|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-520 |
5.60e-50 |
|
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: 182.73 E-value: 5.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 6 FFKLLP--KKDIILYIIFALLYSCQGIVIPVIIQMAghID----SSDSRDLIVFTFSSISLWVVVYAFMYIENILLRSII 79
Cdd:COG2274 147 FLRLLRryRRLLLQVLLASLLINLLALATPLFTQVV--IDrvlpNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 80 RAFNVSLSENILkNHAV-----FPKNISDSELCSLLtQDLGIVdQEFLQSFLIS-PVWGASVLVSVIYLLKQNLIVGSLF 153
Cdd:COG2274 225 QRIDLRLSSRFF-RHLLrlplsFFESRSVGDLASRF-RDVESI-REFLTGSLLTaLLDLLFVLIFLIVLFFYSPPLALVV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 154 TVGAFLMILPQFIFKRKLKESGELLSSSKEKNLRAITDFGKGIETIICNQAEKENVKQTLITLSEMETTQFKYYTLQNLV 233
Cdd:COG2274 302 LLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 234 MFWTGPLKAVGLIGPFVIG--LVMKQN-SITTLIAMMSASTYLINPLQQILEAIASIQSSQVIKDKL---LTFGSESEIP 307
Cdd:COG2274 382 STLSGLLQQLATVALLWLGayLVIDGQlTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLddiLDLPPEREEG 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 308 SKGLHIHTLE-EIQLKNVTKSYDNQE--IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRE 384
Cdd:COG2274 462 RSKLSLPRLKgDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 385 LTPNL--DNIAIIHQNPYVFHTSVRHNLTL-YQDYSDSLLISTLKKVGLWEACC---HQLDYELT--GDNFSGGQIIKLE 456
Cdd:COG2274 542 IDPASlrRQIGVVLQDVFLFSGTIRENITLgDPDATDEEIIEAARLAGLHDFIEalpMGYDTVVGegGSNLSGGQRQRLA 621
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348497 457 IARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAHHYK-LEDYDAVYRIENKSIV 520
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLStIRLADRIIVLDKGRIV 688
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-501 |
4.39e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 164.18 E-value: 4.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 12 KKDIILYIIFALLYSCQGIVIPVIIQMA--GHIDSSDSRDLIVFTFSSISLWVVVYAFMYIENILL----RSIIRAFNVS 85
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIidALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLarlaQRVVADLRRD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 86 LSENILKNHAVFPKNISDSELCSLLTQDLGIVdQEFLQSFLISPVWGA-SVLVSVIYLLKQNLIVGSLFTVGAFLMILPQ 164
Cdd:COG1132 100 LFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAV-EQFLAHGLPQLVRSVvTLIGALVVLFVIDWRLALIVLLVLPLLLLVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 165 FIFKRKLKESGELLSSSKEKNLRAITDFGKGIETIICNQAEKENVKQTLITLSEMETTQFKYYTLQNLVMFWTGPLKAVG 244
Cdd:COG1132 179 RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 245 LIGPFVIG--LVMKQN-SITTLIAMMSASTYLINPLQQILEAIASIQSSQVIKDKLLTF-GSESEIPSKGLHIHTLE--- 317
Cdd:COG1132 259 LALVLLVGglLVLSGSlTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELlDEPPEIPDPPGAVPLPPvrg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSYDN-QEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDG---RELTPN--LDN 391
Cdd:COG1132 339 EIEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI---LIDGvdiRDLTLEslRRQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 IAIIHQNPYVFHTSVRHNLTLY-QDYSDSLLISTLKKVGLWE---ACCHQLDYELT--GDNFSGGQIIKLEIARAILREK 465
Cdd:COG1132 416 IGVVPQDTFLFSGTIRENIRYGrPDATDEEVEEAAKAAQAHEfieALPDGYDTVVGerGVNLSGGQRQRIAIARALLKDP 495
|
490 500 510
....*....|....*....|....*....|....*....
gi 1081348497 466 QVLLADEMMASLDAASSKEISNVLKQLPN---SIIeIAH 501
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMKgrtTIV-IAH 533
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
318-520 |
5.76e-40 |
|
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: 152.22 E-value: 5.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSYDN-QEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTpNLD------ 390
Cdd:COG4988 336 SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI---LINGVDLS-DLDpaswrr 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 NIAIIHQNPYVFHTSVRHNLTLYQ-DYSDSLLISTLKKVGLWE---ACCHQLDYELT--GDNFSGGQIIKLEIARAILRE 464
Cdd:COG4988 412 QIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEfvaALPDGLDTPLGegGRGLSGGQAQRLALARALLRD 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348497 465 KQVLLADEMMASLDAASSKEISNVLKQLPNS--IIEIAHHYK-LEDYDAVYRIENKSIV 520
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLAlLAQADRILVLDDGRIV 550
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
232-520 |
2.62e-33 |
|
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: 133.35 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 232 LVMFWTGPLKAVGLI-GPFVIGLVMkqnsiTTLiAMMSASTYLINPLQQILEAIASIQS-SQVIKDK-LLTFGSESEIPS 308
Cdd:COG4987 256 AVLWLAAPLVAAGALsGPLLALLVL-----AAL-ALFEALAPLPAAAQHLGRVRAAARRlNELLDAPpAVTEPAEPAPAP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 309 KGLHIhtleeiQLKNVTKSYDNQE--IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELT 386
Cdd:COG4987 330 GGPSL------ELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI---TLGGVDLR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 387 pNLD------NIAIIHQNPYVFHTSVRHNLTL-YQDYSDSLLISTLKKVGL--W-EACCHQLDYEL--TGDNFSGGQIIK 454
Cdd:COG4987 401 -DLDeddlrrRIAVVPQRPHLFDTTLRENLRLaRPDATDEELWAALERVGLgdWlAALPDGLDTWLgeGGRRLSGGERRR 479
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348497 455 LEIARAILREKQVLLADEMMASLDAASSKEI-SNVLKQLPN-SIIEIAHHYK-LEDYDAVYRIENKSIV 520
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALlADLLEALAGrTVLLITHRLAgLERMDRILVLEDGRIV 548
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
319-516 |
4.43e-33 |
|
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: 123.65 E-value: 4.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDN--QEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNL--DNIAI 394
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNPYVFHTSVRHNLtlyqdysdsllistlkkvglweacchqldyeltgdnFSGGQIIKLEIARAILREKQVLLADEMM 474
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348497 475 ASLDAASSKEISNVLKQLPN--SIIEIAHHYK-LEDYDAVYRIEN 516
Cdd:cd03228 125 SALDPETEALILEALRALAKgkTVIVIAHRLStIRDADRIIVLDD 169
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
318-520 |
2.19e-27 |
|
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: 109.51 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSY--DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTT----LFRLISgqdkAYSGKIIfksIDGRELT--PNL 389
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE----LSSGSIL---IDGVDISkiGLH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 390 D---NIAIIHQNPYVFHTSVRHNLTLYQDYSDSLLISTLKKVGLWEACCHQ---LDYELT--GDNFSGGQIIKLEIARAI 461
Cdd:cd03244 75 DlrsRISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLpggLDTVVEegGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348497 462 LREKQVLLADEMMASLDAASSKEISNVLKQ-LPNS-IIEIAHHykLE---DYDAVYRIENKSIV 520
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREaFKDCtVLTIAHR--LDtiiDSDRILVLDKGRVV 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
318-501 |
9.91e-25 |
|
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: 102.28 E-value: 9.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSYDNQEI--FRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNL--DNIA 393
Cdd:cd03245 2 RIEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNPYVFHTSVRHNLTL-YQDYSDSLLISTLKKVGLWE-ACCHQLDYELT----GDNFSGGQIIKLEIARAILREKQV 467
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLgAPLADDERILRAAELAGVTDfVNKHPNGLDLQigerGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081348497 468 LLADEMMASLDAASSKEISNVLKQL--PNSIIEIAH 501
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITH 197
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
320-516 |
1.01e-24 |
|
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: 101.77 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 320 QLKNVTKSYDNQE--IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPN--LDNIAII 395
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 396 HQNP--YVFHTSVR-------HNLTLYQDYSDSLLISTLKKVGLWeaccHQLDYELtgDNFSGGQIIKLEIARAILREKQ 466
Cdd:cd03225 81 FQNPddQFFGPTVEeevafglENLGLPEEEIEERVEEALELVGLE----GLRDRSP--FTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348497 467 VLLADEMMASLDAASSKEISNVLKQLPN---SIIEIAH--HYKLEDYDAVYRIEN 516
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHdlDLLLELADRVIVLED 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
319-504 |
4.36e-23 |
|
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: 97.33 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLDNIAIIHQN 398
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVF-HTSVRHNLT--LYQDYSDSLLIStlKKVgLWEACCHQLDYELTG--DNFSGGQIIKLEIARAILREKQVLLADEM 473
Cdd:cd03301 81 YALYpHMTVYDNIAfgLKLRKVPKDEID--ERV-REVAELLQIEHLLDRkpKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1081348497 474 MASLDA----ASSKEISNVLKQLPNSIIEIAHHYK 504
Cdd:cd03301 158 LSNLDAklrvQMRAELKRLQQRLGTTTIYVTHDQV 192
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
319-492 |
4.65e-23 |
|
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: 97.18 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQ----EIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPN------ 388
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 389 LDNIAIIHQNPYVF-HTSVRHNLTLYQDYSDSL-------LISTLKKVGLwEACCHQLDYELtgdnfSGGQIIKLEIARA 460
Cdd:cd03255 81 RRHIGFVFQSFNLLpDLTALENVELPLLLAGVPkkerrerAEELLERVGL-GDRLNHYPSEL-----SGGQQQRVAIARA 154
|
170 180 190
....*....|....*....|....*....|..
gi 1081348497 461 ILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLREL 186
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
319-521 |
1.25e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.27 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDN-QEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELT-------PNL- 389
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL---VNGQDLSrlkrreiPYLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 390 DNIAIIHQN-PYVFHTSVRHNLTL---YQDYSDSLL----ISTLKKVGLWE---ACCHQLdyeltgdnfSGGQIIKLEIA 458
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALplrVTGKSRKEIrrrvREVLDLVGLSDkakALPHEL---------SGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 459 RAILREKQVLLADEMMASLDAASSKEISNVLKQLpN----SIIeIAHHYK--LEDYDA-VYRIENKSIVR 521
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NrrgtTVL-IATHDLelVDRMPKrVLELEDGRLVR 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
276-501 |
1.35e-22 |
|
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: 101.21 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 276 PLQQI-------LEAIASIQSSQ-VIKDKLLTFGSESEIPSkgLHIHTLEeiqLKNVTKSY-DNQEIFRDVTVTFSLSQH 346
Cdd:TIGR02857 276 PLRQLgaqyharADGVAAAEALFaVLDAAPRPLAGKAPVTA--APASSLE---FSGVSVAYpGRRPALRPVSFTVPPGER 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 347 NLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPN-----LDNIAIIHQNPYVFHTSVRHNLTLYQ-DYSDSL 420
Cdd:TIGR02857 351 VALVGPSGAGKSTLLNLLLGFVDPTEGSI---AVNGVPLADAdadswRDQIAWVPQHPFLFAGTIAENIRLARpDASDAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 421 LISTLKKVGLWE---ACCHQLDYELtGDN---FSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN 494
Cdd:TIGR02857 428 IREALERAGLDEfvaALPQGLDTPI-GEGgagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ 506
|
....*....
gi 1081348497 495 --SIIEIAH 501
Cdd:TIGR02857 507 grTVLLVTH 515
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
319-492 |
1.75e-22 |
|
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: 96.10 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAY-----SGKIIF--KSIDGRELTPNL-- 389
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLdgKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 390 DNIAIIHQNPYVFHTSVRHNLTL---YQDYSDSLLIST-----LKKVGLWEACCHQLDyeltGDNFSGGQIIKLEIARAI 461
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYglrLHGIKLKEELDErveeaLRKAALWDEVKDRLH----ALGLSGGQQQRLCLARAL 156
|
170 180 190
....*....|....*....|....*....|.
gi 1081348497 462 LREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAEL 187
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
319-479 |
9.41e-22 |
|
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: 93.69 E-value: 9.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDN----QEIFRDVTvtFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNLDNI 392
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDIS--LSVEEGEFvaLVGPSGCGKSTLLRIIAGLERPTSGEV---LVDGEPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 AIIHQNPYVF-HTSVRHNLTL-----------YQDYSDSLlistLKKVGLWE---ACCHQLdyeltgdnfSGGQIIKLEI 457
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALglelqgvpkaeARERAEEL----LELVGLSGfenAYPHQL---------SGGMRQRVAL 142
|
170 180
....*....|....*....|..
gi 1081348497 458 ARAILREKQVLLADEMMASLDA 479
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDA 164
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
319-492 |
1.29e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 93.57 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQE----IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPN------ 388
Cdd:COG1136 5 LELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 389 LDNIAIIHQNPYVF-HTSVRHNLTLYQDYS-------DSLLISTLKKVGLwEACCHQLDYELtgdnfSGGQIIKLEIARA 460
Cdd:COG1136 85 RRHIGFVFQFFNLLpELTALENVALPLLLAgvsrkerRERARELLERVGL-GDRLDHRPSQL-----SGGQQQRVAIARA 158
|
170 180 190
....*....|....*....|....*....|..
gi 1081348497 461 ILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLREL 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-491 |
1.53e-21 |
|
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: 92.54 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTvtFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNL-DNIAII 395
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLS--FTLAAGEAlaLTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 396 -HQNPYVFHTSVRHNLTLYQDY-----SDSLLISTLKKVGL---WEACCHQLdyeltgdnfSGGQIIKLEIARAILREKQ 466
Cdd:COG4133 81 gHADGLKPELTVRENLRFWAALyglraDREAIDEALEAVGLaglADLPVRQL---------SAGQKRRVALARLLLSPAP 151
|
170 180
....*....|....*....|....*
gi 1081348497 467 VLLADEMMASLDAASSKEISNVLKQ 491
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAA 176
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
98-520 |
1.94e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 97.59 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 98 PKNIS---DSELCSLLTQDLGIVDQEFLQsfLISPVWGASVLVSVIYL------LKQNLIVGSLFTvgAFLMILPqFIFK 168
Cdd:PRK11160 108 PAGLAryrQGDLLNRLVADVDTLDHLYLR--LISPLVAALVVILVLTIglsffdLTLALTLGGILL--LLLLLLP-LLFY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 169 RKLKESGELLSSSKeKNLR-AITDFGKGietiicnQAE------KENVKQTLI-TLSEMETTQFKYYTL----QNLVMFW 236
Cdd:PRK11160 183 RLGKKPGQDLTHLR-AQYRvQLTEWLQG-------QAEltlfgaEDRYRQQLEqTEQQWLAAQRRQANLtglsQALMILA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 237 TGplKAVGLIGPFVIGLVMKQNSITTLIAMMS----ASTYLINPL----QQILEAIASIQS-SQVIKDK-LLTFGSESEI 306
Cdd:PRK11160 255 NG--LTVVLMLWLAAGGVGGNAQPGALIALFVfaalAAFEALMPVagafQHLGQVIASARRiNEITEQKpEVTFPTTSTA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 307 PSKGLhihtleEIQLKNVTKSYDNQE--IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRE 384
Cdd:PRK11160 333 AADQV------SLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI---LLNGQP 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 385 LT----PNL-DNIAIIHQNPYVFHTSVRHNLTLYQ-DYSDSLLISTLKKVGLweacchqlDYELTGDN------------ 446
Cdd:PRK11160 404 IAdyseAALrQAISVVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGL--------EKLLEDDKglnawlgeggrq 475
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348497 447 FSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLP--NSIIEIAHH-YKLEDYDAVYRIENKSIV 520
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAqnKTVLMITHRlTGLEQFDRICVMDNGQII 552
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
305-508 |
2.15e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.57 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 305 EIPSKGLHIHTLEEIQLKNVT-KSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFksidgr 383
Cdd:COG4178 349 PEAASRIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 384 eltPNLDNIAIIHQNPYVFHTSVRHNLtLY----QDYSDSLLISTLKKVGLwEACCHQLDYELTGDN-FSGGQIIKLEIA 458
Cdd:COG4178 423 ---PAGARVLFLPQRPYLPLGTLREAL-LYpataEAFSDAELREALEAVGL-GHLAERLDEEADWDQvLSLGEQQRLAFA 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081348497 459 RAILREKQVLLADEMMASLDAASSKEISNVLKQ-LPNS-IIEIAHHYKLEDY 508
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGTtVISVGHRSTLAAF 549
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
319-492 |
1.14e-20 |
|
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: 89.17 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELT-------PNLDN 391
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI---LIDGEDLTdledelpPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 IAIIHQNPYVF-HTSVRHNLTLyqdysdsllistlkkvGLweacchqldyeltgdnfSGGQIIKLEIARAILREKQVLLA 470
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIAL----------------GL-----------------SGGQQQRVALARALAMDPDVLLL 124
|
170 180
....*....|....*....|..
gi 1081348497 471 DEMMASLDAASSKEISNVLKQL 492
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSL 146
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
318-511 |
2.69e-20 |
|
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: 89.01 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSY--DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTL----FRLIsgqdKAYSGKIifkSIDGRE-----LT 386
Cdd:cd03369 6 EIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLilalFRFL----EAEEGKI---EIDGIDistipLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 387 PNLDNIAIIHQNPYVFHTSVRHNLTLYQDYSDSLLISTLKKVGlweacchqldyelTGDNFSGGQIIKLEIARAILREKQ 466
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSE-------------GGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348497 467 VLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAHHYK-LEDYDAV 511
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTnsTILTIAHRLRtIIDYDKI 193
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
320-492 |
2.73e-20 |
|
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: 89.13 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 320 QLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNLDNIAIIHQNP 399
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI---RVFGKPLEKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 400 YV---FHTSVR--------HNLTLYQDYSDS---LLISTLKKVGLWEACCHQLDyELtgdnfSGGQIIKLEIARAILREK 465
Cdd:cd03235 78 SIdrdFPISVRdvvlmglyGHKGLFRRLSKAdkaKVDEALERVGLSELADRQIG-EL-----SGGQQQRVLLARALVQDP 151
|
170 180
....*....|....*....|....*..
gi 1081348497 466 QVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLREL 178
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
318-502 |
3.44e-20 |
|
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: 89.59 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSYDNQE-IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPN--LDNIAI 394
Cdd:cd03254 2 EIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNPYVFHTSVRHNLTLYQDYS-DSLLISTLKKVGLweaccHQ--------LDYELT--GDNFSGGQIIKLEIARAILR 463
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGA-----HDfimklpngYDTVLGenGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081348497 464 EKQVLLADEMMASLDAASSKEISNVLKQLPN---SIIeIAHH 502
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKgrtSII-IAHR 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
295-520 |
6.93e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 295 DKLLTFGSESEIPSKG----LHIHTLEEIQLKN-VTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQdK 369
Cdd:PRK11174 322 ESLVTFLETPLAHPQQgekeLASNDPVTIEAEDlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-L 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 370 AYSGKIifkSIDGRELTpNLD------NIAIIHQNPYVFHTSVRHNLTLYQ-DYSDSLLISTLKKVGLWE---ACCHQLD 439
Cdd:PRK11174 401 PYQGSL---KINGIELR-ELDpeswrkHLSWVGQNPQLPHGTLRDNVLLGNpDASDEQLQQALENAWVSEflpLLPQGLD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 440 YELtGDN---FSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPNS--IIEIAHHYK-LEDYDAVYR 513
Cdd:PRK11174 477 TPI-GDQaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRqtTLMVTHQLEdLAQWDQIWV 555
|
....*..
gi 1081348497 514 IENKSIV 520
Cdd:PRK11174 556 MQDGQIV 562
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
232-485 |
1.31e-19 |
|
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: 92.04 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 232 LVMFWTG-PLKAVGLIGPFVIGLVMkqnsITTLiAMMSASTYLINPLQQILEAIASIQS-SQVIKDKLLtfGSESEIPSK 309
Cdd:TIGR02868 253 LGALWAGgPAVADGRLAPVTLAVLV----LLPL-AAFEAFAALPAAAQQLTRVRAAAERiVEVLDAAGP--VAEGSAPAA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 310 GLHIHTLEEIQLKNVTKSY-DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPN 388
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 389 LDN--IAIIHQNPYVFHTSVRHNLTLYQ-DYSDSLLISTLKKVGL--W-EACCHQLDYELTGDN--FSGGQIIKLEIARA 460
Cdd:TIGR02868 406 EVRrrVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLadWlRALPDGLDTVLGEGGarLSGGERQRLALARA 485
|
250 260
....*....|....*....|....*
gi 1081348497 461 ILREKQVLLADEMMASLDAASSKEI 485
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADEL 510
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
319-520 |
1.68e-19 |
|
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: 87.56 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVT--VTFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIIFksiDGRELTPNLD---- 390
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALddVSFSIKKGETlgLVGESGSGKSTLARAILGLLKPTSGSIIF---DGKDLLKLSRrlrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 ----NIAIIHQNPY--------VFHtSVRHNLTLYQDYSDSLLIST-----LKKVGLWEACCHQLDYELtgdnfSGGQII 453
Cdd:cd03257 79 irrkEIQMVFQDPMsslnprmtIGE-QIAEPLRIHGKLSKKEARKEavlllLVGVGLPEEVLNRYPHEL-----SGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348497 454 KLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN----SIIEIAHhykleDYDAVYRIENKSIV 520
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelglTLLFITH-----DLGVVAKIADRVAV 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
319-492 |
2.19e-19 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 87.42 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQ-EIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTPNLD------- 390
Cdd:COG3638 3 LELRNLSKRYPGGtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEIL---VDGQDVTALRGralrrlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 -NIAIIHQNPY-VFHTSVRHNLtlyqdysdslLISTLKKVGLW------------EACCHQLD--------YELTgDNFS 448
Cdd:COG3638 80 rRIGMIFQQFNlVPRLSVLTNV----------LAGRLGRTSTWrsllglfppedrERALEALErvgladkaYQRA-DQLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1081348497 449 GGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRI 192
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
319-492 |
2.23e-19 |
|
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: 86.80 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELT---PNLDNIAII 395
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI---LIDGRDVTgvpPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 396 HQNPYVF-HTSVRHNL-------TLYQDYSDSLLISTLKKVGLwEACCHQLDYELtgdnfSGGQIIKLEIARAILREKQV 467
Cdd:cd03259 78 FQDYALFpHLTVAENIafglklrGVPKAEIRARVRELLELVGL-EGLLNRYPHEL-----SGGQQQRVALARALAREPSL 151
|
170 180
....*....|....*....|....*
gi 1081348497 468 LLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKEL 176
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
334-472 |
2.31e-19 |
|
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: 84.62 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 334 FRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNLD-----NIAIIHQNPYVF-HTSVR 407
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI---LLDGQDLTDDERkslrkEIGYVFQDPQLFpRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348497 408 HNL-------TLYQDYSDSLLISTLKKVGLWEACCHQLDYelTGDNFSGGQIIKLEIARAILREKQVLLADE 472
Cdd:pfam00005 78 ENLrlglllkGLSKREKDARAEEALEKLGLGDLADRPVGE--RPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
320-516 |
4.64e-19 |
|
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: 84.22 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 320 QLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTP--NLDNIAIIHQ 397
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 398 npyvfhtsvrhnltlyqdysdsllistlkkvglweacchqldyeltgdnFSGGQIIKLEIARAILREKQVLLADEMMASL 477
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1081348497 478 DAASSKEISNVLKQLPN---SIIEIAHHYKLEDY--DAVYRIEN 516
Cdd:cd00267 112 DPASRERLLELLRELAEegrTVIIVTHDPELAELaaDRVIVLKD 155
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
319-479 |
3.01e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 84.37 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY----DNQEIFRDVTVTFS----LSqhnlIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNLD 390
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAagefVA----LVGPSGCGKSTLLRLIAGLEKPTSGEV---LVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 NIAIIHQNPYVF-HTSVRHNLTL-----------YQDYSDSLListlKKVGLWEAC---CHQLdyeltgdnfSGGQIIKL 455
Cdd:COG1116 81 DRGVVFQEPALLpWLTVLDNVALglelrgvpkaeRRERARELL----ELVGLAGFEdayPHQL---------SGGMRQRV 147
|
170 180
....*....|....*....|....
gi 1081348497 456 EIARAILREKQVLLADEMMASLDA 479
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDA 171
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
319-492 |
9.16e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.00 E-value: 9.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELT---PNLDNIAII 395
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM---LDGQDIThvpAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 396 HQNPYVF-HTSVRHNLT-------LYQDYSDSLLISTLKKVGLWEAC---CHQLdyeltgdnfSGGQIIKLEIARAILRE 464
Cdd:PRK09452 92 FQSYALFpHMTVFENVAfglrmqkTPAAEITPRVMEALRMVQLEEFAqrkPHQL---------SGGQQQRVAIARAVVNK 162
|
170 180
....*....|....*....|....*...
gi 1081348497 465 KQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKAL 190
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
319-514 |
9.49e-18 |
|
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: 82.55 E-value: 9.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSID-----GRELTPNLDNIA 393
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNPYVF-HTSVRHN--LTLYQ--DYSDSLL----ISTLKKVGLwEACCHQLDYELtgdnfSGGQIIKLEIARAILRE 464
Cdd:cd03261 81 MLFQSGALFdSLTVFENvaFPLREhtRLSEEEIreivLEKLEAVGL-RGAEDLYPAEL-----SGGMKKRVALARALALD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081348497 465 KQVLLADEMMASLDAASSKEISNVL----KQLPNSIIEIAHhykleDYDAVYRI 514
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTH-----DLDTAFAI 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
319-492 |
1.24e-17 |
|
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: 82.23 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQ-EIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNL-----DNI 392
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 AIIHQNP------YVF----------HTSVRHNLTLYQDYSDSLLISTLKKVGLweacchqLDYELT-GDNFSGGQIIKL 455
Cdd:cd03256 81 GMIFQQFnlierlSVLenvlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGL-------LDKAYQrADQLSGGQQQRV 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081348497 456 EIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRI 190
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-501 |
2.66e-17 |
|
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: 84.77 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 6 FFKLLP-----KKDIILYIIFALLYSCQGIVIPVIIQ-MAGHIDSSDSRDLIVFtfssISLWVVVYAFM-----YIENIL 74
Cdd:TIGR02203 2 FRRLWSyvrpyKAGLVLAGVAMILVAATESTLAALLKpLLDDGFGGRDRSVLWW----VPLVVIGLAVLrgicsFVSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 75 L----RSIIRAFNVSLSENILKNHAVFPKNISDSELCSLLTQDLGIVDQEFLQSFLISPVWGASVLVSVIYLLKQN---- 146
Cdd:TIGR02203 78 LswvsNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSwqlt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 147 LIVGSLFTVGAFLMILPQFIFKRKLKES----GELLSSSKE--KNLRAITDF-GKGIETIICNQAEKENVKQTLitlsEM 219
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVSKRLRRISKEIqnsmGQVTTVAEEtlQGYRVVKLFgGQAYETRRFDAVSNRNRRLAM----KM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 220 ETTQFKYYTLQNLVMfwtgplkAVGLIGPFVIGLVMKQNSITT---LIAMMSASTYLINPLQQILEAIASIQSSQVIKDK 296
Cdd:TIGR02203 234 TSAGSISSPITQLIA-------SLALAVVLFIALFQAQAGSLTagdFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAES 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 297 LLTF-GSESEIPSKGLHIHTLE-EIQLKNVTKSY--DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYS 372
Cdd:TIGR02203 307 LFTLlDSPPEKDTGTRAIERARgDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 373 GKIIFKSIDGRELTpnLDN----IAIIHQNPYVFHTSVRHNLTlY---QDYSDSLLISTLKKVGLWE---ACCHQLDYEL 442
Cdd:TIGR02203 387 GQILLDGHDLADYT--LASlrrqVALVSQDVVLFNDTIANNIA-YgrtEQADRAEIERALAAAYAQDfvdKLPLGLDTPI 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348497 443 --TGDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL-PN-SIIEIAH 501
Cdd:TIGR02203 464 geNGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmQGrTTLVIAH 526
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
319-492 |
3.75e-17 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 80.74 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFksiDGRELT---PNLDNIAII 395
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL---DGKDITnlpPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 396 HQNPYVF-HTSVRHNLTLyqdysdSLLISTLKKVGLWEACCHQLDY-ELTG------DNFSGGQIIKLEIARAILREKQV 467
Cdd:cd03300 78 FQNYALFpHLTVFENIAF------GLRLKKLPKAEIKERVAEALDLvQLEGyanrkpSQLSGGQQQRVAIARALVNEPKV 151
|
170 180
....*....|....*....|....*
gi 1081348497 468 LLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRL 176
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
319-492 |
4.25e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 79.88 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTPNLDNIAIIHQN 398
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII---IDGLKLTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 -PYVF-------HTSVRHNLTLYQ--------DYSDSLLISTLKKVGLweacCHQLDY---ELtgdnfSGGQIIKLEIAR 459
Cdd:cd03262 78 vGMVFqqfnlfpHLTVLENITLAPikvkgmskAEAEERALELLEKVGL----ADKADAypaQL-----SGGQQQRVAIAR 148
|
170 180 190
....*....|....*....|....*....|...
gi 1081348497 460 AILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDL 181
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
319-514 |
5.72e-17 |
|
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: 80.17 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFksiDGRELTpNLDNIAIIH-- 396
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF---DGEDIT-GLPPHEIARlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 397 -----QNPYVFHT-SVRHNL----TLYQDYSDSLLISTLKKVGLWEACCHQLDY-ELTG------DNFSGGQIIKLEIAR 459
Cdd:cd03219 77 igrtfQIPRLFPElTVLENVmvaaQARTGSGLLLARARREEREARERAEELLERvGLADladrpaGELSYGQQRRLEIAR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348497 460 AILREKQVLLADEMMASLDAASSKEISNVLKQLPN---SIIEIAHhykleDYDAVYRI 514
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRErgiTVLLVEH-----DMDVVMSL 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
319-501 |
7.00e-17 |
|
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: 79.89 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYD---NQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLIsgqDKAY---SGKIIFKSIDGRELTPNL--D 390
Cdd:cd03249 1 IEFKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERFYdptSGEILLDGVDIRDLNLRWlrS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 NIAIIHQNPYVFHTSVRHNLTLYQDY-SDSLLISTLKKvglweACCHQL------DYE-LTGDN---FSGGQIIKLEIAR 459
Cdd:cd03249 78 QIGLVSQEPVLFDGTIAENIRYGKPDaTDEEVEEAAKK-----ANIHDFimslpdGYDtLVGERgsqLSGGQKQRIAIAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1081348497 460 AILREKQVLLADEMMASLDAASSKEISNVLKQLPNS--IIEIAH 501
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-501 |
1.52e-16 |
|
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: 82.26 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIfRDVT----VTFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIIFksiDGRELTPNLD-- 390
Cdd:COG1123 261 LEVRNLSKRYPVRGK-GGVRavddVSLTLRRGETlgLVGESGSGKSTLARLLLGLLRPTSGSILF---DGKDLTKLSRrs 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 ------NIAIIHQNPYV----FHT---SVRHNLTLYQDYSDS----LLISTLKKVGLWEACCHQLDYEltgdnFSGGQII 453
Cdd:COG1123 337 lrelrrRVQMVFQDPYSslnpRMTvgdIIAEPLRLHGLLSRAerreRVAELLERVGLPPDLADRYPHE-----LSGGQRQ 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081348497 454 KLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN----SIIEIAH 501
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelglTYLFISH 463
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
318-492 |
1.80e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 78.92 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLDNIAIIHQ 397
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 398 NPYVF-HTSVRHNLTL------YQDYSDSLLI-----STLKKVGL-WEA--CCHQLdyeltgdnfSGGQIIKLEIARAIL 462
Cdd:cd03296 82 HYALFrHMTVFDNVAFglrvkpRSERPPEAEIrakvhELLKLVQLdWLAdrYPAQL---------SGGQRQRVALARALA 152
|
170 180 190
....*....|....*....|....*....|
gi 1081348497 463 REKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRL 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
319-517 |
4.64e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 75.65 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVT-KSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFksidgreltPNLDNIAIIHQ 397
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 398 NPYvfhtsvrhnltlyqdysdsLLISTLKkvglwEACCHQLDyeltgDNFSGGQIIKLEIARAILREKQVLLADEMMASL 477
Cdd:cd03223 72 RPY-------------------LPLGTLR-----EQLIYPWD-----DVLSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081348497 478 DAASSKEISNVLKQLPNSIIEIAHHYKLEDY-DAVYRIENK 517
Cdd:cd03223 123 DEESEDRLYQLLKELGITVISVGHRPSLWKFhDRVLDLDGE 163
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
319-502 |
1.15e-15 |
|
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: 75.99 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYdnQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLDNIAIIHQN 398
Cdd:cd03298 1 VRLDKIRFSY--GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVF-HTSVRHNLTLYQDYSDSL-------LISTLKKVGLWEacchqLDYELTGDnFSGGQIIKLEIARAILREKQVLLA 470
Cdd:cd03298 79 NNLFaHLTVEQNVGLGLSPGLKLtaedrqaIEVALARVGLAG-----LEKRLPGE-LSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081348497 471 DEMMASLDAASSKE----ISNVLKQLPNSIIEIAHH 502
Cdd:cd03298 153 DEPFAALDPALRAEmldlVLDLHAETKMTVLMVTHQ 188
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
319-520 |
1.94e-15 |
|
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: 75.73 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQE--IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELT-PNL-DNIAI 394
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlASLrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNPYVFHTSVRHNLTlY--QDYSDSLLISTLKKvglweACCHQLDYEL----------TGDNFSGGQIIKLEIARAIL 462
Cdd:cd03251 81 VSQDVFLFNDTVAENIA-YgrPGATREEVEEAARA-----ANAHEFIMELpegydtvigeRGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348497 463 REKQVLLADEMMASLDAASSKEISNVLKQL--PNSIIEIAHHYK-LEDYDAVYRIENKSIV 520
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLStIENADRIVVLEDGKIV 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-514 |
2.50e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 73.62 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNldniaiihqn 398
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI---LVDGKEVSFA---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 pyvfhtSVRHNLTLyqdysdsllistlkkvGLweACCHQLdyeltgdnfSGGQIIKLEIARAILREKQVLLADEMMASLD 478
Cdd:cd03216 68 ------SPRDARRA----------------GI--AMVYQL---------SVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081348497 479 AASSKEISNVLKQLPN---SIIEIAHhyKLEDydaVYRI 514
Cdd:cd03216 115 PAEVERLFKVIRRLRAqgvAVIFISH--RLDE---VFEI 148
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-513 |
6.81e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 6.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYS-----GKIIF--KSIDGRELTPN--L 389
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFfnQNIYERRVNLNrlR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 390 DNIAIIHQNPYVFHTSVRHNLTlyqdYS------------DSLLISTLKKVGLWEACCHQLdyELTGDNFSGGQIIKLEI 457
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVA----YGvkivgwrpkleiDDIVESALKDADLWDEIKHKI--HKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348497 458 ARAILREKQVLLADEMMASLDAASSKEISNVLKQLP----NSIIEIAHHY----KLEDYDAVYR 513
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLhqvsRLSDFTAFFK 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
319-501 |
1.00e-14 |
|
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: 73.80 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYD-NQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTpnLD----NIA 393
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT--LDslrrAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNPYVFHTSVRHNLtLY--QDYSDSLLISTLKKvglweACCHQLDYELT----------GDNFSGGQIIKLEIARAI 461
Cdd:cd03253 79 VVPQDTVLFNDTIGYNI-RYgrPDATDEEVIEAAKA-----AQIHDKIMRFPdgydtivgerGLKLSGGEKQRVAIARAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081348497 462 LREKQVLLADEMMASLDAASSKEISNVLKQLPNS--IIEIAH 501
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAH 194
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
319-492 |
2.04e-14 |
|
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: 72.61 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEifRDVT----VTFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKII-----FKSIDGRELTP 387
Cdd:cd03258 2 IELKNVSKVFGDTG--GKVTalkdVSLSVPKGEIfgIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 388 NLDNIAIIHQNPYVFHT-SVRHNLTLyqdysdSLLISTLKKVGLWEACCHQLdyELTG---------DNFSGGQIIKLEI 457
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSrTVFENVAL------PLEIAGVPKAEIEERVLELL--ELVGledkadaypAQLSGGQKQRVGI 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1081348497 458 ARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDI 186
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
319-479 |
2.37e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.49 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDN-QEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGR---ELTPNLDNIAI 394
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI---WIGGRvvnELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNpYVF--HTSVRHNLTlY----------------QDYSDSLLISTLkkvglweacchqLD---YELtgdnfSGGQII 453
Cdd:PRK11650 81 VFQN-YALypHMSVRENMA-YglkirgmpkaeieervAEAARILELEPL------------LDrkpREL-----SGGQRQ 141
|
170 180
....*....|....*....|....*.
gi 1081348497 454 KLEIARAILREKQVLLADEMMASLDA 479
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
229-502 |
2.57e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.91 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 229 LQNLVMFWTGPLKAVGLI-GPFVIG--LVMKQN-SITTLIAMMSASTYLINPLQQILEAIASIQSSQVIKDKLLTF-GSE 303
Cdd:TIGR00958 382 LAYAGYLWTTSVLGMLIQvLVLYYGgqLVLTGKvSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYlDRK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 304 SEIPSKGLHIHTLEE--IQLKNVTKSYDN---QEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfk 378
Cdd:TIGR00958 462 PNIPLTGTLAPLNLEglIEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL-- 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 379 sIDGRELtPNLDN------IAIIHQNPYVFHTSVRHNLTLYQDYSDSLLISTLKKvglwEACCHQLDYELT--------- 443
Cdd:TIGR00958 540 -LDGVPL-VQYDHhylhrqVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAK----AANAHDFIMEFPngydtevge 613
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 444 -GDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPNSIIEIAHH 502
Cdd:TIGR00958 614 kGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHR 673
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
319-501 |
4.58e-14 |
|
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: 69.40 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIdgreltpnlDNIAIIHQn 398
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST---------VKIGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 pyvfhtsvrhnltlyqdysdsllistlkkvglweacchqldyeltgdnFSGGQIIKLEIARAILREKQVLLADEMMASLD 478
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180
....*....|....*....|...
gi 1081348497 479 AASSKEISNVLKQLPNSIIEIAH 501
Cdd:cd03221 103 LESIEALEEALKEYPGTVILVSH 125
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
318-515 |
8.25e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.74 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFR-------LISGqdKAYSGKIIF--KSIDGRELTPN 388
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPG--FRVEGKVTFhgKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 389 --LDNIAIIHQNPYVFHTSVRHNLTL------YQDYSDSLLISTLKKVGLWEACCHQLdyELTGDNFSGGQIIKLEIARA 460
Cdd:PRK14243 88 evRRRIGMVFQKPNPFPKSIYDNIAYgaringYKGDMDELVERSLRQAALWDEVKDKL--KQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348497 461 ILREKQVLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAHHY----KLEDYDAVYRIE 515
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHNMqqaaRVSDMTAFFNVE 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
320-502 |
1.08e-13 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 70.84 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 320 QLKNVTKSydnqeiFRDVT----VTFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIIFksiDGRELTpNLDNIA 393
Cdd:COG0411 6 EVRGLTKR------FGGLVavddVSLEVERGEIvgLIGPNGAGKTTLFNLITGFYRPTSGRILF---DGRDIT-GLPPHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIH-------QNPYVFHT-SVRHNLTL-YQDYSDSLLISTLKKVGLW--------EACCHQLDY-ELTG------DNFSG 449
Cdd:COG0411 76 IARlgiartfQNPRLFPElTVLENVLVaAHARLGRGLLAALLRLPRArreerearERAEELLERvGLADradepaGNLSY 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348497 450 GQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN----SIIEIAHH 502
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDergiTILLIEHD 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
319-492 |
1.11e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.42 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLDNIAIIHQN 398
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVF-HTSVRHN----LTLY--QDYSDSLLIStlKKV-GLWEACchQLDY--ELTGDNFSGGQIIKLEIARAILREKQVL 468
Cdd:PRK10851 83 YALFrHMTVFDNiafgLTVLprRERPNAAAIK--AKVtQLLEMV--QLAHlaDRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180
....*....|....*....|....
gi 1081348497 469 LADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQL 182
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-501 |
1.20e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 7 FKLLPKKDIILYIIFALLYSCQGIVIPVIIQMAG----HIDSSDSRDLIVFTFSSISLWVVVYAFM--YIENILLRSIIR 80
Cdd:PTZ00265 51 FKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGvimkNMNLGENVNDIIFSLVLIGIFQFILSFIssFCMDVVTTKILK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 81 AFNVSLSENILKNHAVFPKNISDSELCSLLTQDLGIVDQEFLQSFLISPVWGASVLVSVIYLLKQNLIVGSLFTVGAFLM 160
Cdd:PTZ00265 131 TLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 161 ILPQFIFKRKLKESGELLSSSKEKNLRAITDFGKGIETIICNQAEKENVKQtlITLSEmetTQFKYYTLQNLVMfwtgPL 240
Cdd:PTZ00265 211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKK--FNLSE---KLYSKYILKANFM----ES 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 241 KAVGLIGPFV---------------IGLVMKQNS---------ITTLIAMMSASTYLINPLQQILEAIASIQSS----QV 292
Cdd:PTZ00265 282 LHIGMINGFIlasyafgfwygtriiISDLSNQQPnndfhggsvISILLGVLISMFMLTIILPNITEYMKSLEATnslyEI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 293 IKDKLLTfgsesEIPSKGLHIHTLEEIQLKNVTKSYDNQ---EIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDK 369
Cdd:PTZ00265 362 INRKPLV-----ENNDDGKKLKDIKKIQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 370 AYSGKIIFKsiDGRELTP-NL----DNIAIIHQNPYVFHTSVRHNLTL-------------------------------- 412
Cdd:PTZ00265 437 PTEGDIIIN--DSHNLKDiNLkwwrSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqenknkrnsc 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 413 --------------------------YQDYSDSLLISTLKKVGLWEACCHQLD-YE-LTGDN---FSGGQIIKLEIARAI 461
Cdd:PTZ00265 515 rakcagdlndmsnttdsneliemrknYQTIKDSEVVDVSKKVLIHDFVSALPDkYEtLVGSNaskLSGGQKQRISIARAI 594
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1081348497 462 LREKQVLLADEMMASLDAAS----SKEISNvLKQLPNSI-IEIAH 501
Cdd:PTZ00265 595 IRNPKILILDEATSSLDNKSeylvQKTINN-LKGNENRItIIIAH 638
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-502 |
1.94e-13 |
|
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: 72.63 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIF--RDVTVTFSLSQHNLIVGDSGIGKTTLFRLISG---QDKAYSGKIIFKSIDGRELTPNL--DN 391
Cdd:COG1123 5 LEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALrgRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 IAIIHQNPYVFHTSVR---------HNLTLYQDYSDSLLISTLKKVGL---WEACCHQLdyeltgdnfSGGQIIKLEIAR 459
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgdqiaealENLGLSRAEARARVLELLEAVGLerrLDRYPHQL---------SGGQRQRVAIAM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081348497 460 AILREKQVLLADEMMASLDAASSKEISNVLKQLPN----SIIEIAHH 502
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRergtTVLLITHD 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
349-492 |
2.02e-13 |
|
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: 69.25 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 349 IVGDSGIGKTTLFRLISGQDKAYSGKIIF---------KSIDgreLTPNLDNIAIIHQNPYVF-HTSVRHNLT--LYQDY 416
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsrKKIN---LPPQQRKIGLVFQQYALFpHLNVRENLAfgLKRKR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348497 417 SDSLLISTLKKVGLWeacchQLDyELTG---DNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03297 105 NREDRISVDELLDLL-----GLD-HLLNrypAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
319-505 |
2.09e-13 |
|
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: 69.81 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQ---EIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELtPNLDN---- 391
Cdd:cd03248 12 VKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVL---LDGKPI-SQYEHkylh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 --IAIIHQNPYVFHTSVRHNLT-------------LYQDYSDSLLISTLKKvGLWEacchqlDYELTGDNFSGGQIIKLE 456
Cdd:cd03248 88 skVSLVGQEPVLFARSLQDNIAyglqscsfecvkeAAQKAHAHSFISELAS-GYDT------EVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081348497 457 IARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAHHYKL 505
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAHRLST 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
319-478 |
2.25e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.79 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLDNIAIIHQN 398
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVF-HTSVRHNLT--LYQDYSDSLLISTlkKVGLWEACCHQLDY-ELTGDNFSGGQIIKLEIARAILREKQVLLADEMM 474
Cdd:PRK11607 100 YALFpHMTVEQNIAfgLKQDKLPKAEIAS--RVNEMLGLVHMQEFaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
....
gi 1081348497 475 ASLD 478
Cdd:PRK11607 178 GALD 181
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
320-492 |
3.09e-13 |
|
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: 67.85 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 320 QLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELT--PNLD---NIAI 394
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI---LLDGKDLAslSPKElarKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNpyvfhtsvrhnltlyqdysdsllistLKKVGLW---EACCHQLdyeltgdnfSGGQIIKLEIARAILREKQVLLAD 471
Cdd:cd03214 78 VPQA--------------------------LELLGLAhlaDRPFNEL---------SGGERQRVLLARALAQEPPILLLD 122
|
170 180
....*....|....*....|.
gi 1081348497 472 EMMASLDAASSKEISNVLKQL 492
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRL 143
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
243-520 |
3.39e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.97 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 243 VGLIGPFVIGLVMKQNSITTLIAMMSASTY---------LINPLQQILEAIASIQSSQVIKDKLLTF-GSESEIPSKGLH 312
Cdd:PRK11176 255 IQLIASLALAFVLYAASFPSVMDTLTAGTItvvfssmiaLMRPLKSLTNVNAQFQRGMAACQTLFAIlDLEQEKDEGKRV 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 313 IHTLE-EIQLKNVTKSYDNQEI--FRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELT-PN 388
Cdd:PRK11176 335 IERAKgDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlAS 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 389 L-DNIAIIHQNPYVFHTSVRHNLTLYQD--YSDSLLISTLK---KVGLWEACCHQLDyELTGDN---FSGGQIIKLEIAR 459
Cdd:PRK11176 415 LrNQVALVSQNVHLFNDTIANNIAYARTeqYSREQIEEAARmayAMDFINKMDNGLD-TVIGENgvlLSGGQRQRIAIAR 493
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348497 460 AILREKQVLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAHHYK-LEDYDAVYRIENKSIV 520
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLStIEKADEILVVEDGEIV 557
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
319-501 |
4.08e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLDNIAIIHQN 398
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 pYVFHTsvrhNLTLYQDYSDSLLISTLKKVGLWEACCH-----QLDYEL--TGDNFSGGQIIKLEIARAILREKQVLLAD 471
Cdd:PRK11000 84 -YALYP----HLSVAENMSFGLKLAGAKKEEINQRVNQvaevlQLAHLLdrKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190
....*....|....*....|....*....|....
gi 1081348497 472 EMMASLDAA----SSKEISNVLKQLPNSIIEIAH 501
Cdd:PRK11000 159 EPLSNLDAAlrvqMRIEISRLHKRLGRTMIYVTH 192
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
319-491 |
4.18e-13 |
|
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: 68.59 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEI-FRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTpNLDNIAIihq 397
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIR---VNGQDVS-DLRGRAI--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 398 nPY-------VFHTS-VRHNLTLYQDYSDSLLIS-------------TLKKVGLwEACCHQLDYELtgdnfSGGQIIKLE 456
Cdd:cd03292 74 -PYlrrkigvVFQDFrLLPDRNVYENVAFALEVTgvppreirkrvpaALELVGL-SHKHRALPAEL-----SGGEQQRVA 146
|
170 180 190
....*....|....*....|....*....|....*
gi 1081348497 457 IARAILREKQVLLADEMMASLDAASSKEISNVLKQ 491
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKK 181
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
321-501 |
4.48e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 321 LKNVTKSYDNQEIFRDVTvtFSLSQHNLI--VGDSGIGKTTLFRLISGQDKAYSGKIIfksidgreLTPNLDnIAIIHQN 398
Cdd:COG0488 1 LENLSKSFGGRPLLDDVS--LSINPGDRIglVGRNGAGKSTLLKILAGELEPDSGEVS--------IPKGLR-IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVF-HTSVRHNL---------------TLYQDYSDSL--------LISTLKKVGLWEA-----------CCHQLDYELT 443
Cdd:COG0488 70 PPLDdDLTVLDTVldgdaelraleaeleELEAKLAEPDedlerlaeLQEEFEALGGWEAearaeeilsglGFPEEDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348497 444 GDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASskeIS---NVLKQLPNSIIEIAH 501
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwleEFLKNYPGTVLVVSH 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
319-520 |
5.02e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.46 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQeifrdvTVTFSLS----QHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLDNIAI 394
Cdd:PRK10771 2 LKLTDITWLYHHL------PMRFDLTvergERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNPYVF-HTSVRHNLTL-------YQDYSDSLLISTLKKVGLwEACCHQLDYELtgdnfSGGQIIKLEIARAILREKQ 466
Cdd:PRK10771 76 LFQENNLFsHLTVAQNIGLglnpglkLNAAQREKLHAIARQMGI-EDLLARLPGQL-----SGGQRQRVALARCLVREQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348497 467 VLLADEMMASLDAASSKEISNVLKQLPN----SIIEIAHHykLEDydaVYRIENKSIV 520
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQerqlTLLMVSHS--LED---AARIAPRSLV 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
319-492 |
1.90e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 69.75 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQE----IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGkiIFKsIDGREL-TPNLDNIA 393
Cdd:PRK10535 5 LELKDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG--TYR-VAGQDVaTLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNPYVF---------HTSVRHNLTLYQDYSDS-------LLISTLKKVGLWEacchQLDYELTgdNFSGGQIIKLEI 457
Cdd:PRK10535 82 QLRREHFGFifqryhllsHLTAAQNVEVPAVYAGLerkqrllRAQELLQRLGLED----RVEYQPS--QLSGGQQQRVSI 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1081348497 458 ARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQL 190
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
319-492 |
1.97e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.76 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDV--TVTFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIIFKsidGRELT-------P 387
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQTDVlhNVSFSIGEGEMmaIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN---GQPMSklssaakA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 388 NLDN--IAIIHQnpyvFHtSVRHNLTLYQDYSDSLLI-------------STLKKVGLwEACCHQLDYELtgdnfSGGQI 452
Cdd:PRK11629 83 ELRNqkLGFIYQ----FH-HLLPDFTALENVAMPLLIgkkkpaeinsralEMLAAVGL-EHRANHRPSEL-----SGGER 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081348497 453 IKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL 191
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
319-492 |
2.51e-12 |
|
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: 66.30 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFksiDGRELTP------NLDNI 392
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF---DGRDITGlppherARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 AIIHQNPYVFHT-SVRHNLTL-YQDYSDSLLISTLKKVglweacchqldYEL----------TGDNFSGGQIIKLEIARA 460
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLgAYARRRAKRKARLERV-----------YELfprlkerrkqLAGTLSGGEQQMLAIARA 146
|
170 180 190
....*....|....*....|....*....|..
gi 1081348497 461 ILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL 178
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
319-478 |
3.24e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY--DNQEIFRDVTVTFSLSQHNLIVGDSGIGKT----TLFRLISGQdkaySGKIIFKSIDGRE--LTPNLD 390
Cdd:PLN03130 1238 IKFEDVVLRYrpELPPVLHGLSFEISPSEKVGIVGRTGAGKSsmlnALFRIVELE----RGRILIDGCDISKfgLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 NIAIIHQNPYVFHTSVRHNLTLYQDYSDSLLISTLKKVGLWEACCHQ---LDYELT--GDNFSGGQIIKLEIARAILREK 465
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNslgLDAEVSeaGENFSVGQRQLLSLARALLRRS 1393
|
170
....*....|...
gi 1081348497 466 QVLLADEMMASLD 478
Cdd:PLN03130 1394 KILVLDEATAAVD 1406
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
319-479 |
4.28e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.44 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELT----PNLDnIAI 394
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF---IDGEDVThrsiQQRD-ICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNPYVF-HTSVRHNLtlyqDYSdsllistLKKVGLWEACCHQLDYE------LTG------DNFSGGQIIKLEIARAI 461
Cdd:PRK11432 83 VFQSYALFpHMSLGENV----GYG-------LKMLGVPKEERKQRVKEalelvdLAGfedryvDQISGGQQQRVALARAL 151
|
170
....*....|....*...
gi 1081348497 462 LREKQVLLADEMMASLDA 479
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDA 169
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-492 |
4.55e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 66.21 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFslsQHNLI---VGDSGIGKTTLFR-------LISGQdkAYSGKIIFksiDGRE-LTP 387
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDI---PENKVtalIGPSGCGKSTLLRclnrmndLIPGA--RVEGEILL---DGEDiYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 388 NLD------NIAIIHQNPYVFHTSVRHN----LTLYQDYSDSLL--I--STLKKVGLWEACCHQLD---YELtgdnfSGG 450
Cdd:COG1117 84 DVDvvelrrRVGMVFQKPNPFPKSIYDNvaygLRLHGIKSKSELdeIveESLRKAALWDEVKDRLKksaLGL-----SGG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081348497 451 QIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
318-511 |
7.10e-12 |
|
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: 68.43 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSY--DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTT----LFRLisgqDKAYSGKIIfksIDGRELTP-NLD 390
Cdd:TIGR00957 1284 RVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRI----NESAEGEII---IDGLNIAKiGLH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 N----IAIIHQNPYVFHTSVRHNLTLYQDYSD-----SLLISTLKkvGLWEACCHQLDYELT--GDNFSGGQIIKLEIAR 459
Cdd:TIGR00957 1357 DlrfkITIIPQDPVLFSGSLRMNLDPFSQYSDeevwwALELAHLK--TFVSALPDKLDHECAegGENLSVGQRQLVCLAR 1434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348497 460 AILREKQVLLADEMMASLDAASSKEI-SNVLKQLPN-SIIEIAHHYK-LEDYDAV 511
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIqSTIRTQFEDcTVLTIAHRLNtIMDYTRV 1489
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
322-513 |
9.45e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.05 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 322 KNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNLDNIA-----IIH 396
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV---LLNGGPLDFQRDSIArgllyLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 397 QNPYVFHTSVRHNLTLYQ-DYSDSLLISTLKKVGLW---EACCHQLdyeltgdnfSGGQIIKLEIARAILREKQVLLADE 472
Cdd:cd03231 81 APGIKTTLSVLENLRFWHaDHSDEQVEEALARVGLNgfeDRPVAQL---------SAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081348497 473 MMASLDAASSKEISNVLKQ--LPNSIIEIAHHYKLEDYDAVYR 513
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGhcARGGMVVLTTHQDLGLSEAGAR 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
319-492 |
1.20e-11 |
|
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: 64.31 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDG-RELTPNLDNIAIIHQ 397
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 398 NPyvfhtSVRHNLTLYQDysdsLLI-----------------STLKKVGLWEACCHQLDYeltgdnFSGGQIIKLEIARA 460
Cdd:cd03265 81 DL-----SVDDELTGWEN----LYIharlygvpgaerreridELLDFVGLLEAADRLVKT------YSGGMRRRLEIARS 145
|
170 180 190
....*....|....*....|....*....|..
gi 1081348497 461 ILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKL 177
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
319-501 |
1.38e-11 |
|
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: 63.00 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY--DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTP-NLDNIAii 395
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR---LDGADISQwDPNELG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 396 hqnpyvfhtsvRHNLTLYQDysDSLLISTLKkvglweacchqldyeltgDN-FSGGQIIKLEIARAILREKQVLLADEMM 474
Cdd:cd03246 76 -----------DHVGYLPQD--DELFSGSIA------------------ENiLSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190
....*....|....*....|....*....|
gi 1081348497 475 ASLDAASSKEISNVLKQLP---NSIIEIAH 501
Cdd:cd03246 125 SHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
318-501 |
1.41e-11 |
|
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: 64.93 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSYDN--QEIFRDVTVTFSLSQHNLIVGDSGIGKTTL----FRLISgqdkAYSGKIIFKSIDGRELTPNL-- 389
Cdd:cd03288 19 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVD----IFDGKIVIDGIDISKLPLHTlr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 390 DNIAIIHQNPYVFHTSVRHNLTLYQDYSDSLL-----ISTLKKVglWEACCHQLDYELT--GDNFSGGQIIKLEIARAIL 462
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECKCTDDRLwealeIAQLKNM--VKSLPGGLDAVVTegGENFSVGQRQLFCLARAFV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348497 463 REKQVLLADEMMASLDAASskeiSNVLKQL------PNSIIEIAH 501
Cdd:cd03288 173 RKSSILIMDEATASIDMAT----ENILQKVvmtafaDRTVVTIAH 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
249-480 |
1.42e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.91 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 249 FVIGLVMKQN---SITTLIAMMSASTYLINPLQQILEAIASIQSSQVikdKLLTFGS------ESEIPSKGLHIHTLE-E 318
Cdd:PRK13657 258 LVLGAALVQKgqlRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAP---KLEEFFEvedavpDVRDPPGAIDLGRVKgA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDN--QEIFrDVTVTFSLSQHNLIVGDSGIGKTTLFRLISgqdKAY---SGKIIFKSIDGRELTPN--LDN 391
Cdd:PRK13657 335 VEFDDVSFSYDNsrQGVE-DVSFEAKPGQTVAIVGPTGAGKSTLINLLQ---RVFdpqSGRILIDGTDIRTVTRAslRRN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 IAIIHQNPYVFHTSVRHNLTL-YQDYSDSLLISTLKKVGLWEACCHQLDYELT-----GDNFSGGQIIKLEIARAILREK 465
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVgRPDATDEEMRAAAERAQAHDFIERKPDGYDTvvgerGRQLSGGERQRLAIARALLKDP 490
|
250
....*....|....*
gi 1081348497 466 QVLLADEMMASLDAA 480
Cdd:PRK13657 491 PILILDEATSALDVE 505
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-402 |
1.89e-11 |
|
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: 66.36 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 5 NFFKLL--PKKDIILYIIFALLYS--CQGIVIPVIIQMAGHIDSSDSRDLIVFtfssISLWVVVYAFMYIENILL----R 76
Cdd:COG4615 2 NLLRLLlrESRWLLLLALLLGLLSglANAGLIALINQALNATGAALARLLLLF----AGLLVLLLLSRLASQLLLtrlgQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 77 SIIRAFNVSLSENILknHAVFPK--NISDSELCSLLTQDLGIVDQ------EFLQSFLIspvwgasVLVSVIYLLkqnLI 148
Cdd:COG4615 78 HAVARLRLRLSRRIL--AAPLERleRIGAARLLAALTEDVRTISQafvrlpELLQSVAL-------VLGCLAYLA---WL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 149 VGSLFTVGAFLMILPQFIFKRKLKESGELLSSSKE------KNLRAITD---------------FGKGIETIIcNQAEKE 207
Cdd:COG4615 146 SPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREaedrlfKHFRALLEgfkelklnrrrrrafFDEDLQPTA-ERYRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 208 NVKQTLITLSEMETTQFKYYTLQNLVMFWtgpLKAVGLIGPFVIGLVmkqnsITTLIammsastYLINPLQQILEAIASI 287
Cdd:COG4615 225 RIRADTIFALANNWGNLLFFALIGLILFL---LPALGWADPAVLSGF-----VLVLL-------FLRGPLSQLVGALPTL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 288 QSSQV-------IKDKLLTFGSESEIPSKGLHIHTLEEIQLKNVTKSY---DNQEIFR----DVT-----VTFslsqhnl 348
Cdd:COG4615 290 SRANValrkieeLELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYpgeDGDEGFTlgpiDLTirrgeLVF------- 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348497 349 IVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTP-NLD----NIAIIHQNPYVF 402
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEI---LLDGQPVTAdNREayrqLFSAVFSDFHLF 418
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
319-501 |
2.83e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.89 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY-DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTpNL------DN 391
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR---LDGRPLS-SLshsvlrQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 IAIIHQNPYVFHTSVRHNLTLYQDYSDSLLISTLKKVGLWE---ACCHQLDYEL--TGDNFSGGQIIKLEIARAILREKQ 466
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAElarSLPDGLYTPLgeQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081348497 467 VLLADEMMASLDAASSKEISNVLKQL--PNSIIEIAH 501
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH 533
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-502 |
3.11e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.91 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 323 NVTKSY---DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNLD--------- 390
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKI---KVDGKVLYFGKDifqidaikl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 --NIAIIHQNPYVF-HTSVRHNLTL------YQDYSD--SLLISTLKKVGLWEACCHQLDYelTGDNFSGGQIIKLEIAR 459
Cdd:PRK14246 89 rkEVGMVFQQPNPFpHLSIYDNIAYplkshgIKEKREikKIVEECLRKVGLWKEVYDRLNS--PASQLSGGQQQRLTIAR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348497 460 AILREKQVLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAHH 502
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
321-481 |
3.45e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 62.38 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 321 LKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNL-DNIAII-HQN 398
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhENILYLgHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVFHTSVRHNLTLYQD---YSDSLLISTLKKVGL---WEACCHQLdyeltgdnfSGGQIIKLEIARAILREKQVLLADE 472
Cdd:TIGR01189 83 GLKPELSALENLHFWAAihgGAQRTIEDALAAVGLtgfEDLPAAQL---------SAGQQRRLALARLWLSRRPLWILDE 153
|
....*....
gi 1081348497 473 MMASLDAAS 481
Cdd:TIGR01189 154 PTTALDKAG 162
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
319-485 |
4.24e-11 |
|
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: 62.49 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQE-----IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSidgreltpnldNIA 393
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNPYVFHTSVRHNLTLYQDYSDSLLISTLKkvglweACCHQLDYEL--TGD---------NFSGGQIIKLEIARAIL 462
Cdd:cd03250 70 YVSQEPWIQNGTIRENILFGKPFDEERYEKVIK------ACALEPDLEIlpDGDlteigekgiNLSGGQKQRISLARAVY 143
|
170 180
....*....|....*....|...
gi 1081348497 463 REKQVLLADEMMASLDAASSKEI 485
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHI 166
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
318-492 |
4.46e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGREL----TPNLDNIA 393
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL---NIAGHQFdfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQN-PYVF-------HTSVRHNLT------LYQDYSDSL-----LISTLK---KVGLWEAcchqldyeltgdNFSGGQ 451
Cdd:COG4161 79 LLRQKvGMVFqqynlwpHLTVMENLIeapckvLGLSKEQARekamkLLARLRltdKADRFPL------------HLSGGQ 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081348497 452 IIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL 187
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
319-492 |
4.93e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.72 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGREL----TPNLDNIAI 394
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL---NIAGNHFdfskTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQN-PYVF-------HTSVRHNLtlyqdysdsllISTLKKV-GLWEACCHQLDYELT--------GDNF----SGGQII 453
Cdd:PRK11124 80 LRRNvGMVFqqynlwpHLTVQQNL-----------IEAPCRVlGLSKDQALARAEKLLerlrlkpyADRFplhlSGGQQQ 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081348497 454 KLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL 187
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
319-501 |
5.20e-11 |
|
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: 62.89 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY--DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELT---PNL--DN 391
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL---VDGHDLAladPAWlrRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 IAIIHQNPYVFHTSVRHNLTLYQDYSDSLLISTLKKVglweACCHQLDYEL----------TGDNFSGGQIIKLEIARAI 461
Cdd:cd03252 78 VGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKL----AGAHDFISELpegydtivgeQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081348497 462 LREKQVLLADEMMASLDAASSKEI-SNVLKQLPN-SIIEIAH 501
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAImRNMHDICAGrTVIIIAH 195
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
319-492 |
6.78e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.56 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEifRDVTVtfsLSQHNL---------IVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTpNL 389
Cdd:COG1135 2 IELENLSKTFPTKG--GPVTA---LDDVSLtiekgeifgIIGYSGAGKSTLIRCINLLERPTSGSVL---VDGVDLT-AL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 390 D---------NIAIIHQNPYVFHT-SVRHNLTLyqdysdSLLISTLKK-------------VGLWEaccHQLDY--ELtg 444
Cdd:COG1135 73 SerelraarrKIGMIFQHFNLLSSrTVAENVAL------PLEIAGVPKaeirkrvaellelVGLSD---KADAYpsQL-- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348497 445 dnfSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:COG1135 142 ---SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI 186
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
135-292 |
1.08e-10 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 62.46 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 135 VLVSVIYLLKQNLIVGSLFTVGAFLMILPQFIFKRKLKESGELLSSSKEKNLRAITDFGKGIETIICNQAEKENVKQTLI 214
Cdd:cd18570 129 VIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 215 TLSEMETTQFKYYTLQNLVMFWTGPLKAVGLIGPFVIG--LVMKQN-SITTLIAMMSASTYLINPLQQILEAIASIQSSQ 291
Cdd:cd18570 209 KFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGsyLVIKGQlSLGQLIAFNALLGYFLGPIENLINLQPKIQEAK 288
|
.
gi 1081348497 292 V 292
Cdd:cd18570 289 V 289
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
349-501 |
1.09e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.19 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 349 IVGDSGIGKTTLFRLISGQDKAYSGKIIFKsidGRELTPNLD--------NIAIIHQNPYvfhTSVRHNLTLYQDYSDSL 420
Cdd:PRK15079 52 VVGESGCGKSTFARAIIGLVKATDGEVAWL---GKDLLGMKDdewravrsDIQMIFQDPL---ASLNPRMTIGEIIAEPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 421 LI---------------STLKKVGLWEACCHQLDYEltgdnFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEI 485
Cdd:PRK15079 126 RTyhpklsrqevkdrvkAMMLKVGLLPNLINRYPHE-----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180
....*....|....*....|
gi 1081348497 486 SNVLKQLPN----SIIEIAH 501
Cdd:PRK15079 201 VNLLQQLQRemglSLIFIAH 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
330-510 |
1.12e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 330 NQEIFRDVTvtFSLSQHN--LIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLDNIAIIHQNPYVFHTSVR 407
Cdd:PRK13539 14 GRVLFSGLS--FTLAAGEalVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 408 HNLTLYQDY---SDSLLISTLKKVGLweacchQLDYELTGDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKE 484
Cdd:PRK13539 92 ENLEFWAAFlggEELDIAAALEAVGL------APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180 190
....*....|....*....|....*....|
gi 1081348497 485 ISNV----LKQlpNSIIEIAHHYKLEDYDA 510
Cdd:PRK13539 166 FAELirahLAQ--GGIVIAATHIPLGLPGA 193
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
315-508 |
1.25e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 315 TLEEIQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSID---GRELtPNLDN 391
Cdd:COG2401 27 VAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDnqfGREA-SLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 IAIIHQnpyvFHTSVRhnltlyqdysdSLLISTLKKVGLWEACCHQLdyeltgdnfSGGQIIKLEIARAILREKQVLLAD 471
Cdd:COG2401 106 IGRKGD----FKDAVE-----------LLNAVGLSDAVLWLRRFKEL---------STGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081348497 472 EMMASLDAASSKEIS-NVLK---QLPNSIIEIAHHYKLEDY 508
Cdd:COG2401 162 EFCSHLDRQTAKRVArNLQKlarRAGITLVVATHHYDVIDD 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
349-501 |
1.31e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 349 IVGDSGIGKTT----LFRLISGQdkaySGKIIFKSIDGRE--LTPNLDNIAIIHQNPYVFHTSVRHNLTLYQDYSDSLLI 422
Cdd:PLN03232 1267 VVGRTGAGKSSmlnaLFRIVELE----KGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLW 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 423 STLKKVGLWEACCHQ---LDYELT--GDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPNS-- 495
Cdd:PLN03232 1343 EALERAHIKDVIDRNpfgLDAEVSegGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSct 1422
|
....*.
gi 1081348497 496 IIEIAH 501
Cdd:PLN03232 1423 MLVIAH 1428
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
323-499 |
2.04e-10 |
|
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: 61.02 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 323 NVTKSYDNQEIFRDVTVTFSLSQhnlIV---GDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTP-NLDN-----IA 393
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGE---IVgllGPNGAGKTTTFYMIVGLVKPDSGKIL---LDGQDITKlPMHKrarlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNPYVFHT-SVRHNL-------TLYQDYSDSLLISTLKKVGLwEACCHQLDYELtgdnfSGGQIIKLEIARAILREK 465
Cdd:cd03218 79 YLPQEASIFRKlTVEENIlavleirGLSKKEREEKLEELLEEFHI-THLRKSKASSL-----SGGERRRVEIARALATNP 152
|
170 180 190
....*....|....*....|....*....|....
gi 1081348497 466 QVLLADEMMASLDAASSKEISNVLKQLPNSIIEI 499
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGV 186
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
319-472 |
2.05e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifksidgrELTPNLdNIAIIHQN 398
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGETV-KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 pyvfHTSVRHNLTLYQ---DYSDSL----LISTL-----------KKVGlweacchqldyeltgdNFSGGQIIKLEIARA 460
Cdd:COG0488 387 ----QEELDPDKTVLDelrDGAPGGteqeVRGYLgrflfsgddafKPVG----------------VLSGGEKARLALAKL 446
|
170
....*....|..
gi 1081348497 461 ILREKQVLLADE 472
Cdd:COG0488 447 LLSPPNVLLLDE 458
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-501 |
2.65e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.01 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLIS-----GQDKAYSGKIifkSIDGREL-TPNLDNI 392
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEV---RLFGRNIySPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 AI------IHQNPYVF-HTSVRHNLTL---------YQDYSDSLLISTLKKVGLWEACCHQL-DYEltgDNFSGGQIIKL 455
Cdd:PRK14267 82 EVrrevgmVFQYPNPFpHLTIYDNVAIgvklnglvkSKKELDERVEWALKKAALWDEVKDRLnDYP---SNLSGGQRQRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348497 456 EIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAH 501
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
61-487 |
3.02e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 61 WV-VVYAFM--------------YIENIL-----LRSIIRA--FNVSLSeniLKNHAvfPKNISDSELCSLLTQDLGIVD 118
Cdd:PLN03232 338 WVgYVYAFLiffgvtfgvlcesqYFQNVGrvgfrLRSTLVAaiFHKSLR---LTHEA--RKNFASGKVTNMITTDANALQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 119 QEFLQsflISPVWGAS--VLVSVIyLLKQNLIVGSLF-TVGAFLMILPQFIFKRKLKESGELLSSSKEKNLRAITDFGKG 195
Cdd:PLN03232 413 QIAEQ---LHGLWSAPfrIIVSMV-LLYQQLGVASLFgSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILAS 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 196 IETIICNQAEKeNVKQTLITLSEMETTQFKyyTLQNLVMFWTGPLKAVgligPFVIGLV------MKQNSITTLIAMMSA 269
Cdd:PLN03232 489 MDTVKCYAWEK-SFESRIQGIRNEELSWFR--KAQLLSAFNSFILNSI----PVVVTLVsfgvfvLLGGDLTPARAFTSL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 270 STY---------LINPLQQILEAIASIQSsqvIKDKLLtfgSESEIPSKGLHIHT-LEEIQLKNVTKSYD---NQEIFRD 336
Cdd:PLN03232 562 SLFavlrsplnmLPNLLSQVVNANVSLQR---IEELLL---SEERILAQNPPLQPgAPAISIKNGYFSWDsktSKPTLSD 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 337 VTVTFSLSQHNLIVGDSGIGKTTLFRLISGQ-DKAYSGKIIFKSidgreltpnldNIAIIHQNPYVFHTSVRHNLTLYQD 415
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGElSHAETSSVVIRG-----------SVAYVPQVSWIFNATVRENILFGSD 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 416 YSDSLLISTLKKVGLWeaccHQLD----YELT-----GDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEIS 486
Cdd:PLN03232 705 FESERYWRAIDVTALQ----HDLDllpgRDLTeigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
.
gi 1081348497 487 N 487
Cdd:PLN03232 781 D 781
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
319-472 |
3.25e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.93 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFksiDGrELTPNLD-------- 390
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF---DG-ENIPAMSrsrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 -NIAIIHQNPYVF-----HTSVRHNLTLYQDYSDSLLIST----LKKVGLWEACchqldyELTGDNFSGGQIIKLEIARA 460
Cdd:PRK11831 84 kRMSMLFQSGALFtdmnvFDNVAYPLREHTQLPAPLLHSTvmmkLEAVGLRGAA------KLMPSELSGGMARRAALARA 157
|
170
....*....|..
gi 1081348497 461 ILREKQVLLADE 472
Cdd:PRK11831 158 IALEPDLIMFDE 169
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
319-485 |
3.67e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.89 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY-DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSID-----GRELTPNLDNI 392
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlkNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 AIIHQNPYVFHtsvrhNLTLYQDYSDSLLIS-------------TLKKVGLweacchqLDyelTGDNF----SGGQIIKL 455
Cdd:PRK10908 82 GMIFQDHHLLM-----DRTVYDNVAIPLIIAgasgddirrrvsaALDKVGL-------LD---KAKNFpiqlSGGEQQRV 146
|
170 180 190
....*....|....*....|....*....|
gi 1081348497 456 EIARAILREKQVLLADEMMASLDAASSKEI 485
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
321-492 |
4.15e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.46 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 321 LKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIdgrELTPNLDNIAIIHQN-- 398
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA---PLAEAREDTRLMFQDar 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 --PYvfhTSVRHN--LTLYQDYSDSLLiSTLKKVGL------WEACchqldyeltgdnFSGGQIIKLEIARAILREKQVL 468
Cdd:PRK11247 92 llPW---KKVIDNvgLGLKGQWRDAAL-QALAAVGLadraneWPAA------------LSGGQKQRVALARALIHRPGLL 155
|
170 180
....*....|....*....|....
gi 1081348497 469 LADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESL 179
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
319-511 |
5.21e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.73 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNL--DNIAIIH 396
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 397 QNPYVFHTSVRHNLTL-YQDYSDS----LLISTLKKVGLWEaccHQLDYELTgdNFSGGQIIKLEIARAILREKQVLLAD 471
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFpWQIRNQQpdpaIFLDDLERFALPD---TILTKNIA--ELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081348497 472 EMMASLDaASSKEISNvlkqlpnsiiEIAHHYKLEDYDAV 511
Cdd:PRK10247 163 EITSALD-ESNKHNVN----------EIIHRYVREQNIAV 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
319-501 |
5.49e-10 |
|
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: 59.66 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIfRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLDNIAIIHQN 398
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVF-HTSVRHNL-------TLYQDYSDSLLISTLKKVGLweacCHQLD-YELTgdnFSGGQIIKLEIARAILREKQVLL 469
Cdd:cd03299 80 YALFpHMTVYKNIayglkkrKVDKKEIERKVLEIAEMLGI----DHLLNrKPET---LSGGEQQRVAIARALVVNPKILL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081348497 470 ADEMMASLDAASS----KEISNVLKQLPNSIIEIAH 501
Cdd:cd03299 153 LDEPFSALDVRTKeklrEELKKIRKEFGVTVLHVTH 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
349-492 |
5.61e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 349 IVGDSGIGKTT----LFRLISGQdkaysGKIIFK-----SIDGRELTPNLDNIAIIHQNPYvfhTSVRHNLTLYQDYSDS 419
Cdd:PRK15134 317 LVGESGSGKSTtglaLLRLINSQ-----GEIWFDgqplhNLNRRQLLPVRHRIQVVFQDPN---SSLNPRLNVLQIIEEG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 420 L---------------LISTLKKVGLWEACCHQLDYEltgdnFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKE 484
Cdd:PRK15134 389 LrvhqptlsaaqreqqVIAVMEEVGLDPETRHRYPAE-----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQ 463
|
....*...
gi 1081348497 485 ISNVLKQL 492
Cdd:PRK15134 464 ILALLKSL 471
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
319-492 |
7.75e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.34 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELT-PNLDNIAI--- 394
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI---VDGLKVNdPKVDERLIrqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 ---IHQNPYVF-HTSVRHNLT--------LYQDYSDSLLISTLKKVGLWEACCHqldY--ELtgdnfSGGQIIKLEIARA 460
Cdd:PRK09493 79 agmVFQQFYLFpHLTALENVMfgplrvrgASKEEAEKQARELLAKVGLAERAHH---YpsEL-----SGGQQQRVAIARA 150
|
170 180 190
....*....|....*....|....*....|..
gi 1081348497 461 ILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDL 182
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
328-512 |
8.29e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.64 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 328 YDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIF--KSID--GRELTPNLDNIAIIHQNP--YV 401
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgKPLDysKRGLLALRQQVATVFQDPeqQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 402 FHTSVrhnltlyqdysDSLLISTLKKVGLWEA-CCHQLDYELT---GDNF--------SGGQIIKLEIARAILREKQVLL 469
Cdd:PRK13638 91 FYTDI-----------DSDIAFSLRNLGVPEAeITRRVDEALTlvdAQHFrhqpiqclSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348497 470 ADEMMASLDAASSKEISNVLKQLP---NSIIEIAHHYKL--EDYDAVY 512
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVaqgNHVIISSHDIDLiyEISDAVY 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
319-501 |
9.42e-10 |
|
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: 59.24 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY-DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTP-NLD-NIAII 395
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvELRrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 396 HQNPYVF-HTSVRHNLTL-----------YQDYSDSLListlKKVGLWEACC-----HQLdyeltgdnfSGGQIIKLEIA 458
Cdd:cd03295 81 IQQIGLFpHMTVEENIALvpkllkwpkekIRERADELL----ALVGLDPAEFadrypHEL---------SGGQQQRVGVA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081348497 459 RAILREKQVLLADEMMASLD----AASSKEISNVLKQLPNSIIEIAH 501
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDpitrDQLQEEFKRLQQELGKTIVFVTH 194
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
317-479 |
1.30e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 59.11 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 317 EEIQLKNVTKSYDN----QEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELT-PNLDN 391
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI---TLDGVPVTgPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 iAIIHQN----PYVfhtSVRHNLTL-----------YQDYSDSLListlKKVGLWEACCHQLdYELtgdnfSGGQIIKLE 456
Cdd:COG4525 79 -GVVFQKdallPWL---NVLDNVAFglrlrgvpkaeRRARAEELL----ALVGLADFARRRI-WQL-----SGGMRQRVG 144
|
170 180
....*....|....*....|...
gi 1081348497 457 IARAILREKQVLLADEMMASLDA 479
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDA 167
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
319-521 |
2.93e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 56.77 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQD--KAYSGKIIFKSIDGRELTPN---LDNIA 393
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEeraRLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNPYVFHtSVRhnltlyqdysdslLISTLKKVGlweacchqldyeltgDNFSGGQIIKLEIAR-AILREKQVLLaDE 472
Cdd:cd03217 81 LAFQYPPEIP-GVK-------------NADFLRYVN---------------EGFSGGEKKRNEILQlLLLEPDLAIL-DE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348497 473 MMASLDAASSKEISNVLKQLPN---SIIEIAHHYKLEDY---DAVYRIENKSIVR 521
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYikpDRVHVLYDGRIVK 185
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
319-501 |
3.18e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.08 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQE--IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELT-PNL----DN 391
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI---KIDGITISkENLkeirKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 IAIIHQNP--YVFHTSVR-------HNLTLYQDYSDSLLISTLKKVGLWEacchQLDYEltGDNFSGGQIIKLEIARAIL 462
Cdd:PRK13632 85 IGIIFQNPdnQFIGATVEddiafglENKKVPPKKMKDIIDDLAKKVGMED----YLDKE--PQNLSGGQKQRVAIASVLA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081348497 463 REKQVLLADEMMASLDAASSKEISNVLKQLPN----SIIEIAH 501
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITH 201
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
320-520 |
3.41e-09 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 57.15 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 320 QLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFksiDGRELTPNLDN------IA 393
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRL---DGEDITKLPPHeraragIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNPYVF-HTSVRHNLtlyqdysdsllistlkKVGLwEAC---CHQLD---YEL----------TGDNFSGGQIIKLE 456
Cdd:TIGR03410 79 YVPQGREIFpRLTVEENL----------------LTGL-AALprrSRKIPdeiYELfpvlkemlgrRGGDLSGGQQQQLA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 457 IARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN----SIIEIAHHYK--LEDYDAVYRIENKSIV 520
Cdd:TIGR03410 142 IARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAeggmAILLVEQYLDfaRELADRYYVMERGRVV 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
335-492 |
3.59e-09 |
|
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: 57.09 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 335 RDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELT-PNLDNIaIIHQN----PYVfhtSVRHN 409
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI---LEGKQITePGPDRM-VVFQNysllPWL---TVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 410 LTLYQDY---------SDSLLISTLKKVGLWEACcHQLDYELtgdnfSGGQIIKLEIARAILREKQVLLADEMMASLDAA 480
Cdd:TIGR01184 75 IALAVDRvlpdlskseRRAIVEEHIALVGLTEAA-DKRPGQL-----SGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170
....*....|..
gi 1081348497 481 SSKEISNVLKQL 492
Cdd:TIGR01184 149 TRGNLQEELMQI 160
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
319-520 |
5.16e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYD-NQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTP-NLDNI---- 392
Cdd:PRK13652 4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL---IRGEPITKeNIREVrkfv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 AIIHQNP--YVFHTSVRH-------NLTLYQDYSDSLLISTLKKVGLWEAcchqldYELTGDNFSGGQIIKLEIARAILR 463
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQdiafgpiNLGLDEETVAHRVSSALHMLGLEEL------RDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348497 464 EKQVLLADEMMASLDAASSKEISNVLKQLPN----SIIEIAHHYKL--EDYDAVYRIENKSIV 520
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLvpEMADYIYVMDKGRIV 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
349-520 |
5.25e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 349 IVGDSGIGKTT----LFRLISGQdkaySGKIIF--KSID---GRELTPNLDNIAIIHQNPY------------VFHTSVR 407
Cdd:PRK10261 355 LVGESGSGKSTtgraLLRLVESQ----GGEIIFngQRIDtlsPGKLQALRRDIQFIFQDPYasldprqtvgdsIMEPLRV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 408 HNLtLYQDYSDSLLISTLKKVGLWEAccHQLDYEltgDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISN 487
Cdd:PRK10261 431 HGL-LPGKAAAARVAWLLERVGLLPE--HAWRYP---HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
170 180 190
....*....|....*....|....*....|...
gi 1081348497 488 VLKQLPNSiIEIAHHYKLEDYDAVYRIENKSIV 520
Cdd:PRK10261 505 LLLDLQRD-FGIAYLFISHDMAVVERISHRVAV 536
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
313-492 |
5.51e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.11 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 313 IHTLEEIqlKNVTKSYDNQ---------EIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGR 383
Cdd:PRK15112 1 VETLLEV--RNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL---IDDH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 384 ELT-----PNLDNIAIIHQNP-----------YVFHTSVRHNLTLYQDYSDSLLISTLKKVGLWEAccHQLDYEltgDNF 447
Cdd:PRK15112 76 PLHfgdysYRSQRIRMIFQDPstslnprqrisQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPD--HASYYP---HML 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348497 448 SGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
319-501 |
6.04e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.07 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSL--SQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKS--IDGRELTPNLDNIAI 394
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIpkGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNP----------YVFHTSVRHNLTLYQDYSdSLLISTLKKVGLWEacchQLDYEltGDNFSGGQIIKLEIARAILRE 464
Cdd:PRK13648 88 VFQNPdnqfvgsivkYDVAFGLENHAVPYDEMH-RRVSEALKQVDMLE----RADYE--PNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081348497 465 KQVLLADEMMASLDAASSKEISNVLKQLPN----SIIEIAH 501
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITH 201
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
335-501 |
6.90e-09 |
|
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: 57.37 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 335 RDVTVTFSLSQHNL-----------------IVGDSGIGKTTLFRLISGQDKAY---SGKIIFksiDGRELTpNLD---- 390
Cdd:COG0444 5 RNLKVYFPTRRGVVkavdgvsfdvrrgetlgLVGESGSGKSTLARAILGLLPPPgitSGEILF---DGEDLL-KLSekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 ------NIAIIHQNPYvfhTS----------VRHNLTLYQDYSDS----LLISTLKKVGLWEACC------HQldyeltg 444
Cdd:COG0444 81 rkirgrEIQMIFQDPM---TSlnpvmtvgdqIAEPLRIHGGLSKAeareRAIELLERVGLPDPERrldrypHE------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348497 445 dnFSGGQ---IIkleIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN----SIIEIAH 501
Cdd:COG0444 151 --LSGGMrqrVM---IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelglAILFITH 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
339-492 |
7.89e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.16 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 339 VTFSLSQ-HNL-IVGDSGIGKTTL----FRLIsgqdkAYSGKIIFK-----SIDGRELTPNLDNIAIIHQNPYvfhTSV- 406
Cdd:COG4172 305 VSLTLRRgETLgLVGESGSGKSTLglalLRLI-----PSEGEIRFDgqdldGLSRRALRPLRRRMQVVFQDPF---GSLs 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 407 -RHN--------LTLYQDYSDS-----LLISTLKKVGLWEACCHQLDYEltgdnFSGGQIIKLEIARAILREKQVLLADE 472
Cdd:COG4172 377 pRMTvgqiiaegLRVHGPGLSAaerraRVAEALEEVGLDPAARHRYPHE-----FSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180
....*....|....*....|
gi 1081348497 473 MMASLDAASSKEISNVLKQL 492
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDL 471
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
15-292 |
9.80e-09 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 56.79 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 15 IILYIIFALLYSCQGIVIPVIIQMAghIDSS----DSRDLIVFTFSSISLWVVVYAFMYIENILLR----SIIRAFNVSL 86
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLL--IDDVipagDLSLLLWIALLLLLLALLRALLSYLRRYLAArlgqRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 87 SENILKNHAVFPKNISDSELCSLLTQDLGIVdQEFLQSFLISPVWGA-SVLVSVIYLLKQNLIVGSLFTVGAFLMILPQF 165
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAV-QNLVSSGLLQLLSDVlTLIGALVILFYLNWKLTLVALLLLPLYVLILR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 166 IFKRKLKESGELLSSSKEKNLRAITDFGKGIETIICNQAEKENVKQTLITLSEMETTQFKYYTLQNLVMFWTGPLKAVGL 245
Cdd:cd07346 158 YFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1081348497 246 IGPFVIG--LVMKQN-SITTLIAMMSASTYLINPLQQILEAIASIQSSQV 292
Cdd:cd07346 238 ALVLLYGgyLVLQGSlTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALA 287
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
319-522 |
1.15e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLD---NIAII 395
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 396 HQNPYVFHT-SVRHNLTLYQ------------DYSDSLLIST--LKKVGLweacchQLDYELTGDNFSGGQIIKLEIARA 460
Cdd:PRK09700 86 YQELSVIDElTVLENLYIGRhltkkvcgvniiDWREMRVRAAmmLLRVGL------KVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 461 ILREKQVLLADEMMASLDAASSKEISNVLKQLPN---SIIEIAHHYK-----------LEDYDAVYR-----IENKSIVR 521
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAeirricdrytvMKDGSSVCSgmvsdVSNDDIVR 239
|
.
gi 1081348497 522 I 522
Cdd:PRK09700 240 L 240
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
318-501 |
1.16e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSY---DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLI------------------------------ 364
Cdd:PTZ00265 1165 KIEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 365 ---------------------SGQDKAY---SGKIIFKSIDGRELT-PNLDNI-AIIHQNPYVFHTSVRHNLTLYQDYSD 418
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggSGEDSTVfknSGKILLDGVDICDYNlKDLRNLfSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 419 SLLISTLKKVG----LWEACCHQLDYELT--GDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PTZ00265 1325 REDVKRACKFAaideFIESLPNKYDTNVGpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250
....*....|...
gi 1081348497 493 PN----SIIEIAH 501
Cdd:PTZ00265 1405 KDkadkTIITIAH 1417
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
319-511 |
1.27e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.39 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY-DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIF--KSID-GRELTPNL-DNIA 393
Cdd:PRK13636 6 LKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFdgKPIDySRKGLMKLrESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNP--YVFHTSVRH-------NLTLYQDYSDSLLISTLKKVGLwEACCHQLDYELtgdnfSGGQIIKLEIARAILRE 464
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQdvsfgavNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCL-----SFGQKKRVAIAGVLVME 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348497 465 KQVLLADEMMASLDAASSKEISNVLKQLPNSI---IEIAHHykleDYDAV 511
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgltIIIATH----DIDIV 205
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
319-492 |
1.41e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 56.73 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEifRDVTVtfsLSQHNL---------IVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTpNL 389
Cdd:PRK11153 2 IELKNISKVFPQGG--RTIHA---LNNVSLhipageifgVIGASGAGKSTLIRCINLLERPTSGRVL---VDGQDLT-AL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 390 D---------NIAIIHQnpyvfhtsvrH-NL----TLYQDYSDSLLISTLKK-------------VGLWEaccHQLDYEl 442
Cdd:PRK11153 73 SekelrkarrQIGMIFQ----------HfNLlssrTVFDNVALPLELAGTPKaeikarvtellelVGLSD---KADRYP- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348497 443 tgDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK11153 139 --AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI 186
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
318-491 |
1.89e-08 |
|
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: 55.63 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSY--DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLF----RLISGQdkaysGKIifkSIDGRE-----LT 386
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNTE-----GDI---QIDGVSwnsvpLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 387 PNLDNIAIIHQNPYVFHTSVRHNLTLYQDYSDSLLISTLKKVGL---WEACCHQLDYELT--GDNFSGGQIIKLEIARAI 461
Cdd:cd03289 74 KWRKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLksvIEQFPGQLDFVLVdgGCVLSHGHKQLMCLARSV 153
|
170 180 190
....*....|....*....|....*....|
gi 1081348497 462 LREKQVLLADEMMASLDAASSKEISNVLKQ 491
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
105-485 |
1.97e-08 |
|
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: 57.26 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 105 ELCSLLTQDLgivdQEFLQ-SFLISPVWGASV-LVSVIYLLKQNLIVGSLFTVGAFLMILP-QFIFKRKLKESGELLSSS 181
Cdd:TIGR00957 416 EIVNLMSVDA----QRFMDlATYINMIWSAPLqVILALYFLWLNLGPSVLAGVAVMVLMVPlNAVMAMKTKTYQVAHMKS 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 182 KEKNLRAITDFGKGIETIICNQAEKENVKQTL-ITLSEMETTQFKYYTLQNLVMFWTGPLKAVGLIGPFVIGLVMKQNSI 260
Cdd:TIGR00957 492 KDNRIKLMNEILNGIKVLKLYAWELAFLDKVEgIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNIL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 261 TTLIAMMSASTYLI--NPLQQILEAIASIQSSQVIKDKLLTFGSESEIPSKGLHIHTLEE-----IQLKNVTKSYDNQEI 333
Cdd:TIGR00957 572 DAEKAFVSLALFNIlrFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPgegnsITVHNATFTWARDLP 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 334 FRDVTVTFSLSQHNLI--VGDSGIGKTTLFRLISGQDKAYSGKIIFKSidgreltpnldNIAIIHQNPYVFHTSVRHNLT 411
Cdd:TIGR00957 652 PTLNGITFSIPEGALVavVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------SVAYVPQQAWIQNDSLRENIL 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 412 LYQDYSDSLLISTLkkvglwEACCHQLDYEL--TGD---------NFSGGQIIKLEIARAILREKQVLLADEMMASLDAA 480
Cdd:TIGR00957 721 FGKALNEKYYQQVL------EACALLPDLEIlpSGDrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
....*
gi 1081348497 481 SSKEI 485
Cdd:TIGR00957 795 VGKHI 799
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
319-514 |
1.99e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY------DNqeifrdvtVTFSLSQ---HNLiVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTPN- 388
Cdd:COG1129 5 LEMRGISKSFggvkalDG--------VSLELRPgevHAL-LGENGAGKSTLMKILSGVYQPDSGEIL---LDGEPVRFRs 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 389 ----LDN-IAIIHQNPYVF-HTSVRHNLTLYQDYSDSLLIST----------LKKVGLweacchQLD-YELTGDnFSGG- 450
Cdd:COG1129 73 prdaQAAgIAIIHQELNLVpNLSVAENIFLGREPRRGGLIDWramrrrarelLARLGL------DIDpDTPVGD-LSVAq 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348497 451 -QIIklEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN---SIIEIAHhyKLEDydaVYRI 514
Cdd:COG1129 146 qQLV--EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISH--RLDE---VFEI 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
319-501 |
2.00e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.87 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTvtFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIIF-KSIDgreltpnldnIAII 395
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLS--FKLPPGGIvgVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVK----------LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 396 HQnpyvFHTSVRHNLTLYQDYSDSLLISTL----------------------KKVGlweacchQLdyeltgdnfSGGQII 453
Cdd:TIGR03719 391 DQ----SRDALDPNKTVWEEISGGLDIIKLgkreipsrayvgrfnfkgsdqqKKVG-------QL---------SGGERN 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348497 454 KLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPNSIIEIAH 501
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISH 498
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-501 |
2.03e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.30 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAY-----SGKIIfksIDGRELTpNLDNIA 393
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVY---LDGQDIF-KMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNPYVFHT-SVRHNLTLYQDYSDSLLIS---------------TLKKVGLWEACCHQLDyeLTGDNFSGGQIIKLEI 457
Cdd:PRK14247 80 LRRRVQMVFQIpNPIPNLSIFENVALGLKLNrlvkskkelqervrwALEKAQLWDEVKDRLD--APAGKLSGGQQQRLCI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081348497 458 ARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAH 501
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
319-492 |
2.09e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.40 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISG---QDKAYSGKI-IFKSIDGRELTPNLDNIAI 394
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIeLLGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNPYVFHtsvRHNLTLYQDYSDSLLISTLKKVGLWEACCHQLDYE--------LTG-----------DNFSGGQIIKL 455
Cdd:PRK09984 85 RANTGYIFQ---QFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREqkqralqaLTRvgmvhfahqrvSTLSGGQQQRV 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081348497 456 EIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDI 198
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-507 |
2.17e-08 |
|
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: 55.09 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQD-KAYSGKI-IFksidGREL----------- 385
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVrLF----GERRggedvwelrkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 386 ----TPNLdniaiihQNPYVFHTSVRH--------NLTLYQDYSD---SLLISTLKKVGLWeacchqldyELTGDNF--- 447
Cdd:COG1119 80 iglvSPAL-------QLRFPRDETVLDvvlsgffdSIGLYREPTDeqrERARELLELLGLA---------HLADRPFgtl 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348497 448 SGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL---PN-SIIEIAHHykLED 507
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaeGApTLVLVTHH--VEE 205
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
319-492 |
3.26e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.71 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELT-PNLDNIAIIHQ 397
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI---TLDGKPVEgPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 398 NPYVFHTSVRHNLTL-------YQDYSDSLLISTLKKVGLWEACCHQLdYELtgdnfSGGQIIKLEIARAILREKQVLLA 470
Cdd:PRK11248 79 EGLLPWRNVQDNVAFglqlagvEKMQRLEIAHQMLKKVGLEGAEKRYI-WQL-----SGGQRQRVGIARALAANPQLLLL 152
|
170 180
....*....|....*....|..
gi 1081348497 471 DEMMASLDAASSKEISNVLKQL 492
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKL 174
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
336-478 |
3.71e-08 |
|
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: 53.87 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 336 DVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGREL------TPNLDNIAIIHQNPYVFHTSVRHN 409
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPsfeatrSRNRYSVAYAAQKPWLLNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 410 LTLYQDYSDSllistlKKVGLWEACCHQLDYEL-----------TGDNFSGGQIIKLEIARAILREKQVLLADEMMASLD 478
Cdd:cd03290 99 ITFGSPFNKQ------RYKAVTDACSLQPDIDLlpfgdqteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
319-502 |
6.46e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.06 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDV---TVTFSLSQHNLI--VGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNLDN-- 391
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKgldNISFELEEGSFValVGHTGSGKSTLMQHFNALLKPSSGTI---TIAGYHITPETGNkn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 -------IAIIHQNPYV--FHTSVRH-------NLTLYQDYSDSLLISTLKKVGLWEACCHQLDYELtgdnfSGGQIIKL 455
Cdd:PRK13641 80 lkklrkkVSLVFQFPEAqlFENTVLKdvefgpkNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFEL-----SGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348497 456 EIARAILREKQVLLADEMMASLDAASSKEISNVLKQLP---NSIIEIAHH 502
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQkagHTVILVTHN 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
318-491 |
6.48e-08 |
|
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: 55.69 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSY--DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLF----RLISGQdkaysGKIifkSIDGRE-----LT 386
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTE-----GEI---QIDGVSwnsvtLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 387 PNLDNIAIIHQNPYVFHTSVRHNLTLYQDYSDSLLISTLKKVGL---WEACCHQLDYELT--GDNFSGGQIIKLEIARAI 461
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLksvIEQFPDKLDFVLVdgGYVLSNGHKQLMCLARSI 1368
|
170 180 190
....*....|....*....|....*....|
gi 1081348497 462 LREKQVLLADEMMASLDAASSKEISNVLKQ 491
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
73-485 |
6.88e-08 |
|
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: 55.69 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 73 ILLRSIIRAFNVSLSENILKNhavfpknISDSELCSLLTQDLGIVDQEF-LQSFlispVWGASVLVSVIYLLKQNLIVGS 151
Cdd:TIGR01271 155 IALFSLIYKKTLKLSSRVLDK-------ISTGQLVSLLSNNLNKFDEGLaLAHF----VWIAPLQVILLMGLIWELLEVN 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 152 LFTVGAFLMILPQF-------IFKRKLKESGEL-----LSSSKEKNLRAITDFG--KGIETIIcnqaekENVKQTLITLS 217
Cdd:TIGR01271 224 GFCGLGFLILLALFqaclgqkMMPYRDKRAGKIserlaITSEIIENIQSVKAYCweEAMEKII------KNIRQDELKLT 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 218 EmETTQFKYYTlqNLVMFWTGPLKAVGLIGPFVIGLVMKQNSITTLIAM-----MSASTYLINPLQQILEAIASIQSSQV 292
Cdd:TIGR01271 298 R-KIAYLRYFY--SSAFFFSGFFVVFLSVVPYALIKGIILRRIFTTISYcivlrMTVTRQFPGAIQTWYDSLGAITKIQD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 293 IKDKlltfgSESEIPSKGLhihTLEEIQLKNVTKSYDN--QEIFRDV------------------------------TVT 340
Cdd:TIGR01271 375 FLCK-----EEYKTLEYNL---TTTEVEMVNVTASWDEgiGELFEKIkqnnkarkqpngddglffsnfslyvtpvlkNIS 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 341 FSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGReltpnldnIAIIHQNPYVFHTSVRHNLTLYQDYSD 418
Cdd:TIGR01271 447 FKLEKGQLlaVAGSTGSGKSSLLMMIMGELEPSEGKI---KHSGR--------ISFSPQTSWIMPGTIKDNIIFGLSYDE 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 419 SLLISTLKkvglweACchQLDYELT-------------GDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEI 485
Cdd:TIGR01271 516 YRYTSVIK------AC--QLEEDIAlfpekdktvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
319-521 |
7.01e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQdKAY---SGKIIFKSIDGRELTPNLDN---I 392
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAYkilEGDILFKGESILDLEPEERAhlgI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 AIIHQNPY-------------VFHTSVRHN-------LTLYQdysdsLLISTLKKVGLWEACCHQLdyelTGDNFSGGQI 452
Cdd:CHL00131 87 FLAFQYPIeipgvsnadflrlAYNSKRKFQglpeldpLEFLE-----IINEKLKLVGMDPSFLSRN----VNEGFSGGEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348497 453 IKLEIARAILREKQVLLADEMMASLDAASSKEIS---NVLKQLPNSIIEIAHHYKLEDY---DAVYRIENKSIVR 521
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAegiNKLMTSENSIILITHYQRLLDYikpDYVHVMQNGKIIK 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-496 |
1.06e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.72 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 349 IVGDSGIGKTTLFRLISGQDKAYSGKII------FKSIDGRELTPNLDNIAIIHQNPYVF-HTSVRHNLtLY------QD 415
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVlngrvlFDAEKGICLPPEKRRIGYVFQDARLFpHYKVRGNL-RYgmaksmVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 416 YSDSLlistlkkVGLWeACCHQLD-YELTgdnFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN 494
Cdd:PRK11144 108 QFDKI-------VALL-GIEPLLDrYPGS---LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176
|
..
gi 1081348497 495 SI 496
Cdd:PRK11144 177 EI 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
319-501 |
1.42e-07 |
|
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: 54.04 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQE--IFRDV-TVTFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIIFKS----IDGRELTPNL 389
Cdd:TIGR03269 280 IKVRNVSKRYISVDrgVVKAVdNVSLEVKEGEIfgIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 390 DN-----IAIIHQNPYVF-HTSVRHNLT--LYQDYSDSL----LISTLKKVGLWEACCHQLDYELTgDNFSGGQIIKLEI 457
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYpHRTVLDNLTeaIGLELPDELarmkAVITLKMVGFDEEKAEEILDKYP-DELSEGERHRVAL 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348497 458 ARAILREKQVLLADEMMASLD----AASSKEISNVLKQLPNSIIEIAH 501
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSH 486
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
319-520 |
1.58e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 52.74 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFR-----DVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLDNI- 392
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 ---AIIHQNP--YVFHTSVRH-------NLTLYQDYSDSLLISTLKKVGlweacchqLDYELTGD----NFSGGQIIKLE 456
Cdd:PRK13637 83 kkvGLVFQYPeyQLFEETIEKdiafgpiNLGLSEEEIENRVKRAMNIVG--------LDYEDYKDkspfELSGGQKRRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348497 457 IARAILREKQVLLADEMMASLDAASSKEISNVLKQL----PNSIIEIAHhyKLEDydaVYRIENKSIV 520
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSH--SMED---VAKLADRIIV 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
333-502 |
2.53e-07 |
|
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: 51.50 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 333 IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQD---KAYSGKIIFksiDGRELTPNL--DNIAIIHQNPY-VFHTSV 406
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILF---NGQPRKPDQfqKCVAYVRQDDIlLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 407 RHNLTLY-----QDYSDSLLISTLKKVGLWEACCHQL--DYELTGdnFSGGQIIKLEIARAILREKQVLLADEMMASLDA 479
Cdd:cd03234 99 RETLTYTailrlPRKSSDAIRKKRVEDVLLRDLALTRigGNLVKG--ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180
....*....|....*....|....*
gi 1081348497 480 ASSKEISNVLKQLP--NSIIEIAHH 502
Cdd:cd03234 177 FTALNLVSTLSQLArrNRIVILTIH 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
319-492 |
2.88e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 51.67 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSID---GRELTPNLDNIAII 395
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 396 HQN-PYVF-------HTSVRHNLT--------LYQDYSDSLLISTLKKVGlweacchqldyeLTGDN------FSGGQII 453
Cdd:PRK11264 84 RQHvGFVFqnfnlfpHRTVLENIIegpvivkgEPKEEATARARELLAKVG------------LAGKEtsyprrLSGGQQQ 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081348497 454 KLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQL 190
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-502 |
2.94e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 323 NVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISG-QDKA----YSGKIIF--KSI-DGRELTPNLDNIAI 394
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVsgyrYSGDVLLggRSIfNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNPYVFHTSVR---------HNLTLYQDYSdSLLISTLKKVGLWEACCHQLDYelTGDNFSGGQIIKLEIARAILREK 465
Cdd:PRK14271 106 LFQRPNPFPMSIMdnvlagvraHKLVPRKEFR-GVAQARLTEVGLWDAVKDRLSD--SPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081348497 466 QVLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAHH 502
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
319-399 |
3.34e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.04 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYD-NQEIFRDVTVTFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTPN-----LD 390
Cdd:PRK13650 5 IEVKNLTFKYKeDQEKYTLNDVSFHVKQGEWlsIIGHNGSGKSTTVRLIDGLLEAESGQII---IDGDLLTEEnvwdiRH 81
|
....*....
gi 1081348497 391 NIAIIHQNP 399
Cdd:PRK13650 82 KIGMVFQNP 90
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
319-375 |
3.48e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 3.48e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTvtFSLSQhNLIVG---DSGIGKTTLFRLISGQDKAYSGKI 375
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLS--FSLPP-GGIVGiigPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
326-492 |
4.63e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.12 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 326 KSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKII---------------FKSIDGRELTPNLD 390
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVvngqtinlvrdkdgqLKVADKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 NIAIIHQNPYVF-HTSVRHN--------LTLYQDYSDSLLISTLKKVGLWEACchQLDYELtgdNFSGGQIIKLEIARAI 461
Cdd:PRK10619 93 RLTMVFQHFNLWsHMTVLENvmeapiqvLGLSKQEARERAVKYLAKVGIDERA--QGKYPV---HLSGGQQQRVSIARAL 167
|
170 180 190
....*....|....*....|....*....|.
gi 1081348497 462 LREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQL 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
331-479 |
5.42e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 331 QEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSidgreltpnldNIAIIHQNPYVFHTSVRHNL 410
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-----------SIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348497 411 tLYQDYSDSLLISTLKKVGLWEACCHQLDYEL------TGDNFSGGQIIKLEIARAILREKQVLLADEMMASLDA 479
Cdd:PTZ00243 742 -LFFDEEDAARLADAVRVSQLEADLAQLGGGLeteigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
330-491 |
5.63e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.02 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 330 NQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELtpNLDN----IAIIHQNPYVFHTS 405
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL--QLDSwrsrLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 406 VRHNLTLYQDYSDSLLISTLKKVglweACCHQ--------LDYEL--TGDNFSGGQIIKLEIARAILREKQVLLADEMMA 475
Cdd:PRK10789 405 VANNIALGRPDATQQEIEHVARL----ASVHDdilrlpqgYDTEVgeRGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170
....*....|....*.
gi 1081348497 476 SLDAASSKEISNVLKQ 491
Cdd:PRK10789 481 AVDGRTEHQILHNLRQ 496
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
319-511 |
6.17e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISG--QDKAYSGKIIFksiDGRELTPN------LD 390
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIF---EGEELQASnirdteRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 NIAIIHQN-PYVFHTSVRHNLTL--------YQDYSDSLLIST--LKKVGLweacchQLDYELTGDNFSGGQIIKLEIAR 459
Cdd:PRK13549 83 GIAIIHQElALVKELSVLENIFLgneitpggIMDYDAMYLRAQklLAQLKL------DINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348497 460 AILREKQVLLADEMMASLDAASSKEISNVLKQLPN---SIIEIAHhyKLEDYDAV 511
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISH--KLNEVKAI 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
319-492 |
6.75e-07 |
|
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: 51.73 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQD--KAYSGKIIFK-------------SIDGR 383
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 384 -------ELTP------NLDN---------IAIIHQNPYVFH---TSVRHNLTLYQDYSDSLLISTLKKVGLWEACchQL 438
Cdd:TIGR03269 81 pcpvcggTLEPeevdfwNLSDklrrrirkrIAIMLQRTFALYgddTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV--QL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348497 439 DYELT--GDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:TIGR03269 159 SHRIThiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEA 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
319-514 |
8.12e-07 |
|
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: 50.72 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY---------------DNQEIFRDVTVTFSLSQHNL---------IVGDSGIGKTTLFRLISGQDKAYSGK 374
Cdd:cd03294 1 IKIKGLYKIFgknpqkafkllakgkSKEEILKKTGQTVGVNDVSLdvregeifvIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 375 IIfksIDGRELTpNLDN----------IAIIHQNPYVF-HTSVRHNLTLyqdysdSLLIS-------------TLKKVGL 430
Cdd:cd03294 81 VL---IDGQDIA-AMSRkelrelrrkkISMVFQSFALLpHRTVLENVAF------GLEVQgvpraereeraaeALELVGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 431 --WEaccHQLDYELtgdnfSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL----PNSIIEIAHhyk 504
Cdd:cd03294 151 egWE---HKYPDEL-----SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqaelQKTIVFITH--- 219
|
250
....*....|
gi 1081348497 505 leDYDAVYRI 514
Cdd:cd03294 220 --DLDEALRL 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
322-495 |
8.14e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 50.28 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 322 KNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGREL---TPNLDNIAIIHQN 398
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVFHT-----------SVRHNLTLYQ--DYSDSLL----ISTLKkvglweacchqldyELTGDNFSGGQIIKLEIARAI 461
Cdd:PRK10895 87 ASIFRRlsvydnlmavlQIRDDLSAEQreDRANELMeefhIEHLR--------------DSMGQSLSGGERRRVEIARAL 152
|
170 180 190
....*....|....*....|....*....|....
gi 1081348497 462 LREKQVLLADEMMASLDAASSKEISNVLKQLPNS 495
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS 186
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
319-520 |
8.95e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.37 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY-DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELT--PNLDNI-AI 394
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSklQGIRKLvGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNP---YVFHTSVR------HNLTLYQDYSDSLLISTLKKVGLwEACCHQldyelTGDNFSGGQIIKLEIARAILREK 465
Cdd:PRK13644 82 VFQNPetqFVGRTVEEdlafgpENLCLPPIEIRKRVDRALAEIGL-EKYRHR-----SPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348497 466 QVLLADEMMASLDAASSKEISNVLKQL---PNSIIEIAHHY-KLEDYDAVYRIENKSIV 520
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLhekGKTIVYITHNLeELHDADRIIVMDRGKIV 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
319-492 |
9.25e-07 |
|
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: 49.59 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFksiDGRELTpnldnIAIIHQN 398
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF---DGKPLD-----IAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYvfhtsVRHNLTLYQDYS--DSLL-ISTLKKVGLWEAcCHQLDY-----ELTG------DNFSGGQIIKLEIARAILRE 464
Cdd:cd03269 73 GY-----LPEERGLYPKMKviDQLVyLAQLKGLKKEEA-RRRIDEwlerlELSEyankrvEELSKGNQQKVQFIAAVIHD 146
|
170 180
....*....|....*....|....*...
gi 1081348497 465 KQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIREL 174
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
319-492 |
9.36e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGR---ELTPNLDN---I 392
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL---EIGGNpcaRLTPAKAHqlgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 AIIHQNPYVF-HTSVRHN----LTLYQDysdsllisTLKKVG--LWEACCH-QLDYELTGDNFSGGQIIklEIARAILRE 464
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENilfgLPKRQA--------SMQKMKqlLAALGCQlDLDSSAGSLEVADRQIV--EILRGLMRD 158
|
170 180
....*....|....*....|....*...
gi 1081348497 465 KQVLLADEMMASLDAAsskEISNVLKQL 492
Cdd:PRK15439 159 SRILILDEPTASLTPA---ETERLFSRI 183
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
319-492 |
1.16e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.77 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDK-----AYSGKIIFKsidGREL-TPNLDN- 391
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYN---GHNIySPRTDTv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 -----IAIIHQNPYVFHTSVRHN------LTLYQDYS--DSLLISTLKKVGLWEACCHQLDYELTGdnFSGGQIIKLEIA 458
Cdd:PRK14239 83 dlrkeIGMVFQQPNPFPMSIYENvvyglrLKGIKDKQvlDEAVEKSLKGASIWDEVKDRLHDSALG--LSGGQQQRVCIA 160
|
170 180 190
....*....|....*....|....*....|....
gi 1081348497 459 RAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGL 194
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
319-511 |
1.31e-06 |
|
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: 50.98 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISG--QDKAYSGKIIFksiDGRELTPN------LD 390
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYW---SGSPLKASnirdteRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 391 NIAIIHQN-PYVFHTSVRHNLTLYQDYSdslLISTLKKVGLWEACCHQLDYELTGD---------NFSGGQIIKLEIARA 460
Cdd:TIGR02633 79 GIVIIHQElTLVPELSVAENIFLGNEIT---LPGGRMAYNAMYLRAKNLLRELQLDadnvtrpvgDYGGGQQQLVEIAKA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081348497 461 ILREKQVLLADEMMASLDAASSKEISNVLKQLPN---SIIEIAHhyKLEDYDAV 511
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISH--KLNEVKAV 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
334-490 |
1.42e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 334 FRDVTVTF----SLSQ----------HNLIvGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGREL-----TPNLD-NIA 393
Cdd:PRK11288 7 FDGIGKTFpgvkALDDisfdcragqvHALM-GENGAGKSTLLKILSGNYQPDAGSI---LIDGQEMrfastTAALAaGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQN-PYVFHTSVRHNLTLYQ--------DYSdsLLIST----LKKVGLweacchQLDYELTGDNFSGGQIIKLEIARA 460
Cdd:PRK11288 83 IIYQElHLVPEMTVAENLYLGQlphkggivNRR--LLNYEareqLEHLGV------DIDPDTPLKYLSIGQRQMVEIAKA 154
|
170 180 190
....*....|....*....|....*....|
gi 1081348497 461 ILREKQVLLADEMMASLdaaSSKEISNVLK 490
Cdd:PRK11288 155 LARNARVIAFDEPTSSL---SAREIEQLFR 181
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
318-492 |
2.41e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 49.25 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSYDNQEIFR-----DVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNLDN- 391
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV---TIGERVITAGKKNk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 --------IAIIHQNP--YVFHTSVRH-------NLTLYQDYSDSLLISTLKKVGLWEACCHQLDYELtgdnfSGGQIIK 454
Cdd:PRK13634 79 klkplrkkVGIVFQFPehQLFEETVEKdicfgpmNFGVSEEDAKQKAREMIELVGLPEELLARSPFEL-----SGGQMRR 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081348497 455 LEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKL 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
319-520 |
2.64e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.72 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFksiDGRELTP------NLDNI 392
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF---DGKDITDwqtakiMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 AIIHQNPYVF-HTSVRHNLTLYQDYSDSLLIST-LKKVGLWEACCHQLDYELTGdNFSGGQIIKLEIARAILREKQVLLA 470
Cdd:PRK11614 83 AIVPEGRRVFsRMTVEENLAMGGFFAERDQFQErIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348497 471 DEMMASLDAASSKEISNVLKQLPNS-----IIEIAHHYKLEDYDAVYRIENKSIV 520
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQgmtifLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
308-375 |
2.85e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 2.85e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348497 308 SKGLHIHTLEeiqLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKI 375
Cdd:PRK15064 312 DKKLHRNALE---VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-383 |
2.98e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.77 E-value: 2.98e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348497 320 QLKNVTKSYDNQEIFRDVTvtFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGR 383
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVS--FDLYPGEVlgIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ 71
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
321-507 |
3.08e-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: 50.40 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 321 LKNVTKSYD--NQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTPNLD----NIAI 394
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL---VGGKDIETNLDavrqSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 395 IHQNPYVF-HTSVRHNLTLY-------QDYSDSLLISTLKKVGLWeaccHQLDYEltGDNFSGGQIIKLEIARAILREKQ 466
Cdd:TIGR01257 1008 CPQHNILFhHLTVAEHILFYaqlkgrsWEEAQLEMEAMLEDTGLH----HKRNEE--AQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081348497 467 VLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAHHYKLED 507
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSgrTIIMSTHHMDEAD 1124
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
15-277 |
4.70e-06 |
|
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: 48.41 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 15 IILYIIFALLYSCQGIVIPVIIQ--MAGHIDSSDSRD----------LIVFTFSSISLWVVVYAFMYIeNILLRSIIRAf 82
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGriLDVLLPDGDPETqalnvyslalLLLGLAQFILSFLQSYLLNHT-GERLSRRLRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 83 nvSLSENILKNHAVFPKNISDSELCSLLTQDLGIVDQEFLQSF--LISPVWGASVLVSVIYLLKQNLIVGSLFTVgaFLM 160
Cdd:pfam00664 79 --KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLglLFQSLATIVGGIIVMFYYGWKLTLVLLAVL--PLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 161 ILPQFIFKRKLKESGELLSSSKEKNLRAITDFGKGIETIICNQAEKENVKQTLITLSEMETTQFKYYTLQNLVMFWTGPL 240
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1081348497 241 KAVGLIGPFVIG--LVMK-QNSITTLIAMMSASTYLINPL 277
Cdd:pfam00664 235 GYLSYALALWFGayLVISgELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
332-492 |
7.06e-06 |
|
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: 46.78 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 332 EIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQ--DKAYSGKIIfksIDGRELTPNL--DNIAIIHQNPYVFHT-SV 406
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVL---INGRPLDKRSfrKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 407 RHNLtlyqDYSdsllistlkkvglweACCHQLdyeltgdnfSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEIS 486
Cdd:cd03213 100 RETL----MFA---------------AKLRGL---------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
....*.
gi 1081348497 487 NVLKQL 492
Cdd:cd03213 152 SLLRRL 157
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
348-492 |
8.13e-06 |
|
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: 46.87 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 348 LIVGDSGIGKTTLFRLISGQDKAY---SGKIIFKSIDGREltpnldnIAIIHQNPYVF---HTSVRHNLTLYQdysdsll 421
Cdd:cd03233 37 LVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKE-------FAEKYPGEIIYvseEDVHFPTLTVRE------- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348497 422 isTLKKVGlweacchqldyELTGDNF----SGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:cd03233 103 --TLDFAL-----------RCKGNEFvrgiSGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTM 164
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
319-492 |
8.36e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY-DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFK----SIDGRELTPNLDNIA 393
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepiKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 IIHQNP--YVFHTSVRH-------NLTLYQDYSDSLLISTLKKVGLweacchqLDYELTG-DNFSGGQIIKLEIARAILR 463
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEdvafgplNLGLSKEEVEKRVKEALKAVGM-------EGFENKPpHHLSGGQKKRVAIAGILAM 154
|
170 180
....*....|....*....|....*....
gi 1081348497 464 EKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDL 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
320-501 |
9.28e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 320 QLKNVTKSYD-NQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIfksidgreLTPNLdNIAIIHQN 398
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------PQPGI-KVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVFHT-SVRHNL---------------TLYQDYS------DSL------LISTLKKVGLWEacchqLDYELT------- 443
Cdd:TIGR03719 77 PQLDPTkTVRENVeegvaeikdaldrfnEISAKYAepdadfDKLaaeqaeLQEIIDAADAWD-----LDSQLEiamdalr 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348497 444 ---GD----NFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPNSIIEIAH 501
Cdd:TIGR03719 152 cppWDadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTH 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
319-502 |
1.11e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 47.04 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY-DNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNLD-----NI 392
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV---KVMGREVNAENEkwvrsKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 393 AIIHQNP--YVFHTSVRH-------NLTLYQDYSDSLLISTLKKVGLWEAcCHQLDYELtgdnfSGGQIIKLEIARAILR 463
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDdvafgpvNMGLDKDEVERRVEEALKAVRMWDF-RDKPPYHL-----SYGQKKRVAIAGVLAM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081348497 464 EKQVLLADEMMASLDAASSKEISNVLKQLPN--SIIEIAHH 502
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgKTVIVATH 196
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
349-501 |
1.14e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 349 IVGDSGIGKTTLF----RLIsgqdKAYSGKIIfksIDGRE-----LTPNLDNIAIIHQNPYVFHTSVRHNLTLYQDYSDS 419
Cdd:PTZ00243 1341 IVGRTGSGKSTLLltfmRMV----EVCGGEIR---VNGREigaygLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSA 1413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 420 LLISTLKKVGLWEACCHQ---LDYELT--GDNFSGGQIIKLEIARAIL-REKQVLLADEMMASLDAASSKEISN-VLKQL 492
Cdd:PTZ00243 1414 EVWAALELVGLRERVASEsegIDSRVLegGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQAtVMSAF 1493
|
170
....*....|
gi 1081348497 493 PN-SIIEIAH 501
Cdd:PTZ00243 1494 SAyTVITIAH 1503
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
319-511 |
1.61e-05 |
|
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: 46.27 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY-----DNQEI--FRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGReltpnLDn 391
Cdd:COG4778 5 LEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGW-----VD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 IAiihqnpyvfHTSVRHNLTLYQD---YSDSLL-----ISTLKKV-----------------------------GLWEAc 434
Cdd:COG4778 79 LA---------QASPREILALRRRtigYVSQFLrviprVSALDVVaepllergvdreearararellarlnlpeRLWDL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 435 chqldYELTgdnFSGGQIIKLEIARAILREKQVLLADEMMASLDAASS---KEISNVLKQLPNSIIEIAHHykLEDYDAV 511
Cdd:COG4778 149 -----PPAT---FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvVELIEEAKARGTAIIGIFHD--EEVREAV 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
268-503 |
1.71e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.27 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 268 SASTY------LINPLQQILEAIASIQSSQVIKDKLLTFG-----SESEIPSKGLHIHTLEeiqLKNVTKSYDNQEiFRD 336
Cdd:PRK10522 264 VAATYsltllfLRTPLLSAVGALPTLLSAQVAFNKLNKLAlapykAEFPRPQAFPDWQTLE---LRNVTFAYQDNG-FSV 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 337 VTVTFSLSQHNLI--VGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTP-NLDN----IAIIHQNPYVFHtsvrHN 409
Cdd:PRK10522 340 GPINLTIKRGELLflIGGNGSGKSTLAMLLTGLYQPQSGEIL---LDGKPVTAeQPEDyrklFSAVFTDFHLFD----QL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 410 LTLYQDYSDSLLIST-LKKVGLWEACCHQlDYELTGDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNV 488
Cdd:PRK10522 413 LGPEGKPANPALVEKwLERLKMAHKLELE-DGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV 491
|
250 260
....*....|....*....|.
gi 1081348497 489 L----KQLPNSIIEIAH--HY 503
Cdd:PRK10522 492 LlpllQEMGKTIFAISHddHY 512
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
333-494 |
1.76e-05 |
|
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: 46.77 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 333 IFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGReltpnldnIAIIHQNPYVFHTSVRHNLTL 412
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHSGR--------ISFSSQFSWIMPGTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 413 YQDYSDSLLISTLKKVGLWE--ACCHQLDYELTGD---NFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEI-- 485
Cdd:cd03291 121 GVSYDEYRYKSVVKACQLEEdiTKFPEKDNTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfe 200
|
....*....
gi 1081348497 486 SNVLKQLPN 494
Cdd:cd03291 201 SCVCKLMAN 209
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
303-478 |
3.55e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 303 ESEIPSkglHIHTLEE----IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISG-QDKAYSGKII- 376
Cdd:PRK10938 244 EPDEPS---ARHALPAneprIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTl 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 377 FKSIDGRELTpnldnIAIIHQN-PYV---FH------TSVRH--------NLTLYQDYSDSLlistLKKVGLWEACCHqL 438
Cdd:PRK10938 321 FGRRRGSGET-----IWDIKKHiGYVsssLHldyrvsTSVRNvilsgffdSIGIYQAVSDRQ----QKLAQQWLDILG-I 390
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081348497 439 DYELTGDNF---SGGQIIKLEIARAILREKQVLLADEMMASLD 478
Cdd:PRK10938 391 DKRTADAPFhslSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-386 |
4.53e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 45.15 E-value: 4.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELT 386
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV---RLNGRPLA 67
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
319-501 |
5.74e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.08 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVT-VTFSLSQHNL--IVGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTP-NLDN--- 391
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgVSFSITKGEWvsIIGQNGSGKSTTARLIDGLFEEFEGKV---KIDGELLTAeNVWNlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 392 -IAIIHQNP--YVFHTSVRHNLTLYQDYSDSLLISTLKKVGLWEACCHQLDYELTGD-NFSGGQIIKLEIARAILREKQV 467
Cdd:PRK13642 82 kIGMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPaRLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081348497 468 LLADEMMASLDAASSKEISNVLKQLPN----SIIEIAH 501
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEkyqlTVLSITH 199
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
316-516 |
1.03e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 316 LEEIQLKNVTKSYDNQEIFRDVTVTfslsqhnLIVGDSGIGKTTLF----------------------RLISGQDKAYSG 373
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLT-------LIVGQNGAGKTTIIealkyaltgelppnskggahdpKLIREGEVRAQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 374 KIIFKSIDGRELTpnldniaiIHQNPYVFhtsvRHNLTLYQDYSDSLLISTLKKVglweacchqldyeltgdnfSGGQ-- 451
Cdd:cd03240 74 KLAFENANGKKYT--------ITRSLAIL----ENVIFCHQGESNWPLLDMRGRC-------------------SGGEkv 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348497 452 ----IIKLEIARAILREKQVLLADEMMASLDAASSKE-----ISNVLKQLPNSIIEIAHHYKLEDY-DAVYRIEN 516
Cdd:cd03240 123 laslIIRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDAaDHIYRVEK 197
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
319-501 |
1.17e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.00 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDN-----QEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKI------IFKSIDGRELTP 387
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvdditITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 388 NLDNIAIIHQNP--YVFHTSVRH-----------NLTLYQDYSDSLLIstlkKVGLWEACCHQLDYELtgdnfSGGQIIK 454
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVEReiifgpknfkmNLDEVKNYAHRLLM----DLGFSRDVMSQSPFQM-----SGGQMRK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081348497 455 LEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLP----NSIIEIAH 501
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSH 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
319-492 |
1.57e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHN----LIVGDSGIGKT----TLFRLISGQDKAY-SGKIIF--KSI---DGRE 384
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAgetlALVGESGSGKSvtalSILRLLPSPPVVYpSGDIRFhgESLlhaSEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 385 LTP-NLDNIAIIHQNPYV----FHT---SVRHNLTLY----QDYSDSLLISTLKKVGLWEACCHQLDYEltgDNFSGGQI 452
Cdd:PRK15134 86 LRGvRGNKIAMIFQEPMVslnpLHTlekQLYEVLSLHrgmrREAARGEILNCLDRVGIRQAAKRLTDYP---HQLSGGER 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081348497 453 IKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQL 492
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
319-496 |
1.87e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.18 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIifksidgrELTPNLdNIAIIHQN 398
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKL-RIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVFHT---SVRHNLTLYQDYSDSLLISTLKKVglweACCHQLDYELtgDNFSGGQIIKLEIARAILREKQVLLADEMMA 475
Cdd:PRK09544 76 LYLDTTlplTVNRFLRLRPGTKKEDILPALKRV----QAGHLIDAPM--QKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180
....*....|....*....|.
gi 1081348497 476 SLDAASSKEISNVLKQLPNSI 496
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRREL 170
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
319-506 |
2.07e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.86 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDnqeifrDVT----VTFSLSQ---HNLiVGDSGIGKTTLFRLISGQDKAYSGKIIfksIDGRELTPN--- 388
Cdd:COG3845 6 LELRGITKRFG------GVVanddVSLTVRPgeiHAL-LGENGAGKSTLMKILYGLYQPDSGEIL---IDGKPVRIRspr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 389 --LDN-IAIIHQNPYVFHT-SVRHNLTLYQDYSDSLLIST----------LKKVGL---WEACCHQLdyeltgdnfSGGQ 451
Cdd:COG3845 76 daIALgIGMVHQHFMLVPNlTVAENIVLGLEPTKGGRLDRkaararirelSERYGLdvdPDAKVEDL---------SVGE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348497 452 IIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPN---SIIEIAHhyKLE 506
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAegkSIIFITH--KLR 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
323-494 |
2.41e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.71 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 323 NVTKSYDNQEIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISG--QDKAYSGKIIfksIDGRELT-PNLDNIAIIHQNP 399
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTIL---ANNRKPTkQILKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 400 YVF-HTSVRHNL----------TLYQDYSDSLLISTLKKVGLweACCHQldyELTGDNF----SGGQIIKLEIARAILRE 464
Cdd:PLN03211 150 ILYpHLTVRETLvfcsllrlpkSLTKQEKILVAESVISELGL--TKCEN---TIIGNSFirgiSGGERKRVSIAHEMLIN 224
|
170 180 190
....*....|....*....|....*....|
gi 1081348497 465 KQVLLADEMMASLDAASSKEISNVLKQLPN 494
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQ 254
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
323-481 |
4.66e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.47 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 323 NVTKSYDNQEIFRDVTvtFSLSQHNLI--VGDSGIGKTTLFRLISGQDKAYSGKIIF--KSIDGreltpnlDNIAIIHQN 398
Cdd:PRK13540 6 ELDFDYHDQPLLQQIS--FHLPAGGLLhlKGSNGAGKTTLLKLIAGLLNPEKGEILFerQSIKK-------DLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 399 PYVFH-TSVRHNLTLYQD-YSDSLLISTlkKVGLWEACC-----HQLDYELtgDNFSGGQIIKLEIARAILREKQVLLAD 471
Cdd:PRK13540 77 CFVGHrSGINPYLTLRENcLYDIHFSPG--AVGITELCRlfsleHLIDYPC--GLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170
....*....|
gi 1081348497 472 EMMASLDAAS 481
Cdd:PRK13540 153 EPLVALDELS 162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-495 |
7.06e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.08 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 320 QLKNVTkSYDNQEIfRDVTvtFSLSQHNLI--VGDSGIGKTTLFRLISGQDKAYSGKIifkSIDGRELTPNLDNIAIIHQ 397
Cdd:PRK09700 267 EVRNVT-SRDRKKV-RDIS--FSVCRGEILgfAGLVGSGRTELMNCLFGVDKRAGGEI---RLNGKDISPRSPLDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 398 NPYVfhTSVR------HNLTLYQDYSDSLLISTLKKVGLW-------------------EACCHQLDYELTgdNFSGGQI 452
Cdd:PRK09700 340 MAYI--TESRrdngffPNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrtaenqrellALKCHSVNQNIT--ELSGGNQ 415
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081348497 453 IKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPNS 495
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD 458
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
349-485 |
7.80e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.94 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 349 IVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTPNLdniaiiHQNP-YVFHT-------SVRHNLTLYQ----DY 416
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY------HQDLlYLGHQpgiktelTALENLRFYQrlhgPG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348497 417 SDSLLISTLKKVGLW---EACCHQLdyeltgdnfSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEI 485
Cdd:PRK13538 106 DDEALWEALAQVGLAgfeDVPVRQL---------SAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
349-479 |
1.20e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 349 IVGDSGIGKTTLFRLISGQDKAYSGKIIFksIDGReltpnldnIAIIHQNPYVFHTSVRHNLTLYQDYSDSLLISTLKKV 428
Cdd:PLN03130 648 IVGSTGEGKTSLISAMLGELPPRSDASVV--IRGT--------VAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVT 717
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 429 GLWeaccHQLDYELTGD---------NFSGGQIIKLEIARAILREKQVLLADEMMASLDA 479
Cdd:PLN03130 718 ALQ----HDLDLLPGGDlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-508 |
1.38e-03 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 40.43 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 349 IVGDSGIGKTTLFRLISGQDKAYSGKI--------IFKSIDGRELTPNL-----DNIAIIHQNPYVFH--TSVRHNLtly 413
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEFRGSELQNYFtklleGDVKVIVKPQYVDLipKAVKGKV--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 414 qdysdSLLISTLKKVGLWEACCHQLdyELTG------DNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISN 487
Cdd:cd03236 108 -----GELLKKKDERGKLDELVDQL--ELRHvldrniDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170 180
....*....|....*....|....
gi 1081348497 488 VLKQL---PNSIIEIAHHYKLEDY 508
Cdd:cd03236 181 LIRELaedDNYVLVVEHDLAVLDY 204
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
321-507 |
3.01e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 321 LKNVTKSYDNQEIFRDVTVTF-SLSQHNLIvGDSGIGKTTLFRLISGQDKAYSGKIIF--KSIDGRELTPNLDN-IAIIH 396
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVrPHSIHALM-GENGAGKSTLLKCLFGIYQKDSGSILFqgKEIDFKSSKEALENgISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 397 QN-PYVFHTSVRHNLTLYQDYSDSLLISTLKKVGLWEACCHQLDYEL----TGDNFSGGQIIKLEIARAILREKQVLLAD 471
Cdd:PRK10982 80 QElNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIdpraKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081348497 472 EMMASLdaaSSKEIS------NVLKQLPNSIIEIAHhyKLED 507
Cdd:PRK10982 160 EPTSSL---TEKEVNhlftiiRKLKERGCGIVYISH--KMEE 196
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
319-502 |
3.29e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSYDNQEIFrDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIdgreltpNLDNIA----- 393
Cdd:PRK13541 2 LSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNC-------NINNIAkpyct 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 394 -IIHQNPYVFHTSVRHNLTLYQDYSDSL-----LISTLKKVGLWEACCHQLdyeltgdnfSGGQIIKLEIARAILREKQV 467
Cdd:PRK13541 74 yIGHNLGLKLEMTVFENLKFWSEIYNSAetlyaAIHYFKLHDLLDEKCYSL---------SSGMQKIVAIARLIACQSDL 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081348497 468 LLADEMMASLDAASSKEISNVLKQLPNS--IIEIAHH 502
Cdd:PRK13541 145 WLLDEVETNLSKENRDLLNNLIVMKANSggIVLLSSH 181
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
319-383 |
4.74e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 38.91 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 319 IQLKNVTKSY----DNQEIFRDVTVTFSLSQHNL------------------IVGDSGIGKTTLFRLISGQDKAYSGKII 376
Cdd:COG1134 5 IEVENVSKSYrlyhEPSRSLKELLLRRRRTRREEfwalkdvsfevergesvgIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
....*..
gi 1081348497 377 fksIDGR 383
Cdd:COG1134 85 ---VNGR 88
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
318-520 |
5.23e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 38.91 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 318 EIQLKNVTKSYDNQ-----EIFRDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIF----KSIDGRELTPN 388
Cdd:PRK13651 2 QIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 389 LDNIAIIHQNPYV----FHTSVRHNL-TLYQDYSDSLLISTLKK----------VGLWEACCHQLDY-ELTG-------- 444
Cdd:PRK13651 82 KVLEKLVIQKTRFkkikKIKEIRRRVgVVFQFAEYQLFEQTIEKdiifgpvsmgVSKEEAKKRAAKYiELVGldesylqr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 445 --DNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEISNVLKQLPNS---IIEIAHhykleDYDAVYRIENKSI 519
Cdd:PRK13651 162 spFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgktIILVTH-----DLDNVLEWTKRTI 236
|
.
gi 1081348497 520 V 520
Cdd:PRK13651 237 F 237
|
|
| PRK13830 |
PRK13830 |
conjugal transfer protein TrbE; Provisional |
346-387 |
5.39e-03 |
|
conjugal transfer protein TrbE; Provisional
Pssm-ID: 237525 [Multi-domain] Cd Length: 818 Bit Score: 39.44 E-value: 5.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1081348497 346 HNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTP 387
Cdd:PRK13830 458 HTLIFGPTGSGKSTLLALIAAQFRRYAGAQIFAFDKGRSMLP 499
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-520 |
6.50e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.35 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 348 LIVGDSGIGKTTLFRLISGQDKAYSGKIIFksIDGRELTPNLDNIAiihqnpyvfhtsvrhnltlyqdysdsllistlkk 427
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQL---------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 428 vglweaccHQLDYELTGDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAASSKEIS---------NVLKQLPNSIIE 498
Cdd:smart00382 50 --------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlllLLKSEKNLTVIL 121
|
170 180
....*....|....*....|..
gi 1081348497 499 IAHHYKLEDYDAVYRIENKSIV 520
Cdd:smart00382 122 TTNDEKDLGPALLRRRFDRRIV 143
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
335-517 |
7.29e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 38.86 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 335 RDVTVTFSLSQHNLIVGDSGIGKTTLFRLISGQDKAYSGKIIFKSIDGRELTP------NLDNIAIIHQNPYVF-HTSVR 407
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMpHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348497 408 HNLTLYQDYS-------DSLLISTLKKVGLwEACCHQLDyeltgDNFSGGQIIKLEIARAILREKQVLLADEMMASLDAA 480
Cdd:PRK10070 125 DNTAFGMELAginaeerREKALDALRQVGL-ENYAHSYP-----DELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081348497 481 SSKEISNVLKQL----PNSIIEIAHhykleDYDAVYRIENK 517
Cdd:PRK10070 199 IRTEMQDELVKLqakhQRTIVFISH-----DLDEAMRIGDR 234
|
|
| |
