 608 EGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
..
gi 2258881611 576 SE 577
Cdd:TIGR01193 687 IE 688
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
364-575 |
9.18e-37 |
|
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: 134.83 E-value: 9.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-YKPNSFQWHKKIGYV 442
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSINLIDD-TVEANIAFgcdkidkealdnavdsaqlrqfvnslpnglkttigergirvSGGERQRISIARALYRNPEVL 521
Cdd:cd03230 79 PEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 522 IFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKN-CDRIFKIENGKL 575
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
364-577 |
9.28e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 139.83 E-value: 9.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNfKYLNSKKNT---LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSF-QW 435
Cdd:COG1135 2 IELENLS-KTFPTKGGPvtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvdlTALSERELrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 436 HKKIGYVAQSINLIDD-TVEANIAFG--CDKIDKEALDNAVDSaqLRQFV------NSLPNGLkttigergirvSGGERQ 506
Cdd:COG1135 81 RRKIGMIFQHFNLLSSrTVAENVALPleIAGVPKAEIRKRVAE--LLELVglsdkaDAYPSQL-----------SGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 507 RISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKLSE 577
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
364-575 |
1.63e-36 |
|
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: 136.09 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQWH-KK 438
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgediSGLSEAELYRLrRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDD-TVEANIAFG-----------CDKIDKEALDnAVDsaqLRQFVNSLPNGLkttigergirvSGGERQ 506
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPlrehtrlseeeIREIVLEKLE-AVG---LRGAEDLYPAEL-----------SGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 507 RISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVST-LKNCDRIFKIENGKL 575
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTaFAIADRIAVLYDGKI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
364-577 |
1.62e-35 |
|
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: 140.04 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPE---KGNVLIDAQ--YKPNSFQWHKK 438
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdlLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQS--INLIDDTVEANIAFGC--DKIDKEALDNAVDSAqLRQFvnslpnGLKTTIGERGIRVSGGERQRISIARAL 514
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEALenLGLSRAEARARVLEL-LEAV------GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 515 YRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVST-LKNCDRIFKIENGKLSE 577
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVvAEIADRVVVMDDGRIVE 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
364-577 |
1.97e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.37 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQW--HKKIGY 441
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWdvRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSIN--LIDDTVEANIAFGCDKID------KEALDNAVDSAQLRQFVNSLPNglkttigergiRVSGGERQRISIARA 513
Cdd:PRK13635 86 VFQNPDnqFVGATVQDDVAFGLENIGvpreemVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 514 LYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
364-575 |
4.69e-35 |
|
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: 132.41 E-value: 4.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNS-----FQWHKK 438
Cdd:COG1127 6 IEVRNLTKSF-GDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekelYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDD-TVEANIAFGCD---KIDKEALDNAV----DSAQLRQFVNSLPNGLkttigergirvSGGERQRISI 510
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFPLRehtDLSEAEIRELVleklELVGLPGAADKMPSEL-----------SGGMRKRVAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 511 ARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKL 575
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKI 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
364-574 |
8.20e-35 |
|
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: 129.61 E-value: 8.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQWHKKI 439
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedlTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDD-TVEANIAFGcdkidkealdnavdsaqlrqfvnslpnglkttigergirVSGGERQRISIARALYRNP 518
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVS-TLKNCDRIFKIENGK 574
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
380-573 |
2.14e-34 |
|
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: 129.76 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 380 TLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKG-----NVLIDAQYKPNSFQWHK-KIGYVAQSINLIDDTV 453
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsNKNESEPSFEATRSRNRySVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 EANIAFGcDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSA 533
Cdd:cd03290 96 EENITFG-SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2258881611 534 TEKQLM-ETIDTIC--DAHTVIMIAHRVSTLKNCDRIFKIENG 573
Cdd:cd03290 175 LSDHLMqEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
363-579 |
3.19e-34 |
|
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: 129.07 E-value: 3.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHKKIG 440
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdiSTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQSINLIDDTVEANIafgcDKIDKEaldnavDSAQLRQfvnslpnGLKttIGERGIRVSGGERQRISIARALYRNPEV 520
Cdd:cd03369 86 IIPQDPTLFSGTIRSNL----DPFDEY------SDEEIYG-------ALR--VSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 521 LIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSEVR 579
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
361-575 |
3.30e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 131.01 E-value: 3.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 361 TKSIEFNNVNFKY-LNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHK-- 437
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIrh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 KIGYVAQSIN--LIDDTVEANIAFGCD------KIDKEALDNAVDSAQLRQFVNSLPNglkttigergiRVSGGERQRIS 509
Cdd:PRK13650 82 KIGMVFQNPDnqFVGATVEDDVAFGLEnkgiphEEMKERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 510 IARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
364-578 |
9.53e-34 |
|
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: 127.64 E-value: 9.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYVA 443
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLIDD-TVEANIAFGCD--KIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRISIARALYR 516
Cdd:cd03259 79 QDYALFPHlTVAENIAFGLKlrGVPKAEIRARVRELlelvGLEGLLNRYPHEL-----------SGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVS-TLKNCDRIFKIENGKLSEV 578
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQV 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
364-578 |
3.09e-33 |
|
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: 126.91 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLL-----RPEKGNVLIDAQ------YKPNS 432
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdiydldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 433 FQwhKKIGYVAQSINLIDDTVEANIAFGcDKI----DKEALDNAVDSAqLRQFvnSLPNGLKTTIGERGIrvSGGERQRI 508
Cdd:cd03260 79 LR--RRVGMVFQKPNPFPGSIYDNVAYG-LRLhgikLKEELDERVEEA-LRKA--ALWDEVKDRLHALGL--SGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 509 SIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAH------RVStlkncDRIFKIENGKLSEV 578
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRVA-----DRTAFLLNGRLVEF 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
364-575 |
6.47e-33 |
|
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: 125.60 E-value: 6.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ----YKPNSFQW-HKK 438
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdLRGRAIPYlRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDD-TVEANIAFGCDKIDK------EALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIA 511
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALEVTGVppreirKRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 512 RALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNC--DRIFKIENGKL 575
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
376-577 |
3.49e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 132.94 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 376 SKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRP-EKGNVLIDAqykpnsfqwhkKIGYVAQSINLIDDTVE 454
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRG-----------TVAYVPQVSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 455 ANIAFGCDkIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSAT 534
Cdd:PLN03130 697 DNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2258881611 535 EKQLMET-IDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:PLN03130 776 GRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
363-575 |
4.67e-32 |
|
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: 122.27 E-value: 4.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNF----KYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPE--KGNVLIDAQYKPnSFQWH 436
Cdd:cd03213 3 TLSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLD-KRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 437 KKIGYVAQsinliDDtveanIAFGCDKIdKEALDNavdSAQLRQfvnslpnglkttigergirVSGGERQRISIARALYR 516
Cdd:cd03213 82 KIIGYVPQ-----DD-----ILHPTLTV-RETLMF---AAKLRG-------------------LSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTICDAH-TVIMIAHRVSTL--KNCDRIFKIENGKL 575
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGrTIICSIHQPSSEifELFDKLLLLSQGRV 190
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
364-577 |
5.56e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.45 E-value: 5.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKK--NTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY-----KPNSFQWH 436
Cdd:PRK11153 2 IELKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltalsEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 437 KKIGYVAQSINLIDD-TVEANIAFgcdkidkeALDNA-VDSAQLRQFVNSLPN--GLkttiGERGIR----VSGGERQRI 508
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVAL--------PLELAgTPKAEIKARVTELLElvGL----SDKADRypaqLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 509 SIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICD--AHTVIMIAHRVSTLKN-CDRIFKIENGKLSE 577
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
301-572 |
1.18e-31 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 131.30 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 301 MIGLLSGYLYAGFRL---MPGLNRIINDLNALKSVIPSIDRVhqeyiafESKSNYVDETSFRFTKSIEFNNVNFKYlNSK 377
Cdd:PTZ00265 324 VISILLGVLISMFMLtiiLPNITEYMKSLEATNSLYEIINRK-------PLVENNDDGKKLKDIKKIQFKNVRFHY-DTR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 378 KNT--LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQ---WHKKIGYVAQSINLIDDT 452
Cdd:PTZ00265 396 KDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINlkwWRSKIGVVSQDPLLFSNS 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 453 VEANIAFGCDKI-DKEALDN--------------------------------AVDSAQLRQ------------------- 480
Cdd:PTZ00265 476 IKNNIKYSLYSLkDLEALSNyynedgndsqenknkrnscrakcagdlndmsnTTDSNELIEmrknyqtikdsevvdvskk 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 481 -----FVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTI--CDAHTVIM 553
Cdd:PTZ00265 556 vlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITII 635
|
330
....*....|....*....
gi 2258881611 554 IAHRVSTLKNCDRIFKIEN 572
Cdd:PTZ00265 636 IAHRLSTIRYANTIFVLSN 654
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
278-577 |
1.43e-31 |
|
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: 131.22 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 278 ILFVGLF-VLTISYLCMGhespmqMIGLLSGYlyaGFRLMPGLNRIINDLNALKSVIPSIDRVhQEYIAFESKSNYVDE- 355
Cdd:TIGR00957 1203 VLFAALFaVISRHSLSAG------LVGLSVSY---SLQVTFYLNWLVRMSSEMETNIVAVERL-KEYSETEKEAPWQIQe 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 356 ----TSFRFTKSIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YK 429
Cdd:TIGR00957 1273 tappSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLniAK 1352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 430 PNSFQWHKKIGYVAQSINLIDDTVEANI-AFGcdKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRI 508
Cdd:TIGR00957 1353 IGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS--QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLV 1430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 509 SIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAE 1499
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
364-574 |
1.18e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.86 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnskKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-------YK-PNS--F 433
Cdd:COG3840 2 LRLDDLTYRY----GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppAErPVSmlF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 434 QWHkkigyvaqsiNLIDD-TVEANIAFG------CDKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQ 506
Cdd:COG3840 78 QEN----------NLFPHlTVAQNIGLGlrpglkLTAEQRAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 507 RISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVS-TLKNCDRIFKIENGK 574
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEdAARIADRVLLVADGR 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
361-584 |
4.53e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 126.63 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 361 TKSIEFNNVNFKY-LNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRP-EKGNVLIDAQykpnsfqwhkk 438
Cdd:PLN03232 612 APAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGS----------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIAFGCDkIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNP 518
Cdd:PLN03232 681 VAYVPQVSWIFNATVRENILFGSD-FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 519 EVLIFDEATSALDSATEKQLMET-IDTICDAHTVIMIAHRVSTLKNCDRIFKI------ENGKLSEVRKDSVL 584
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVsegmikEEGTFAELSKSGSL 832
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
363-575 |
7.76e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 120.59 E-value: 7.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-------YKPNsfqw 435
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppEKRN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 436 hkkIGYVAQSI----NLiddTVEANIAFG--CDKIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGER 505
Cdd:COG3842 79 ---VGMVFQDYalfpHL---TVAENVAFGlrMRGVPKAEIRARVAELlelvGLEGLADRYPHQL-----------SGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 506 QRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAH------RVStlkncDRIFKIENGKL 575
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHdqeealALA-----DRIAVMNDGRI 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
364-578 |
8.17e-30 |
|
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: 117.79 E-value: 8.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPnsFQWHKKI 439
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgediREQDP--VELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDD-TVEANIAF--GCDKIDKEALDNAVDsaQLRQFVNSLPNGLKttigERGIR-VSGGERQRISIARALY 515
Cdd:cd03295 78 GYVIQQIGLFPHmTVEENIALvpKLLKWPKEKIRERAD--ELLALVGLDPAEFA----DRYPHeLSGGQQQRVGVARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 516 RNPEVLIFDEATSALDSATEKQLMETIDTICDA--HTVIMIAHRV-STLKNCDRIFKIENGKLSEV 578
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQV 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
368-575 |
9.07e-30 |
|
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: 116.20 E-value: 9.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 368 NVNFKYlNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSfQWHKKIGYVAQSIN 447
Cdd:cd03226 4 NISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-ERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 448 --LIDDTVEANIAFGCDKIDKealDNAVDSAQLRQFVnslPNGLKttigERGIR-VSGGERQRISIARALYRNPEVLIFD 524
Cdd:cd03226 82 yqLFTDSVREELLLGLKELDA---GNEQAETVLKDLD---LYALK----ERHPLsLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 525 EATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKN-CDRIFKIENGKL 575
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQgKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
364-531 |
1.51e-29 |
|
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: 116.09 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ----YKPNSFQWHKKI 439
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDD-TVEANIAFGCDKIDKEALDNAVDSA-QLRQFVnslpnGLKTTIGERGIRVSGGERQRISIARALYRN 517
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITLAPIKVKGMSKAEAEERAlELLEKV-----GLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170
....*....|....
gi 2258881611 518 PEVLIFDEATSALD 531
Cdd:cd03262 154 PKVMLFDEPTSALD 167
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
364-575 |
1.60e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.88 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNT----LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLI---DAQYKPNSFQWH 436
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdglDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 437 KKIGYVAQSIN--LIDDTVEANIAFGCDKID------KEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRI 508
Cdd:PRK13633 85 NKAGMVFQNPDnqIVATIVEEDVAFGPENLGippeeiRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 509 SIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
363-531 |
2.17e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.41 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-------YKPNsfqw 435
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppKDRN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 436 hkkIGYVAQSINLIDD-TVEANIAFGCD--KIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRI 508
Cdd:COG3839 77 ---IAMVFQSYALYPHmTVYENIAFPLKlrKVPKAEIDRRVREAaellGLEDLLDRKPKQL-----------SGGQRQRV 142
|
170 180
....*....|....*....|...
gi 2258881611 509 SIARALYRNPEVLIFDEATSALD 531
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLD 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
363-578 |
3.73e-29 |
|
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: 123.52 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykpnsfqwhkkIGYV 442
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSINLIDDTVEANIAFGCdKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLI 522
Cdd:TIGR00957 705 PQQAWIQNDSLRENILFGK-ALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 523 FDEATSALDSATEKQLMETI---DTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSEV 578
Cdd:TIGR00957 784 FDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEM 842
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
302-577 |
4.07e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 123.55 E-value: 4.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 302 IGLLSGYLYAGFRLMPGL----NRIINDLNalksvipSIDRVhQEYIAFESKSNYVDE-----TSFRFTKSIEFNNVNFK 372
Cdd:PLN03232 1172 MGLLLSYTLNITTLLSGVlrqaSKAENSLN-------SVERV-GNYIDLPSEATAIIEnnrpvSGWPSRGSIKFEDVHLR 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 373 YLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDaQYKPNSF---QWHKKIGYVAQSINLI 449
Cdd:PLN03232 1244 YRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMID-DCDVAKFgltDLRRVLSIIPQSPVLF 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 450 DDTVEANIAFGCDKIDKEaLDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSA 529
Cdd:PLN03232 1323 SGTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2258881611 530 LDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
363-578 |
7.18e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 117.56 E-value: 7.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykpNSFQWHK----K 438
Cdd:COG1118 2 SIEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR---DLFTNLPprerR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSI----NLiddTVEANIAFG--CDKIDKEALDNAVDS----AQLRQFVNSLPNGLkttigergirvSGGERQRI 508
Cdd:COG1118 77 VGFVFQHYalfpHM---TVAENIAFGlrVRPPSKAEIRARVEEllelVQLEGLADRYPSQL-----------SGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 509 SIARALYRNPEVLIFDEATSALDSAT----EKQLMETIDTIcdAHTVIMIAH------RVstlknCDRIFKIENGKLSEV 578
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVrkelRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQV 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
381-575 |
7.89e-29 |
|
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: 112.14 E-value: 7.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-YKPNSfqwhkkigyvaqsinliddtveaniaf 459
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKeVSFAS--------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 460 gcdkiDKEALDnavdsaqlrqfvnslpnglkttigeRGIRV----SGGERQRISIARALYRNPEVLIFDEATSALDSATE 535
Cdd:cd03216 69 -----PRDARR-------------------------AGIAMvyqlSVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2258881611 536 KQLMETIDTICDA-HTVIMIAHRVSTLKN-CDRIFKIENGKL 575
Cdd:cd03216 119 ERLFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
363-574 |
1.06e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.92 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNS---KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQW 435
Cdd:PRK13637 2 SIKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvdiTDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 436 HKKIGYVAQ--SINLIDDTVEANIAFGCDK--IDKEALDNAVDSAQlrQFVNSLPNGLKTtigERGIRVSGGERQRISIA 511
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGPINlgLSEEEIENRVKRAM--NIVGLDYEDYKD---KSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 512 RALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTL-KNCDRIFKIENGK 574
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGK 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
364-575 |
3.44e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.93 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDA--QYKPNSFQWHKKI-G 440
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidTGDFSKLQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQS--INLIDDTVEANIAFGCDKI------DKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIAR 512
Cdd:PRK13644 81 IVFQNpeTQFVGRTVEEDLAFGPENLclppieIRKRVDRALAEIGLEKYRHRSPKTL-----------SGGQGQCVALAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 513 ALYRNPEVLIFDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
274-577 |
4.71e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 120.23 E-value: 4.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 274 MGIEILFVG--LFVLTISYLCMGH---ESPM----QMiGLLSGYLYAGFRLMPGLNRII----NDLNAlksvipsIDRVh 340
Cdd:PLN03130 1139 LAIRLETLGglMIWLTASFAVMQNgraENQAafasTM-GLLLSYALNITSLLTAVLRLAslaeNSLNA-------VERV- 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 341 QEYIAFESKSNYVDET-----SFRFTKSIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLL 415
Cdd:PLN03130 1210 GTYIDLPSEAPLVIENnrpppGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIV 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 416 RPEKGNVLIDAqYKPNSF---QWHKKIGYVAQSINLIDDTVEANIAFGCDKIDKEaLDNAVDSAQLRQFVNSLPNGLKTT 492
Cdd:PLN03130 1290 ELERGRILIDG-CDISKFglmDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDAD-LWESLERAHLKDVIRRNSLGLDAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 493 IGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIEN 572
Cdd:PLN03130 1368 VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDA 1447
|
....*
gi 2258881611 573 GKLSE 577
Cdd:PLN03130 1448 GRVVE 1452
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
364-578 |
9.91e-28 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 111.66 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKkntLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYVA 443
Cdd:cd03299 1 LKVENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLIDD-TVEANIAFGcdkIDKEALDNAVDSAQLRQFVNSLpnGLKTTIGERGIRVSGGERQRISIARALYRNPEVLI 522
Cdd:cd03299 78 QNYALFPHmTVYKNIAYG---LKKRKVDKKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 523 FDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKLSEV 578
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQV 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
364-575 |
9.96e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.54 E-value: 9.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-YKPNSFQ-WHKKIGY 441
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaITDDNFEkLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSIN--LIDDTVEANIAFGC-------DKIdKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIAR 512
Cdd:PRK13648 88 VFQNPDnqFVGSIVKYDVAFGLenhavpyDEM-HRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 513 ALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
367-573 |
1.10e-27 |
|
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: 112.64 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 367 NNVNFKYLNSKKN-TLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVlidaqykpnsfQWHKKIGYVAQS 445
Cdd:cd03291 38 NNLFFSNLCLVGApVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGRISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 446 INLIDDTVEANIAFGCdKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDE 525
Cdd:cd03291 107 SWIMPGTIKENIIFGV-SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 526 ATSALDSATEKQLMETidTICD---AHTVIMIAHRVSTLKNCDRIFKIENG 573
Cdd:cd03291 186 PFGYLDVFTEKEIFES--CVCKlmaNKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
364-577 |
1.15e-27 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 111.92 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHKKIGY 441
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdiSKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSINLIDDTVEANIAFGCdKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVL 521
Cdd:cd03288 100 ILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 522 IFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:cd03288 179 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
364-531 |
1.46e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 111.24 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNfKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY-KPNSFQWHK---KI 439
Cdd:COG1126 2 IEIENLH-KSFGDLE-VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDlTDSKKDINKlrrKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDD-TVEANIAFGCDKIDKEALDNAVDSAQ-------LRQFVNSLPNGLkttigergirvSGGERQRISIA 511
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLAPIKVKKMSKAEAEERAMellervgLADKADAYPAQL-----------SGGQQQRVAIA 148
|
170 180
....*....|....*....|
gi 2258881611 512 RALYRNPEVLIFDEATSALD 531
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALD 168
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
364-572 |
1.68e-27 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 118.59 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLnSKKNT--LSNINLKINKGESVGIVGHTGSGKSTLIDLILG----------LLRPEKGNVLIDAQYKP- 430
Cdd:PTZ00265 1166 IEIMDVNFRYI-SRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhiVFKNEHTNDMTNEQDYQg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 431 -----------NSFQWHKKIGY----------------------------------VAQSINLIDDTVEANIAFGCDKID 465
Cdd:PTZ00265 1245 deeqnvgmknvNEFSLTKEGGSgedstvfknsgkilldgvdicdynlkdlrnlfsiVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 466 KEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTI 545
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260
....*....|....*....|....*....
gi 2258881611 546 CDA--HTVIMIAHRVSTLKNCDRIFKIEN 572
Cdd:PTZ00265 1405 KDKadKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
381-575 |
1.98e-27 |
|
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: 110.08 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKIN---KGESVGIVGHTGSGKSTLIDLILGLLRPEKGN------VLIDAQYKPNSFQWHKKIGYVAQSINLIDD 451
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtVLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 452 -TVEANIAFG----CDKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEA 526
Cdd:cd03297 90 lNVRENLAFGlkrkRNREDRISVDELLDLLGLDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 527 TSALDSATEKQLM-ETIDTICDAH-TVIMIAHRVSTL-KNCDRIFKIENGKL 575
Cdd:cd03297 159 FSALDRALRLQLLpELKQIKKNLNiPVIFVTHDLSEAeYLADRIVVMEDGRL 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
381-567 |
3.66e-27 |
|
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: 112.07 E-value: 3.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRP---EKGNVLID----AQYKPNSFQ--WHKKIGYVAQ----SIN 447
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgedlLKLSEKELRkiRGREIQMIFQdpmtSLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 448 -------LIDDTVEANiaFGCDKidKEALDNAVDSAQL------RQFVNSLPNGLkttigergirvSGGERQRISIARAL 514
Cdd:COG0444 101 pvmtvgdQIAEPLRIH--GGLSK--AEARERAIELLERvglpdpERRLDRYPHEL-----------SGGMRQRVMIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 515 YRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRI 567
Cdd:COG0444 166 ALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEiADRV 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
364-574 |
4.67e-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: 110.17 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNV--LIDAQY-KPNSFQWHKKIG 440
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLFGERRgGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQSINL---IDDTVEANIAFG-CDKIDkeaLDNAVDSAQ-------LRQFvnslpnGLKTTIGERGIRVSGGERQRIS 509
Cdd:COG1119 82 LVSPALQLrfpRDETVLDVVLSGfFDSIG---LYREPTDEQrerarelLELL------GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 510 IARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNC-DRIFKIENGK 574
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
363-578 |
8.61e-27 |
|
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: 108.97 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKknTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYV 442
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSINLIDD-TVEANIAFGC-----------DKIdKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISI 510
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGLrvkprserppeAEI-RAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 511 ARALYRNPEVLIFDEATSALDSATEKQLMETIDTICD--AHTVIMIAH-RVSTLKNCDRIFKIENGKLSEV 578
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQV 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
362-575 |
1.04e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.80 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 362 KSIEFNNVNFKY-LNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHKK 438
Cdd:PRK13642 3 KILEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEllTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSIN--LIDDTVEANIAFGCDK--IDKEALDNAVDSAQLRqfVNSLpnGLKTtigERGIRVSGGERQRISIARAL 514
Cdd:PRK13642 83 IGMVFQNPDnqFVGATVEDDVAFGMENqgIPREEMIKRVDEALLA--VNML--DFKT---REPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 515 YRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
364-578 |
1.54e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.59 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLI-------DLILGLlRPEkGNVLIDAQ--YKP--NS 432
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGA-RVE-GEILLDGEdiYDPdvDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 433 FQWHKKIGYVAQSINLIDDTVEANIAFGCdKI----DKEALDNAVDSAqLRQfVNsLPNGLKTTIGERGIRVSGGERQRI 508
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGL-RLhgikSKSELDEIVEES-LRK-AA-LWDEVKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 509 SIARALYRNPEVLIFDEATSALDS-ATEKqLMETIDTICDAHTVIMIAH------RVStlkncDRIFKIENGKLSEV 578
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPiSTAK-IEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEF 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
364-575 |
1.79e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 107.19 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnskKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYVA 443
Cdd:cd03298 1 VRLDKIRFSY----GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLIDD-TVEANIAFG------CDKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYR 516
Cdd:cd03298 77 QENNLFAHlTVEQNVGLGlspglkLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTIC--DAHTVIMIAHRVS-TLKNCDRIFKIENGKL 575
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLHaeTKMTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
381-573 |
2.51e-26 |
|
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: 107.55 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY----KPNSFqwhkkigYVAQSINLID-DTVEA 455
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQitepGPDRM-------VVFQNYSLLPwLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 456 NIAFGCDKIDKEAldnavDSAQLRQFVNSLPN--GLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSA 533
Cdd:TIGR01184 74 NIALAVDRVLPDL-----SKSERRAIVEEHIAlvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2258881611 534 TEKQLMETIDTICDAH--TVIMIAHRV-STLKNCDRIFKIENG 573
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
381-583 |
3.17e-26 |
|
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: 107.13 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID------------AQYKPnsfqwhKKIGYVAQSINL 448
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAgqdlfaldedarARLRA------RHVGFVFQSFQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 449 IDD-TVEANIA-----FGcdkiDKEALDNAVDSAQ---LRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPE 519
Cdd:COG4181 102 LPTlTALENVMlplelAG----RRDARARARALLErvgLGHRLDHYPAQL-----------SGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 520 VLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIENGKLSEVRKDSV 583
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
381-573 |
3.60e-26 |
|
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: 114.24 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVlidaqykpnsfQWHKKIGYVAQSINLIDDTVEANIAFG 460
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGRISFSPQTSWIMPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 461 CdKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLME 540
Cdd:TIGR01271 511 L-SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
170 180 190
....*....|....*....|....*....|....*.
gi 2258881611 541 TidTICD---AHTVIMIAHRVSTLKNCDRIFKIENG 573
Cdd:TIGR01271 590 S--CLCKlmsNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
381-567 |
3.97e-26 |
|
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: 106.02 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSF-QWHKKIGYVAQSINLIDD-TVEANIA 458
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAReDYRRRLAYLGHADGLKPElTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 459 FGCD----KIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEATSALDSAT 534
Cdd:COG4133 98 FWAAlyglRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180 190
....*....|....*....|....*....|....
gi 2258881611 535 EKQLMETIDTICDAHTVIMIA-HRVSTLKNCDRI 567
Cdd:COG4133 167 VALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
378-575 |
5.10e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 113.72 E-value: 5.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 378 KNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDaqykpnsfqwhKKIGYVAQSINLIDDTVEANI 457
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-----------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 458 AFgCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQ 537
Cdd:PTZ00243 742 LF-FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2258881611 538 LMEtiDTICDA---HTVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:PTZ00243 821 VVE--ECFLGAlagKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
364-578 |
9.27e-26 |
|
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: 105.41 E-value: 9.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNsfqwHKKI 439
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvTDLPPK----DRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDD-TVEANIAFGCD--KIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRISIAR 512
Cdd:cd03301 75 AMVFQNYALYPHmTVYDNIAFGLKlrKVPKDEIDERVREVaellQIEHLLDRKPKQL-----------SGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 513 ALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAH-RVSTLKNCDRIFKIENGKLSEV 578
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLgtTTIYVTHdQVEAMTMADRIAVMNDGQIQQI 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
363-577 |
1.97e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.09 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDlILGLLR-PEKGNVLI-----DAQYKPNSFQ-- 434
Cdd:COG4161 2 SIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLEtPDSGQLNIaghqfDFSQKPSEKAir 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 435 -WHKKIGYVAQSINL------IDDTVEANIafgcdKIDKEALDNAVDSA-------QLRQFVNSLPNGLkttigergirv 500
Cdd:COG4161 79 lLRQKVGMVFQQYNLwphltvMENLIEAPC-----KVLGLSKEQAREKAmkllarlRLTDKADRFPLHL----------- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 501 SGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH-TVIMIAHRVS-TLKNCDRIFKIENGKLSE 577
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEfARKVASQVVYMEKGRIIE 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
363-590 |
2.22e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNS---KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLI-DAQYKPNSF----- 433
Cdd:PRK13641 2 SIKFENVDYIYSPGtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHITPETGnknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 434 QWHKKIGYVAQ--SINLIDDTVEANIAFGCDKI---DKEALDNAVDsaQLRQFvnslpnGLKTTIGERG-IRVSGGERQR 507
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFgfsEDEAKEKALK--WLKKV------GLSEDLISKSpFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 508 ISIARALYRNPEVLIFDEATSALDSATEKQLMET-IDTICDAHTVIMIAHRVSTL-KNCDRIFKIENGKL------SEVR 579
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLikhaspKEIF 233
|
250
....*....|.
gi 2258881611 580 KDSVLAMSHHI 590
Cdd:PRK13641 234 SDKEWLKKHYL 244
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
364-581 |
4.72e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.64 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKyLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ----YKPNsfQWHKKI 439
Cdd:PRK10247 8 LQLQNVGYL-AGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistLKPE--IYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDDTVEANIAFGCdKIDKEALDNAVDSAQLRQFvnslpnGLKTTIGERGIR-VSGGERQRISIARALYRNP 518
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPW-QIRNQQPDPAIFLDDLERF------ALPDTILTKNIAeLSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 519 EVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIE--NGKLSEVRKD 581
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITLQphAGEMQEARYE 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
364-575 |
6.41e-25 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 102.66 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESvGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQ-WHKKIGYV 442
Cdd:cd03264 1 LQLENLTKRY--GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQkLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSINLIDD-TVEANIAFGC------DKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALY 515
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYIAwlkgipSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 516 RNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKN-CDRIFKIENGKL 575
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKL 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
364-575 |
6.74e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.88 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGN---VLIDAQYKPNSFQW--HKK 438
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWdiREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSIN--LIDDTVEANIAFGcdkidkeaLDN-AVDSAQLRQFVNSLPN--GLKTTIGERGIRVSGGERQRISIARA 513
Cdd:PRK13640 86 VGIVFQNPDnqFVGATVGDDVAFG--------LENrAVPRPEMIKIVRDVLAdvGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 514 LYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
364-575 |
7.24e-25 |
|
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: 102.97 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY-KPNSFQWHKKIGYV 442
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSiRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSiNLIDD--TVEANIAFGC------DKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARAL 514
Cdd:cd03263 81 PQF-DALFDelTVREHLRFYArlkglpKSEIKEEVELLLRVLGLTDKANKRARTL-----------SGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 515 YRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKN-CDRIFKIENGKL 575
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
381-574 |
7.38e-25 |
|
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: 102.90 E-value: 7.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLI---DAQYKPNSFQWHKKIGYVAQSINLIDD-TVEAN 456
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrDITGLPPHERARAGIGYVPEGRRIFPElTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAFGCDKIDKEALDNAVDSAqLRQFvnslPNgLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEK 536
Cdd:cd03224 96 LLLGAYARRRAKRKARLERV-YELF----PR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2258881611 537 QLMETIDTICDAH-TVIMIAHRVS-TLKNCDRIFKIENGK 574
Cdd:cd03224 170 EIFEAIRELRDEGvTILLVEQNARfALEIADRAYVLERGR 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
371-556 |
1.23e-24 |
|
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: 102.35 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 371 FKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEK---GNVLIDAQyKPNSFQWHKKIGYVAQSIN 447
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ-PRKPDQFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 448 LIDD-TVEANIAFgcdkIDKEALDNAVDSAQLRQFVNSLpnGLK----TTIGERGIR-VSGGERQRISIARALYRNPEVL 521
Cdd:cd03234 92 LLPGlTVRETLTY----TAILRLPRKSSDAIRKKRVEDV--LLRdlalTRIGGNLVKgISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 2258881611 522 IFDEATSALDSATEKQLMETIDTICDAH-TVIMIAH 556
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNrIVILTIH 201
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
363-577 |
1.90e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKknTLSNINLKINKGESVGIVGHTGSGKSTLIDlILGLLR-PEKGNVLI-----DAQYKPNS---F 433
Cdd:PRK11124 2 SIQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIagnhfDFSKTPSDkaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 434 QWHKKIGYVAQSINL------IDDTVEANI-AFGCDKidKEALDNA---VDSAQLRQFVNSLPnglkttigergIRVSGG 503
Cdd:PRK11124 79 ELRRNVGMVFQQYNLwphltvQQNLIEAPCrVLGLSK--DQALARAeklLERLRLKPYADRFP-----------LHLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 504 ERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH-TVIMIAHRVSTL-KNCDRIFKIENGKLSE 577
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVArKTASRVVYMENGHIVE 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
383-578 |
2.00e-24 |
|
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: 103.11 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQW----HKKIGYVAQSINLIDD-TVEA 455
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiAAMSRKELrelrRKKISMVFQSFALLPHrTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 456 NIAFG------CDKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEATSA 529
Cdd:cd03294 122 NVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 530 LDSATEKQLMETIDTICDAH--TVIMIAHRVS-TLKNCDRIFKIENGKLSEV 578
Cdd:cd03294 191 LDPLIRREMQDELLRLQAELqkTIVFITHDLDeALRLGDRIAIMKDGRLVQV 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
381-567 |
2.49e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID-AQYKPNSFQ--WHKKIGYVAQSINLIDD-TVEAN 456
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgKPVRIRSPRdaIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAFGCDKIDKEALDNAVDSAQLRQFVNSLpnGLK----TTIGErgirVSGGERQRISIARALYRNPEVLIFDEATSAL-D 531
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAARARIRELSERY--GLDvdpdAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVLtP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2258881611 532 SATEkQLMETIDTICDA-HTVIMIAHR---VstLKNCDRI 567
Cdd:COG3845 175 QEAD-ELFEILRRLAAEgKSIIFITHKlreV--MAIADRV 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
381-567 |
2.78e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.64 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID-AQYKPNSFQ--WHKKIGYVAQSINLIDD-TVEAN 456
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgEPVRFRSPRdaQAAGIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAFGCDK-----IDKEALdNAVDSAQLRQFvnSLPNGLKTTIGERGIrvsgGERQRISIARALYRNPEVLIFDEATSALD 531
Cdd:COG1129 100 IFLGREPrrgglIDWRAM-RRRARELLARL--GLDIDPDTPVGDLSV----AQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 2258881611 532 SATEKQLMETIDTICDA-HTVIMIAHRVSTLKN-CDRI 567
Cdd:COG1129 173 EREVERLFRIIRRLKAQgVAIIYISHRLDEVFEiADRV 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
364-578 |
4.10e-24 |
|
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: 101.16 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYVA 443
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLIDD-TVEANIAFGCD--KIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRISIARALYR 516
Cdd:cd03300 79 QNYALFPHlTVFENIAFGLRlkKLPKAEIKERVAEAldlvQLEGYANRKPSQL-----------SGGQQQRVAIARALVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTICD--AHTVIMIAHRVS-TLKNCDRIFKIENGKLSEV 578
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQI 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
364-556 |
9.14e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 9.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnsKKNT------LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNV-----LIDAQYKPNS 432
Cdd:PRK13634 3 ITFQKVEHRY---QYKTpferraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigerVITAGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 433 FQ-WHKKIGYVAQ--SINLIDDTVEANIAFGCDKI---DKEALDNAvdsAQLRQFVnslpnGLKTTIGERG-IRVSGGER 505
Cdd:PRK13634 80 LKpLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFgvsEEDAKQKA---REMIELV-----GLPEELLARSpFELSGGQM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 506 QRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAH 556
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTH 204
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
364-575 |
1.10e-23 |
|
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: 99.21 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYVA 443
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLIDD-TVEANIAFGC------DKIDKEALDNAvdsaqlrqfvnslpnGLKTTIGERGIRVSGGERQRISIARALYR 516
Cdd:cd03268 79 EAPGFYPNlTARENLRLLArllgirKKRIDEVLDVV---------------GLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRVSTL-KNCDRIFKIENGKL 575
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDqGITVLISSHLLSEIqKVADRIGIINKGKL 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
376-578 |
1.76e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 376 SKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLI--LGLLRPE---KGNVLIDAQ--YKPN--SFQWHKKIGYVAQSI 446
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniYSPRtdTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 447 NLIDDTVEANIAFGCdKI----DKEALDNAVDSAqLRQfvNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLI 522
Cdd:PRK14239 96 NPFPMSIYENVVYGL-RLkgikDKQVLDEAVEKS-LKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 523 FDEATSALDSATEKQLMETIDTICDAHTVIMIAH------RVStlkncDRIFKIENGKLSEV 578
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRsmqqasRIS-----DRTGFFLDGDLIEY 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
385-558 |
2.17e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 385 NLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYVAQSINLIDD-TVEANIAFGCD- 462
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHlTVAQNIGLGLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 463 --KID---KEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQ 537
Cdd:PRK10771 99 glKLNaaqREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180
....*....|....*....|...
gi 2258881611 538 LMETIDTICDAH--TVIMIAHRV 558
Cdd:PRK10771 168 MLTLVSQVCQERqlTLLMVSHSL 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
364-574 |
2.69e-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: 95.98 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVlidaqykpnsfQWHK--KIGY 441
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------TWGStvKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQsinliddtveaniafgcdkidkealdnavdsaqlrqfvnslpnglkttigergirVSGGERQRISIARALYRNPEVL 521
Cdd:cd03221 68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 522 IFDEATSALDSATEKQLMETIDTIcdAHTVIMIAHRVSTLKN-CDRIFKIENGK 574
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEY--PGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
318-573 |
2.89e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.73 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 318 GLNRIINDLNALKSVIPSIDRVHQEYIAFEsksnyvdetsfrftksiefnNVNFkYLNSKKNTLSNINLKINKGESVGIV 397
Cdd:COG4178 337 GFEEALEAADALPEAASRIETSEDGALALE--------------------DLTL-RTPDGRPLLEDLSLSLKPGERLLIT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 398 GHTGSGKSTLIDLILGL--------LRPEKGNVLidaqykpnsfqwhkkigYVAQSINLIDDTVEANIAF--GCDKIDKE 467
Cdd:COG4178 396 GPSGSGKSTLLRAIAGLwpygsgriARPAGARVL-----------------FLPQRPYLPLGTLREALLYpaTAEAFSDA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 468 ALDNAVDSAQLRQFVNSLpnglkTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICD 547
Cdd:COG4178 459 ELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP 533
|
250 260
....*....|....*....|....*.
gi 2258881611 548 AHTVIMIAHRVSTLKNCDRIFKIENG 573
Cdd:COG4178 534 GTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
364-556 |
3.39e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.39 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVN---FKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ---YKPnSFQWHK 437
Cdd:COG1101 2 LELKNLSktfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtKLP-EYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 KIGYVAQ------SINLiddTVEANIA------------FGCDKIDKEALdnavdSAQLRQFVNSLPNGLKTTIGErgir 499
Cdd:COG1101 81 YIGRVFQdpmmgtAPSM---TIEENLAlayrrgkrrglrRGLTKKRRELF-----RELLATLGLGLENRLDTKVGL---- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 500 VSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAH 556
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTH 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
381-575 |
4.14e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKpnsfqwhkkIGYVAQSINLIDD-TV------ 453
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR---------IGYLPQEPPLDDDlTVldtvld 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 ---------------EANIAFGCDKIDKEA-LDNAVDS-------AQLRQFVNSLpnGLKTTIGERGIR-VSGGERQRIS 509
Cdd:COG0488 85 gdaelraleaeleelEAKLAEPDEDLERLAeLQEEFEAlggweaeARAEEILSGL--GFPEEDLDRPVSeLSGGWRRRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 510 IARALYRNPEVLIFDEATSALDsatekqlMETI----DTICD-AHTVIMIAH------RVstlknCDRIFKIENGKL 575
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLD-------LESIewleEFLKNyPGTVLVVSHdryfldRV-----ATRILELDRGKL 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
381-581 |
6.21e-23 |
|
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: 97.89 E-value: 6.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFqWHKKIGYVAQSINLIDD-TVEA 455
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgediTGLPPHEI-ARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 456 NIAFGCDKIDKEALDNAVDSAQLRQ----------FVNsLPNGLKTTIGErgirVSGGERQRISIARALYRNPEVLIFDE 525
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREareraeelleRVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 526 ATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKN-CDRIF------KIENGKLSEVRKD 581
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSlADRVTvldqgrVIAEGTPDEVRNN 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
381-577 |
7.10e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.90 E-value: 7.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKG-----NVLIDA-----QYKPNSFQWHKKIGYVAQSINLID 450
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTarslsQQKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 451 D-TVEANIAFGCDKIDKEALDNAVdsAQLRQFVNSLPNGLKTTIGERgiRVSGGERQRISIARALYRNPEVLIFDEATSA 529
Cdd:PRK11264 99 HrTVLENIIEGPVIVKGEPKEEAT--ARARELLAKVGLAGKETSYPR--RLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2258881611 530 LDSATEKQLMETIDTIC-DAHTVIMIAHRVSTLKN-CDRIFKIENGKLSE 577
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
364-577 |
7.30e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.86 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY----KPNSFQWHKKI 439
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDD-TVEANIAFGCDKIDKEALDNAVDSAQ-------LRQFVNSLPNGLkttigergirvSGGERQRISIA 511
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENVMFGPLRVRGASKEEAEKQARellakvgLAERAHHYPSEL-----------SGGQQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 512 RALYRNPEVLIFDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRVS-TLKNCDRIFKIENGKLSE 577
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEeGMTMVIVTHEIGfAEKVASRLIFIDKGRIAE 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
377-591 |
1.32e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 97.57 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 377 KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQ---WHKKIGYVAQ-SINLID 450
Cdd:TIGR02769 23 RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlYQLDRKQrraFRRDVQLVFQdSPSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 451 --DTVEANIAfgcdkidkEALDNAVD---SAQLRQFVNSLPN-GLKTTIGERGIR-VSGGERQRISIARALYRNPEVLIF 523
Cdd:TIGR02769 103 prMTVRQIIG--------EPLRHLTSldeSEQKARIAELLDMvGLRSEDADKLPRqLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 524 DEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKLSEVRKDS-VLAMSHHIG 591
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAqLLSFKHPAG 246
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
364-591 |
1.75e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYL-NS--KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLI-DAQYKPNSFQWH--- 436
Cdd:PRK13643 2 IKFEKVNYTYQpNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 437 --KKIGYVAQ--SINLIDDTVEANIAFGCDK--IDKEALDNAvdSAQLRQFVnslpnGLKTTIGERG-IRVSGGERQRIS 509
Cdd:PRK13643 82 vrKKVGVVFQfpESQLFEETVLKDVAFGPQNfgIPKEKAEKI--AAEKLEMV-----GLADEFWEKSpFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 510 IARALYRNPEVLIFDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRVSTLKN-CDRIFKIENGKL------SEVRKD 581
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIiscgtpSDVFQE 234
|
250
....*....|
gi 2258881611 582 SVLAMSHHIG 591
Cdd:PRK13643 235 VDFLKAHELG 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
364-575 |
2.35e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.07 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ---YKPNSF-QWHKKI 439
Cdd:PRK13639 2 LETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikYDKKSLlEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSIN--LIDDTVEANIAFG--CDKIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRISIA 511
Cdd:PRK13639 81 GIVFQNPDdqLFAPTVEEDVAFGplNLGLSKEEVEKRVKEAlkavGMEGFENKPPHHL-----------SGGQKKRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 512 RALYRNPEVLIFDEATSALDSATEKQLMETI-DTICDAHTVIMIAHRVSTL-KNCDRIFKIENGKL 575
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKI 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
364-577 |
3.86e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVlidaqykpnsfQWHK--KIGY 441
Cdd:COG0488 316 LELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----------KLGEtvKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSINLIDD--TVEANIAfgcdkidkEALDNAvDSAQLRQFVNSLpnGLKttiGERG---IRV-SGGERQRISIARALY 515
Cdd:COG0488 383 FDQHQEELDPdkTVLDELR--------DGAPGG-TEQEVRGYLGRF--LFS---GDDAfkpVGVlSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 516 RNPEVLIFDEATSALDsatekqlMETIDTICDA-----HTVIMIAH-R--VSTLknCDRIFKIENGKLSE 577
Cdd:COG0488 449 SPPNVLLLDEPTNHLD-------IETLEALEEAlddfpGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
381-556 |
5.04e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.84 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAqykpnsfqwHKKIGYVAQSINLIDD---TVEANI 457
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSlplTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 458 AFG----------CDKIDKEALDNAVDSAQLRQFvnslpngLKTTIGErgirVSGGERQRISIARALYRNPEVLIFDEAT 527
Cdd:NF040873 79 AMGrwarrglwrrLTRDDRAAVDDALERVGLADL-------AGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|
gi 2258881611 528 SALDSATEKQLMETIDTICDAH-TVIMIAH 556
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGaTVVVVTH 177
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
363-556 |
5.32e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.39 E-value: 5.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNS---KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID-----AQYKPNSF- 433
Cdd:PRK13646 2 TIRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDdititHKTKDKYIr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 434 QWHKKIGYVAQ--SINLIDDTVEANIAFG-------CDKIDKEALDNAVDSAQLRQFVNSLPnglkttigergIRVSGGE 504
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpknfkmnLDEVKNYAHRLLMDLGFSRDVMSQSP-----------FQMSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 505 RQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTIC--DAHTVIMIAH 556
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSH 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
371-575 |
8.42e-22 |
|
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: 93.97 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 371 FKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDA-QYKPNSFQWHKKIGYVAQSINLI 449
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLGFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 450 DD-TVEANIAF--GCDKIDKEALDNAVD--SAQLrqfvnslpnGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFD 524
Cdd:cd03266 91 DRlTARENLEYfaGLYGLKGDELTARLEelADRL---------GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 525 EATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKN-CDRIFKIENGKL 575
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVLHRGRV 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
384-589 |
1.48e-21 |
|
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: 96.33 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 384 INLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQW-----HK-KIGYVAQSINLIDD-TVEAN 456
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiflppEKrRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAFGCDKIDKEalDNAVDSAQLRQFVnslpnGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEK 536
Cdd:TIGR02142 96 LRYGMKRARPS--ERRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 537 QLMETIDTICDaHT---VIMIAHRVS-TLKNCDRIFKIENGK------LSEVRKDSVLAMSHH 589
Cdd:TIGR02142 169 EILPYLERLHA-EFgipILYVSHSLQeVLRLADRVVVLEDGRvaaagpIAEVWASPDLPWLAR 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
364-575 |
1.54e-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: 94.92 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEkGNVLIDA-QYKPNSFQ-WHKKIGY 441
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGvSWNSVPLQkWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSINLIDDTVEANI-AFGCDKiDKEALDNAvDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEV 520
Cdd:cd03289 82 IPQKVFIFSGTFRKNLdPYGKWS-DEEIWKVA-EEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 521 LIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
361-575 |
1.76e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.99 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 361 TKSIEFNNVNFKY-------------LNSKKNT-------LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKG 420
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelLLRRRRTrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 421 NVLIDaqykpnsfqwhkkiGYVAQSINL-----IDDTVEANIAFGC-------DKIDkEALDNAVDSAQLRQFVNsLPng 488
Cdd:COG1134 82 RVEVN--------------GRVSALLELgagfhPELTGRENIYLNGrllglsrKEID-EKFDEIVEFAELGDFID-QP-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 489 LKTTigergirvSGGERQRISIARALYRNPEVLIFDEATSALDSA-TEK--QLMETIdtICDAHTVIMIAHRVSTLKN-C 564
Cdd:COG1134 144 VKTY--------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKclARIREL--RESGRTVIFVSHSMGAVRRlC 213
|
250
....*....|.
gi 2258881611 565 DRIFKIENGKL 575
Cdd:COG1134 214 DRAIWLEKGRL 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
364-575 |
1.78e-21 |
|
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: 93.37 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNT--------------------LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVL 423
Cdd:cd03220 1 IELENVSKSYPTYKGGSsslkklgilgrkgevgefwaLKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 424 IDaqykpnsfqwhkkiGYVAQSINL---IDD--TVEANIAFGC------DKIDKEALDNAVDSAQLRQFVNsLPngLKTt 492
Cdd:cd03220 81 VR--------------GRVSSLLGLgggFNPelTGRENIYLNGrllglsRKEIDEKIDEIIEFSELGDFID-LP--VKT- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 493 igergirVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTIC-DAHTVIMIAHRVSTLKN-CDRIFKI 570
Cdd:cd03220 143 -------YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLkQGKTVILVSHDPSSIKRlCDRALVL 215
|
....*
gi 2258881611 571 ENGKL 575
Cdd:cd03220 216 EKGKI 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
363-575 |
2.21e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.43 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNS---KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID-----AQYKPNSF- 433
Cdd:PRK13649 2 GINLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitSTSKNKDIk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 434 QWHKKIGYVAQ--SINLIDDTVEANIA-----FGCDKIDKEALdnAVDSAQLRqfvnslpnGLKTTIGERG-IRVSGGER 505
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAfgpqnFGVSQEEAEAL--AREKLALV--------GISESLFEKNpFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 506 QRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTI-CDAHTVIMIAHRVSTLKN-CDRIFKIENGKL 575
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKL 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
383-574 |
2.58e-21 |
|
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: 95.55 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQW---HK-KIGYVAQsinliDD----- 451
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlQDSARGIFlppHRrRIGYVFQ-----EArlfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 452 -TVEANIAFGCDKI----DKEALDNAVD----SAQLRQFVNSLpnglkttigergirvSGGERQRISIARALYRNPEVLI 522
Cdd:COG4148 92 lSVRGNLLYGRKRApraeRRISFDEVVEllgiGHLLDRRPATL---------------SGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 523 FDEATSALDSATEKQLMETIDTICDAHT--VIMIAHR---VSTLknCDRIFKIENGK 574
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDipILYVSHSldeVARL--ADHVVLLEQGR 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
377-575 |
3.02e-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: 92.99 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 377 KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ---YKPNSFQWHKKIGYVAQ--SInLIDD 451
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditKLPMHKRARLGIGYLPQeaSI-FRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 452 TVEANIafgcdkidKEALDNA-VDSAQLRQFVNSLPN--GLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATS 528
Cdd:cd03218 91 TVEENI--------LAVLEIRgLSKKEREEKLEELLEefHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2258881611 529 ALDSATEKQLMETIDTICDAHTVIMIA-HRVS-TLKNCDRIFKIENGKL 575
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKV 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
381-573 |
4.11e-21 |
|
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: 92.50 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYkpnsfQW---------------HKKIGYVAQS 445
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-----GWvdlaqaspreilalrRRTIGYVSQF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 446 INLI-----DDTV-EANIAFGCDKidKEALDNAvdSAQLRQFvnSLPNGL----KTTIgergirvSGGERQRISIARALY 515
Cdd:COG4778 102 LRVIprvsaLDVVaEPLLERGVDR--EEARARA--RELLARL--NLPERLwdlpPATF-------SGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 516 RNPEVLIFDEATSALDSATEKQLMETIDTICDAHT-VIMIAHRVSTLKN-CDRIFKIENG 573
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
363-587 |
5.20e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 97.93 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQwhKK 438
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNgreiGAYGLRELR--RQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDDTVEANIAFGCDKIDKEALdNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALY-RN 517
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNVDPFLEASSAEVW-AALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 518 PEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSEVRKDSVLAMS 587
Cdd:PTZ00243 1465 SGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMN 1534
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
383-592 |
5.65e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.10 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ---YKPNSfqwHKKIGYVAQSINLIDD-TVEANIA 458
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPA---ERGVGMVFQSYALYPHlSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 459 FGCD--KIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEATSALDS 532
Cdd:PRK11000 98 FGLKlaGAKKEEINQRVNQVaevlQLAHLLDRKPKAL-----------SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 533 ATEKQLMETIDTIcdaH-----TVIMIAH-RVSTLKNCDRIFKIENGKLSEVRKDsvLAMSHHIGN 592
Cdd:PRK11000 167 ALRVQMRIEISRL---HkrlgrTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKP--LELYHYPAN 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
364-538 |
5.69e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.01 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNfKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYVA 443
Cdd:PRK09452 15 VELRGIS-KSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLIDD-TVEANIAFG--CDKIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRISIARALYR 516
Cdd:PRK09452 93 QSYALFPHmTVFENVAFGlrMQKTPAAEITPRVMEAlrmvQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVN 161
|
170 180
....*....|....*....|..
gi 2258881611 517 NPEVLIFDEATSALDSATEKQL 538
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQM 183
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
363-538 |
1.25e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.61 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNfKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYV 442
Cdd:PRK10851 2 SIEIANIK-KSFGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSINLIDD-TVEANIAFGC------DKIDKEALDNAV----DSAQLRQFVNSLPNGLkttigergirvSGGERQRISIA 511
Cdd:PRK10851 80 FQHYALFRHmTVFDNIAFGLtvlprrERPNAAAIKAKVtqllEMVQLAHLADRYPAQL-----------SGGQKQRVALA 148
|
170 180
....*....|....*....|....*..
gi 2258881611 512 RALYRNPEVLIFDEATSALDSATEKQL 538
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKEL 175
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
374-539 |
1.47e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.40 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 374 LNSKKnTLSNINLKIN-----KGESvGIVGHTGSGKSTLIDLILGLLRPEKG------NVLIDAQYKPNSFQWHKKIGYV 442
Cdd:PRK11144 4 LNFKQ-QLGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDAEKGICLPPEKRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSINLIDD-TVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPnglkttigergIRVSGGERQRISIARALYRNPEVL 521
Cdd:PRK11144 82 FQDARLFPHyKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELL 150
|
170
....*....|....*...
gi 2258881611 522 IFDEATSALDSATEKQLM 539
Cdd:PRK11144 151 LMDEPLASLDLPRKRELL 168
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
383-575 |
1.52e-20 |
|
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: 90.51 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLI---DAQYKPNSFQwhKKIGYVAQSINLIDD-------T 452
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghDVVREPREVR--RRIGIVFQDLSVDDEltgwenlY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 453 VEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLpngLKTtigergirVSGGERQRISIARALYRNPEVLIFDEATSALDS 532
Cdd:cd03265 96 IHARLYGVPGAERRERIDELLDFVGLLEAADRL---VKT--------YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2258881611 533 ATEKQLMETIDTICDAH--TVIMIAHRVSTL-KNCDRIFKIENGKL 575
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFgmTILLTTHYMEEAeQLCDRVAIIDHGRI 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
381-531 |
1.67e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.87 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQW---HKKIGYVAQ----SIN--Li 449
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdiTGLSGRELrplRRRMQMVFQdpyaSLNprM- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 450 ddTVEANIAfgcdkidkEALDNA--VDSAQLRQFVNSLPN--GLKTTIGERGIR-VSGGERQRISIARALYRNPEVLIFD 524
Cdd:COG4608 113 --TVGDIIA--------EPLRIHglASKAERRERVAELLElvGLRPEHADRYPHeFSGGQRQRIGIARALALNPKLIVCD 182
|
....*..
gi 2258881611 525 EATSALD 531
Cdd:COG4608 183 EPVSALD 189
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
367-583 |
2.01e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 96.13 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 367 NNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEkGNVLIDA-QYKPNSFQ-WHKKIGYVAQ 444
Cdd:TIGR01271 1221 QGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvSWNSVTLQtWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 445 SINLIDDTVEANIAFGCDKIDKEaLDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFD 524
Cdd:TIGR01271 1300 KVFIFSGTFRKNLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 525 EATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTLKNCDRIFKIENGKLSevRKDSV 583
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVK--QYDSI 1435
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
378-556 |
2.17e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.36 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 378 KNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYVAQSINLIDD-TVEAN 456
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAFGC--DKIDKEALDNAVDS----AQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEATSAL 530
Cdd:PRK11607 112 IAFGLkqDKLPKAEIASRVNEmlglVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180
....*....|....*....|....*...
gi 2258881611 531 DSA-TEKQLMETIDTICDAH-TVIMIAH 556
Cdd:PRK11607 181 DKKlRDRMQLEVVDILERVGvTCVMVTH 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
383-568 |
2.20e-20 |
|
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: 94.75 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEkGNVLID----AQYKPNSFQ-WHKKIGYVAQ----SIN---LID 450
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDgqdlDGLSRRALRpLRRRMQVVFQdpfgSLSprmTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 451 DTVEANIAFGCDKIDKEALDNAVDSAqLRQfVnslpnGLKTTIGERGIR-VSGGERQRISIARALYRNPEVLIFDEATSA 529
Cdd:COG4172 383 QIIAEGLRVHGPGLSAAERRARVAEA-LEE-V-----GLDPAARHRYPHeFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 530 LDSATEKQLMETIDTICDAH-----------TVI-MIAHRVSTLKN--------CDRIF 568
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHglaylfishdlAVVrALAHRVMVMKDgkvveqgpTEQVF 514
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
364-574 |
2.32e-20 |
|
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: 89.65 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDaqYKPNSFQWHKKIGYVA 443
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD--GKPLDIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLIDDTveaniafgcdKIdkeaLDNAVDSAQLRqfvnslpnGLKTTIGERGIR------------------VSGGER 505
Cdd:cd03269 77 EERGLYPKM----------KV----IDQLVYLAQLK--------GLKKEEARRRIDewlerlelseyankrveeLSKGNQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 506 QRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKN-CDRIFKIENGK 574
Cdd:cd03269 135 QKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGR 205
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
363-575 |
3.43e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYlNSKKN----TLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWH-- 436
Cdd:PRK13631 21 ILRVKNLYCVF-DEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 437 ----------------KKIGYVAQ--SINLIDDTVEANIAFG--CDKIDKEaldnavDSAQLRQF-VNSLpnGLKTTIGE 495
Cdd:PRK13631 100 itnpyskkiknfkelrRRVSMVFQfpEYQLFKDTIEKDIMFGpvALGVKKS------EAKKLAKFyLNKM--GLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 496 RG-IRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETI-DTICDAHTVIMIAHRV-STLKNCDRIFKIEN 572
Cdd:PRK13631 172 RSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMeHVLEVADEVIVMDK 251
|
...
gi 2258881611 573 GKL 575
Cdd:PRK13631 252 GKI 254
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
364-575 |
5.93e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNT--LSNINLKINKGESVGIVGHTGSGKSTLIDlILGLL-RPEKGNVLID------------AQY 428
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAgqdvatldadalAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 429 KPNSFqwhkkiGYVAQSINLIDD-TVEANIafgcdkiDKEALDNAVDSAQLRQFVNSLPN--GLKTTIGERGIRVSGGER 505
Cdd:PRK10535 84 RREHF------GFIFQRYHLLSHlTAAQNV-------EVPAVYAGLERKQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 506 QRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRVSTLKNCDRIFKIENGKL 575
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
358-575 |
9.20e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.07 E-value: 9.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 358 FRFTKSIEFNNVNFKYlnSKKN-----TLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNS 432
Cdd:PRK13645 1 FDFSKDIILDNVSYTY--AKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 433 FQ-------WHKKIGYVAQ--SINLIDDTVEANIAFGCDKI--DKEALDNAVdsAQLRQFVnSLPnglKTTIGERGIRVS 501
Cdd:PRK13645 79 LKkikevkrLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLgeNKQEAYKKV--PELLKLV-QLP---EDYVKRSPFELS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 502 GGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHT--VIMIAHRV-STLKNCDRIFKIENGKL 575
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMdQVLRIADEVIVMHEGKV 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
381-574 |
9.88e-20 |
|
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: 88.50 E-value: 9.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPnsfqwHKK----IGYVAQSINLIDD- 451
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgediTGLPP-----HRIarlgIGYVPEGRRIFPSl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 452 TVEANIAFGCdkidkEALDNAVDSAQLRQFVNSL-PNgLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSAL 530
Cdd:COG0410 94 TVEENLLLGA-----YARRDRAEVRADLERVYELfPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2258881611 531 DSATEKQLMETIDTICDA-HTVIMI---AHRVstLKNCDRIFKIENGK 574
Cdd:COG0410 168 APLIVEEIFEIIRRLNREgVTILLVeqnARFA--LEIADRAYVLERGR 213
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
37-329 |
1.91e-19 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits 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. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 89.14 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 37 FALVVSLLEVVTASVIVVFAQVLNDPSV--GQKYFQKLGITENL-SPGKTVFYVAIAVGVVYVVKNLIAAAEVFFQN-FS 112
Cdd:cd18553 3 FSIFVSLIETIGISAIMPFISVASNFSLilSNKYYKFIYNFFGFsSPVNFVIFFGIILIGFYIFRSLYNIFYTYLLNrFS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 113 IQKMcFEFKNKLLHRYAQADYGFYLTRNSSFGLQVVGSDVEQaFSSGMVSLARSLSEGSVFIFLVGMIVYVN--PTLVLI 190
Cdd:cd18553 83 FGRY-HSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASN-LSQVIQSFLFILSEIFVILFIYSLLLYVNwkITLVLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 191 IFVIGMTLGLLtsKFLLPKFYYWGQNLQQTGFHTHKNLMQFFHSFKEIVLLGKKESFVKAYQVHSKERSKVQAIQTATNA 270
Cdd:cd18553 161 LFLGLNVFFIT--KIVSKKIKKQGKKREESQKKFYKILSETFGNFKIIKLKSNEKEILKNFSQASLKFAKANIINQTLQT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 271 LPRMGIEILFVGLFVLTISYLCMGHESPMQMIGLLSGYLYAGFRLMPGLNRIINDLNAL 329
Cdd:cd18553 239 VPRLILETIGFSLLILIVLYILYKYSDASAVLPIISMYALALYRLLPSVNRILSSYNQI 297
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
376-575 |
3.37e-19 |
|
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: 85.56 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 376 SKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-YKPNSF-QWHKK-IGYVA---QSINLI 449
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpVTRRSPrDAIRAgIAYVPedrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 450 DD-TVEANIAfgcdkidkealdnavdsaqlrqfvnsLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEATS 528
Cdd:cd03215 91 LDlSVAENIA--------------------------LSSLL-----------SGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 529 ALDSATEKQLMETIDTICDA-HTVIMIahrvST-----LKNCDRIFKIENGKL 575
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAgKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
364-558 |
4.12e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.22 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKY--LNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDaqykpnsfqwHKKI-- 439
Cdd:COG4525 4 LTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLD----------GVPVtg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 -----GYVAQsinliDD------TVEANIAF-----GCDKIDKEALdnavdSAQLRQFVnslpnGLKTTIGERGIRVSGG 503
Cdd:COG4525 74 pgadrGVVFQ-----KDallpwlNVLDNVAFglrlrGVPKAERRAR-----AEELLALV-----GLADFARRRIWQLSGG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 504 ERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDA--HTVIMIAHRV 558
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITHSV 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
364-572 |
6.87e-19 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 84.13 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKNtLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVlidaqYKPnsfqWHKKIGYVA 443
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----GMP----EGEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLIDDTVEANIAFGCDKIdkealdnavdsaqlrqfvnslpnglkttigergirVSGGERQRISIARALYRNPEVLIF 523
Cdd:cd03223 71 QRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 524 DEATSALDSATEKQLMEtidtICDAH--TVIMIAHRVSTLKNCDRIFKIEN 572
Cdd:cd03223 116 DEATSALDEESEDRLYQ----LLKELgiTVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
381-578 |
8.39e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.94 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQ--WHKKIGYVAQSINLIDD-TV 453
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiAKISDAELRevRRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 EANIAFGCD-------KIDKEALDnAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEA 526
Cdd:PRK10070 124 LDNTAFGMElaginaeERREKALD-ALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 527 TSALDSATEKQLMETIDTICDAH--TVIMIAHRV-STLKNCDRIFKIENGKLSEV 578
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLdEAMRIGDRIAIMQNGEVVQV 246
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
364-575 |
1.07e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWHKKIGY 441
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpiTKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSIN--LIDDTVEANIAFG-CD-KIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRISIARA 513
Cdd:PRK13652 83 VFQNPDdqIFSPTVEQDIAFGpINlGLDEETVAHRVSSAlhmlGLEELRDRVPHHL-----------SGGEKKRVAIAGV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 514 LYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKL 575
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEmADYIYVMDKGRI 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
363-575 |
1.44e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.59 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNsfQWHKK 438
Cdd:PRK13548 2 MLEARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrplADWSPA--ELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINL-IDDTVEANIAFG------CDKIDKEALDNA---VDSAQLRQ-FVNSLpnglkttigergirvSGGERQR 507
Cdd:PRK13548 78 RAVLPQHSSLsFPFTVEEVVAMGraphglSRAEDDALVAAAlaqVDLAHLAGrDYPQL---------------SGGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 508 ISIARAL------YRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVstlkN-----CDRIFKIENGK 574
Cdd:PRK13548 143 VQLARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDL----NlaaryADRIVLLHQGR 218
|
.
gi 2258881611 575 L 575
Cdd:PRK13548 219 L 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
355-559 |
1.45e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.99 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 355 ETSFRFTKSIEFNNVNFKYLNSKknTLSNINLKINKGESVGIVGHTGSGKSTLI-------DLILGLlRPE-----KGNV 422
Cdd:PRK14243 2 STLNGTETVLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGF-RVEgkvtfHGKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 423 LIDAQYKPNSFQwhKKIGYVAQSINLIDDTVEANIAFGCdKID--KEALDNAVDSAqLRQFVnsLPNGLKTTIGERGIRV 500
Cdd:PRK14243 79 LYAPDVDPVEVR--RRIGMVFQKPNPFPKSIYDNIAYGA-RINgyKGDMDELVERS-LRQAA--LWDEVKDKLKQSGLSL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 501 SGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAH------RVS 559
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVS 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
378-591 |
3.16e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 378 KNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNV---------LIDAQYKpnSFQwhKKIGYVAQsinl 448
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplakLNRAQRK--AFR--RDIQMVFQ---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 449 idDTVEA-NIAFGCDKIDKE------ALDNAVDSAQLRQFVNSLpnGLKTTIGER-GIRVSGGERQRISIARALYRNPEV 520
Cdd:PRK10419 97 --DSISAvNPRKTVREIIREplrhllSLDKAERLARASEMLRAV--DLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 521 LIFDEATSALDSATE-------KQLMETIDTICdahtvIMIAHRVSTLKN-CDRIFKIENGKLSEVRKDS-VLAMSHHIG 591
Cdd:PRK10419 173 LILDEAVSNLDLVLQagvirllKKLQQQFGTAC-----LFITHDLRLVERfCQRVMVMDNGQIVETQPVGdKLTFSSPAG 247
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
367-575 |
3.35e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.73 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 367 NNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLidAQYKPNS---------FQ--- 434
Cdd:PRK11247 16 NAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--AGTAPLAearedtrlmFQdar 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 435 ---WhKKIgyvaqsinlIDdtveaNIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIA 511
Cdd:PRK11247 92 llpW-KKV---------ID-----NVGLGLKGQWRDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 512 RALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVS-TLKNCDRIFKIENGKL 575
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
364-575 |
6.37e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.00 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQW-HKK 438
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdiTRLKNREVPFlRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLI-DDTVEANIAF-----GCDKID-KEALDNAVDSAQLRQFVNSLPnglkttigergIRVSGGERQRISIA 511
Cdd:PRK10908 81 IGMIFQDHHLLmDRTVYDNVAIpliiaGASGDDiRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 512 RALYRNPEVLIFDEATSALDSATEK---QLMETIDTIcdAHTVIMIAHRVSTLKNCD-RIFKIENGKL 575
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEgilRLFEEFNRV--GVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
381-556 |
7.87e-18 |
|
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: 82.16 E-value: 7.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykPNSFQ---WHKKIGYVAQSINLIDD-TVEAN 456
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG--PLDFQrdsIARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEATSALDSATEK 536
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLNGFEDRPVAQL-----------SAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|.
gi 2258881611 537 QLMETIDTICDA-HTVIMIAH 556
Cdd:cd03231 163 RFAEAMAGHCARgGMVVLTTH 183
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
364-575 |
8.23e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.37 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlNSKK----NTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLI-----DAQYKPNSFQ 434
Cdd:PRK13651 3 IKVKNIVKIF-NKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 435 WH---------------------KKIGYVAQ--SINLIDDTVEANIAF-----GCDKidKEALDNAVDSAQLRqfvnslp 486
Cdd:PRK13651 82 KVleklviqktrfkkikkikeirRRVGVVFQfaEYQLFEQTIEKDIIFgpvsmGVSK--EEAKKRAAKYIELV------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 487 nGLKTTIGERG-IRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRV-STLKN 563
Cdd:PRK13651 153 -GLDESYLQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLdNVLEW 231
|
250
....*....|..
gi 2258881611 564 CDRIFKIENGKL 575
Cdd:PRK13651 232 TKRTIFFKDGKI 243
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
377-525 |
1.91e-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: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 377 KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-------YKpnsfQWHKKIGYVAQ--SI- 446
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmHK----RARLGIGYLPQeaSIf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 447 -NLiddTVEANIAfgcdkidkealdnAV------DSAQLRQFVNSLpnglkttIGE---------RGIRVSGGERQRISI 510
Cdd:COG1137 91 rKL---TVEDNIL-------------AVlelrklSKKEREERLEEL-------LEEfgithlrksKAYSLSGGERRRVEI 147
|
170
....*....|....*
gi 2258881611 511 ARALYRNPEVLIFDE 525
Cdd:COG1137 148 ARALATNPKFILLDE 162
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
378-556 |
2.36e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.05 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 378 KNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQwhkkiGYVAQSINLID-DTVE 454
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvEGPGAER-----GVVFQNEGLLPwRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 455 ANIAFGcdkidkeaLDNA-VDSAQLRQFVNSLPN--GLKTTiGERGI-RVSGGERQRISIARALYRNPEVLIFDEATSAL 530
Cdd:PRK11248 89 DNVAFG--------LQLAgVEKMQRLEIAHQMLKkvGLEGA-EKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*...
gi 2258881611 531 DSATEKQLMETIDTIC--DAHTVIMIAH 556
Cdd:PRK11248 160 DAFTREQMQTLLLKLWqeTGKQVLLITH 187
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
381-584 |
2.43e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.51 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLI--DAQYKPNSFQWHKKIGYVAQSINL-IDDTVEANI 457
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagDDVEALSARAASRRVASVPQDTSLsFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 458 AFG----------CDKIDKEALDNAVDSAQLRQFVnslpnglkttigERGI-RVSGGERQRISIARALYRNPEVLIFDEA 526
Cdd:PRK09536 99 EMGrtphrsrfdtWTETDRAAVERAMERTGVAQFA------------DRPVtSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 527 TSALDSATEKQLMETIDTICD-AHTVIMIAHRVS-TLKNCDRIFKIENGKLSEV-RKDSVL 584
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAgPPADVL 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
367-577 |
3.59e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.02 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 367 NNVNFKYLNSKKNT--LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQyKPNSFQ-------WHK 437
Cdd:PRK11629 9 DNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ-PMSKLSsaakaelRNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 KIGYVAQSINLIDD-TVEANIAFGCdKIDKEALDNAVDSAqlRQFVNSLpnGLKTTIGERGIRVSGGERQRISIARALYR 516
Cdd:PRK11629 88 KLGFIYQFHHLLPDfTALENVAMPL-LIGKKKPAEINSRA--LEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
381-573 |
4.69e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.21 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEK---------GN-VLIDAQYKPNSFQWHKKIGYVAQSINLID 450
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRtVQREGRLARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 451 D-TVEANI---AFGCDKIDKEALdNAVDSAQLRQFVNSLPN-GLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDE 525
Cdd:PRK09984 100 RlSVLENVligALGSTPFWRTCF-SWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 526 ATSALDSATEKQLMETIDTI--CDAHTVIMIAHRVS-TLKNCDRIFKIENG 573
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQG 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
361-591 |
5.05e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 361 TKSIEFNNVNFKYLNskKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNV-LIDAQYKPNSFQWHKKI 439
Cdd:PRK13536 39 TVAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINL-IDDTVEANIA-----FGCDKIDKEA-LDNAVDSAQLRQFVNSlpnglkttigeRGIRVSGGERQRISIAR 512
Cdd:PRK13536 117 GVVPQFDNLdLEFTVRENLLvfgryFGMSTREIEAvIPSLLEFARLESKADA-----------RVSDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 513 ALYRNPEVLIFDEATSALDSATEKQLMETIDT-ICDAHTVIMIAHRVSTLKN-CDRIFKIENG-KLSEVRKDSVLamSHH 589
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHALI--DEH 263
|
..
gi 2258881611 590 IG 591
Cdd:PRK13536 264 IG 265
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
364-574 |
6.42e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.43 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKkNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNS----FQWHKKI 439
Cdd:PRK13636 6 LKVEELNYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkglMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSIN--LIDDTVEANIAFGCD--KIDKEALDNAVDSAQLRQFVNSLPNglKTTIGergirVSGGERQRISIARALY 515
Cdd:PRK13636 85 GMVFQDPDnqLFSASVYQDVSFGAVnlKLPEDEVRKRVDNALKRTGIEHLKD--KPTHC-----LSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 516 RNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLK-NCDRIFKIENGK 574
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGR 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
376-587 |
1.13e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 376 SKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID-AQYKPNSFQ--WHKKIGYV-----AQSIN 447
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgKPVRIRSPRdaIRAGIAYVpedrkGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 448 LiDDTVEANIAFGCDK-------IDKEALDNAVdsaqlRQFVNSLpnGLKTTIGERGIRV-SGGERQRISIARALYRNPE 519
Cdd:COG1129 343 L-DLSIRENITLASLDrlsrgglLDRRRERALA-----EEYIKRL--RIKTPSPEQPVGNlSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 520 VLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIahrvST-----LKNCDRIFKIENGKL------SEVRKDSVLAMS 587
Cdd:COG1129 415 VLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVI----SSelpelLGLSDRILVMREGRIvgeldrEEATEEAIMAAA 490
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
361-574 |
1.34e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 361 TKSIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPN-SFQWHKKI 439
Cdd:PRK13537 5 VAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSrARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDD-TVEANIA-----FGcdkidkealdnaVDSAQLRQFVNSL------PNGLKTTIGErgirVSGGERQR 507
Cdd:PRK13537 83 GVVPQFDNLDPDfTVRENLLvfgryFG------------LSAAAARALVPPLlefaklENKADAKVGE----LSGGMKRR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 508 ISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKN-CDRIFKIENGK 574
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGR 215
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
364-575 |
1.45e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.74 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNSFQwhKKI 439
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvATTPSRELA--KRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDD-TVEANIAFG--------CDKIDKEALDNAVDSAQLR----QFVNSLpnglkttigergirvSGGERQ 506
Cdd:COG4604 78 AILRQENHINSRlTVRELVAFGrfpyskgrLTAEDREIIDEAIAYLDLEdladRYLDEL---------------SGGQRQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 507 RISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVstlkN-----CDRIFKIENGKL 575
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDI----NfascyADHIVAMKDGRV 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
379-577 |
1.89e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.67 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 379 NTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWH----KKIGYVAQSINLIDdT 452
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplHQMDEEARAklraKHVGFVFQSFMLIP-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 453 VEAniafgCDKIDKEALDNAVDSAQLRQFVNSLPNGLKttIGER----GIRVSGGERQRISIARALYRNPEVLIFDEATS 528
Cdd:PRK10584 103 LNA-----LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 529 ALDSatekqlmETIDTICD---------AHTVIMIAHRVSTLKNCDRIFKIENGKLSE 577
Cdd:PRK10584 176 NLDR-------QTGDKIADllfslnrehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
364-574 |
2.66e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.39 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-YKPNSFQW-HKKIGY 441
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGReVNAENEKWvRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSIN--LIDDTVEANIAFGCD--KIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRISIARA 513
Cdd:PRK13647 84 VFQDPDdqVFSSTVWDDVAFGPVnmGLDKDEVERRVEEAlkavRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 514 LYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIA-HRVS-TLKNCDRIFKIENGK 574
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGR 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
378-575 |
4.25e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.01 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 378 KNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ---YKPNSFQWHKKIGYVAQSINL-----I 449
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisLLPLHARARRGIGYLPQEASIfrrlsV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 450 DDTVEANIAFGCDKIDKEALDNAVDsaQLRQF-VNSLPNGLkttigerGIRVSGGERQRISIARALYRNPEVLIFDEATS 528
Cdd:PRK10895 96 YDNLMAVLQIRDDLSAEQREDRANE--LMEEFhIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2258881611 529 ALDSATEKQLMETIDTICDAHTVIMIA-HRV-STLKNCDRIFKIENGKL 575
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHL 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
363-581 |
4.89e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.00 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAqyKPNSFQWHKKIGYv 442
Cdd:COG4152 1 MLELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG--EPLDPEDRRRIGY- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 aqsinLIDD-------TVEANIAF-----GCDKidKEALDNAvdSAQLRQFvnSLPNGLKTTIGErgirVSGGERQRISI 510
Cdd:COG4152 76 -----LPEErglypkmKVGEQLVYlarlkGLSK--AEAKRRA--DEWLERL--GLGDRANKKVEE----LSKGNQQKVQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 511 ARALYRNPEVLIFDEATSALDS-ATEKqLMETIDTICDA-HTVIMIAHR---VSTLknCDRIF------KIENGKLSEVR 579
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPvNVEL-LKDVIRELAAKgTTVIFSSHQmelVEEL--CDRIViinkgrKVLSGSVDEIR 217
|
..
gi 2258881611 580 KD 581
Cdd:COG4152 218 RQ 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
378-542 |
5.64e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.76 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 378 KNT-LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYVAQSINLIDD-TVEA 455
Cdd:PRK11432 18 SNTvIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHmSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 456 NIAFGCD--KIDKEALDNAVDSA----QLRQFvnslpnglkttiGERGI-RVSGGERQRISIARALYRNPEVLIFDEATS 528
Cdd:PRK11432 98 NVGYGLKmlGVPKEERKQRVKEAlelvDLAGF------------EDRYVdQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170
....*....|....
gi 2258881611 529 ALDSATEKQLMETI 542
Cdd:PRK11432 166 NLDANLRRSMREKI 179
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
355-575 |
5.70e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 355 ETSFRFtksiefNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykP---- 430
Cdd:PRK10575 9 DTTFAL------RNVSFRV--PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ--Plesw 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 431 NSFQWHKKIGYVAQSINLIDD-TVEANIAFG----------CDKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergir 499
Cdd:PRK10575 79 SSKAFARKVAYLPQQLPAAEGmTVRELVAIGrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDSL---------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 500 vSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVS-TLKNCDRIFKIENGKL 575
Cdd:PRK10575 149 -SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEM 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
381-586 |
8.64e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPN---SFQWHKKIGYVAQSINLIDD-TVEAN 456
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldhKLAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAFGCDKIDKEALDNAVDSAQLRQFVNSLPN--GLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSAT 534
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIIDWREMRVRAAMMLLrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 535 EKQLMETIDTI-CDAHTVIMIAHRVSTLKN-CDRIFKIENGK------LSEVRKDSVLAM 586
Cdd:PRK09700 181 VDYLFLIMNQLrKEGTAIVYISHKLAEIRRiCDRYTVMKDGSsvcsgmVSDVSNDDIVRL 240
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
371-575 |
1.23e-15 |
|
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: 76.60 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 371 FKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIdAQYKPnsfqWHKKIGYVAQsINLId 450
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-AGLVP----WKRRKKFLRR-IGVV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 451 dtveaniaFGCDK--------IDKEALDNA---VDSAQLRQFVNSLPNGLKTT-IGERGIR-VSGGERQRISIARALYRN 517
Cdd:cd03267 100 --------FGQKTqlwwdlpvIDSFYLLAAiydLPPARFKKRLDELSELLDLEeLLDTPVRqLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 518 PEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTL-KNCDRIFKIENGKL 575
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRL 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
381-577 |
1.67e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.55 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY---------------KPNSFQWHKKIGYVAQS 445
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvadKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 446 INL------IDDTVEANI-AFGCDKidKEALDNAVdsaqlrQFVNslpnglKTTIGERG-----IRVSGGERQRISIARA 513
Cdd:PRK10619 101 FNLwshmtvLENVMEAPIqVLGLSK--QEARERAV------KYLA------KVGIDERAqgkypVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 514 LYRNPEVLIFDEATSALDSATEKQLMETIDTIC-DAHTVIMIAHRVSTLKNCDR--IFkIENGKLSE 577
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVSShvIF-LHQGKIEE 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
364-575 |
1.90e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.07 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykpNSFQWH------K 437
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK---DITDWQtakimrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 KIGYVAQSINLIDD-TVEANIAFGCDKIDKEALDNAVDSaqlrqfVNSLPNGLKTTIGERGIRVSGGERQRISIARALYR 516
Cdd:PRK11614 81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKW------VYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVS--TLKNCDRIFKIENGKL 575
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHV 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
381-569 |
2.03e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykPNSFQ-----WHKKIGYVAQSINLIDD-TVE 454
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ--EMRFAsttaaLAAGVAIIYQELHLVPEmTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 455 ANIAFGcdkidkeALDNA---VDSAQLRQFVNSLPNGLKTTI--GERGIRVSGGERQRISIARALYRNPEVLIFDEATSA 529
Cdd:PRK11288 98 ENLYLG-------QLPHKggiVNRRLLNYEAREQLEHLGVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2258881611 530 LDSATEKQLMETIDTICDAHTVIM-IAHR---VSTLknCDRI--FK 569
Cdd:PRK11288 171 LSAREIEQLFRVIRELRAEGRVILyVSHRmeeIFAL--CDAItvFK 214
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
366-570 |
3.12e-15 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 74.61 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 366 FNNVNF--KYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLL----RPEkGNVLIDA-QYKPNSFQWHKK 438
Cdd:cd03233 6 WRNISFttGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnvSVE-GDIHYNGiPYKEFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQsinliDD------TVEANIAFGCdkidkealdnavdSAQLRQFVnslpnglkttigeRGIrvSGGERQRISIAR 512
Cdd:cd03233 85 IIYVSE-----EDvhfptlTVRETLDFAL-------------RCKGNEFV-------------RGI--SGGERKRVSIAE 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 513 ALYRNPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMiahrVSTLKNCDRIFKI 570
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlKTTTF----VSLYQASDEIYDL 186
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-556 |
4.00e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.33 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGL--LRPE---KGNVLIDAQ--YKPNSFQWHKKIGYVAQSINLIDD-T 452
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQdiFKMDVIELRRRVQMVFQIPNPIPNlS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 453 VEANIAFGCdKIDK---------EALDNAVDSAQLRQFVnslpnglKTTIGERGIRVSGGERQRISIARALYRNPEVLIF 523
Cdd:PRK14247 99 IFENVALGL-KLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190
....*....|....*....|....*....|...
gi 2258881611 524 DEATSALDSATEKQLMETIDTICDAHTVIMIAH 556
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
364-590 |
5.74e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKknTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYkpnsfqwhkKIGYVA 443
Cdd:PRK09544 5 VSLENVSVSFGQRR--VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL---------RIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLiDDTVEANIA-F-----GCDKIDKEALDNAVDSAQLRQFVNSlpnglkttigergiRVSGGERQRISIARALYRN 517
Cdd:PRK09544 74 QKLYL-DTTLPLTVNrFlrlrpGTKKEDILPALKRVQAGHLIDAPMQ--------------KLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 518 PEVLIFDEATSALDSATEKQLMETIDTI-----CdahTVIMIAHRVstlkncdrifkiengKLSEVRKDSVLAMSHHI 590
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLrreldC---AVLMVSHDL---------------HLVMAKTDEVLCLNHHI 198
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
364-558 |
1.27e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.42 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNskKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKP-----NSFQWHKK 438
Cdd:PRK11831 8 VDMRGVSFTRGN--RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPamsrsRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINLIDD-TVEANIAFgcdkidkealdnavdsaQLRQFVNSLPNGLKTT-------IGERGI------RVSGGE 504
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAY-----------------PLREHTQLPAPLLHSTvmmkleaVGLRGAaklmpsELSGGM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 505 RQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRV 558
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDV 204
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
147-425 |
1.44e-14 |
|
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: 76.76 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 147 VVGSDVeQAFSSGMVSLARSLSEGSVFIFLVGMIVYVNPTLVLIIFVIgMTLGLLtskfllpkFYYWGQNLQQTGFHT-- 224
Cdd:COG4615 110 ALTEDV-RTISQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVL-LGLGVA--------GYRLLVRRARRHLRRar 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 225 ------HKNLMQFFHSFKEIVL-LGKKESFV-KAYQVHS----KERSKVQAIQTATNALprmgIEILFVG-----LFVLT 287
Cdd:COG4615 180 eaedrlFKHFRALLEGFKELKLnRRRRRAFFdEDLQPTAeryrDLRIRADTIFALANNW----GNLLFFAligliLFLLP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 288 IsylcMGHESPMQMIGLLSGYLYagfrLMPGLNRIINDLNALKSVIPSIDRV----HQEYIAFESKSNYVDETSFRFTKS 363
Cdd:COG4615 256 A----LGWADPAVLSGFVLVLLF----LRGPLSQLVGALPTLSRANVALRKIeeleLALAAAEPAAADAAAPPAPADFQT 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 364 IEFNNVNFKYLNSKKN---TLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID 425
Cdd:COG4615 328 LELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD 392
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
353-539 |
1.82e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.72 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 353 VDETSFRFTKSIEFnnvnFKylNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYkpns 432
Cdd:COG4167 7 VRNLSKTFKYRTGL----FR--RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 433 fQWHKKIGYVAQSINLI----DDTVEANIAFGcdKIDKEALDNAVD-SAQLRQfvnslpNGLKTTIGERGIR-------- 499
Cdd:COG4167 77 -LEYGDYKYRCKHIRMIfqdpNTSLNPRLNIG--QILEEPLRLNTDlTAEERE------ERIFATLRLVGLLpehanfyp 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2258881611 500 --VSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLM 539
Cdd:COG4167 148 hmLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQII 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
371-556 |
2.10e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 371 FKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIdliLGLLR--PEKGNVLIDAQykPNSfQWHKK--------IG 440
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTG---LALLRliNSQGEIWFDGQ--PLH-NLNRRqllpvrhrIQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQSINLIDD---TVEANIAFGCdKIDKEALDNAVDSAQLRQFVNSLpnGLKTTIGER-GIRVSGGERQRISIARALYR 516
Cdd:PRK15134 366 VVFQDPNSSLNprlNVLQIIEEGL-RVHQPTLSAAQREQQVIAVMEEV--GLDPETRHRyPAEFSGGQRQRIAIARALIL 442
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTICDAHTV--IMIAH 556
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISH 484
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
364-578 |
3.08e-14 |
|
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: 75.61 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGL--LRPEKGNVLIDAQYKP----------- 430
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEkcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 431 --------NSFQ------WH----------KKIGYVAQSINLI--DDTVEANIAFGCDKID---KEALDNAVDsaqLRQF 481
Cdd:TIGR03269 79 gepcpvcgGTLEpeevdfWNlsdklrrrirKRIAIMLQRTFALygDDTVLDNVLEALEEIGyegKEAVGRAVD---LIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 482 VNslpngLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMI--AHRVS 559
Cdd:TIGR03269 156 VQ-----LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltSHWPE 230
|
250 260
....*....|....*....|
gi 2258881611 560 TLKN-CDRIFKIENGKLSEV 578
Cdd:TIGR03269 231 VIEDlSDKAIWLENGEIKEE 250
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-578 |
3.40e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.76 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 359 RFTKSIEFNNVNFKYLNSKknTLSNINLKINKGESVGIVGHTGSGKSTLIDlILGLLRPEKGNVLIDA----------QY 428
Cdd:PRK14258 3 KLIPAIKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGrveffnqniyER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 429 KPNSFQWHKKIGYVAQSINLIDDTVEANIAFGCDKID---KEALDNAVDSAqLRQfvNSLPNGLKTTIGERGIRVSGGER 505
Cdd:PRK14258 80 RVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpKLEIDDIVESA-LKD--ADLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 506 QRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTIC--DAHTVIMIAH---RVSTLKNCDRIFKIENGKLSEV 578
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHnlhQVSRLSDFTAFFKGNENRIGQL 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
384-567 |
3.48e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.97 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 384 INLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWH---KKIGYVAQ----SIN---LIDD 451
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdlLGMKDDEWRavrSDIQMIFQdplaSLNprmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 452 TVEANIAFGCDKIDKEALDNAVDSAQLRqfVNSLPNglktTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALD 531
Cdd:PRK15079 120 IIAEPLRTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 2258881611 532 SATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRI 567
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRV 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
383-578 |
4.54e-14 |
|
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: 74.84 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKG--NVLIDAQY----KP---NSFQWHKKIGYVAQSINLI-DDT 452
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEWvdmtKPgpdGRGRAKRYIGILHQEYDLYpHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 453 VEANI--AFGCDKIDKEALDNAV--------DSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLI 522
Cdd:TIGR03269 382 VLDNLteAIGLELPDELARMKAVitlkmvgfDEEKAEEILDKYPDEL-----------SEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 523 FDEATSALDSATEKQLMETI--DTICDAHTVIMIAHRVSTLKN-CDRIFKIENGKLSEV 578
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKI 509
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
378-559 |
5.79e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 378 KNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPE---KGNVLIDAQyKPNSFQWHKKIGYVAQ-SINLIDDTV 453
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM-PIDAKEMRAISAYVQQdDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 EANIAFgcdkidkEA---LDNAVDSAQLRQFVN------SLPNGLKTTIGERGIR--VSGGERQRISIARALYRNPEVLI 522
Cdd:TIGR00955 117 REHLMF-------QAhlrMPRRVTKKEKRERVDevlqalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 2258881611 523 FDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRVS 559
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQkGKTIICTIHQPS 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-577 |
6.52e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 369 VNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLI-------DLILGLLRpeKGNVLIDAQ----YKpNSFQWHK 437
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGYRY--SGDVLLGGRsifnYR-DVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 KIGYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRN 517
Cdd:PRK14271 102 RVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 518 PEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVS-TLKNCDRIFKIENGKLSE 577
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVE 242
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
377-587 |
8.14e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 377 KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPE--KGNVLIDAQyKPNSfQWHKKIGYVAQsinliDD--- 451
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNR-KPTK-QILKRTGFVTQ-----DDily 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 452 ---TVEANIAF--------GCDKIDKEALDNAVDSAQlrqfvnSLPNGLKTTIGERGIR-VSGGERQRISIARALYRNPE 519
Cdd:PLN03211 153 phlTVRETLVFcsllrlpkSLTKQEKILVAESVISEL------GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 520 VLIFDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRVSTlkncdRIFKIengklsevrKDSVLAMS 587
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQkGKTIVTSMHQPSS-----RVYQM---------FDSVLVLS 281
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
379-567 |
1.01e-13 |
|
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: 69.66 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 379 NTLSNINLKINKGESVGIVGHTGSGKSTLIdliLGLLRPEKGNVLIDAQYKPNsfqwHKKIGYVAQSINLIDdtveania 458
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV---NEGLYASGKARLISFLPKFS----RNKLIFIDQLQFLID-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 459 fgcdkidkealdnavdsaqlrqfvnslpNGLK-TTIGERGIRVSGGERQRISIARALYRNPE--VLIFDEATSALDSATE 535
Cdd:cd03238 74 ----------------------------VGLGyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|...
gi 2258881611 536 KQLMETIDTICD-AHTVIMIAHRVSTLKNCDRI 567
Cdd:cd03238 126 NQLLEVIKGLIDlGNTVILIEHNLDVLSSADWI 158
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
371-541 |
2.21e-13 |
|
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: 70.13 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 371 FKYLNSKKnTLSNINLK-----INKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykpnsfqwhkKIGYVAQS 445
Cdd:cd03237 1 YTYPTMKK-TLGEFTLEveggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD----------TVSYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 446 INL-IDDTVEaniAFGCDKIDkealdnavDSAQLRQFVNSLPNGLK-TTIGERGIR-VSGGERQRISIARALYRNPEVLI 522
Cdd:cd03237 70 IKAdYEGTVR---DLLSSITK--------DFYTHPYFKTEIAKPLQiEQILDREVPeLSGGELQRVAIAACLSKDADIYL 138
|
170
....*....|....*....
gi 2258881611 523 FDEATSALDSatEKQLMET 541
Cdd:cd03237 139 LDEPSAYLDV--EQRLMAS 155
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
362-560 |
2.58e-13 |
|
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: 72.66 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 362 KSIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYkpnsfqwhkKIGY 441
Cdd:TIGR03719 321 KVIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 442 VAQSINLIDD--TVEANIAFGCDKIDkealdnaVDSAQL--RQFVNSLpnGLKTTIGERGIRV-SGGERQRISIARALYR 516
Cdd:TIGR03719 390 VDQSRDALDPnkTVWEEISGGLDIIK-------LGKREIpsRAYVGRF--NFKGSDQQKKVGQlSGGERNRVHLAKTLKS 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2258881611 517 NPEVLIFDEATSALDSATEKQLMETIDTIcdAHTVIMIAH------RVST 560
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
381-586 |
2.78e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.27 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLrPE---KGNVLIDAQykPNSFQ-----WHKKIGYVAQSINLIDD- 451
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGE--ELQASnirdtERAGIAIIHQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 452 TVEANIAFGCD-----KIDKEALDNAVDS--AQLRQFVNslPNglkTTIGERGirvsGGERQRISIARALYRNPEVLIFD 524
Cdd:PRK13549 98 SVLENIFLGNEitpggIMDYDAMYLRAQKllAQLKLDIN--PA---TPVGNLG----LGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 525 EATSALdsaTEKQLMETIDTICD--AHTV--IMIAHRVSTLKN-CDRIFKIENGK------LSEVRKDSVLAM 586
Cdd:PRK13549 169 EPTASL---TESETAVLLDIIRDlkAHGIacIYISHKLNEVKAiSDTICVIRDGRhigtrpAAGMTEDDIITM 238
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
381-542 |
2.85e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID--AQYKPNSFQwhkKIGYVAQSiNLIDD--TVEAN 456
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDggDIDDPDVAE---ACHYLGHR-NAMKPalTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAF--GCDKIDKEALDNAVDSAQLrQFVNSLPNGLkttigergirVSGGERQRISIARAL--YRNpeVLIFDEATSALDS 532
Cdd:PRK13539 94 LEFwaAFLGGEELDIAAALEAVGL-APLAHLPFGY----------LSAGQKRRVALARLLvsNRP--IWILDEPTAALDA 160
|
170
....*....|
gi 2258881611 533 ATEKQLMETI 542
Cdd:PRK13539 161 AAVALFAELI 170
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
371-577 |
4.16e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.69 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 371 FKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--------YKPNSFQWHKKIGYV 442
Cdd:PRK14246 17 YLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdiFQIDAIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSINLIDD-TVEANIAFGCDK---IDKEALDNAVDSAqLRQFvnslpnGLKTTIGER----GIRVSGGERQRISIARAL 514
Cdd:PRK14246 96 FQQPNPFPHlSIYDNIAYPLKShgiKEKREIKKIVEEC-LRKV------GLWKEVYDRlnspASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 515 YRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAHRVSTL-KNCDRIFKIENGKLSE 577
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVE 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
363-578 |
7.94e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.72 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGL--LRPE---KGNVLIDAQ--YKP--NSF 433
Cdd:PRK14267 4 AIETVNLRVYY--GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEarvEGEVRLFGRniYSPdvDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 434 QWHKKIGYVAQSINLIDD-TVEANIAFGCdKID-----KEALDNAVDSAQLRQfvnSLPNGLKTTIGERGIRVSGGERQR 507
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHlTIYDNVAIGV-KLNglvksKKELDERVEWALKKA---ALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 508 ISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHTVIMIAH------RVStlkncDRIFKIENGKLSEV 578
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaqaaRVS-----DYVAFLYLGKLIEV 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
362-588 |
9.72e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 9.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 362 KSIEFNNVNFKYLNSKkNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ----YKPNSFQwhK 437
Cdd:PRK10522 321 QTLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpvtaEQPEDYR--K 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 KIGYVAQSINLIDDTveaniafgcdkIDKEAldNAVDSAQLRQFVNSLPNGLKTTIGE---RGIRVSGGERQRISIARAL 514
Cdd:PRK10522 398 LFSAVFTDFHLFDQL-----------LGPEG--KPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 515 YRNPEVLIFDEATSALDSATEK--------QLMETidticdAHTVIMIAHRVSTLKNCDRIFKIENGKLSEVRKDSVLAM 586
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRRefyqvllpLLQEM------GKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAA 538
|
..
gi 2258881611 587 SH 588
Cdd:PRK10522 539 SR 540
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
390-561 |
1.11e-12 |
|
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: 65.86 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 390 KGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVlidaqykpnsfqwhkkigyvaqsinliddtveanIAFGCDKIDKEAL 469
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------IYIDGEDILEEVL 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 470 DNAvdsaqlrqfvnslpngLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH 549
Cdd:smart00382 47 DQL----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
170
....*....|....*....
gi 2258881611 550 -------TVIMIAHRVSTL 561
Cdd:smart00382 111 lkseknlTVILTTNDEKDL 129
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
381-579 |
1.38e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.06 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ----YKPNSFqWHKKIGYVA---QSINLIDD-T 452
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditgLSPRER-RRLGVAYIPedrLGRGLVPDmS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 453 VEANIAFGcdKIDKEALDNA--VDSAQLRQFVNSL-------PNGLKTTIGergiRVSGGERQRISIARALYRNPEVLIF 523
Cdd:COG3845 353 VAENLILG--RYRRPPFSRGgfLDRKAIRAFAEELieefdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 524 DEATSALD-SATE---KQLMETidtiCDAHTVIMIahrVST-----LKNCDRIFKIENGKLSEVR 579
Cdd:COG3845 427 AQPTRGLDvGAIEfihQRLLEL----RDAGAAVLL---ISEdldeiLALSDRIAVMYEGRIVGEV 484
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
363-573 |
2.12e-12 |
|
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: 66.11 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYL--NSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGllRPE----KGNVLIDAQYKPNSFQwh 436
Cdd:cd03232 3 VLTWKNLNYTVPvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTagviTGEILINGRPLDKNFQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 437 KKIGYVAQ-SINLIDDTVEANIAFgcdkidkealdnavdSAQLRqfvnslpnGLkttigergirvSGGERQRISIARALY 515
Cdd:cd03232 79 RSTGYVEQqDVHSPNLTVREALRF---------------SALLR--------GL-----------SVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 516 RNPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVS--TLKNCDRIFKIENG 573
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSgQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
387-532 |
2.71e-12 |
|
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: 69.43 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 387 KINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPnsfQwhkkigYVAQSinlIDDTVEANIafgcdki 464
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisYKP---Q------YISPD---YDGTVEEFL------- 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 465 dKEALDNAVDSAQLR-QFVNSLpnGLKtTIGERGIR-VSGGERQRISIARALYRNPEVLIFDEATSALDS 532
Cdd:COG1245 423 -RSANTDDFGSSYYKtEIIKPL--GLE-KLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
381-575 |
2.83e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.19 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIdAQYKPnsfqWHKKIGYVAQsINLIddtveaniaFG 460
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV-LGYVP----FKRRKEFARR-IGVV---------FG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 461 -----------CD---------KIDKEALDNAVD--------SAQLRQFVNSLpnglkttigergirvSGGERQRISIAR 512
Cdd:COG4586 103 qrsqlwwdlpaIDsfrllkaiyRIPDAEYKKRLDelvelldlGELLDTPVRQL---------------SLGQRMRCELAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 513 ALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKL 575
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
379-585 |
5.16e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 379 NTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLrPEKGNVLID----AQYKPNSFQWHKkiGYVAQSIN-LIDDTV 453
Cdd:PRK03695 10 TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAgqplEAWSAAELARHR--AYLSQQQTpPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 EANIA-FGCDKIDKEALDNAVDsaQLRQFVNsLPNGLKTTIGergiRVSGGERQRISIARALYR-----NPE--VLIFDE 525
Cdd:PRK03695 87 FQYLTlHQPDKTRTEAVASALN--EVAEALG-LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 526 ATSALDSATEKQLMETIDTICDAH-TVIMIAHRVS-TLKNCDRIFKIENGKL------SEVRKDSVLA 585
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGiAVVMSSHDLNhTLRHADRVWLLKQGKLlasgrrDEVLTPENLA 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
377-557 |
7.34e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 377 KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLL--RPEKGNVLIDaqykPNSFqWHKKIgyVAQSINLIDDTVE 454
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP----DNQF-GREAS--LIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 455 AniafgcdkidKEALDNA--VDSAQLRQFVNSLpnglkttigergirvSGGERQRISIARALYRNPEVLIFDEATSALDS 532
Cdd:COG2401 115 A----------VELLNAVglSDAVLWLRRFKEL---------------STGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*..
gi 2258881611 533 ATEKQLMETIDTICDAH--TVIMIAHR 557
Cdd:COG2401 170 QTAKRVARNLQKLARRAgiTLVVATHH 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
381-587 |
8.07e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID--AQYKPNSFQWHK-KIGYVAQSINLIDD-TVEAN 456
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnPCARLTPAKAHQlGIYLVPQEPLLFPNlSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAFGCDKidkealdNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSggERQRISIARALYRNPEVLIFDEATSALDSATEK 536
Cdd:PRK15439 107 ILFGLPK-------RQASMQKMKQLLAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 537 QLMETIDTICD-AHTVIMIAHRVSTLKN-CDRIFKIENG------KLSEVRKDSVL-AMS 587
Cdd:PRK15439 178 RLFSRIRELLAqGVGIVFISHKLPEIRQlADRISVMRDGtialsgKTADLSTDDIIqAIT 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
377-575 |
1.79e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.65 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 377 KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID----AQYKPNsfQWHKKIGYVAQsINLIDD- 451
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdkpiSMLSSR--QLARRLALLPQ-HHLTPEg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 452 -TVEANIAFG----------CDKIDKEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEV 520
Cdd:PRK11231 91 iTVRELVAYGrspwlslwgrLSAEDNARVNQAMEQTRINHLADRRLTDL-----------SGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 521 LIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVS-TLKNCDRIFKIENGKL 575
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNqASRYCDHLVVLANGHV 216
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
381-531 |
1.99e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ--YKPNSFQWH---KKIGYVAQ----SIN---L 448
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdlLKADPEAQKllrQKIQIVFQnpygSLNprkK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 449 IDDTVEANIAFGCDkidkeaLDNAVDSAQLRQFVNSLpnGLKTtigERGIR----VSGGERQRISIARALYRNPEVLIFD 524
Cdd:PRK11308 111 VGQILEEPLLINTS------LSAAERREKALAMMAKV--GLRP---EHYDRyphmFSGGQRQRIAIARALMLDPDVVVAD 179
|
....*..
gi 2258881611 525 EATSALD 531
Cdd:PRK11308 180 EPVSALD 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
381-574 |
2.09e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.39 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGlLRPE---KGNVLIDAQ-YKPNSFQ--WHKKIGYVAQSINLIDD-TV 453
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSpLKASNIRdtERAGIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 EANIAFGCD---KIDKEALDNAVDSAQ--LRQF-VNSLPNGLktTIGERGirvsGGERQRISIARALYRNPEVLIFDEAT 527
Cdd:TIGR02633 96 AENIFLGNEitlPGGRMAYNAMYLRAKnlLRELqLDADNVTR--PVGDYG----GGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 528 SALdsaTEKQLMETIDTICD--AHTV--IMIAHRVSTLKN-CDRIFKIENGK 574
Cdd:TIGR02633 170 SSL---TEKETEILLDIIRDlkAHGVacVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
371-585 |
2.16e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 371 FKYLNSKknTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLidAQYKPNSFQWHKKIGYVAQSINLID 450
Cdd:PRK13638 9 FRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVL--WQGKPLDYSKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 451 D--------TVEANIAFGCDK--IDKEALDNAVDSAQlrqfvnslpnglkTTIGERGIR------VSGGERQRISIARAL 514
Cdd:PRK13638 85 DpeqqifytDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 515 YRNPEVLIFDEATSALDSATEKQLMETIDTIC-DAHTVIMIAHRVstlkncDRIFKIENGkLSEVRKDSVLA 585
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDI------DLIYEISDA-VYVLRQGQILT 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
372-568 |
2.49e-11 |
|
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: 66.50 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 372 KYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYkpnsfqwhkKIGYVAQSINLIDD 451
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI---------KVGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 452 -TVEANIAFGC------------------------DKIDKE--ALDNAVDSA-------QLRQFVNSL---PNGLKTTig 494
Cdd:TIGR03719 83 kTVRENVEEGVaeikdaldrfneisakyaepdadfDKLAAEqaELQEIIDAAdawdldsQLEIAMDALrcpPWDADVT-- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 495 ergiRVSGGERQRISIARALYRNPEVLIFDEATSALDSAT----EKQLMETidticdAHTVIMIAHrvstlkncDRIF 568
Cdd:TIGR03719 161 ----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQEY------PGTVVAVTH--------DRYF 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
368-577 |
2.72e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 368 NVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLrpeKGNVLIDAQYKPNSFQW----HKKIGYV- 442
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL---AANGRIGGSATFNGREIlnlpEKELNKLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 443 AQSINLI--DDTVEAN--------------IAFGCDKidKEALD------NAVDSAQLRQFVNSLPNglkttigergiRV 500
Cdd:PRK09473 96 AEQISMIfqDPMTSLNpymrvgeqlmevlmLHKGMSK--AEAFEesvrmlDAVKMPEARKRMKMYPH-----------EF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 501 SGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKLSE 577
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGiCDKVLVMYAGRTME 242
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
384-531 |
2.97e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.25 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 384 INLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDA----QYKPNSfqwhKKIGYVAQSINLIDD-TVEANIA 458
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnELEPAD----RDIAMVFQNYALYPHmSVRENMA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 459 FGCD--KIDKEALDNAVDSA----QLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEATSALD 531
Cdd:PRK11650 99 YGLKirGMPKAEIEERVAEAarilELEPLLDRKPREL-----------SGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
383-581 |
3.93e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.47 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY---KPNsfqwHK--KIGYVA--QSINLIDD-TV- 453
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPG----HQiaRMGVVRtfQHVRLFREmTVi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 -----------EANIAFGCDKI------DKEALDNA---VDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARA 513
Cdd:PRK11300 99 enllvaqhqqlKTGLFSGLLKTpafrraESEALDRAatwLERVGLLEHANRQAGNL-----------AYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 514 LYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIE------NGKLSEVRKD 581
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGiSDRIYVVNqgtplaNGTPEEIRNN 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
377-540 |
4.10e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 377 KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQY--KPNSFQWHKKIGYVAQSINLIDD-TV 453
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqHYASKEVARRIGLLAQNATTPGDiTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 EANIAFG----------CDKIDKEALDNAVDSAQL----RQFVNSLpnglkttigergirvSGGERQRISIARALYRNPE 519
Cdd:PRK10253 99 QELVARGryphqplftrWRKEDEEAVTKAMQATGIthlaDQSVDTL---------------SGGQRQRAWIAMVLAQETA 163
|
170 180
....*....|....*....|.
gi 2258881611 520 VLIFDEATSALDSATEKQLME 540
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLE 184
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
381-589 |
5.58e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.16 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPekgNVLIDAqykpNSFQWhkkigyvaQSINLIDDTVEA----- 455
Cdd:COG4170 23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD---NWHVTA----DRFRW--------NGIDLLKLSPRErrkii 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 456 --NIAFgcdkIDKEALDNAVDSAQL-RQFVNSLPNG-LKTTIGER---------------GIR------------VSGGE 504
Cdd:COG4170 88 grEIAM----IFQEPSSCLDPSAKIgDQLIEAIPSWtFKGKWWQRfkwrkkraiellhrvGIKdhkdimnsypheLTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 505 RQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTLKN-CDRIFKIENGKLSEV-RK 580
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLISHDLESISQwADTITVLYCGQTVESgPT 243
|
....*....
gi 2258881611 581 DSVLAMSHH 589
Cdd:COG4170 244 EQILKSPHH 252
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
381-586 |
7.41e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 7.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNvlIDAQYKPNSFQWHKK-----IGYVAQSINLIDD-TVE 454
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGS--ILYLGKEVTFNGPKSsqeagIGIIHQELNLIPQlTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 455 ANI--------AFGC---DKIDKEAldnavdsAQLRQFVNsLPNGLKTTIGERGIrvsgGERQRISIARALYRNPEVLIF 523
Cdd:PRK10762 98 ENIflgrefvnRFGRidwKKMYAEA-------DKLLARLN-LRFSSDKLVGELSI----GEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 524 DEATSAL-DSATEkQLMETIDTICDAHTVIM-IAHRvstLKN----CDRIFKIENGK------LSEVRKDSVLAM 586
Cdd:PRK10762 166 DEPTDALtDTETE-SLFRVIRELKSQGRGIVyISHR---LKEifeiCDDVTVFRDGQfiaereVADLTEDSLIEM 236
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
375-567 |
1.61e-10 |
|
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: 61.86 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 375 NSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGllrPEKGNVLIDAQYKPNSFQWHKKIGYVAQSINL----ID 450
Cdd:cd03271 5 GARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLY---PALARRLHLKKEQPGNHDRIEGLEHIDKVIVIdqspIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 451 DTVEANIA-----------FGCD------------------KIDKEALDNAVDSAqlRQFVNSLP---NGLKT------- 491
Cdd:cd03271 82 RTPRSNPAtytgvfdeireLFCEvckgkrynretlevrykgKSIADVLDMTVEEA--LEFFENIPkiaRKLQTlcdvglg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 492 --TIGERGIRVSGGERQRISIARALYR---NPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKNCD 565
Cdd:cd03271 160 yiKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNLDVIKCAD 239
|
..
gi 2258881611 566 RI 567
Cdd:cd03271 240 WI 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
388-531 |
3.09e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 388 INKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVL--IDAQYKPnsfQwhkkigYVAQSinlIDDTVEANIAFGCDKID 465
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpeLKISYKP---Q------YIKPD---YDGTVEDLLRSITDDLG 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 466 kealDNAVDSAQLRQFvnSLPNGLKTTIGErgirVSGGERQRISIARALYRNPEVLIFDEATSALD 531
Cdd:PRK13409 430 ----SSYYKSEIIKPL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
353-572 |
3.44e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 353 VDETSfRFTKSI-EFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYkpn 431
Cdd:PRK11147 309 VEEAS-RSGKIVfEMENVNYQI--DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 432 sfqwhkKIGYVAQSINLID--DTVEANIAFGcdkiDKEALDNAVDS---AQLRQFVNSlPNGLKTTIGErgirVSGGERQ 506
Cdd:PRK11147 383 ------EVAYFDQHRAELDpeKTVMDNLAEG----KQEVMVNGRPRhvlGYLQDFLFH-PKRAMTPVKA----LSGGERN 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 507 RISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTIcdAHTVIMIAHrvstlkncDRIFkIEN 572
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY--QGTVLLVSH--------DRQF-VDN 502
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
383-577 |
4.21e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.57 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykPNSFqwhKKIGYVAQSINLI--DDTVEAN---- 456
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH--PLHF---GDYSYRSQRIRMIfqDPSTSLNprqr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAFGCD-------KIDKEALDNAVDSAqLRQF------VNSLPNGLKTtigergirvsgGERQRISIARALYRNPEVLIF 523
Cdd:PRK15112 106 ISQILDfplrlntDLEPEQREKQIIET-LRQVgllpdhASYYPHMLAP-----------GQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881611 524 DEATSALDSATEKQLMETIDTICDAHTV--IMIAHRVSTLKN-CDRIFKIENGKLSE 577
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHiSDQVLVMHQGEVVE 230
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
381-577 |
5.35e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykpnsfqwhkkIGYVAQSINL------IDDTVE 454
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLngqltgIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 455 ANIAFGCDKID-KEALDNAVDSAQLRQFVNslpNGLKTtigergirVSGGERQRISIARALYRNPEVLIFDEATSALDSA 533
Cdd:PRK13545 109 KGLMMGLTKEKiKEIIPEIIEFADIGKFIY---QPVKT--------YSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2258881611 534 TEKQLMETIDTICD-AHTVIMIAHRVSTLKN-CDRIFKIENGKLSE 577
Cdd:PRK13545 178 FTKKCLDKMNEFKEqGKTIFFISHSLSQVKSfCTKALWLHYGQVKE 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
368-556 |
6.56e-10 |
|
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: 61.62 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 368 NVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPE----KGNVLIDAQ---YKPNSfQWHK--- 437
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQdllGLSER-ELRRirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 -KIGYVAQ----SIN-LIddTVEANIAfgcdkidkEALD--NAVDSAQLRQFVNSLpngLKTTigerGIR---------- 499
Cdd:COG4172 92 nRIAMIFQepmtSLNpLH--TIGKQIA--------EVLRlhRGLSGAAARARALEL---LERV----GIPdperrldayp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 500 --VSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAH 556
Cdd:COG4172 155 hqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITH 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
377-575 |
6.96e-10 |
|
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: 59.08 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 377 KKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPE--KGNVLIDAQykpnsfqwhkkigyvaqsiNLIDDTVE 454
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGE-------------------DITDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 455 AN------IAFgcdkidKEALdnAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEATS 528
Cdd:cd03217 73 ERarlgifLAF------QYPP--EIPGVKNADFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2258881611 529 ALDSATEKQLMETIDTICDAHT-VIMIAH--RVSTLKNCDRIFKIENGKL 575
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKsVLIITHyqRLLDYIKPDRVHVLYDGRI 183
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
384-575 |
8.72e-10 |
|
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: 61.95 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 384 INLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQykpnsfQWHKKIGYVAQSINLIDdtvEANIAFGCDK 463
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK------DIETNLDAVRQSLGMCP---QHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 464 IDKEAL------DNAVDSAQLRQFVNSLPNGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQ 537
Cdd:TIGR01257 1020 VAEHILfyaqlkGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190
....*....|....*....|....*....|....*....
gi 2258881611 538 LMETIDTICDAHTVIMIAHRVSTLKNC-DRIFKIENGKL 575
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRL 1138
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
391-561 |
1.01e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 391 GESVGIVGHTGSGKSTLIDLILGLLRPEKGNV--------LIDAqYKPNSFQ-WHKKI--GYVA-----QSINLIDDTVE 454
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDE-FRGSELQnYFTKLleGDVKvivkpQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 455 ANIAFGCDKID-KEALDNAVDSAQLRQFVnslpnglkttigERGI-RVSGGERQRISIARALYRNPEVLIFDEATSALDS 532
Cdd:cd03236 105 GKVGELLKKKDeRGKLDELVDQLELRHVL------------DRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190
....*....|....*....|....*....|...
gi 2258881611 533 ateKQLMETIDTI----CDAHTVIMIAHRVSTL 561
Cdd:cd03236 173 ---KQRLNAARLIrelaEDDNYVLVVEHDLAVL 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
381-542 |
1.63e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.57 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYkpnsfqwhkKIGYVAQSinliddtveaNIAFg 460
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI---------KLGYFAQH----------QLEF- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 461 cDKIDKEALDNAVDSA------QLRQFVNSLP-NGLKTTigERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSA 533
Cdd:PRK10636 388 -LRADESPLQHLARLApqeleqKLRDYLGGFGfQGDKVT--EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
....*....
gi 2258881611 534 TEKQLMETI 542
Cdd:PRK10636 465 MRQALTEAL 473
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
383-531 |
1.91e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVL-----IDaqykPNSFQWHKKIGYVAQSINLIDD-TVEAN 456
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVD----AGDIATRRRVGYMSQAFSLYGElTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IA-----FGCDKID-KEALDNAVDSAQLRQFVNSLPNGLkttigergirvSGGERQRISIARALYRNPEVLIFDEATSAL 530
Cdd:NF033858 360 LElharlFHLPAAEiAARVAEMLERFDLADVADALPDSL-----------PLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
.
gi 2258881611 531 D 531
Cdd:NF033858 429 D 429
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
381-531 |
3.15e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLidaqYKPNSFQWHKKI---------------GYVAQs 445
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH----YRMRDGQLRDLYalseaerrrllrtewGFVHQ- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 446 iNLIDD---TVEA--NIA----------FGcdKIDKEALD--NAVDSAQLRqfVNSLPnglkTTIgergirvSGGERQRI 508
Cdd:PRK11701 97 -HPRDGlrmQVSAggNIGerlmavgarhYG--DIRATAGDwlERVEIDAAR--IDDLP----TTF-------SGGMQQRL 160
|
170 180
....*....|....*....|...
gi 2258881611 509 SIARALYRNPEVLIFDEATSALD 531
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
347-578 |
5.69e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 347 ESKSNYVDETSFrftksiEFNNVNFKylnsKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID- 425
Cdd:PRK09700 255 ENVSNLAHETVF------EVRNVTSR----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 426 AQYKPNS--FQWHKKIGYVAQS------------------------------INLIDDTVEANIAfgcdkiDKEALDNAV 473
Cdd:PRK09700 325 KDISPRSplDAVKKGMAYITESrrdngffpnfsiaqnmaisrslkdggykgaMGLFHEVDEQRTA------ENQRELLAL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 474 DSAQLRQFVNSLpnglkttigergirvSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICD-AHTVI 552
Cdd:PRK09700 399 KCHSVNQNITEL---------------SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADdGKVIL 463
|
250 260
....*....|....*....|....*..
gi 2258881611 553 MIAHRV-STLKNCDRIFKIENGKLSEV 578
Cdd:PRK09700 464 MVSSELpEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
390-531 |
6.09e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 390 KGESVGIVGHTGSGKSTLIDLILGLLRPEKGNV--------LIDAqYKPNSFQWH------------KKIGYVAQSINLI 449
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKR-FRGTELQNYfkklyngeikvvHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 450 DDTVeaniafgcdkidKEALDNAVDSAQLRQFVNSLpnGLKTTIgERGIRV-SGGERQRISIARALYRNPEVLIFDEATS 528
Cdd:PRK13409 177 KGKV------------RELLKKVDERGKLDEVVERL--GLENIL-DRDISElSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
...
gi 2258881611 529 ALD 531
Cdd:PRK13409 242 YLD 244
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
381-577 |
6.22e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIdaqykPNSFQwhkkIGYVAQSINLID----DTV--- 453
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF-----PGNWQ----LAWVNQETPALPqpalEYVidg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 -------EANIAFGCDKIDKEA-------LDnAVDSAQLRQFVNSLPNGL--KTTIGERGIR-VSGGERQRISIARALYR 516
Cdd:PRK10636 88 dreyrqlEAQLHDANERNDGHAiatihgkLD-AIDAWTIRSRAASLLHGLgfSNEQLERPVSdFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 517 NPEVLIFDEATSALDSAT----EKQLMETidticdAHTVIMIAHRVSTLKN-CDRIFKIENGKLSE 577
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAviwlEKWLKSY------QGTLILISHDRDFLDPiVDKIIHIEQQSLFE 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
390-531 |
6.71e-09 |
|
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: 58.64 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 390 KGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDA-------QYKPNSFQWH--------KKIGYVAQSINLIDDTVE 454
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdevlkRFRGTELQDYfkklangeIKVAHKPQYVDLIPKVFK 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 455 ANIafgcdkidKEALDNAVDSAQLRQFVNSLpnGLKTTIgERGIRV-SGGERQRISIARALYRNPEVLIFDEATSALD 531
Cdd:COG1245 178 GTV--------RELLEKVDERGKLDELAEKL--GLENIL-DRDISElSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
329-555 |
1.00e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 329 LKSVIPSIDRVHQEY------IAFESKSNYVDETSFRFTKSieFNNVNFKYLNS------------KKNTLSNINLKINK 390
Cdd:TIGR00956 9 VKNFRKLIDSDPIYYkpyklgVAYKNLSAYGVAADSDYQPT--FPNALLKILTRgfrklkkfrdtkTFDILKPMDGLIKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 391 GESVGIVGHTGSGKSTLIDLIL----GLLRPEKGNVLIDAqYKPNSFQWHKK--IGYVAQS-INLIDDTVEANIAFGC-- 461
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG-ITPEEIKKHYRgdVVYNAETdVHFPHLTVGETLDFAArc 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 462 -------DKIDKEALDNAVDSAQLRQFvnSLPNGLKTTIGERGIR-VSGGERQRISIARALYRNPEVLIFDEATSALDSA 533
Cdd:TIGR00956 166 ktpqnrpDGVSREEYAKHIADVYMATY--GLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSA 243
|
250 260
....*....|....*....|...
gi 2258881611 534 TEKQLMETIDTICD-AHTVIMIA 555
Cdd:TIGR00956 244 TALEFIRALKTSANiLDTTPLVA 266
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
361-565 |
1.01e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 361 TKSIEFNNVNFKYLNSKkNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQwHKKIG 440
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ-KNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 441 YVAQSIN-------LIDDTVEANiAFG-------CDKIDKEALDNA---VDSAQLRQfvnslpnglkTTIGErgirVSGG 503
Cdd:PRK15056 82 YVPQSEEvdwsfpvLVEDVVMMG-RYGhmgwlrrAKKRDRQIVTAAlarVDMVEFRH----------RQIGE----LSGG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 504 ERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRV-STLKNCD 565
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDeGKTMLVSTHNLgSVTEFCD 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
363-539 |
1.07e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.79 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 363 SIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLrPE------------KGNVLIDAQYKP 430
Cdd:PRK15134 7 AIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypsgdirfHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 431 NSFQWHKKIGYVAQ----SINLIDdTVEANIA--------FGCDKIDKEALDnAVDSAQLRQFVNSL---PNGLkttige 495
Cdd:PRK15134 86 LRGVRGNKIAMIFQepmvSLNPLH-TLEKQLYevlslhrgMRREAARGEILN-CLDRVGIRQAAKRLtdyPHQL------ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2258881611 496 rgirvSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLM 539
Cdd:PRK15134 158 -----SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
354-577 |
1.46e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 354 DETSFRFTKSIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSF 433
Cdd:PRK10261 5 DELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 434 QwhKKIGYVAQSINLIDDTVEANIAFgcdkIDKEALD--NAV--------DSAQLRQFVNS---------------LPNG 488
Cdd:PRK10261 85 R--QVIELSEQSAAQMRHVRGADMAM----IFQEPMTslNPVftvgeqiaESIRLHQGASReeamveakrmldqvrIPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 489 lKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICD--AHTVIMIAHRVSTLKN-CD 565
Cdd:PRK10261 159 -QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKemSMGVIFITHDMGVVAEiAD 237
|
250
....*....|..
gi 2258881611 566 RIFKIENGKLSE 577
Cdd:PRK10261 238 RVLVMYQGEAVE 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
382-576 |
1.86e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 382 SNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-YKPNSFQWHKKIGYV-----AQSINL-IDDTVE 454
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKeINALSTAQRLARGLVylpedRQSSGLyLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 455 ANIafgCDKIDKEA---LDNAVDSAQLRQFVNSLpnGLKTTIGERGIR-VSGGERQRISIARALYRNPEVLIFDEATSAL 530
Cdd:PRK15439 360 WNV---CALTHNRRgfwIKPARENAVLERYRRAL--NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2258881611 531 DSATEKQLMETIDTICDAHT-VIMIA---HRVSTLknCDRIFKIENGKLS 576
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVaVLFISsdlEEIEQM--ADRVLVMHQGEIS 482
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
383-539 |
2.12e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ----YKPNSFQ-WHKKIGYVAQS--------INLI 449
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtLSPGKLQaLRRDIQFIFQDpyasldprQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 450 DDTVEANIAFGCdkIDKEALDNAVdsAQLRQFVNSLPnglkttigERGIR----VSGGERQRISIARALYRNPEVLIFDE 525
Cdd:PRK10261 422 DSIMEPLRVHGL--LPGKAAAARV--AWLLERVGLLP--------EHAWRypheFSGGQRQRICIARALALNPKVIIADE 489
|
170
....*....|....
gi 2258881611 526 ATSALDSATEKQLM 539
Cdd:PRK10261 490 AVSALDVSIRGQII 503
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
346-553 |
2.40e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 346 FESKSNYVDETSFRFTKSIEFNNVNF--KYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRP---EKG 420
Cdd:TIGR00956 742 SDDVNDEKDMEKESGEDIFHWRNLTYevKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGG 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 421 NVLIDAQYKPNSFQwhKKIGYVAQS-INLIDDTVEANIAFGC-----DKIDKEALDNAVDSA----QLRQFVNSLpnglk 490
Cdd:TIGR00956 822 DRLVNGRPLDSSFQ--RSIGYVQQQdLHLPTSTVRESLRFSAylrqpKSVSKSEKMEYVEEVikllEMESYADAV----- 894
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 491 ttIGERGIRVSGGERQRISIARALYRNPEVLIF-DEATSALDSATEKQLMETIDTICDAHTVIM 553
Cdd:TIGR00956 895 --VGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAIL 956
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
376-589 |
2.76e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 376 SKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLidaqykpNSFQWHKKIGYvAQSINLIDDTVEA 455
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ-------SQFSHITRLSF-EQLQKLVSDEWQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 456 N----IAFGCDKIDKEA----LDNAVDSAQLRQFVNSLpnGLKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEAT 527
Cdd:PRK10938 86 NntdmLSPGEDDTGRTTaeiiQDEVKDPARCEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 528 SALDSATEKQLMETIDTICDA-HTVIMIAHR----------VSTLKNCDRifkIENGKLSEVRKDSVLAMSHH 589
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQSgITLVLVLNRfdeipdfvqfAGVLADCTL---AETGEREEILQQALVAQLAH 233
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
381-584 |
3.67e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.82 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVlidaqykpnsfQWHKKIGYVAQSINLIDD-TVEANIAF 459
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLSGQlTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 460 GC------DKIDKEALDNAVDSAQLRQFvnslpnglkttIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSA 533
Cdd:PRK13546 109 KMlcmgfkRKEIKAMTPKIIEFSELGEF-----------IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2258881611 534 TEKQLMETIDTICDAH-TVIMIAHRVSTLKN-CDRIFKIENGKLSEV-RKDSVL 584
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNkTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYgELDDVL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
364-531 |
3.88e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLlRPEKGN---VLIDAQYKPNSFQW--HKK 438
Cdd:PRK10938 261 IVLNNGVVSY-NDRP-ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQGYSndlTLFGRRRGSGETIWdiKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQSINL---IDDTVEANIAFG-CDKIdkeALDNAVDSAQ---LRQFVNSLpnGLKTTIGERGIR-VSGGERQRISI 510
Cdd:PRK10938 338 IGYVSSSLHLdyrVSTSVRNVILSGfFDSI---GIYQAVSDRQqklAQQWLDIL--GIDKRTADAPFHsLSWGQQRLALI 412
|
170 180
....*....|....*....|.
gi 2258881611 511 ARALYRNPEVLIFDEATSALD 531
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLD 433
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
364-531 |
5.16e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYkpnsfqwhkKIGYVA 443
Cdd:PRK11819 325 IEAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLIDD--TVEANIAFGCDKI---DKEaldnaVDSaqlRQFVNSLpnGLKTT-----IGErgirVSGGERQRISIARA 513
Cdd:PRK11819 394 QSRDALDPnkTVWEEISGGLDIIkvgNRE-----IPS---RAYVGRF--NFKGGdqqkkVGV----LSGGERNRLHLAKT 459
|
170
....*....|....*...
gi 2258881611 514 LYRNPEVLIFDEATSALD 531
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLD 477
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
368-565 |
5.28e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 368 NVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-YKPNSFQWHKKIGYVAQSI 446
Cdd:PRK13540 6 ELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsIKKDLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 447 NLIDD-TVEANIAFGCDKIDKE-ALDNAVDSAQLRQFVNsLPNGLkttigergirVSGGERQRISIARALYRNPEVLIFD 524
Cdd:PRK13540 84 GINPYlTLRENCLYDIHFSPGAvGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2258881611 525 EATSALDSATekqlMETIDTICDAH-----TVIMIAHRVSTLKNCD 565
Cdd:PRK13540 153 EPLVALDELS----LLTIITKIQEHrakggAVLLTSHQDLPLNKAD 194
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
381-586 |
5.65e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIdaQYKPNSFQWHKK-----IGYVAQSINLI-DDTVE 454
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF--QGKEIDFKSSKEalengISMVHQELNLVlQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 455 ANIAFGcdKIDKEALdnAVDSAQLRQFVNSLPNGLKTTIG--ERGIRVSGGERQRISIARALYRNPEVLIFDEATSALds 532
Cdd:PRK10982 92 DNMWLG--RYPTKGM--FVDQDKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL-- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 533 aTEKQ---LMETIDTICDAHT-VIMIAHRV-STLKNCDRIFKIENGK------LSEVRKDSVLAM 586
Cdd:PRK10982 166 -TEKEvnhLFTIIRKLKERGCgIVYISHKMeEIFQLCDEITILRDGQwiatqpLAGLTMDKIIAM 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
381-543 |
8.26e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-YKPNSFQWHKKIGYVAQSINLIDD------TV 453
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHeVVTRSPQDGLANGIVYISEDRKRDglvlgmSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 EANIAF--------GCDKIDKEALDNAVDSAqLRQFVNSLPNgLKTTIGErgirVSGGERQRISIARALYRNPEVLIFDE 525
Cdd:PRK10762 348 KENMSLtalryfsrAGGSLKHADEQQAVSDF-IRLFNIKTPS-MEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDE 421
|
170
....*....|....*...
gi 2258881611 526 ATSALDSATEKQLMETID 543
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLIN 439
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
32-205 |
8.28e-08 |
|
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: 53.97 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 32 LGIVGFALVVSLLEVVTASVIvvfaqvlndpsvgQKYFQKLGITENLSpgkTVFYVAIAVGVVYVVKNLIAaaevFFQNF 111
Cdd:cd18552 2 ALAILGMILVAATTAALAWLL-------------KPLLDDIFVEKDLE---ALLLVPLAIIGLFLLRGLAS----YLQTY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 112 SI----QKMCFEFKNKLLHRYAQADYGFYLTRNSSFGLQVVGSDVEQ---AFSSGMVSLARslsEGSVFIFLVGMIVYVN 184
Cdd:cd18552 62 LMayvgQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQvqnALTSALTVLVR---DPLTVIGLLGVLFYLD 138
|
170 180
....*....|....*....|.
gi 2258881611 185 PTLVLIIFVIGMTLGLLTSKF 205
Cdd:cd18552 139 WKLTLIALVVLPLAALPIRRI 159
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
372-568 |
1.34e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 372 KYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKpnsfqwhkkIGYVAQSINLIDD 451
Cdd:PRK11819 14 KVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIK---------VGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 452 -TVEANIAFGC----DKIDK--------------------------EALDNA----VDSaQLRQFVNSL---PNGLKTTI 493
Cdd:PRK11819 85 kTVRENVEEGVaevkAALDRfneiyaayaepdadfdalaaeqgelqEIIDAAdawdLDS-QLEIAMDALrcpPWDAKVTK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 494 gergirVSGGERQRISIARALYRNPEVLIFDEATSALDSAT----EKQLMETidticdAHTVIMIAHrvstlkncDRIF 568
Cdd:PRK11819 164 ------LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHDY------PGTVVAVTH--------DRYF 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
343-575 |
2.19e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 343 YIAFESksnyvDETSFRftKSIEFNNVNFKYlnSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNV 422
Cdd:PRK15064 306 FIRFEQ-----DKKLHR--NALEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 423 lidaqykpnsfQWHKK--IGYVAQsinliDDTVEaniaFGCDKidkealdNAVD-SAQLRQfvnslPNGLKTTIgeRGI- 498
Cdd:PRK15064 377 -----------KWSENanIGYYAQ-----DHAYD----FENDL-------TLFDwMSQWRQ-----EGDDEQAV--RGTl 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 499 --------------RV-SGGERQRISIARALYRNPEVLIFDEATSALDsatekqlMETIDTICDA-----HTVIMIAH-R 557
Cdd:PRK15064 423 grllfsqddikksvKVlSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNMAlekyeGTLIFVSHdR 495
|
250 260
....*....|....*....|
gi 2258881611 558 --VSTLKNcdRIFKIENGKL 575
Cdd:PRK15064 496 efVSSLAT--RIIEITPDGV 513
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
375-575 |
2.82e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.29 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 375 NSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPE-KGNVLIDAqyKPNSFQWHKKIgyVAQSINLIDDT- 452
Cdd:TIGR02633 270 NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFING--KPVDIRNPAQA--IRAGIAMVPEDr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 453 ----------VEANIAF-------GCDKIDKEALDNAVDSA----QLRQFVNSLPNGlkttigergiRVSGGERQRISIA 511
Cdd:TIGR02633 346 krhgivpilgVGKNITLsvlksfcFKMRIDAAAELQIIGSAiqrlKVKTASPFLPIG----------RLSGGNQQKAVLA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881611 512 RALYRNPEVLIFDEATSALDSATEKQLMETIDTIC-DAHTVIMIAHRVS-TLKNCDRIFKIENGKL 575
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAeVLGLSDRVLVIGEGKL 481
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
368-567 |
4.84e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.09 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 368 NVNFKYL---NSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILgllRPEKGNVLIDAQYKPNSF------QWHKK 438
Cdd:TIGR00630 608 PGNGKFLtlkGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTL---YPALANRLNGAKTVPGRYtsieglEHLDK 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 439 IGYVAQS-------------INLIDD-------TVEA------------NIAFG------------------------CD 462
Cdd:TIGR00630 685 VIHIDQSpigrtprsnpatyTGVFDEirelfaeTPEAkvrgytpgrfsfNVKGGrceacqgdgvikiemhflpdvyvpCE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 463 ------------------KIDKEALDNAVDSAqlRQFVNSLPN---GLKT---------TIGERGIRVSGGERQRISIAR 512
Cdd:TIGR00630 765 vckgkrynretlevkykgKNIADVLDMTVEEA--YEFFEAVPSisrKLQTlcdvglgyiRLGQPATTLSGGEAQRIKLAK 842
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881611 513 ALYR---NPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKNCDRI 567
Cdd:TIGR00630 843 ELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNLDVIKTADYI 901
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
381-556 |
6.65e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGllRPEkgnvlidaqYKPNSfqwhKKIGYVAQSINLIDDTVEAN---- 456
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPA---------YKILE----GDILFKGESILDLEPEERAHlgif 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 457 IAF-------GCDKID----------KEALDNAVDSAQLRQFVNSLPN--GLKTTIGERGIR--VSGGERQRISIARALY 515
Cdd:CHL00131 88 LAFqypieipGVSNADflrlaynskrKFQGLPELDPLEFLEIINEKLKlvGMDPSFLSRNVNegFSGGEKKRNEILQMAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2258881611 516 RNPEVLIFDEATSALDSATEKQLMETIDTICDAHT-VIMIAH 556
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMTSENsIILITH 209
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
388-532 |
1.39e-06 |
|
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: 48.72 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 388 INKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNV---LIDAQYKPnsfqwhkkigyvaQSINLiddtveaniafgcdki 464
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDewdGITPVYKP-------------QYIDL---------------- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 465 dkealdnavdsaqlrqfvnslpnglkttigergirvSGGERQRISIARALYRNPEVLIFDEATSALDS 532
Cdd:cd03222 73 ------------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
383-540 |
1.76e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLR-PekGNVLIDA-QYKPNSFQW---HKKIGYVAQSINLI--DDTVEA 455
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMAEKlEFNGQDLQRiseKERRNLVGAEVAMIfqDPMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 456 NIAFGCDKIDKEALdnavdsaQLRQfvnslpNGLKTTIGERGI--------------------RVSGGERQRISIARALY 515
Cdd:PRK11022 103 NPCYTVGFQIMEAI-------KVHQ------GGNKKTRRQRAIdllnqvgipdpasrldvyphQLSGGMSQRVMIAMAIA 169
|
170 180
....*....|....*....|....*
gi 2258881611 516 RNPEVLIFDEATSALDSATEKQLME 540
Cdd:PRK11022 170 CRPKLLIADEPTTALDVTIQAQIIE 194
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
384-562 |
2.05e-06 |
|
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: 50.90 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 384 INLKINKGESVGIVGHTGSGKSTLIDlILGLLRPEKGNVLidaqYKPNSfqwhKKIGYVAQSINLIDDTVEANIAFGcDK 463
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRL----TKPAK----GKLFYVPQRPYMTLGTLRDQIIYP-DS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 464 IDkEALDNAVDSAQLRQFVN--SLPNGLKTTIGERGIR-----VSGGERQRISIARALYRNPEVLIFDEATSALDSATEK 536
Cdd:TIGR00954 541 SE-DMKRRGLSDKDLEQILDnvQLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|....*.
gi 2258881611 537 QLMETIDTIcdAHTVIMIAHRVSTLK 562
Cdd:TIGR00954 620 YMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
375-575 |
3.32e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 375 NSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEK-GNVLIDAQ----------------YKPNSfqwHK 437
Cdd:PRK13549 272 NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKpvkirnpqqaiaqgiaMVPED---RK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 KIGYVAQSinliddTVEANIAFGC-DKIDK-EALDNAVDSAQLRQFVNSLPngLKTTIGERGI-RVSGGERQRISIARAL 514
Cdd:PRK13549 349 RDGIVPVM------GVGKNITLAAlDRFTGgSRIDDAAELKTILESIQRLK--VKTASPELAIaRLSGGNQQKAVLAKCL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881611 515 YRNPEVLIFDEATSALDSATEKQLMETIDTICDAH-TVIMIAHRV-STLKNCDRIFKIENGKL 575
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGvAIIVISSELpEVLGLSDRVLVMHEGKL 483
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
361-565 |
4.32e-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: 50.01 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 361 TKSIEFNNVNFKYLNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQ-YKPNSFQWHKKI 439
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsILTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQsINLIDDTVEaniafGCDKIDKEALDNAVDSAQLRQFVN----SLpnGLKTTIGERGIRVSGGERQRISIARALY 515
Cdd:TIGR01257 2015 GYCPQ-FDAIDDLLT-----GREHLYLYARLRGVPAEEIEKVANwsiqSL--GLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2258881611 516 RNPEVLIFDEATSALDSATEKQLMETIDTIC-DAHTVIMIAHrvsTLKNCD 565
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSH---SMEECE 2134
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
384-531 |
4.81e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 384 INLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAqyKPNSFqwHKKIGYVAQSINLI-DD----------T 452
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG--KPIDI--RSPRDAIRAGIMLCpEDrkaegiipvhS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 453 VEANIAFGCDKIDKEA---LDNAVDSAQLRQFVNSLpnGLKTTIGERGIR-VSGGERQRISIARALYRNPEVLIFDEATS 528
Cdd:PRK11288 348 VADNINISARRHHLRAgclINNRWEAENADRFIRSL--NIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
...
gi 2258881611 529 ALD 531
Cdd:PRK11288 426 GID 428
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
364-531 |
7.62e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 364 IEFNNVNFKYLNSKKnTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSFQWHKKIGYVA 443
Cdd:PLN03073 509 ISFSDASFGYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 444 QSINLIddtveaniafgcdkidkealdnavdsAQLRQFVNSLPNGLKTTIGERGIR----------VSGGERQRISIARA 513
Cdd:PLN03073 588 SSNPLL--------------------------YMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAFAKI 641
|
170
....*....|....*...
gi 2258881611 514 LYRNPEVLIFDEATSALD 531
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLD 659
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
384-531 |
1.48e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 384 INLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLIDAQYKPNSfQWHKKIGYVAQSINLiddtveaniafgcdK 463
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-DRSRFMAYLGHLPGL--------------K 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 464 IDKEALDNAvdsaqlrQFVNSL--------PNGLKTTIGERG-----IR-VSGGERQRISIARaLYRNPEVL-IFDEATS 528
Cdd:PRK13543 95 ADLSTLENL-------HFLCGLhgrrakqmPGSALAIVGLAGyedtlVRqLSAGQKKRLALAR-LWLSPAPLwLLDEPYA 166
|
...
gi 2258881611 529 ALD 531
Cdd:PRK13543 167 NLD 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
381-576 |
1.56e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLI------------------DLILGLL-----RPEKGNVLidaqykpnsfqwhk 437
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMkilngevllddgriiyeqDLIVARLqqdppRNVEGTVY-------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 438 kiGYVAQSINLIDDTVEANIAF----GCDKIDK-----EALDNAVDSAQLRQFVNSLPNGLK-------TTIGErgirVS 501
Cdd:PRK11147 85 --DFVAEGIEEQAEYLKRYHDIshlvETDPSEKnlnelAKLQEQLDHHNLWQLENRINEVLAqlgldpdAALSS----LS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 502 GGERQRISIARALYRNPEVLIFDEATSALDSAT----EKQLMETIDTIcdahtvIMIAHRVSTLKN-CDRIFKIENGKLS 576
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiewlEGFLKTFQGSI------IFISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
381-575 |
2.20e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLL----RPE----KGNVLID----AQYKPNSF---------QWHKKI 439
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRgarvTGDVTLNgeplAAIDAPRLarlravlpqAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 440 GYVAQSINLIDDTVEANIAFGCDKIDKEALDNAVDSAqlrqfvnslpnGLKTTIGERGIRVSGGERQRISIARAL----- 514
Cdd:PRK13547 97 AFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-----------GATALVGRDVTTLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881611 515 ----YRNPEVLIFDEATSALDSATEKQLMETIDTIC-DAHT-VIMIAHRVS-TLKNCDRIFKIENGKL 575
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLgVLAIVHDPNlAARHADRIAMLADGAI 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
383-581 |
3.83e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLL--RPEKGNVLIDAqyKPNSFQ-----WHKKIGYVAQS-----INLID 450
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDG--KEVDVStvsdaIDAGLAYVTEDrkgygLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 451 DtVEANI-AFGCDKIDKEALdnaVDSAQLRQFVNSLPNGLKT---TIGERGIRVSGGERQRISIARALYRNPEVLIFDEA 526
Cdd:NF040905 356 D-IKRNItLANLGKVSRRGV---IDENEEIKVAEEYRKKMNIktpSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881611 527 TSALDSATEKQLMETIDTICDA-HTVIMIahrvST-----LKNCDRIFKIENGKLS-EVRKD 581
Cdd:NF040905 432 TRGIDVGAKYEIYTIINELAAEgKGVIVI----SSelpelLGMCDRIYVMNEGRITgELPRE 489
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
503-589 |
4.65e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.95 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 503 GERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAH--TVIMIAHRVSTL-KNCDRIFKIENGKLSE-V 578
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLsQWADKINVLYCGQTVEtA 241
|
90
....*....|.
gi 2258881611 579 RKDSVLAMSHH 589
Cdd:PRK15093 242 PSKELVTTPHH 252
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
500-575 |
7.79e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 500 VSGGERQRISIARALY---RNPEVLIFDEATSALDSATEKQLMETIDTICD-AHTVIMIAHRVSTLKNCDRIFKI--ENG 573
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHqGHTVVIIEHNMHVVKVADYVLELgpEGG 889
|
..
gi 2258881611 574 KL 575
Cdd:PRK00635 890 NL 891
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
489-579 |
1.90e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 489 LKTTIGERGIRVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTIC-DAHTVIM----------IAHR 557
Cdd:NF000106 134 LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLttqymeeaeqLAHE 213
|
90 100
....*....|....*....|..
gi 2258881611 558 VSTLkncDRIFKIENGKLSEVR 579
Cdd:NF000106 214 LTVI---DRGRVIADGKVDELK 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
490-578 |
2.16e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 490 KTTIGErgirVSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETIDTICDAHT-VIMIAHRVSTLKN-CDRI 567
Cdd:PRK10982 386 RTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMPELLGiTDRI 461
|
90
....*....|.
gi 2258881611 568 FKIENGKLSEV 578
Cdd:PRK10982 462 LVMSNGLVAGI 472
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
396-559 |
3.07e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 396 IVGHTGSGKSTLIDLILGllRPEKGNVLIDAQYK--PNSFQWHKKI-GYVAQS-INLIDDTVEANIAFGC-----DKIDK 466
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISgfPKKQETFARIsGYCEQNdIHSPQVTVRESLIYSAflrlpKEVSK 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 467 EALDNAVDsaQLRQFVnSLPNGLKTTIGERGIR-VSGGERQRISIARALYRNPEVLIFDEATSALDSATEKQLMETI-DT 544
Cdd:PLN03140 989 EEKMMFVD--EVMELV-ELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNT 1065
|
170
....*....|....*
gi 2258881611 545 ICDAHTVIMIAHRVS 559
Cdd:PLN03140 1066 VDTGRTVVCTIHQPS 1080
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
493-573 |
4.17e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 493 IGERGIRVSGGERQRISIARALY---RNPEVLIFDEATSALDSATEKQLMETIDT-ICDAHTVIMIAHRVSTLKNCDRIF 568
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
....*
gi 2258881611 569 KIENG 573
Cdd:PRK00635 1773 EMGPG 1777
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
375-567 |
6.65e-04 |
|
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: 41.47 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 375 NSKKNTLSNINLKINKGESVGIVGHTGSGKSTL-IDLILGllrpekgnvliDAQYKpnsfqwhkkigYVaqsinlidDTV 453
Cdd:cd03270 5 GAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIYA-----------EGQRR-----------YV--------ESL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 EANIAFGCDKIDKEALDN--------AVDSAQLRQFVNSLPnGLKTTI--------GERGIR------------------ 499
Cdd:cd03270 55 SAYARQFLGQMDKPDVDSieglspaiAIDQKTTSRNPRSTV-GTVTEIydylrllfARVGIRerlgflvdvglgyltlsr 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881611 500 ----VSGGERQRISIARALYRN-PEVL-IFDEATSALDSATEKQLMETIDTICDA-HTVIMIAHRVSTLKNCDRI 567
Cdd:cd03270 134 saptLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLgNTVLVVEHDEDTIRAADHV 208
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
501-556 |
6.82e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 6.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 501 SGGERQRISIARALYR---NPEVLIFDEATSALDSATEKQLMETIDTICDA-HTVIMIAH 556
Cdd:COG0178 828 SGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKgNTVVVIEH 887
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
501-531 |
7.54e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 7.54e-04
10 20 30
....*....|....*....|....*....|.
gi 2258881611 501 SGGERQRISIARALYRNPEVLIFDEATSALD 531
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
43-290 |
1.06e-03 |
|
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: 41.09 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 43 LLEVVTASVIVVFAQVLNdPSVGQKYFQKLGITENLSPGKTVFYvAIAVGVVYVVKNLIAAAEVFFQNFSIQKMCFEFKN 122
Cdd:pfam00664 1 LILAILLAILSGAISPAF-PLVLGRILDVLLPDGDPETQALNVY-SLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 123 KLLHRYAQADYGFYLTRNSSFGLQVVGSDVEQ---AFSSGMVSLARSLSegsVFIFLVGMIVYVNPTLVLIIFVIgMTLG 199
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKirdGLGEKLGLLFQSLA---TIVGGIIVMFYYGWKLTLVLLAV-LPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 200 LLTSKFLLPKFyywgQNLQQTGFHTHKNLMQFF----HSFKEIVLLGKKESFVKAYQVHSKERSKVQAIQTATNALPRMG 275
Cdd:pfam00664 155 ILVSAVFAKIL----RKLSRKEQKAVAKASSVAeeslSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGI 230
|
250
....*....|....*
gi 2258881611 276 IEILFVGLFVLTISY 290
Cdd:pfam00664 231 TQFIGYLSYALALWF 245
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
381-583 |
2.77e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 381 LSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLrPE---KGNVLID---AQYKPNSFQWHKKIGYVAQSINLIDD-TV 453
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDgevCRFKDIRDSEALGIVIIHQELALIPYlSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 454 EANIAFGCDK-----ID-KEALDNAvdsAQLRQFVnslpnGLK----TTIGERGIrvsgGERQRISIARALYRNPEVLIF 523
Cdd:NF040905 96 AENIFLGNERakrgvIDwNETNRRA---RELLAKV-----GLDespdTLVTDIGV----GKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 524 DEATSAL---DSATEKQLM-----ETIdticdahTVIMIAHrvstlkncdrifkiengKLSEVRK--DSV 583
Cdd:NF040905 164 DEPTAALneeDSAALLDLLlelkaQGI-------TSIIISH-----------------KLNEIRRvaDSI 209
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
386-419 |
3.05e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.42 E-value: 3.05e-03
10 20 30
....*....|....*....|....*....|....
gi 2258881611 386 LKINKGESVGIVGHTGSGKSTLIDLILGLLRPEK 419
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
374-563 |
3.98e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 374 LNSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLidaqYKPNSFQWHKK--IGYVAQSINL-ID 450
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY----YKNCNINNIAKpyCTYIGHNLGLkLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881611 451 DTVEANIAFGCDKIDK-EALDNAVDSAQLRQFVNslpnglkttigERGIRVSGGERQRISIARALYRNPEVLIFDEATSA 529
Cdd:PRK13541 85 MTVFENLKFWSEIYNSaETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190
....*....|....*....|....*....|....*
gi 2258881611 530 LDSATEKQLMETIDTICDAHTVIMIA-HRVSTLKN 563
Cdd:PRK13541 154 LSKENRDLLNNLIVMKANSGGIVLLSsHLESSIKS 188
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
383-425 |
4.21e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 4.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2258881611 383 NINLKINKGESVGIVGHTGSGKSTLIDLILGLLRPEKGNVLID 425
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
375-412 |
6.37e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 6.37e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2258881611 375 NSKKNTLSNINLKINKGESVGIVGHTGSGKSTLIDLIL 412
Cdd:PRK00349 619 GARENNLKNVDVEIPLGKFTCVTGVSGSGKSTLINETL 656
|
|
| |
