|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-244 |
1.39e-133 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 376.74 E-value: 1.39e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSS-TLVSFRHVRKSWQQ----VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGK 75
Cdd:COG1116 1 MSAAaPALELRGVSKRFPTggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 76 ERGIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQIL 155
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 156 MLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSPRPGRIREVVSLALPHPRQ---RDDAA 232
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDrelRTSPE 240
|
250
....*....|..
gi 695804877 233 FIAACRQIRNLI 244
Cdd:COG1116 241 FAALRAEILDLL 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-222 |
1.27e-114 |
|
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: 327.12 E-value: 1.27e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQ----QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVFQ 82
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 163 ALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSPRPGRIREVVSLAL 222
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-217 |
4.09e-96 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 285.07 E-value: 4.09e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---GI 79
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKrnvGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDE 159
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 160 PFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREV 217
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVM--NDGRIEQV 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-244 |
2.23e-89 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 264.80 E-value: 2.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 17 QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVFQEPRLFPWLNVLDNV 96
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 MLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQEL 176
Cdd:COG4525 98 AFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 177 LQIHQRAGTTTLLVTHDVEEAVALADRVVVLSPRPGRIREVvsLALPHPRQ----------RDDAAFIAACRQIRNLI 244
Cdd:COG4525 178 LDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVER--LELDFSRRflagedaraiKSDPAFIALREELLDII 253
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-217 |
3.37e-86 |
|
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: 255.14 E-value: 3.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---GIVFQE 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 164 LDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREV 217
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM--NEGRIVQV 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-217 |
4.41e-84 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 254.61 E-value: 4.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-KERGI--VFQE 83
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPpKDRNIamVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 164 LDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREV 217
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVM--NDGRIQQV 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-217 |
6.82e-84 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 253.92 E-value: 6.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGE------PVtgvgKERGI--VF 81
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnlPP----RERRVgfVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 162 GALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIREV 217
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMN--QGRIEQV 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-219 |
4.96e-77 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 232.24 E-value: 4.96e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 4 STLVSFRHVRKSWQQ----VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-KER- 77
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSeRELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 -------GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVA 150
Cdd:COG1136 82 rlrrrhiGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 151 RPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDvEEAVALADRVVVLspRPGRIREVVS 219
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRL--RDGRIVSDER 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-217 |
7.90e-77 |
|
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: 231.74 E-value: 7.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-KERGI--VFQE 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPpHKRPVntVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 164 LDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREV 217
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM--NKGKIQQI 212
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-214 |
5.01e-76 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 232.29 E-value: 5.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 9 FRHVRKSWQ-QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE---RGI--VFQ 82
Cdd:COG1125 4 FENVTKRYPdGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelrRRIgyVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQL--SEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:COG1125 84 QIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 161 FGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRI 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-217 |
9.51e-73 |
|
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: 221.83 E-value: 9.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-KERGI--VFQE 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvQERNVgfVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLGL----ADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDE 159
Cdd:cd03296 83 YALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 160 PFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIREV 217
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMN--KGRIEQV 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-214 |
7.46e-72 |
|
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: 218.90 E-value: 7.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQ----VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER----- 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 ----GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQ 153
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695804877 154 ILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDvEEAVALADRVVVLspRPGRI 214
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIEL--RDGKI 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
11-220 |
1.09e-71 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 219.57 E-value: 1.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 11 HVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVFQEPRLFPWL 90
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 91 NVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRH 170
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695804877 171 TLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSPRPGRIREVVSL 220
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPL 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-207 |
3.02e-71 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 217.92 E-value: 3.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 2 TSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---- 77
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 ----GIVFQEPRLFPWLNVLDNVMLGLaDE--KLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVAR 151
Cdd:COG1127 81 rrriGMLFQGGALFDSLTVFENVAFPL-REhtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 152 PQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVL 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-217 |
5.17e-71 |
|
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: 216.35 E-value: 5.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-KERGI--VFQE 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpKDRDIamVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 164 LDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREV 217
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM--NDGQIQQI 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-230 |
8.69e-71 |
|
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: 216.56 E-value: 8.69e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVFQEPRLFPWLNVLDNVMLGL- 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 101 -ADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQI 179
Cdd:TIGR01184 81 rVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695804877 180 HQRAGTTTLLVTHDVEEAVALADRVVVLSPRPG-RIREVVSLALPHPRQRDD 230
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAaNIGQILEVPFPRPRDRLE 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-214 |
1.11e-70 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 220.97 E-value: 1.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--- 77
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENrhv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 158 DEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRI 223
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-234 |
2.10e-69 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 217.21 E-value: 2.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 8 SFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---GIVFQEP 84
Cdd:TIGR03265 6 SIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKrdyGIVFQSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 85 RLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGAL 164
Cdd:TIGR03265 86 ALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 165 DALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIREVvslALP-----HPRQRDDAAFI 234
Cdd:TIGR03265 166 DARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMN--HGVIEQV---GTPqeiyrHPATPFVADFV 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-228 |
3.89e-68 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 210.69 E-value: 3.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 12 VRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVFQEPRLFPWLN 91
Cdd:PRK11247 18 VSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARLLPWKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLGLadeklsRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHT 171
Cdd:PRK11247 98 VIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 172 LQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREVVSLALPHPRQR 228
Cdd:PRK11247 172 MQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIGLDLTVDLPRPRRR 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-207 |
8.57e-68 |
|
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: 209.08 E-value: 8.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVT-ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIV 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrkiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQL--SEFVNALPAQLSGGMAQRVAIARGLVARPQILMLD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695804877 159 EPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIM 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-217 |
2.69e-66 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 209.17 E-value: 2.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 11 HVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGV-GKER--GIVFQEPRLF 87
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLhARDRkvGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 88 PWLNVLDNVMLGLA----DEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:PRK10851 87 RHMTVFDNIAFGLTvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 164 LDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIREV 217
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMS--QGNIEQA 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-207 |
2.39e-65 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 202.92 E-value: 2.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-------G 78
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrrkvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRLFPWLNVLDNVMLGLAD-EKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 158 DEPFGALD-ALTrhtlqQELLQIHQ---RAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:COG1126 161 DEPTSALDpELV-----GEVLDVMRdlaKEGMTMVVVTHEMGFAREVADRVVFM 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-207 |
1.42e-64 |
|
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: 198.95 E-value: 1.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 9 FRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-------GIVF 81
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrriGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPWLNVLDNVMLGladeklsraakrqralemlervqlsefvnalpaqLSGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:cd03229 83 QDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695804877 162 GALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
12-219 |
1.14e-63 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 198.49 E-value: 1.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 12 VRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---GIVFQEPRLFP 88
Cdd:TIGR00968 6 ISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDrkiGFVFQHYALFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 89 WLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALT 168
Cdd:TIGR00968 86 HLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695804877 169 RHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIREVVS 219
Cdd:TIGR00968 166 RKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMS--NGKIEQIGS 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-216 |
2.72e-63 |
|
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: 205.91 E-value: 2.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--------G 78
Cdd:COG1123 266 LSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrrrvQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPR--LFPWLNVLDNVMLGL-ADEKLSRAAKRQRALEMLERVQLS-EFVNALPAQLSGGMAQRVAIARGLVARPQI 154
Cdd:COG1123 346 MVFQDPYssLNPRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 155 LMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:COG1123 426 LILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVM--YDGRIVE 485
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-221 |
1.11e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 196.05 E-value: 1.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG---KER-GIVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPaevRRRiGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 163 ALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLspRPGRIREVVSLA 221
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAII--DKGRIVADGTPD 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-214 |
3.01e-62 |
|
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: 195.03 E-value: 3.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--------G 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRLFPWLNVLDNVMLGLADE-KLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 158 DEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRI 214
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLY--DGKI 215
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-214 |
3.56e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 199.56 E-value: 3.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 18 QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---------GIVFQEPRLFP 88
Cdd:COG4175 39 QTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrkkmSMVFQHFALLP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 89 WLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALT 168
Cdd:COG4175 119 HRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLI 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695804877 169 RHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:COG4175 199 RREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDGRI 242
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-217 |
1.55e-61 |
|
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: 194.01 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 12 VRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---------GIVFQ 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiSMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 163 ALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREV 217
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRLVQV 242
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-208 |
1.55e-60 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 190.24 E-value: 1.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQ-QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIV 80
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEPR--LF-PwlNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:COG1122 81 FQNPDdqLFaP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695804877 158 DEPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLD 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-234 |
5.00e-60 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 193.32 E-value: 5.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSstlVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-KERGI 79
Cdd:PRK11000 1 MAS---VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPpAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 --VFQEPRLFPWLNVLDNVMLGLadeKLSRAAK---RQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQI 154
Cdd:PRK11000 78 gmVFQSYALYPHLSVAENMSFGL---KLAGAKKeeiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 155 LMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIREV-VSLALPH-PRQRDDAA 232
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLD--AGRVAQVgKPLELYHyPANRFVAG 232
|
..
gi 695804877 233 FI 234
Cdd:PRK11000 233 FI 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-218 |
1.09e-59 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 187.95 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQ-VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-------- 77
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695804877 158 DEPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLspRPGRIREVV 218
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLEL--EDGRLVRDE 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-216 |
1.09e-59 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 188.41 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 2 TSSTLVSFRHVRKSWQ----QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER 77
Cdd:COG4181 4 SSAPIIELRGLTKTVGtgagELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 ---------GIVFQEPRLFPWLNVLDNVMLGLadEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGL 148
Cdd:COG4181 84 rarlrarhvGFVFQSFQLLPTLTALENVMLPL--ELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 149 VARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAvALADRVVVLspRPGRIRE 216
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRL--RAGRLVE 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-236 |
3.20e-59 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 191.59 E-value: 3.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGK-ERGI--VFQ 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPyQRPInmMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 163 ALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSP-------RPGRIREvvslalpHPRQRDDAAFIA 235
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRgkfvqigEPEEIYE-------HPTTRYSAEFIG 251
|
.
gi 695804877 236 A 236
Cdd:PRK11607 252 S 252
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-205 |
3.61e-59 |
|
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: 186.20 E-value: 3.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-------VGKERGI 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkknineLRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPWLNVLDNVMLGLAD-EKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695804877 159 EPFGALDAltrhTLQQELLQIHQRA---GTTTLLVTHDVEEAVALADRVV 205
Cdd:cd03262 161 EPTSALDP----ELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-216 |
1.26e-58 |
|
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: 185.40 E-value: 1.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQ----QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---- 77
Cdd:cd03257 1 LLEVKNLSVSFPtgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 ----GIVFQEPR--LFPWLNVLDNVM--LGLADEKLSRAAKRQRALEMLERVQLSE-FVNALPAQLSGGMAQRVAIARGL 148
Cdd:cd03257 81 rkeiQMVFQDPMssLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 149 VARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM--YAGKIVE 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
15-207 |
3.34e-58 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 184.57 E-value: 3.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 15 SWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-KERG--IVFQEPRLFPWLN 91
Cdd:COG3840 8 TYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAERPvsMLFQENNLFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLGL-ADEKLSrAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLV-ARPqILMLDEPFGALDALTR 169
Cdd:COG3840 88 VAQNIGLGLrPGLKLT-AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFSALDPALR 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 695804877 170 HTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:COG3840 166 QEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLV 203
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-237 |
5.95e-57 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 184.23 E-value: 5.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 37 LVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQR 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 114 ALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHD 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695804877 194 VEEAVALADRVVVLspRPGRIREVVS--LALPHPRQRDDAAFIAAC 237
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKIAQIGTpeEIYEEPANLFVARFIGEI 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-215 |
6.03e-57 |
|
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: 180.57 E-value: 6.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIA---AGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGK-------ER--GIVFQEPRLFPW 89
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKkinlppqQRkiGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 90 LNVLDNVMLGLadEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTR 169
Cdd:cd03297 90 LNVRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695804877 170 HTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIR 215
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM--EDGRLQ 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-214 |
1.72e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 180.64 E-value: 1.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 5 TLVSFRHVRKSWQ-QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER------ 77
Cdd:COG3638 1 PMLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 --GIVFQEPRLFPWLNVLDNVMLG-LADEKLSRA-------AKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARG 147
Cdd:COG3638 81 riGMIFQQFNLVPRLSVLTNVLAGrLGRTSTWRSllglfppEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 148 LVARPQILMLDEPFGALD-ALTRHTLQQeLLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:COG3638 161 LVQEPKLILADEPVASLDpKTARQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGL--RDGRV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-208 |
3.62e-56 |
|
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: 178.43 E-value: 3.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 8 SFRHVRKSW--QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----VGKERGIV 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlslkeLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEPRL-FPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDE 159
Cdd:cd03225 81 FQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695804877 160 PFGALDALTRHTLQQELLQIHQrAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-228 |
6.04e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 181.81 E-value: 6.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQ----VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER----- 77
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 ---GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQI 154
Cdd:COG1135 82 rkiGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 155 LMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIRE---VVSLALpHPRQR 228
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLE--NGRIVEqgpVLDVFA-NPQSE 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-207 |
6.06e-56 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 182.23 E-value: 6.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-KERGI 79
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 --VFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:PRK11432 81 cmVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695804877 158 DEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-207 |
1.38e-55 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 181.58 E-value: 1.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVT-ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-KERGI--VFQ 82
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEpADRDIamVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695804877 163 ALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK11650 164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-210 |
2.60e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 177.59 E-value: 2.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIV 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 ---FQEPRLFPwLNVLDNVMLGLADE----KLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQ 153
Cdd:COG1121 81 pqrAEVDWDFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 154 ILMLDEPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLSPR 210
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-236 |
4.06e-54 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 174.28 E-value: 4.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER----GIVFQEPR 85
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqiGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 86 LFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALD 165
Cdd:COG4555 85 LYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695804877 166 ALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLspRPGRIREVVSLAL---PHPRQRDDAAFIAA 236
Cdd:COG4555 165 VMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVIL--HKGKVVAQGSLDElreEIGEENLEDAFVAL 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-216 |
2.34e-53 |
|
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: 172.00 E-value: 2.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQ----VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGV-GKER--- 77
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 ----GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQ 153
Cdd:cd03258 81 rrriGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695804877 154 ILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIRE 216
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVME--KGEVVE 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-232 |
3.77e-53 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 171.91 E-value: 3.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 13 RKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVFQEPR-- 85
Cdd:COG1124 12 GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrvQMVFQDPYas 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 86 LFPWLNVLDNVMLGLADEKLSRAakRQRALEMLERVQL-SEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGAL 164
Cdd:COG1124 92 LHPRHTVDRILAEPLRIHGLPDR--EERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 165 DALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREVVSLALPHPRQRDDAA 232
Cdd:COG1124 170 DVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM--QNGRIVEELTVADLLAGPKHPYT 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
10-217 |
8.53e-53 |
|
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: 170.59 E-value: 8.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTaLQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---GIVFQEPRL 86
Cdd:cd03299 4 ENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNYAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 FPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:cd03299 83 FPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695804877 167 LTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREV 217
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKLIQV 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-214 |
1.27e-52 |
|
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: 170.44 E-value: 1.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 9 FRHVRKSW-QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--------GI 79
Cdd:cd03256 3 VENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrrqiGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPWLNVLDNVMLGLADEK---------LSRAAKrQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVA 150
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695804877 151 RPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGL--KDGRI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
1.36e-52 |
|
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: 177.79 E-value: 1.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL---ESATQGDICINGEPVTGV---- 73
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 74 -GKERGIVFQEPR--LFPwLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVA 150
Cdd:COG1123 81 rGRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 151 RPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVE 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-216 |
1.41e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 170.27 E-value: 1.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-------VGKERG 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvderlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRLFPWLNVLDNVMLG-LADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 158 DEPFGALDALTRHtlqqELLQIHQ---RAGTTTLLVTHDVEEAVALADRVVVLSprPGRIRE 216
Cdd:PRK09493 161 DEPTSALDPELRH----EVLKVMQdlaEEGMTMVIVTHEIGFAEKVASRLIFID--KGRIAE 216
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
11-234 |
1.99e-52 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 173.34 E-value: 1.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 11 HVRKSWQQVTaLQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE-RGI--VFQEPRLF 87
Cdd:NF040840 6 NLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEkRGIayVYQNYMLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 88 PWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDAL 167
Cdd:NF040840 85 PHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695804877 168 TRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRV-VVLSPR---PGRIREVVSlalpHPRQRDDAAFI 234
Cdd:NF040840 165 TRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVgIMLNGRlsqVGDVREVFR----RPKNEFVARFV 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-207 |
1.95e-51 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 165.26 E-value: 1.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER----GIVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPWLNVLDNVmlgladeklsraakrqralemlervqlsefvnalpaQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695804877 163 ALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAIL 168
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-214 |
2.70e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.14 E-value: 2.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 8 SFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVFQ 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrrqvAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPwLNVLDNvmLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPA-QLSGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:COG4619 82 EPALWG-GTVRDN--LPFPFQLRERKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695804877 162 GALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL--EAGRL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-207 |
3.35e-50 |
|
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: 164.83 E-value: 3.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER----G 78
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRiarlG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IV--FQEPRLFPWLNVLDNVMLGL----------ADEKLSRAAK-----RQRALEMLERVQLSEFVNALPAQLSGGMAQR 141
Cdd:COG0411 81 IArtFQNPRLFPELTVLENVLVAAharlgrgllaALLRLPRARReereaRERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 142 VAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-210 |
4.07e-50 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 163.04 E-value: 4.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 8 SFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVG-LESA--TQGDICINGEPVTGVGKER---GIVF 81
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQrriGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPWLNVLDNVMLGLAdEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:COG4136 83 QDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695804877 162 GALDA-LTRHTLQQELLQIHQRAGtTTLLVTHDVEEAVAlADRVVVLSPR 210
Cdd:COG4136 162 SKLDAaLRAQFREFVFEQIRQRGI-PALLVTHDEEDAPA-AGRVLDLGNW 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-207 |
1.04e-49 |
|
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: 161.93 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 15 SWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVFQE---PRLFPwLN 91
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRrsiDRDFP-IS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLGL-----ADEKLSRAAKRqRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:cd03235 87 VRDVVLMGLyghkgLFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695804877 167 LTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-207 |
1.25e-49 |
|
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: 165.23 E-value: 1.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQ----QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESA---TQGDICINGEPVTGVGKE-- 76
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 77 ---RG----IVFQEPrlfpwLNVLDNVM-LG--LAD-----EKLSRAAKRQRALEMLERVQLS---EFVNALPAQLSGGM 138
Cdd:COG0444 81 rkiRGreiqMIFQDP-----MTSLNPVMtVGdqIAEplrihGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695804877 139 AQRVAIARGLVARPQILMLDEPFGALDAltrhTLQQE----LLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDV----TIQAQilnlLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-216 |
3.44e-49 |
|
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: 171.56 E-value: 3.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRkswQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVF 81
Cdd:COG2274 479 VSFRYPG---DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrrqiGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPwLNVLDNVMLGLADeklsraAKRQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAIARGLVA 150
Cdd:COG2274 556 QDVFLFS-GTIRENITLGDPD------ATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 151 RPQILMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDvEEAVALADRVVVLspRPGRIRE 216
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHR-LSTIRLADRIIVL--DKGRIVE 689
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-216 |
4.35e-49 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 160.59 E-value: 4.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQ----QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG------- 74
Cdd:TIGR02211 1 LLKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSsnerakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 75 --KERGIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARP 152
Cdd:TIGR02211 81 rnKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695804877 153 QILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAvALADRVVVLspRPGRIRE 216
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA-KKLDRVLEM--KDGQLFN 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-161 |
5.45e-49 |
|
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: 158.19 E-value: 5.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----VGKERGIVFQEPRLFPWLNVLDNV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 97 MLGLADEKLSRAAKRQRALEMLERVQLSEF----VNALPAQLSGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-207 |
1.68e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 161.08 E-value: 1.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--------G 78
Cdd:TIGR04521 6 VSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrkkvG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEP--RLFPwLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSE-FVNALPAQLSGGMAQRVAIARGLVARPQIL 155
Cdd:TIGR04521 86 LVFQFPehQLFE-ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695804877 156 MLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:TIGR04521 165 ILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVM 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-232 |
1.70e-48 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 163.35 E-value: 1.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIA----AGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV------TGVGKER---GIVFQEPRLFP 88
Cdd:COG4148 11 RGGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRrriGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 89 WLNVLDNVMLGLadeklSRAAKRQRALEMLERVQL---SEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALD 165
Cdd:COG4148 91 HLSVRGNLLYGR-----KRAPRAERRISFDEVVELlgiGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 166 ALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLS----PRPGRIREVVS-LALPHPRQRDDAA 232
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEqgrvVASGPLAEVLSrPDLLPLAGGEEAG 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-207 |
4.75e-48 |
|
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: 158.37 E-value: 4.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG----KERGIV--FQE 83
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpheiARLGIGrtFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLG----------LADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQ 153
Cdd:cd03219 84 PRLFPELTVLENVMVAaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 154 ILMLDEPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVL 216
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-207 |
1.38e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 158.36 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSW--QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING------EPVTGVGKERG 78
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRlfpwlN------VLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARP 152
Cdd:TIGR04520 81 MVFQNPD-----NqfvgatVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 153 QILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVaLADRVVVL 207
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVM 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
15-214 |
6.76e-47 |
|
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: 154.96 E-value: 6.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 15 SWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---GIVFQEPRLFPWLN 91
Cdd:cd03298 7 RFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHT 171
Cdd:cd03298 87 VEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695804877 172 LQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRI 214
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLD--NGRI 207
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-207 |
1.89e-46 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 153.54 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 11 HVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGE---PVTGVGKER------GIVF 81
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKfrreklGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695804877 162 GALDALTRHTLQQELLQIhQRAGTTTLLVTHDVEEAvALADRVVVL 207
Cdd:TIGR03608 163 GSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-207 |
1.92e-46 |
|
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: 153.72 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSW-QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-------- 77
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrrki 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695804877 158 DEPFGALDALTRHTLQQELLQIHQrAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-214 |
8.15e-46 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 153.28 E-value: 8.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----VGKERGIV 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsrreLARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEPRLFPWLNVLDNVMLG----LADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILM 156
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 157 LDEPFGALDAltRHtlQQELLQI----HQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:COG1120 161 LDEPTSHLDL--AH--QLEVLELlrrlARERGRTVVMVLHDLNLAARYADRLVLL--KDGRI 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-216 |
1.03e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 155.73 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 9 FRHVRKSWQQ----VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-----KER-- 77
Cdd:PRK11153 4 LKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelrKARrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 -GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILM 156
Cdd:PRK11153 84 iGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 157 LDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIRE 216
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVID--AGRLVE 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-207 |
1.39e-45 |
|
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: 150.23 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSW--QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GI 79
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkniAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPwLNVLDNVmlgladeklsraakrqralemlervqlsefvnalpaqLSGGMAQRVAIARGLVARPQILMLDE 159
Cdd:cd03228 81 VPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695804877 160 PFGALDALTRHTLQQELLQIHQraGTTTLLVTHDVeEAVALADRVVVL 207
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVL 167
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-217 |
2.98e-45 |
|
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: 151.18 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQG------------DICINGEPVTGVG 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegevlldgkDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 75 KERGIVFQEPRLFPwLNVLDNVMLGLAD-EKLSRAAKRQRALEMLERVQLSEFVN--ALPAQLSGGMAQRVAIARGLVAR 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLhGIKLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 152 PQILMLDEPFGALDALTRHTLQQELLQIHQRagTTTLLVTHDVEEAVALADRVVVLSprPGRIREV 217
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLL--NGRLVEF 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-214 |
6.48e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 150.50 E-value: 6.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 25 FSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---GIVFQEPRLFPWLNVLDNVMLGLA 101
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvSMLFQENNLFSHLTVAQNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 102 DE-KLSRAAKRQRAlEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIH 180
Cdd:PRK10771 98 PGlKLNAAQREKLH-AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176
|
170 180 190
....*....|....*....|....*....|....
gi 695804877 181 QRAGTTTLLVTHDVEEAVALADRVVVLSprPGRI 214
Cdd:PRK10771 177 QERQLTLLMVSHSLEDAARIAPRSLVVA--DGRI 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-216 |
1.20e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 150.16 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGE-----------PVTGVGK 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpsekAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 76 ERGIVFQEPRLFPWLNVLDNVM------LGLadeklSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLV 149
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIeapckvLGL-----SKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 150 ARPQILMLDEPFGALD-ALTRHTLQ--QELlqihQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:COG4161 158 MEPQVLLFDEPTAALDpEITAQVVEiiREL----SQTGITQVIVTHEVEFARKVASQVVYM--EKGRIIE 221
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-208 |
7.85e-44 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 147.01 E-value: 7.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQ-VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER------- 77
Cdd:TIGR02673 1 MIEFHNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 -GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILM 156
Cdd:TIGR02673 81 iGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 157 LDEPFGALDAltrhTLQQELLQIHQR---AGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:TIGR02673 161 ADEPTGNLDP----DLSERILDLLKRlnkRGTTVIVATHDLSLVDRVAHRVIILD 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-215 |
1.15e-43 |
|
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: 146.66 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-GIVFQEPR 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRiGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 86 LFPWLNVLDnVMLGLADEK-LSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGAL 164
Cdd:cd03269 81 LYPKMKVID-QLVYLAQLKgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695804877 165 DALTRHTLQQELLQIhQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIR 215
Cdd:cd03269 160 DPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLL--NKGRAV 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-207 |
1.56e-43 |
|
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: 144.31 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 8 SFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTgvgkergivfqeprlf 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 88 pwlnvldnvmlgladEKLSRAAKRQRALEMlervqlsefvnalpaQLSGGMAQRVAIARGLVARPQILMLDEPFGALDAL 167
Cdd:cd00267 65 ---------------KLPLEELRRRIGYVP---------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 695804877 168 TRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-214 |
1.69e-43 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 147.06 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSW-QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER------- 77
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 -GIVFQEPRLFPWLNVLDNVMLG-LADEKLSRA-------AKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGL 148
Cdd:TIGR02315 81 iGMIFQHYNLIERLTVLENVLHGrLGYKPTWRSllgrfseEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 149 VARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGL--KAGEI 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-217 |
2.33e-43 |
|
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: 145.98 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 11 HVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT----GVGKERGIVFQEPRL 86
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVreprEVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 FPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695804877 167 LTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIREV 217
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIID--HGRIIAE 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-216 |
2.72e-43 |
|
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: 153.76 E-value: 2.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 2 TSSTLVSFRHVRKSWQQ-VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--- 77
Cdd:COG4988 332 AGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrr 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 --GIVFQEPRLFPWlNVLDNVMLGLADeklsraAKRQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAI 144
Cdd:COG4988 412 qiAWVPQNPYLFAG-TIRENLRLGRPD------ASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 145 ARGLVARPQILMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDvEEAVALADRVVVLspRPGRIRE 216
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHR-LALLAQADRILVL--DDGRIVE 551
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-216 |
4.26e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 153.40 E-value: 4.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWqqvtALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVF 81
Cdd:COG1132 345 VSFSYPGDRP----VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrrqiGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPwLNVLDNVMLGLA---DEKLSRAAKrqralemleRVQLSEFVNALP-----------AQLSGGMAQRVAIARG 147
Cdd:COG1132 421 QDTFLFS-GTIRENIRYGRPdatDEEVEEAAK---------AAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 148 LVARPQILMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDVeEAVALADRVVVLSprPGRIRE 216
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRL-STIRNADRILVLD--DGRIVE 554
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-208 |
6.76e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 147.18 E-value: 6.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT-----GVG---KERG 78
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpedrrRIGylpEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 ivfqeprLFPWLNVLDnVMLGLADEK-LSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:COG4152 82 -------LYPKMKVGE-QLVYLARLKgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695804877 158 DEPFGALDALTRHTLQQELLQiHQRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIIN 203
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-216 |
8.69e-43 |
|
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: 152.23 E-value: 8.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSW--QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GI 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrrriAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFpwlN--VLDNVMLGLADeklsraAKRQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAIAR 146
Cdd:COG4987 414 VPQRPHLF---DttLRENLRLARPD------ATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 147 GLVARPQILMLDEPFGALDALTRHTLQQELLQihQRAGTTTLLVTHDvEEAVALADRVVVLspRPGRIRE 216
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLE--ALAGRTVLLITHR-LAGLERMDRILVL--EDGRIVE 549
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-214 |
5.20e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 149.01 E-value: 5.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG----KERG 78
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdaQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 I--VFQEPRLFPWLNVLDNVMLGLADEK---LSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQ 153
Cdd:COG1129 81 IaiIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695804877 154 ILMLDEPFGALDAltRHTlqQELLQIHQR---AGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:COG1129 161 VLILDEPTASLTE--REV--ERLFRIIRRlkaQGVAIIYISHRLDEVFEIADRVTVL--RDGRL 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-208 |
6.72e-42 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 142.26 E-value: 6.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSW--QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT----GVGKERGIV 80
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtdrkAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEPRLFPWLNVLDNVML-----GladekLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQIL 155
Cdd:cd03263 81 PQFDALFDELTVREHLRFyarlkG-----LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695804877 156 MLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMS 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-210 |
7.02e-42 |
|
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: 141.85 E-value: 7.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT----GVGKERGIVF 81
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRdareDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPWLNVLDNvmLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:COG4133 82 HADGLKPELTVREN--LRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695804877 162 GALDALTRHTLQQeLLQIHQRAGTTTLLVTHDVEEavALADRVVVLSPR 210
Cdd:COG4133 160 TALDAAGVALLAE-LIAAHLARGGAVLLTTHQPLE--LAAARVLDLGDF 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-216 |
1.23e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 142.46 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING-------EPVTGVG----KERGIVFQEPRLFPW 89
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSDKAIrelrRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 90 LNVLDNVM------LGLadeklSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:PRK11124 97 LTVQQNLIeapcrvLGL-----SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 164 LDAltRHTLQ-----QELlqihQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:PRK11124 172 LDP--EITAQivsiiREL----AETGITQVIVTHEVEVARKTASRVVYM--ENGHIVE 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-217 |
1.71e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 144.10 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSW-----------QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEP 69
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 70 VTGVGKER--------GIVFQEPR--LFPWLNVLDNVMLGLADEKL-SRAAKRQRALEMLERVQLS-EFVNALPAQLSGG 137
Cdd:COG4608 82 ITGLSGRElrplrrrmQMVFQDPYasLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 138 MAQRVAIARGLVARPQILMLDEPFGALDA---------LTRhtLQQELlqihqraGTTTLLVTHD---VEEavaLADRVV 205
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVsiqaqvlnlLED--LQDEL-------GLTYLFISHDlsvVRH---ISDRVA 229
|
250
....*....|....
gi 695804877 206 V--LsprpGRIREV 217
Cdd:COG4608 230 VmyL----GKIVEI 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-216 |
3.08e-41 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 142.13 E-value: 3.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 4 STLVSFRHVRKSWQQV---------TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG 74
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 75 KERG--------IVFQE------PRlFPWLNVLDNVMLGLADekLSRAAKRQRALEMLERVQLS-EFVNALPAQLSGGMA 139
Cdd:PRK10419 81 RAQRkafrrdiqMVFQDsisavnPR-KTVREIIREPLRHLLS--LDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 140 QRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIRE 216
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMD--NGQIVE 232
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-217 |
1.37e-40 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 138.84 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 25 FSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---GIVFQEPRLFPWLNVLDNVMLGLA 101
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQrpvSMLFQENNLFAHLTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 102 DEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQ 181
Cdd:TIGR01277 97 PGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 695804877 182 RAGTTTLLVTHDVEEAVALADRVVVLSprPGRIREV 217
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAIASQIAVVS--QGKIKVV 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-216 |
3.12e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 139.77 E-value: 3.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING-----EPVTGVGKERGIVFQEP-RLFPWLNVLD 94
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVWDVRRQVGMVFQNPdNQFVGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 95 NVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRhtlqQ 174
Cdd:PRK13635 102 DVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR----R 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695804877 175 ELL----QIHQRAGTTTLLVTHDVEEAvALADRVVVLspRPGRIRE 216
Cdd:PRK13635 178 EVLetvrQLKEQKGITVLSITHDLDEA-AQADRVIVM--NKGEILE 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-215 |
4.30e-40 |
|
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: 137.57 E-value: 4.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 18 QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE----RGIVF--QEPRLFPWLN 91
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHerarAGIGYvpEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLGL-ADEKLSRAAKRQRALEMLERvqLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRH 170
Cdd:cd03224 92 VEENLLLGAyARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695804877 171 TLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLspRPGRIR 215
Cdd:cd03224 170 EIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVL--ERGRVV 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-216 |
6.27e-40 |
|
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: 144.06 E-value: 6.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 13 RKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLEsATQGDICINGEPVTGVGKERG--------IVFQEP 84
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALrplrrrmqVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 85 --RLFPWLNVLDNVMLGLA--DEKLSRAAKRQRALEMLERVQLS-EFVNALPAQLSGGMAQRVAIARGLVARPQILMLDE 159
Cdd:COG4172 372 fgSLSPRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 160 PFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVeeAV--ALADRVVVLspRPGRIRE 216
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQREHGLAYLFISHDL--AVvrALAHRVMVM--KDGKVVE 506
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
10-218 |
7.68e-40 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 137.22 E-value: 7.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---------GIV 80
Cdd:PRK10584 14 KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrakhvGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:PRK10584 94 FQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 161 FGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAvALADRVVVLspRPGRIREVV 218
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRL--VNGQLQEEA 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-213 |
9.32e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 143.24 E-value: 9.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 2 TSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT----GVGKER 77
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirspRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 GI--VFQEPRLFPWLNVLDNVMLGLADEK---LSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARP 152
Cdd:COG3845 81 GIgmVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 153 QILMLDEPFGALdaltrhTLQ--QELLQIHQR---AGTTTLLVTHDVEEAVALADRVVVLspRPGR 213
Cdd:COG3845 161 RILILDEPTAVL------TPQeaDELFEILRRlaaEGKSIIFITHKLREVMAIADRVTVL--RRGK 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-220 |
1.10e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 136.87 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG---------KERGIVFQEPRLFPWLNV 92
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaelrnQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 93 LDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTL 172
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695804877 173 QQELLQIHQRAGTTTLLVTHDVEeavaLADRVV-VLSPRPGRIREVVSL 220
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQ----LAKRMSrQLEMRDGRLTAELSL 229
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
21-214 |
1.30e-38 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 135.98 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT----GVGKERGIVFQEPRLFPWLNVLDNV 96
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVreprKVRRSIGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 MLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQEL 176
Cdd:TIGR01188 88 EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 695804877 177 LQIhQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:TIGR01188 168 RAL-KEEGVTILLTTHYMEEADKLCDRIAII--DHGRI 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-208 |
2.26e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.73 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHvrkSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING-----EPVTGVGKERGIVF 81
Cdd:PRK13632 13 VSFSY---PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEP-RLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:PRK13632 90 QNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDES 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695804877 161 FGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVaLADRVVVLS 208
Cdd:PRK13632 170 TSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFS 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-207 |
5.17e-38 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 132.80 E-value: 5.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 18 QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE----RGIVF--QEPRLFPWLN 91
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriarLGIGYvpEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLG--LADEKLSRAAKRQRALEMLERvqLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTR 169
Cdd:COG0410 95 VEENLLLGayARRDRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 695804877 170 HTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:COG0410 173 EEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVL 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-216 |
9.10e-38 |
|
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: 138.28 E-value: 9.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHV----RKSWQQVTALQNFSLDIAAGELVALVGSSGCGKS----TLLRMLVGLESATQGDICINGEPVTG 72
Cdd:COG4172 1 MMSMPLLSVEDLsvafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 73 V---------GKERGIVFQEP--RLFPWLNVLDNVMLGLA-DEKLSRAAKRQRALEMLERVQLSE---FVNALPAQLSGG 137
Cdd:COG4172 81 LserelrrirGNRIAMIFQEPmtSLNPLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 138 MAQRVAIARGLVARPQILMLDEPFGALDAltrhTLQQELLQ----IHQRAGTTTLLVTHD---VEEavaLADRVVVLspR 210
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDV----TVQAQILDllkdLQRELGMALLLITHDlgvVRR---FADRVAVM--R 231
|
....*.
gi 695804877 211 PGRIRE 216
Cdd:COG4172 232 QGEIVE 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-208 |
1.03e-37 |
|
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: 131.90 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-KER---GIVF--QE 83
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRarlGIGYlpQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695804877 164 LDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIY 207
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
13-216 |
1.27e-37 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 132.62 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 13 RKSWQQVtaLQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT--------GVGKERGIVFQEP 84
Cdd:TIGR02769 20 AKQRAPV--LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldrkqrrAFRRDVQLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 85 rlFPWLNVLDNVMLGLAD-----EKLSRAAKRQRALEMLERVQL-SEFVNALPAQLSGGMAQRVAIARGLVARPQILMLD 158
Cdd:TIGR02769 98 --PSAVNPRMTVRQIIGEplrhlTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 159 EPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIRE 216
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMD--KGQIVE 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-217 |
2.30e-37 |
|
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: 131.12 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSW---QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-----KERG 78
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlrwlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRLFPwLNVLDNVMLGLADEKLS---RAAKRQRAlemlervqlSEFVNALP-----------AQLSGGMAQRVAI 144
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKPDATDEeveEAAKKANI---------HDFIMSLPdgydtlvgergSQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695804877 145 ARGLVARPQILMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDVeEAVALADRVVVLSprPGRIREV 217
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRL-STIRNADLIAVLQ--NGQVVEQ 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
7-225 |
4.05e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 131.78 E-value: 4.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHvrKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT--GVGKER---GIVF 81
Cdd:PRK13650 10 LTFKY--KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRhkiGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEP-RLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIArGLVA-RPQILMLDE 159
Cdd:PRK13650 88 QNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA-GAVAmRPKIIILDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 160 PFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEaVALADRVVVL---------SPRP--GRIREVVSLALPHP 225
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMkngqvestsTPRElfSRGNDLLQLGLDIP 242
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
7-207 |
2.09e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 130.14 E-value: 2.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVT-----ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---- 77
Cdd:PRK13634 3 ITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 -----GIVFQ--EPRLFPwLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNAL-PAQLSGGMAQRVAIARGLV 149
Cdd:PRK13634 83 lrkkvGIVFQfpEHQLFE-ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 150 ARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-207 |
2.55e-36 |
|
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: 126.40 E-value: 2.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVtgvgkergivfqeprlfpw 89
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 90 lnvldnvmlgladEKLSRAAK-RQRAL--EMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:cd03214 64 -------------ASLSPKELaRKIAYvpQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695804877 167 ltRHtlQQELLQI----HQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:cd03214 131 --AH--QIELLELlrrlARERGKTVVMVLHDLNLAARYADRVILL 171
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-216 |
3.07e-36 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 127.33 E-value: 3.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---GIVFQE 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALrriGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLGLadekLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:cd03268 81 PGFYPNLTARENLRLLA----RLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695804877 164 LDALTRHTLQQeLLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:cd03268 157 LDPDGIKELRE-LILSLRDQGITVLISSHLLSEIQKVADRIGII--NKGKLIE 206
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-221 |
5.04e-36 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 130.62 E-value: 5.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIA----AGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGK------ER---GIVFQEPRLFP 88
Cdd:TIGR02142 9 LGDFSLDADftlpGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKgiflppEKrriGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 89 WLNVLDNVMLGLadeKLSRAAKRQRALE-MLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDAL 167
Cdd:TIGR02142 89 HLSVRGNLRYGM---KRARPSERRISFErVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 168 TRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREVVSLA 221
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL--EDGRVAAAGPIA 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-207 |
6.41e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 128.63 E-value: 6.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-------VGKERGIVFQEP--RLFPWLN 91
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvklsdIRKKVGLVFQYPeyQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLD----NVMLGLADEKLSRAAKRqrALEMlerVQLS--EFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALD 165
Cdd:PRK13637 102 EKDiafgPINLGLSEEEIENRVKR--AMNI---VGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 166 ALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-208 |
2.30e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 125.91 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGV-----GKeRGIVF--Q 82
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkrAR-LGIGYlpQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:COG1137 86 EASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695804877 163 ALDALTRHTLQQELLQIHQR-AGtttLLVT-HDVEEAVALADRVVVLS 208
Cdd:COG1137 166 GVDPIAVADIQKIIRHLKERgIG---VLITdHNVRETLGICDRAYIIS 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-223 |
2.41e-35 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 132.54 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 4 STLVSFRHVRKSWQ----QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-- 77
Cdd:PRK10535 2 TALLELKDIRRSYPsgeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 -------GIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVA 150
Cdd:PRK10535 82 qlrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 151 RPQILMLDEPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAvALADRVV-------VLSPRPGRIREVVSLALP 223
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIeirdgeiVRNPPAQEKVNVAGGTEP 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-207 |
2.46e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 129.77 E-value: 2.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG---------KERGIVFQEPRLFPWLN 91
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHT 171
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190
....*....|....*....|....*....|....*.
gi 695804877 172 LQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-214 |
4.69e-35 |
|
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: 124.62 E-value: 4.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSW--QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING------EPVTgVGKERG 78
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqlDPAD-LRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRLFpWLNVLDNVMLGladeklSRAAKRQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAIARG 147
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLG------APLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 148 LVARPQILMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDVeEAVALADRVVVLspRPGRI 214
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRP-SLLDLVDRIIVM--DSGRI 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-207 |
9.39e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 125.71 E-value: 9.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 18 QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG---------VGKERGIVFQ--EPRL 86
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknlkkLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 FPwLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSE-FVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALD 165
Cdd:PRK13641 99 FE-NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 166 ALTRHTLQQeLLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13641 178 PEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-215 |
1.19e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.46 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 18 QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----VGKERGIVFQEPRL-FPWLn 91
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspweLARRRAVLPQHSSLaFPFT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLV-------ARPQILMLDEPFGAL 164
Cdd:COG4559 92 VEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 165 DalTRHtlQQELLQI---HQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIR 215
Cdd:COG4559 172 D--LAH--QHAVLRLarqLARRGGGVVAVLHDLNLAAQYADRILLL--HQGRLV 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-209 |
1.26e-34 |
|
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: 123.70 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTssTLVSFRHVRKSW-------QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICIN--GEPVT 71
Cdd:COG4778 1 MT--TLLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 72 GVG-----------KERGIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNAL-PAQLSGGMA 139
Cdd:COG4778 79 LAQaspreilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 140 QRVAIARGLVARPQILMLDEPFGALDALTRHTLqQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSP 209
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVV-VELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-226 |
2.12e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 123.73 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----VGKERGIVFQEP 84
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaeLARRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 85 RL-FPWLnVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLV------ARPQILML 157
Cdd:PRK13548 86 SLsFPFT-VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 158 DEPFGALDalTRHtlQQELLQI-HQRA---GTTTLLVTHDVEEAVALADRVVVL---------SP----RPGRIREVVSL 220
Cdd:PRK13548 165 DEPTSALD--LAH--QHHVLRLaRQLAherGLAVIVVLHDLNLAARYADRIVLLhqgrlvadgTPaevlTPETLRRVYGA 240
|
....*....
gi 695804877 221 AL---PHPR 226
Cdd:PRK13548 241 DVlvqPHPE 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-207 |
2.29e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 125.46 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 17 QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--------GIVFQEPrlFP 88
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrqkiQIVFQNP--YG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 89 WLNVLDNVMLGLAD-----EKLSRAAKRQRALEMLERVQL-SEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:PRK11308 104 SLNPRKKVGQILEEpllinTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695804877 163 ALDALTRHT-------LQQELlqihqraGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK11308 184 ALDVSVQAQvlnlmmdLQQEL-------GLSYVFISHDLSVVEHIADEVMVM 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-216 |
4.21e-34 |
|
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: 122.72 E-value: 4.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQ-VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-----KERGIV 80
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldslrRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEPRLFpwlN--VLDNVMLG---LADEKLSRAAKrqralemleRVQLSEFVNALPAQ-----------LSGGMAQRVAI 144
Cdd:cd03253 81 PQDTVLF---NdtIGYNIRYGrpdATDEEVIEAAK---------AAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 145 ARGLVARPQILMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDVEEAVAlADRVVVLSprPGRIRE 216
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLK--DGRIVE 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-214 |
4.49e-34 |
|
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: 122.89 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 4 STLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQG-DICINGEPVTGVG----KER- 77
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDvwelRKRi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 GIV---FQEpRLFPWLNVLDNVMLGLAD-----EKLSrAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLV 149
Cdd:COG1119 81 GLVspaLQL-RFPRDETVLDVVLSGFFDsiglyREPT-DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 150 ARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGRV 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-214 |
6.78e-34 |
|
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: 119.84 E-value: 6.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGvgkergivfqeprl 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 fpwlnvldnvmlgladekLSRAAKRQRALEMLervqlsefvnalpAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:cd03216 67 ------------------ASPRDARRAGIAMV-------------YQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695804877 167 LTRHTLQQELLQIhQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:cd03216 116 AEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVL--RDGRV 160
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-207 |
1.59e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 122.04 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 5 TLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL---ESATQGDICINGEPVTGVGK------ 75
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlardir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 76 ----ERGIVFQEPRLFPWLNVLDNVMLG-LADEKLSRA-------AKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVA 143
Cdd:PRK09984 83 ksraNTGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695804877 144 IARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-208 |
2.57e-33 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 119.61 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 11 HVRKSWQQVTALQNFSLDIAAGeLVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE-RGIVF---QEPRL 86
Cdd:cd03264 5 NLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGylpQEFGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 FPWLNVLDNV-----MLGLADEKLsraakRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:cd03264 84 YPNFTVREFLdyiawLKGIPSKEV-----KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695804877 162 GALDALTRHTLqQELLQiHQRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:cd03264 159 AGLDPEERIRF-RNLLS-ELGEDRIVILSTHIVEDVESLCNQVAVLN 203
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-207 |
3.67e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 119.28 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSwqqvTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTgvGKER----GIVFQ 82
Cdd:cd03226 5 ISFSYKKGT----EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKERrksiGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPR--LFPwLNVLDNVMLGLADeklsRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:cd03226 79 DVDyqLFT-DSVREELLLGLKE----LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695804877 161 FGALDaltRHTLQQ--ELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:cd03226 154 TSGLD---YKNMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-216 |
4.45e-33 |
|
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: 120.03 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQ--QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-----KERGI 79
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPWlNVLDNVMLGLADeklsraAKRQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAIARGL 148
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGRPG------ATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 149 VARPQILMLDEPFGALDALTRHTLQQELLQIHQraGTTTLLVTHDVeEAVALADRVVVLSprPGRIRE 216
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRL-STIENADRIVVLE--DGKIVE 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-215 |
4.66e-33 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 119.39 E-value: 4.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 8 SFRHVRKSWQqvtALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING-----EPVTgVGKERGIVFQ 82
Cdd:cd03266 10 RFRDVKKTVQ---AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAE-ARRRLGFVSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:cd03266 86 STGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695804877 163 ALDALTRHTLqQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIR 215
Cdd:cd03266 166 GLDVMATRAL-REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLH--RGRVV 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-207 |
7.83e-33 |
|
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: 124.71 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGV-----GKERGIVFQEPRLFPWlNVLDN 95
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdadswRDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 96 VMLGLADEKlsrAAKRQRAlemLERVQLSEFVNALP-----------AQLSGGMAQRVAIARGLVARPQILMLDEPFGAL 164
Cdd:TIGR02857 416 IRLARPDAS---DAEIREA---LERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695804877 165 DALTRHTLQQELLQIHQraGTTTLLVTHDvEEAVALADRVVVL 207
Cdd:TIGR02857 490 DAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-207 |
2.52e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 119.91 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG---VGKER-G 78
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSrarHARQRvG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLD 158
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695804877 159 EPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVI 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-216 |
3.20e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 117.93 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 5 TLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQG-----DICINGEPVTGVGKER-- 77
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKGLir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 ------GIVFQEPRLFPWLNVLDNVMLG-LADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVA 150
Cdd:PRK11264 82 qlrqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 151 RPQILMLDEPFGALDAltrhTLQQELLQ-IHQRA--GTTTLLVTHDVEEAVALADRVVVLSprPGRIRE 216
Cdd:PRK11264 162 RPEVILFDEPTSALDP----ELVGEVLNtIRQLAqeKRTMVIVTHEMSFARDVADRAIFMD--QGRIVE 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-216 |
3.46e-32 |
|
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: 117.33 E-value: 3.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSW-QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIV 80
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrsmiGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEPRLFPWlNVLDNVMLGladeklSRAAKRQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAIARGLV 149
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 150 ARPQILMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDVeEAVALADRVVVLspRPGRIRE 216
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRL-STIKNADKILVL--DDGKIIE 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-202 |
8.84e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 117.56 E-value: 8.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--- 77
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 -----GIVFQEPRLFPWLNVLDNVMLGLADE-KLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVAR 151
Cdd:PRK11831 82 vrkrmSMLFQSGALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695804877 152 PQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALAD 202
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-214 |
2.20e-31 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 115.51 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 12 VRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEpVTGVGKER-----GIVF-QEPR 85
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKflrriGVVFgQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 86 LFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALD 165
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695804877 166 ALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRI 214
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID--KGRL 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-216 |
3.08e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.84 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERG---- 78
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 --------------IVFQEPRLFPWLNVLDNVM------LGladekLSRAAKRQRALEMLERVQLSEFVNA-LPAQLSGG 137
Cdd:PRK10619 82 adknqlrllrtrltMVFQHFNLWSHMTVLENVMeapiqvLG-----LSKQEARERAVKYLAKVGIDERAQGkYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 138 MAQRVAIARGLVARPQILMLDEPFGALDAltrhTLQQELLQIHQR---AGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQlaeEGKTMVVVTHEMGFARHVSSHVIFL--HQGKI 230
|
..
gi 695804877 215 RE 216
Cdd:PRK10619 231 EE 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-207 |
3.09e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.44 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHVRKSWQ--QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL---ESATQGDICINGEPVTG----- 72
Cdd:PRK13640 2 KDNIVEFKHVSFTYPdsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktvwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 73 VGKERGIVFQEP-RLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVAR 151
Cdd:PRK13640 82 IREKVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 152 PQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAvALADRVVVL 207
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVL 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-207 |
3.74e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.48 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDicingepVTGVGKER-GIVFQ---EPRLFPwLNVLDN 95
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT-------VRRAGGARvAYVPQrseVPDSLP-LTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 96 VMLGL-ADEKLSR---AAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHT 171
Cdd:NF040873 78 VAMGRwARRGLWRrltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 695804877 172 LQQELLQIHqRAGTTTLLVTHDvEEAVALADRVVVL 207
Cdd:NF040873 158 IIALLAEEH-ARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-207 |
6.57e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 115.23 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSWQQVTA--LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----V 73
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnfekL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 74 GKERGIVFQEP-RLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARP 152
Cdd:PRK13648 82 RKHIGIVFQNPdNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 153 QILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVAlADRVVVL 207
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVM 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-207 |
7.48e-31 |
|
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: 113.72 E-value: 7.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVtaLQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVF 81
Cdd:cd03248 17 VTFAYPTRPDTLV--LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlhskvSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPwLNVLDNVMLGLAD---EKLSRAAKRQRALEMLERVQL--SEFVNALPAQLSGGMAQRVAIARGLVARPQILM 156
Cdd:cd03248 95 QEPVLFA-RSLQDNIAYGLQScsfECVKEAAQKAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695804877 157 LDEPFGALDALTRHTLQQELLQIHQRagTTTLLVTHDVeEAVALADRVVVL 207
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRL-STVERADQILVL 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-216 |
8.05e-31 |
|
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: 114.12 E-value: 8.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQ--QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GI 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWlrrqvGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPwLNVLDNVmlGLADEklsrAAKRQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAIARGL 148
Cdd:cd03252 81 VLQENVLFN-RSIRDNI--ALADP----GMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 149 VARPQILMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDVeEAVALADRVVVLSprPGRIRE 216
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRL-STVKNADRIIVME--KGRIVE 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-207 |
1.04e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 116.08 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG---VGKER-G 78
Cdd:PRK13536 38 STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArarLARARiG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLD 158
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695804877 159 EPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVL 245
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-207 |
1.06e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.83 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----VGKERGIVFQEP--RLFPwLNVL 93
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAenekwVRSKVGLVFQDPddQVFS-STVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 94 DNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQ 173
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190
....*....|....*....|....*....|....
gi 695804877 174 QELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13647 179 EILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVL 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-208 |
1.44e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.40 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT-------GVGKERGIVFQEP--RLF-Pwl 90
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllEVRKTVGIVFQNPddQLFaP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 91 NVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRH 170
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 695804877 171 TLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:PRK13639 175 QIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMS 211
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-220 |
5.78e-30 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 111.69 E-value: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL----ESATQGDICINGEPVTGV---GKERGIVFQEPR--LFPWLN 91
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLsirGRHIATIMQNPRtaFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLGL-ADEKLSRAAkRQRALEMLERVQLSEFVNAL---PAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDAL 167
Cdd:TIGR02770 81 MGNHAIETLrSLGKLSKQA-RALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695804877 168 TRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIREVVSL 220
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMD--DGRIVERGTV 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-214 |
6.24e-30 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 110.21 E-value: 6.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT----GVGKERGIVF-QEPR----LFPWLN 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrspRDAIRAGIAYvPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVmlgladeklsraakrqralemlervqlsefvnALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHT 171
Cdd:cd03215 95 VAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695804877 172 LQQELLQIhQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:cd03215 143 IYRLIREL-ADAGKAVLLISSELDELLGLCDRILVM--YEGRI 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
9-223 |
6.79e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.88 E-value: 6.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 9 FRHVRKSwqQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----VGKERGIVFQE 83
Cdd:PRK13642 12 FKYEKES--DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenvwnLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 P-RLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:PRK13642 90 PdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695804877 163 ALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAvALADRVVVLsprpgRIREVVSLALP 223
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVM-----KAGEIIKEAAP 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
7-207 |
7.07e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.53 E-value: 7.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVT-----ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG--------- 72
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 73 VGKERGIVFQ--EPRLFPWlNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSE-FVNALPAQLSGGMAQRVAIARGLV 149
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 150 ARPQILMLDEPFGALDALTRHTLQQELLQIHQrAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVL 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-203 |
1.41e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.41 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL-----ESATQGDICINGEPVTG-------VGKERGIVFQEPRLFP 88
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSprtdtvdLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 89 wLNVLDNVMLGLA------DEKLSRAAKRQ-RALEMLERVQLSEFVNALpaQLSGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:PRK14239 100 -MSIYENVVYGLRlkgikdKQVLDEAVEKSlKGASIWDEVKDRLHDSAL--GLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 162 GALDALTRHTLQQELLQIHQRagTTTLLVTHDVEEAVALADR 203
Cdd:PRK14239 177 SALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDR 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-216 |
1.87e-29 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 115.69 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQ-QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE--R---GIV 80
Cdd:COG5265 358 VRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRaaiGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEPRLFpwlN--VLDNVMLGLAD---EKLSRAAKRqralemlerVQLSEFVNALPAQ-----------LSGGMAQRVAI 144
Cdd:COG5265 438 PQDTVLF---NdtIAYNIAYGRPDaseEEVEAAARA---------AQIHDFIESLPDGydtrvgerglkLSGGEKQRVAI 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 145 ARGLVARPQILMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDVeEAVALADRVVVLspRPGRIRE 216
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRL-STIVDADEILVL--EAGRIVE 572
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-207 |
1.93e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 111.75 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVT-----ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--- 77
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 ------GIVFQEP--RLFPWlNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLS-EFVNALPAQLSGGMAQRVAIARGL 148
Cdd:PRK13643 81 pvrkkvGVVFQFPesQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 149 VARPQILMLDEPFGALDALTRHTLQQELLQIHQrAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-217 |
3.78e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.42 E-value: 3.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--- 77
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 --GIVFQEPRLFPwLNVLDNVMLGLADEKlsRAAKRQRALEMLERVQLSE-FVNALPAQLSGGMAQRVAIARGLVARPQI 154
Cdd:PRK10247 82 qvSYCAQTPTLFG-DTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695804877 155 LMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEaVALADRVVVLSPRPGRIREV 217
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGEMQEA 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-193 |
4.92e-29 |
|
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: 113.99 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 9 FRHVRKSW-QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE---RGIVF--Q 82
Cdd:TIGR02868 337 LRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevrRRVSVcaQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLFPwLNVLDNVMLGLADeklsraAKRQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAIARGLVAR 151
Cdd:TIGR02868 417 DAHLFD-TTVRENLRLARPD------ATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 152 PQILMLDEPFGALDALTRHTLQQELLQIHQraGTTTLLVTHD 193
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-207 |
6.24e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 110.95 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 8 SFRH-VRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING-EPVtgvgKER-------G 78
Cdd:COG4586 23 ALKGlFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPF----KRRkefarriG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVF-QEPRLFPWLNVLDNVMLgLAD-EKLSRAAKRQRALEMLERVQLSEFVNAlPA-QLSGGmaQRVaiaRG-LVA---- 150
Cdd:COG4586 99 VVFgQRSQLWWDLPAIDSFRL-LKAiYRIPDAEYKKRLDELVELLDLGELLDT-PVrQLSLG--QRM---RCeLAAallh 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 151 RPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVI 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-207 |
6.35e-29 |
|
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: 108.33 E-value: 6.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEpvtgvgkeRGIVFQEPrl 86
Cdd:cd03250 6 ASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQEP-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 fpWL---NVLDNVMLGLA-DEklsraakrQRALEMLERVQLSEFVNALPAQ-----------LSGGMAQRVAIARGLVAR 151
Cdd:cd03250 76 --WIqngTIRENILFGKPfDE--------ERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 152 PQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVeEAVALADRVVVL 207
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVL 200
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-207 |
1.16e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 113.40 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 15 SWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLeSATQGDICINGEPVTGVGKER-----GIVFQEPRLFPW 89
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrkhlSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 90 lNVLDNVMLG---LADEKLSRAakrqralemLERVQLSEFVNALP-----------AQLSGGMAQRVAIARGLVARPQIL 155
Cdd:PRK11174 438 -TLRDNVLLGnpdASDEQLQQA---------LENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695804877 156 MLDEPFGALDALTRHTLQQELLQIHQraGTTTLLVTHDVEEaVALADRVVVL 207
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLED-LAQWDQIWVM 556
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-207 |
1.18e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.97 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLL----RMLVGLESA-TQGDICINGE-------PVTGVGKERGIVFQEPRLFP 88
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMNDLIPGArVEGEILLDGEdiydpdvDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 89 wLNVLDNVMLGLAD-EKLSRAAKRQRALEMLERVQLSEFV----NALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:COG1117 106 -KSIYDNVAYGLRLhGIKSKSELDEIVEESLRKAALWDEVkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695804877 164 LDALTrhTLQQELLqIHQRAGTTT-LLVTHDVEEAVALADRVVVL 207
Cdd:COG1117 185 LDPIS--TAKIEEL-ILELKKDYTiVIVTHNMQQAARVSDYTAFF 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-207 |
1.36e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 108.54 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER----GIV--FQEPRLFPWLNVLD 94
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarmGVVrtFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 95 NVML------------GLADEKLSRAAKRQ---RALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDE 159
Cdd:PRK11300 100 NLLVaqhqqlktglfsGLLKTPAFRRAESEaldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695804877 160 PFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-208 |
1.38e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.44 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 14 KSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG----KERGIVF--QEPRLF 87
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlharARRGIGYlpQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 88 PWLNVLDNVMLGLA-DEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:PRK10895 91 RRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 167 LTRHTLQQeLLQIHQRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:PRK10895 171 ISVIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVS 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-207 |
1.63e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.63 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 18 QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVFQEPRL--FPWL 90
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKrakyiGRVFQDPMMgtAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 91 NVLDNvmLGLADEK-----LSRA---AKRQRALEMLERVQLS-EfvNALPAQ---LSGGmaQRVAIArgLV----ARPQI 154
Cdd:COG1101 98 TIEEN--LALAYRRgkrrgLRRGltkKRRELFRELLATLGLGlE--NRLDTKvglLSGG--QRQALS--LLmatlTKPKL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695804877 155 LMLDEPFGALD--------ALTRhtlqqellQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:COG1101 170 LLLDEHTAALDpktaalvlELTE--------KIVEENNLTTLMVTHNMEQALDYGNRLIMM 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-207 |
1.73e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 110.18 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 14 KSW-----QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG--------KERGIV 80
Cdd:PRK15079 24 KQWfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddewravrSDIQMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEP--RLFPWLNVLDNVM--LGLADEKLSRAAKRQRALEMLERVQL-SEFVNALPAQLSGGMAQRVAIARGLVARPQIL 155
Cdd:PRK15079 104 FQDPlaSLNPRMTIGEIIAepLRTYHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 156 MLDEPFGALDAltrhTLQQE---LLQIHQRA-GTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK15079 184 ICDEPVSALDV----SIQAQvvnLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-208 |
2.26e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 107.27 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSW---QQvtALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-------- 74
Cdd:PRK10908 1 MIRFEHVSKAYlggRQ--ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrevpflr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 75 KERGIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQI 154
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 155 LMLDEPFGALD-ALTRHTLQqeLLQIHQRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:PRK10908 159 LLADEPTGNLDdALSEGILR--LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-207 |
4.38e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.31 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL-----ESATQGDICINGE-----PVTGVGKE 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQdifkmDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 77 RGIVFQEPRLFPWLNVLDNVMLGLADEKL--SRAAKRQRALEMLERVQLSEFV----NALPAQLSGGMAQRVAIARGLVA 150
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVkdrlDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 151 RPQILMLDEPFGALDAltRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK14247 164 QPEVLLADEPTANLDP--ENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFL 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-214 |
5.63e-28 |
|
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: 111.05 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 19 VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICIN-GEP--------VTGVGKER---GIVFQEPRL 86
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdmtkpgPDGRGRAKryiGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 FPWLNVLDN----VMLGLADEklsraAKRQRALEMLERVQLSE-----FVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:TIGR03269 377 YPHRTVLDNlteaIGLELPDE-----LARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 158 DEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDGKI 506
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-207 |
1.32e-27 |
|
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: 103.84 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVFQEPRLFPWlNVLDNV 96
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhvGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 mlgladeklsraakrqralemlervqlsefvnalpaqLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQEL 176
Cdd:cd03246 97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|.
gi 695804877 177 LQIhQRAGTTTLLVTHDvEEAVALADRVVVL 207
Cdd:cd03246 140 AAL-KAAGATRIVIAHR-PETLASADRILVL 168
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-208 |
1.52e-27 |
|
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: 105.30 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE----RGI--VFQE 83
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHerarAGIayVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLGLAdekLSRAAKRQRALEMLERVQ-LSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:TIGR03410 84 REIFPRLTVEENLLTGLA---ALPRRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695804877 163 ALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVME 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-193 |
1.53e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 9 FRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGepvtgvGKERGIVFQEPRLFP 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLRIGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 89 WLNVLDNVMLGLA-------------------DEKLSRAAKRQ-------------RALEMLERVQLSEFV-NALPAQLS 135
Cdd:COG0488 75 DLTVLDTVLDGDAelraleaeleeleaklaepDEDLERLAELQeefealggweaeaRAEEILSGLGFPEEDlDRPVSELS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 136 GGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELlqiHQRAGtTTLLVTHD 193
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL---KNYPG-TVLVVSHD 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-207 |
1.56e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.69 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL-----ESATQGDICINGEPVTG-------VGKERGIVFQEPRLFPW 89
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSpdvdpieVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 90 LNVLDNVMLGLADEKLSRAAKR--QRALEMLERVQLSEFV----NALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALWDEVkdrlNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695804877 164 LDALTRHTLQQELLQIhqRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK14267 180 IDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFL 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-207 |
1.86e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 106.33 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVR-KSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING------EPVTGV 73
Cdd:PRK13633 4 MIKCKNVSYKYESnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 74 GKERGIVFQEPRlfpwlN------VLDNVMLGlaDEKLSRAAK--RQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIA 145
Cdd:PRK13633 84 RNKAGMVFQNPD-----NqivatiVEEDVAFG--PENLGIPPEeiRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 146 RGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVAlADRVVVL 207
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVM 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-214 |
3.53e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.57 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT----GVGKERGIVF-QEPR----LFPWLN 91
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirspRDAIRAGIAYvPEDRkgegLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLGLADEK-----LSRAAKRQRALEMLERVQL---SefVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPfga 163
Cdd:COG1129 347 IRENITLASLDRLsrgglLDRRRERALAEEYIKRLRIktpS--PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP--- 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695804877 164 ldalTR----------HTLQQELLqihqRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:COG1129 422 ----TRgidvgakaeiYRLIRELA----AEGKAVIVISSELPELLGLSDRILVM--REGRI 472
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-216 |
8.51e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 108.12 E-value: 8.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQ-QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GI 79
Cdd:PRK13657 334 AVEFDDVSFSYDnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrrniAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPwLNVLDNVMLGLAD---EKLSRAAKRQRALEMLERVQ--LSEFVNALPAQLSGGMAQRVAIARGLVARPQI 154
Cdd:PRK13657 414 VFQDAGLFN-RSIEDNIRVGRPDatdEEMRAAAERAQAHDFIERKPdgYDTVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 155 LMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDVeEAVALADRVVVLSprPGRIRE 216
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRL-STVRNADRILVFD--NGRVVE 549
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-208 |
1.41e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 4 STLVSFRHVRKSWQQVT-ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV----TGVGKER- 77
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 --GIVFQEP--RLFPwLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQ 153
Cdd:PRK13636 83 svGMVFQDPdnQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 154 ILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMK 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-213 |
1.49e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 106.94 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL--ESATQGDICINGEPVTGVG----KE 76
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNirdtER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 77 RGIV--FQEPRLFPWLNVLDNVMLGladEKLSR------AAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGL 148
Cdd:PRK13549 82 AGIAiiHQELALVKELSVLENIFLG---NEITPggimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 149 VARPQILMLDEPFGAL-DALTRHTLqqELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGR 213
Cdd:PRK13549 159 NKQARLLILDEPTASLtESETAVLL--DIIRDLKAHGIACIYISHKLNEVKAISDTICVI--RDGR 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-207 |
1.57e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 101.24 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSW--QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER----GIV 80
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALssliSVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 FQEPRLFpwlnvldNVMLGladeklsraakrqralemlervqlsefvNALPAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:cd03247 81 NQRPYLF-------DTTLR----------------------------NNLGRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695804877 161 FGALDALTrhtlQQELLQI--HQRAGTTTLLVTHDVeEAVALADRVVVL 207
Cdd:cd03247 126 TVGLDPIT----ERQLLSLifEVLKDKTLIWITHHL-TGIEHMDKILFL 169
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-216 |
4.57e-26 |
|
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: 101.03 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHV--RKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GI 79
Cdd:cd03244 3 IEFKNVslRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrsriSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPW---LNvLDnvMLGLA-DEKLSRAakrqralemLERVQLSEFVNALP-----------AQLSGGMAQRVAI 144
Cdd:cd03244 83 IPQDPVLFSGtirSN-LD--PFGEYsDEELWQA---------LERVGLKEFVESLPggldtvveeggENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 145 ARGLVARPQILMLDEPFGALDALTRHTLQQeLLQiHQRAGTTTLLVTHDVeEAVALADRVVVLSprPGRIRE 216
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQK-TIR-EAFKDCTVLTIAHRL-DTIIDSDRILVLD--KGRVVE 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-216 |
8.02e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.57 E-value: 8.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSW-----QQVtaLQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----VGK 75
Cdd:TIGR00958 478 LIEFQDVSFSYpnrpdVPV--LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhyLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 76 ERGIVFQEPRLFPWlNVLDNVMLGLA---DEKLSRAAKRQRAlemlervqlSEFVNALP-----------AQLSGGMAQR 141
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYGLTdtpDEEIMAAAKAANA---------HDFIMEFPngydtevgekgSQLSGGQKQR 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 142 VAIARGLVARPQILMLDEPFGALDALTRHTLQQEllqiHQRAGTTTLLVTHDVeEAVALADRVVVLspRPGRIRE 216
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQES----RSRASRTVLLIAHRL-STVERADQILVL--KKGSVVE 693
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-216 |
8.93e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.17 E-value: 8.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKST----LLRMLvglesATQGDICINGEPVTGVGKER--------GIVFQEPR-- 85
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQllpvrhriQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 86 LFPWLNVLDNVMLGLA--DEKLSRAAKRQRALEMLERVQLS-EFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 163 ALDALTRH---TLQQELLQIHQRAgttTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:PRK15134 455 SLDKTVQAqilALLKSLQQKHQLA---YLFISHDLHVVRALCHQVIVL--RQGEVVE 506
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-216 |
9.70e-26 |
|
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: 105.18 E-value: 9.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHV--RKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT-----GVGKERG 78
Cdd:TIGR02203 330 DVEFRNVtfRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdytlaSLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRLFPwLNVLDNVMLGLADEklsraAKRQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAIARG 147
Cdd:TIGR02203 410 LVSQDVVLFN-DTIANNIAYGRTEQ-----ADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 148 LVARPQILMLDEPFGALDALTRHTLQQELLQIHQraGTTTLLVTHDVeEAVALADRVVVLSprPGRIRE 216
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRL-STIEKADRIVVMD--DGRIVE 547
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-207 |
1.79e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 102.26 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 27 LDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEpvTGVGKERGI-----------VFQEPRLFPWLNVLDN 95
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR--VLFDAEKGIclppekrrigyVFQDARLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 96 VMLGLADeklSRAAKRQRALEMLErvqLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDaLTRhtlQQE 175
Cdd:PRK11144 97 LRYGMAK---SMVAQFDKIVALLG---IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPR---KRE 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 695804877 176 LLQIHQRAG----TTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK11144 167 LLPYLERLAreinIPILYVSHSLDEILRLADRVVVL 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
7-219 |
2.14e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVT-----ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG--------- 72
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 73 VGKERGIVFQ--EPRLFPwLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNAL-PAQLSGGMAQRVAIARGLV 149
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFE-DTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 150 ARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIREVVS 219
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM--KEGSIVSQTS 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-235 |
2.46e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.24 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL----ESA-TQGDICING--------EPVTgVGKERGIVFQEPRLF 87
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndliPGFrVEGKVTFHGknlyapdvDPVE-VRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 88 PwLNVLDNVMLGL--------ADEKLSRAAkRQRAL--EMLERVQLSEFvnalpaQLSGGMAQRVAIARGLVARPQILML 157
Cdd:PRK14243 104 P-KSIYDNIAYGAringykgdMDELVERSL-RQAALwdEVKDKLKQSGL------SLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 158 DEPFGALDALTrhTLQQELLqIHQ-RAGTTTLLVTHDVEEAVALADRV----VVLSPRPGRIREVV-----SLALPHPRQ 227
Cdd:PRK14243 176 DEPCSALDPIS--TLRIEEL-MHElKEQYTIIIVTHNMQQAARVSDMTaffnVELTEGGGRYGYLVefdrtEKIFNSPQQ 252
|
....*...
gi 695804877 228 RDDAAFIA 235
Cdd:PRK14243 253 QATRDYVS 260
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-213 |
3.92e-25 |
|
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: 102.98 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL--ESATQGDICINGEPVTGVG----KERGI 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNirdtERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VF--QEPRLFPWLNVLDNVMLG----LADEKLSRAAKRQRALEMLERVQLSEFVNALP-AQLSGGMAQRVAIARGLVARP 152
Cdd:TIGR02633 81 VIihQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695804877 153 QILMLDEPFGALDALTRHTLqQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGR 213
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEIL-LDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI--RDGQ 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-216 |
6.98e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.48 E-value: 6.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHV----RKSWQQVTALQNFSLDIAAGELVALVGSSGCGKS-TLLRMLVGLESA----TQGDICINGEPV--- 70
Cdd:PRK15134 2 TQPLLAIENLsvafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 71 -----TGV-GKERGIVFQEPRLFpwLNVLDNVMLGLAdEKLS------RAAKRQRALEMLERV---QLSEFVNALPAQLS 135
Cdd:PRK15134 82 seqtlRGVrGNKIAMIFQEPMVS--LNPLHTLEKQLY-EVLSlhrgmrREAARGEILNCLDRVgirQAAKRLTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 136 GGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIR 215
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM--QNGRCV 236
|
.
gi 695804877 216 E 216
Cdd:PRK15134 237 E 237
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-215 |
7.20e-25 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 102.52 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 17 QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVFQEPRLFPWlN 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgrhiGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNV-MLGLAD-EKLSRAAKRQRALEMLERvqlsefvnaLP-----------AQLSGGMAQRVAIARGLVARPQILMLD 158
Cdd:COG4618 422 IAENIaRFGDADpEKVVAAAKLAGVHEMILR---------LPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 159 EPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVeEAVALADRVVVLspRPGRIR 215
Cdd:COG4618 493 EPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVL--RDGRVQ 545
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-216 |
9.04e-25 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.60 E-value: 9.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 19 VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT----GVGkergivFQeprlfPWLNVLD 94
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSllglGGG------FN-----PELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 95 NVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQ 174
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 175 ELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:cd03220 184 RLRELLKQ-GKTVILVSHDPSSIKRLCDRALVL--EKGKIRF 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-213 |
9.90e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.91 E-value: 9.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT----------G 72
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaalaaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 73 VgkerGIVFQEPRLFPWLNVLDNVMLGLADEK---LSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLV 149
Cdd:PRK11288 81 V----AIIYQELHLVPEMTVAENLYLGQLPHKggiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 150 ARPQILMLDEPFGALDAltRHTlQQELLQIHQ-RA-GTTTLLVTHDVEEAVALADRVVVLspRPGR 213
Cdd:PRK11288 157 RNARVIAFDEPTSSLSA--REI-EQLFRVIRElRAeGRVILYVSHRMEEIFALCDAITVF--KDGR 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-236 |
1.16e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 101.67 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGV----GKE 76
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpakAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 77 RGI--VFQEPRLFPWLNVLDNVMLGLAdeKLSRAAKRQRALEMLERVQLSEFVNAlpAQLSGGMAQRVAIARGLVARPQI 154
Cdd:PRK15439 86 LGIylVPQEPLLFPNLSVKENILFGLP--KRQASMQKMKQLLAALGCQLDLDSSA--GSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 155 LMLDEPFGALDALTRHTLQQElLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIreVVSLALphpRQRDDAAFI 234
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSR-IRELLAQGVGIVFISHKLPEIRQLADRISVM--RDGTI--ALSGKT---ADLSTDDII 233
|
..
gi 695804877 235 AA 236
Cdd:PRK15439 234 QA 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-207 |
1.81e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 101.33 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE---RGI--VFQEPRLFPwLNVLDNV 96
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlrQGVamVQQDPVVLA-DTFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 MLGladeklsRAAKRQRALEMLERVQLSEFVNALPA-----------QLSGGMAQRVAIARGLVARPQILMLDEPFGALD 165
Cdd:PRK10790 436 TLG-------RDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 166 ALTRHTLQQELLQIHQRagtTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK10790 509 SGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVL 547
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-207 |
2.24e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 97.26 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER------GI 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimreavAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPWLNVLDNVMLGladeklSRAAKRQRALEMLERV-----QLSEFVNALPAQLSGGMAQRVAIARGLVARPQI 154
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMG------GFFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695804877 155 LMLDEPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVL 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-207 |
3.41e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 100.24 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING------EPVTGVGKERGI 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynklDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPWLNVLDNVMLG-LADEK------LSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARP 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGrHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 153 QILMLDEPfgaLDALTRHTLQQELLQIHQ--RAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK09700 165 KVIIMDEP---TSSLTNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
14-208 |
3.74e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.38 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 14 KSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICI---------NGEPVTGVGKER------- 77
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNPYSKkiknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 -----GIVFQEP--RLFPwLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSE-FVNALPAQLSGGMAQRVAIARGLV 149
Cdd:PRK13631 114 lrrrvSMVFQFPeyQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 150 ARPQILMLDEPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
4.54e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.92 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGE-----PVTGVGK 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 76 ER---------GIVFQEPR--LFPWLNVLDNV---MLGLADEKLSRAakRQRALEMLERVQL-SEFVNALPAQLSGGMAQ 140
Cdd:PRK11701 81 AErrrllrtewGFVHQHPRdgLRMQVSAGGNIgerLMAVGARHYGDI--RATAGDWLERVEIdAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 141 RVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM--KQGRVVE 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-216 |
5.72e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.90 E-value: 5.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRkswQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVF 81
Cdd:PRK11160 344 VSFTYPD---QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrqaiSVVS 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPwlNVL-DNVMLGLA---DEKLSraakrqralEMLERVQLSEFVNALPA----------QLSGGMAQRVAIARG 147
Cdd:PRK11160 421 QRVHLFS--ATLrDNLLLAAPnasDEALI---------EVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 148 LVARPQILMLDEPFGALDALT-RHTLQqeLLQIHQRaGTTTLLVTHdveEAVALA--DRVVVLSprPGRIRE 216
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETeRQILE--LLAEHAQ-NKTVLMITH---RLTGLEqfDRICVMD--NGQIIE 553
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-192 |
6.84e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.87 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 23 QNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPvtgVGKERGIVFQE-----------PRLFPWLN 91
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP---IRRQRDEYHQDllylghqpgikTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNvmlgladEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHT 171
Cdd:PRK13538 95 LRFY-------QRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170 180
....*....|....*....|.
gi 695804877 172 LQQELLQiHQRAGTTTLLVTH 192
Cdd:PRK13538 168 LEALLAQ-HAEQGGMVILTTH 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-207 |
7.34e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.80 E-value: 7.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 19 VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----VGKERGIVFQEP--RLFPwLN 91
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenireVRKFVGLVFQNPddQIFS-PT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHT 171
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 695804877 172 LQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-218 |
9.29e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.95 E-value: 9.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 19 VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG----KERGIVF--QEPR---LFPW 89
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSprerRRLGVAYipEDRLgrgLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 90 LNVLDNVMLGLADEK-------LSRAAKRQRALEMLER--VQLSEfVNALPAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:COG3845 351 MSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEfdVRTPG-PDTPARSLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 161 FGALDALTRHTLQQELLQihQR-AGTTTLLVTHDVEEAVALADRVVVLSprPGRIREVV 218
Cdd:COG3845 430 TRGLDVGAIEFIHQRLLE--LRdAGAAVLLISEDLDEILALSDRIAVMY--EGRIVGEV 484
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-213 |
1.38e-23 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 98.71 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESAT--QGDICINGEPVTGVG----KERGIVF-- 81
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDirdsEALGIVIih 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPWLNVLDNVMLGlaDEKLSR-----AAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILM 156
Cdd:NF040905 85 QELALIPYLSIAENIFLG--NERAKRgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 157 LDEPFGAL-DALTRHTLqqELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGR 213
Cdd:NF040905 163 LDEPTAALnEEDSAALL--DLLLELKAQGITSIIISHKLNEIRRVADSITVL--RDGR 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-208 |
1.69e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 15 SWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER----------------G 78
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlarrlallpqhhltpeG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRLF---PWLNVLDNvmLGLADEKLSRAAkrqralemLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQIL 155
Cdd:PRK11231 91 ITVRELVAYgrsPWLSLWGR--LSAEDNARVNQA--------MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695804877 156 MLDEPFGALDaLTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:PRK11231 161 LLDEPTTYLD-INHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLA 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-207 |
2.16e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 96.33 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 19 VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESA---TQGDICINGEPVTGV---------GKERGIVFQEP-- 84
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLpekelnklrAEQISMIFQDPmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 85 RLFPWLNVLDNVMLGLADEK-LSRAAKRQRALEMLERVQLSEF---VNALPAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAVKMPEArkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695804877 161 FGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-215 |
3.11e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.05 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING------EPVTGVGKERGIVFQEPRL-FPWLNVL 93
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIRKLVGIVFQNPETqFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 94 DNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQ 173
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 174 QELLQIHQRaGTTTLLVTHDVEEaVALADRVVVLSprPGRIR 215
Cdd:PRK13644 177 ERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMD--RGKIV 214
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-229 |
3.14e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.72 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLeSATQGDICINGE-------------PVTGVGKERGIVFQEPRLFP 88
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRveffnqniyerrvNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 89 wLNVLDNVMLGLA----------DEKLSRAAKrqrALEMLERVQLSEFVNALpaQLSGGMAQRVAIARGLVARPQILMLD 158
Cdd:PRK14258 102 -MSVYDNVAYGVKivgwrpkleiDDIVESALK---DADLWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 159 EPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSPRPGRIREVVSLAL-------PH-PRQRD 229
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLtkkifnsPHdSRTRE 254
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-207 |
3.15e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.73 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV-----------TGVGKERGIVFQEPRLFPWL 90
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqidaIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 91 NVLDNVMLGLADEKLSRAAKRQRALE-MLERVQLSEFV----NALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALD 165
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVEeCLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 166 ALTRHTLQQELLQIHQRagTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFL 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-219 |
5.01e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.19 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINgepvtgvgKERGIVF--QEPRLfPWLNVLDNVMLG 99
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP--------AGARVLFlpQRPYL-PLGTLREALLYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 100 LADEKLSRAAkrqrALEMLERVQLSEFVNAL------PAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQ 173
Cdd:COG4178 450 ATAEAFSDAE----LREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695804877 174 QELLQihQRAGTTTLLVTHDvEEAVALADRVVVLSPRPGRIREVVS 219
Cdd:COG4178 526 QLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-216 |
5.75e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.61 E-value: 5.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 9 FRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV----TGVGkergivFQep 84
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSalleLGAG------FH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 85 rlfPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNaLPAQ-LSGGMAQRVAIArglVA---RPQILMLDEP 160
Cdd:COG1134 101 ---PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFID-QPVKtYSSGMRARLAFA---VAtavDPDILLVDEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 161 FGALDALTRHTLQQELLQIhQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:COG1134 174 LAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWL--EKGRLVM 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-209 |
7.01e-23 |
|
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: 91.84 E-value: 7.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRK------SWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLES--ATQGDICINGEPVT--GVGKE 76
Cdd:cd03213 4 LSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDkrSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 77 RGIVFQEPRLFPWLNVldnvmlglaDEKLSRAAKRQralemlervqlsefvnalpaQLSGGMAQRVAIARGLVARPQILM 156
Cdd:cd03213 84 IGYVPQDDILHPTLTV---------RETLMFAAKLR--------------------GLSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 157 LDEPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDV-EEAVALADRVVVLSP 209
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQ 187
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-207 |
1.27e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 94.20 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 19 VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLES----ATQGDICINGEPVTG---------VGKERGIVFQEPR 85
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKlsprerrkiIGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 86 --LFPWLNVLDNVMLGLADEKLS------RAAKRQRALEMLERVQL---SEFVNALPAQLSGGMAQRVAIARGLVARPQI 154
Cdd:COG4170 100 scLDPSAKIGDQLIEAIPSWTFKgkwwqrFKWRKKRAIELLHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695804877 155 LMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-192 |
1.76e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 91.95 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 9 FRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL---ESATQGDICINGEPVTG--VGKERGIVFQE 83
Cdd:cd03234 10 GLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPdqFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDN----VMLGLAdEKLSRAAKRQRALEMLER-VQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLD 158
Cdd:cd03234 90 DILLPGLTVRETltytAILRLP-RKSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190
....*....|....*....|....*....|....
gi 695804877 159 EPFGALDALTRHTLQQELLQIHQRaGTTTLLVTH 192
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-208 |
1.80e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.96 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE--RGI---VFQEPRLFPWlNVLDN 95
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFinyLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 96 VMLGlADEKLSRaakrQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAIARGLVARPQILMLDEPFGAL 164
Cdd:TIGR01193 568 LLLG-AKENVSQ----DEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695804877 165 DALTRHTLQQELLQIHQRagtTTLLVTHDVEEAvALADRVVVLS 208
Cdd:TIGR01193 643 DTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLD 682
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-207 |
2.40e-22 |
|
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: 95.25 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 12 VRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLES--ATQGDICIN----------------GEPVTGV 73
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvGEPCPVC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 74 G----------------------KERGIVFQEP-RLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNAL 130
Cdd:TIGR03269 86 GgtlepeevdfwnlsdklrrrirKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 131 PAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWL 242
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-192 |
7.73e-22 |
|
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: 89.34 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVF----QEPRLFPWLNVLDN 95
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylgHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 96 VMLGLADeklSRAAKRQrALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDAlTRHTLQQE 175
Cdd:TIGR01189 94 LHFWAAI---HGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AGVALLAG 168
|
170
....*....|....*..
gi 695804877 176 LLQIHQRAGTTTLLVTH 192
Cdd:TIGR01189 169 LLRAHLARGGIVLLTTH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-216 |
7.82e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 7.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 5 TLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDIcingepVTGVGKERGIVFQEP 84
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------KLGETVKIGYFDQHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 85 RLF-PWLNVLDNVmlgladEKLSRAAKRQRALEMLERVQLS-EFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:COG0488 388 EELdPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 163 ALDALTRHTLqQELLQihQRAGtTTLLVTHD---VEeavALADRVVVLspRPGRIRE 216
Cdd:COG0488 462 HLDIETLEAL-EEALD--DFPG-TVLLVSHDryfLD---RVATRILEF--EDGGVRE 509
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-207 |
8.93e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.22 E-value: 8.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING----------EPVTGVGKE 76
Cdd:PRK13645 12 VSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkiKEVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 77 RGIVFQEP--RLFPwlnvlDNVMLGLADEKLSRAAKRQRAL----EMLERVQL-SEFVNALPAQLSGGMAQRVAIARGLV 149
Cdd:PRK13645 92 IGLVFQFPeyQLFQ-----ETIEKDIAFGPVNLGENKQEAYkkvpELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 150 ARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-236 |
1.79e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.16 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQG-----DICINGEP------VTGVGKERGIVFQEPRLFP 88
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSifnyrdVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 89 wLNVLDNVMLGLADEKL-SRAAKRQRALEMLERVQLSEFV----NALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDAVkdrlSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 164 LDALTRHTLQQELLQIHQRagTTTLLVTHDVEEAVALADRVVVLSprPGRIRE--VVSLALPHPRQRDDAAFIAA 236
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFF--DGRLVEegPTEQLFSSPKHAETARYVAG 264
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-207 |
2.03e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.94 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVF--QEPRL---FPWLnVLD 94
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpQSEEVdwsFPVL-VED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 95 NVMLG----LADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRH 170
Cdd:PRK15056 100 VVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 695804877 171 TLqQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK15056 180 RI-ISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-217 |
4.36e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 17 QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV--------TGVGKERGIVFQEP--RL 86
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspgklQALRRDIQFIFQDPyaSL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 FPWLNVLDNVMLGLADEKLSRA-AKRQRALEMLERVQL-SEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGAL 164
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGkAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695804877 165 DALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIREV 217
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMY--LGQIVEI 545
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-207 |
4.59e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 88.63 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 4 STLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDIcingepVTGVGKERGIVFQE 83
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLgladeKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:PRK09544 76 LYLDTTLPLTVNRFL-----RLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695804877 164 LDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-214 |
4.67e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.60 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGV-GKER----GIVFQEP 84
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTpSRELakrlAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 85 RLFPWLNVLDNVMLG----------LADEklsraAKRQRALEMLErvqLSEFVNALPAQLSGGMAQRVAIARGLVARPQI 154
Cdd:COG4604 85 HINSRLTVRELVAFGrfpyskgrltAEDR-----EIIDEAIAYLD---LEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695804877 155 LMLDEPFGALDalTRHTLQqeLLQIHQRA----GTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:COG4604 157 VLLDEPLNNLD--MKHSVQ--MMKLLRRLadelGKTVVIVLHDINFASCYADHIVAM--KDGRV 214
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-207 |
6.50e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 89.42 E-value: 6.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL----ESATQGDICINGEPVTG---------VGKERGIVFQEP--R 85
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRisekerrnlVGAEVAMIFQDPmtS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 86 LFPWLNVLDNVMLGL-ADEKLSRAAKRQRALEMLERVQLSEFVNAL---PAQLSGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:PRK11022 102 LNPCYTVGFQIMEAIkVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695804877 162 GALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-214 |
6.57e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.99 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEP----------------- 69
Cdd:PRK13651 8 IVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 70 ------------VTGVGKERGIVFQ--EPRLFPwLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSE-FVNALPAQL 134
Cdd:PRK13651 88 viqktrfkkikkIKEIRRRVGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 135 SGGMAQRVAIARGLVARPQILMLDEPFGALDALTrhtlQQELLQI----HQRaGTTTLLVTHDVEEAVALADRVVVLspR 210
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG----VKEILEIfdnlNKQ-GKTIILVTHDLDNVLEWTKRTIFF--K 239
|
....
gi 695804877 211 PGRI 214
Cdd:PRK13651 240 DGKI 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-193 |
6.97e-21 |
|
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: 91.15 E-value: 6.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLesatqgDICINGEPVTGVGKERGIVFQEPRLFPWLNVLDNVMLGLA 101
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 102 -------------------DEKLSRAAKRQRALEM---------LERvQLSEFVNAL--P------AQLSGGMAQRVAIA 145
Cdd:TIGR03719 95 eikdaldrfneisakyaepDADFDKLAAEQAELQEiidaadawdLDS-QLEIAMDALrcPpwdadvTKLSGGERRRVALC 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695804877 146 RGLVARPQILMLDEPFGALDALTRHTLQQELlqiHQRAGtTTLLVTHD 193
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAESVAWLERHL---QEYPG-TVVAVTHD 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-207 |
2.39e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.15 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 5 TLVSFRHVRKSW---------QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT-GVG 74
Cdd:PRK15112 3 TLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 75 KERG----IVFQEP--RLFPWLNV--LDNVMLGLADEkLSRAAKRQRALEMLERVQL-SEFVNALPAQLSGGMAQRVAIA 145
Cdd:PRK15112 83 SYRSqrirMIFQDPstSLNPRQRIsqILDFPLRLNTD-LEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695804877 146 RGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-192 |
2.69e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.70 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVFQEPR--LFPWLNVLDNV--- 96
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRnaMKPALTVAENLefw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 --MLGLADEKLSRAakrqralemLERVQLSEFVNaLPAQ-LSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRhTLQ 173
Cdd:PRK13539 98 aaFLGGEELDIAAA---------LEAVGLAPLAH-LPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV-ALF 166
|
170
....*....|....*....
gi 695804877 174 QELLQIHQRAGTTTLLVTH 192
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATH 185
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-216 |
9.98e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 84.88 E-value: 9.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICI---NGEPVTGVG-------- 74
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELELYQlseaerrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 75 ---KERGIVFQEPR--LFPWLNVLDNV---MLGLADEKLSRAakRQRALEMLERVQLSEF-VNALPAQLSGGMAQRVAIA 145
Cdd:TIGR02323 83 lmrTEWGFVHQNPRdgLRMRVSAGANIgerLMAIGARHYGNI--RATAQDWLEEVEIDPTrIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695804877 146 RGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRIRE 216
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM--QQGRVVE 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-192 |
1.72e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.02 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESA---TQGDICINGEPVTGVGKER--GIVFQEPRLFPWLNVLDNV 96
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 M----LGLaDEKLSRAAKRQRALEMLERVQLSEFVNALPAQ------LSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:TIGR00955 121 MfqahLRM-PRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180
....*....|....*....|....*.
gi 695804877 167 LTRHTLQQELLQIHQRaGTTTLLVTH 192
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQK-GKTIICTIH 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-216 |
2.54e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.61 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQ--QVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV-----TGVGKERGI 79
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdytlASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFpwlN--VLDNVMLGlADEKLSR-----AAKRQRALEMLERVQ--LSEFVNALPAQLSGGMAQRVAIARGLVA 150
Cdd:PRK11176 422 VSQNVHLF---NdtIANNIAYA-RTEQYSReqieeAARMAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 151 RPQILMLDEPFGALDALTRHTLQQELLQIhqRAGTTTLLVTHDVeEAVALADRVVVLSprPGRIRE 216
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRL-STIEKADEILVVE--DGEIVE 558
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-192 |
2.65e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 82.93 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVtgvGKERGIVFQE-------PRLFPWLNV 92
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL---DFQRDSIARGllylghaPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 93 LDNVMLGLADEKlsraakRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTL 172
Cdd:cd03231 91 LENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 695804877 173 QQELLQiHQRAGTTTLLVTH 192
Cdd:cd03231 165 AEAMAG-HCARGGMVVLTTH 183
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-207 |
3.61e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.90 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRhvrksWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT-------GV 73
Cdd:PRK13638 1 MLATSDLWFR-----YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgllAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 74 GKERGIVFQEPRLFPWLNVLDNVM------LGLADEKLSRaakrqRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARG 147
Cdd:PRK13638 76 RQQVATVFQDPEQQIFYTDIDSDIafslrnLGVPEAEITR-----RVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 148 LVARPQILMLDEPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVL 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-216 |
3.95e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.60 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 26 SLDIAAGELVALVGSSGCGKS----TLLRMLVGLESATQGDICINGEPVTGV---GKERGIVFQEPR--LFPWLNVLDNV 96
Cdd:PRK10418 23 SLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCalrGRKIATIMQNPRsaFNPLHTMHTHA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 MLGLAdeKLSRAAKRQRALEMLERVQLSEFVNAL---PAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQ 173
Cdd:PRK10418 103 RETCL--ALGKPADDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695804877 174 QELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIRE 216
Cdd:PRK10418 181 DLLESIVQKRALGMLLVTHDMGVVARLADDVAVMS--HGRIVE 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-193 |
1.01e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.79 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLesatqgDICINGEPVTGVGKERGIVFQEPRLFPWLNVLDNVMLGLA 101
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 102 D--EKLSR-----------------AAKRQRALEM---------LERvQLSEFVNAL--P------AQLSGGMAQRVAIA 145
Cdd:PRK11819 97 EvkAALDRfneiyaayaepdadfdaLAAEQGELQEiidaadawdLDS-QLEIAMDALrcPpwdakvTKLSGGERRRVALC 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695804877 146 RGLVARPQILMLDEPFGALDALTRHTLQQELlqiHQRAGtTTLLVTHD 193
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAESVAWLEQFL---HDYPG-TVVAVTHD 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-214 |
1.28e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 24 NFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGV----GKERGIVF-QEPR----LFPWLNVLD 94
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdGLANGIVYiSEDRkrdgLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 95 NVMLgLADEKLSRAAKRQRALEmlERVQLSEFVNAL----PAQ------LSGGMAQRVAIARGLVARPQILMLDEPFGAL 164
Cdd:PRK10762 350 NMSL-TALRYFSRAGGSLKHAD--EQQAVSDFIRLFniktPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695804877 165 DALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVM--HEGRI 473
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-207 |
1.43e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRkswQQVTALQNFSLDIAAGELVALVGSSGCGKS----TLLRMLVGLESATQGD-----------ICINGEPVT 71
Cdd:PRK10261 20 IAFMQEQ---QKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDkmllrrrsrqvIELSEQSAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 72 GVGKERG----IVFQEP--RLFPWLNVLDNVM------LGLADEKLSRAAKRqraleMLERVQLSE---FVNALPAQLSG 136
Cdd:PRK10261 97 QMRHVRGadmaMIFQEPmtSLNPVFTVGEQIAesirlhQGASREEAMVEAKR-----MLDQVRIPEaqtILSRYPHQLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 137 GMAQRVAIARGLVARPQILMLDEPFGALDAltrhTLQQELLQ----IHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDV----TIQAQILQlikvLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-210 |
1.46e-18 |
|
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: 79.41 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINgePVTGVGkergivfqeprL 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG--STVKIG-----------Y 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 FPwlnvldnvmlgladeklsraakrqralemlervqlsefvnalpaQLSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:cd03221 68 FE--------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695804877 167 LTRHTLQQELLQIHQragtTTLLVTHDVEEAVALADRVVVLSPR 210
Cdd:cd03221 104 ESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-208 |
2.74e-18 |
|
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: 83.91 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT----GVGKERGIVFQEPRLFPWLNVLDNv 96
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnldAVRQSLGMCPQHNILFHHLTVAEH- 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 MLGLADEKLSRAAKRQRALE-MLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQE 175
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|...
gi 695804877 176 LLQIhqRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:TIGR01257 1104 LLKY--RSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-226 |
3.10e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 83.31 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVF 81
Cdd:COG4615 333 VTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyrqlfSAVF 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPWLnvldnvmLGLADEKLsraakRQRALEMLERVQLSEFV----NAL-PAQLSGGMAQRVAIargLVA----RP 152
Cdd:COG4615 413 SDFHLFDRL-------LGLDGEAD-----PARARELLERLELDHKVsvedGRFsTTDLSQGQRKRLAL---LVAlledRP 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 153 qILMLDE-------PFgaldaltRHTLQQELLQIHQRAGTTTLLVTHDvEEAVALADRVVVLspRPGRIREVVSLALPHP 225
Cdd:COG4615 478 -ILVFDEwaadqdpEF-------RRVFYTELLPELKARGKTVIAISHD-DRYFDLADRVLKM--DYGKLVELTGPAALAA 546
|
.
gi 695804877 226 R 226
Cdd:COG4615 547 S 547
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-195 |
5.18e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 79.68 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 15 SW-QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE------RGIVFQEPRLf 87
Cdd:cd03290 9 SWgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrsrnRYSVAYAAQK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 88 PWL---NVLDNVMLGLADEKlsraakrQRALEMLERVQLSEFVNALP-----------AQLSGGMAQRVAIARGLVARPQ 153
Cdd:cd03290 88 PWLlnaTVEENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695804877 154 ILMLDEPFGALDA-LTRHTLQQELLQIHQRAGTTTLLVTHDVE 195
Cdd:cd03290 161 IVFLDDPFSALDIhLSDHLMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-206 |
1.16e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 12 VRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICingepvtgvgkergIVFQEPRLFPWLN 91
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC--------------VDVPDNQFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVmlGLADEKLSraakrqrALEMLERVQLSEFVN--ALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTR 169
Cdd:COG2401 102 LIDAI--GRKGDFKD-------AVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 695804877 170 HTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVV 206
Cdd:COG2401 173 KRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLI 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-215 |
1.36e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 19 VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV-----TGVGKERGIVFQEPRLFPWLNVL 93
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 94 DNVMLGLADE--KLSRAAKRQRAL--EMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDalTR 169
Cdd:PRK09536 96 QVVEMGRTPHrsRFDTWTETDRAAveRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD--IN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695804877 170 HTLQQ-ELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIR 215
Cdd:PRK09536 174 HQVRTlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLA--DGRVR 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-168 |
1.49e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.20 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 4 STLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG----KERG- 78
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpkssQEAGi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 -IVFQEPRLFPWLNVLDNVMLGlaDEKLSRAAK------RQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVAR 151
Cdd:PRK10762 82 gIIHQELNLIPQLTIAENIFLG--REFVNRFGRidwkkmYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170
....*....|....*..
gi 695804877 152 PQILMLDEPfgaLDALT 168
Cdd:PRK10762 160 SKVIIMDEP---TDALT 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-227 |
1.80e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.23 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSW---QQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICIN-GEPVTGVG-----KER 77
Cdd:PTZ00265 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINlkwwrSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 GIVFQEPRLF--------------------------------------------PWLNVLDNVMLGLADEKLSRAAKRQR 113
Cdd:PTZ00265 463 GVVSQDPLLFsnsiknnikyslyslkdlealsnyynedgndsqenknkrnscraKCAGDLNDMSNTTDSNELIEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 114 ALEMLERVQLS------EFVNALP-----------AQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQEL 176
Cdd:PTZ00265 543 TIKDSEVVDVSkkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 695804877 177 LQIHQRAGTTTLLVTHDVeEAVALADRVVVLSPRPGRIREVVSLALPHPRQ 227
Cdd:PTZ00265 623 NNLKGNENRITIIIAHRL-STIRYANTIFVLSNRERGSTVDVDIIGEDPTK 672
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-214 |
2.61e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE---RGIVFQEPRL---------- 86
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAYLPQQLpaaegmtvre 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 ------FPWLNVLDNvmLGLADeklsraakRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:PRK10575 105 lvaigrYPWHGALGR--FGAAD--------REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 161 FGALDalTRHtlQQELLQIHQRA----GTTTLLVTHDVEEAVALADRVVVLspRPGRI 214
Cdd:PRK10575 175 TSALD--IAH--QVDVLALVHRLsqerGLTVIAVLHDINMAARYCDYLVAL--RGGEM 226
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-211 |
3.01e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 77.58 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 29 IAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVF--QEPRLFPWLNVLDNVMLGLAdekLS 106
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYlgHLPGLKADLSTLENLHFLCG---LH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 107 RAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDaLTRHTLQQELLQIHQRAGTT 186
Cdd:PRK13543 111 GRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLVNRMISAHLRGGGA 189
|
170 180
....*....|....*....|....*
gi 695804877 187 TLLVTHDVEEAVALADRVVVLSPRP 211
Cdd:PRK13543 190 ALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-204 |
3.07e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.55 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG----VGKERGIVFQEPRLFPWLNVLDN 95
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAgdiaTRRRVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 96 VML-----GLADEKLsraakRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRH 170
Cdd:NF033858 360 LELharlfHLPAAEI-----AARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190
....*....|....*....|....*....|....
gi 695804877 171 TLQQELLQIHQRAGTTTLLVTHDVEEAvALADRV 204
Cdd:NF033858 435 MFWRLLIELSREDGVTIFISTHFMNEA-ERCDRI 467
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
7-207 |
2.96e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 76.70 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCG--KSTLLRMLVGLESATQ----GDICINGEPVT-GVGKERGI 79
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRpwrf*TWCANRRALRrTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 VFQEPRLFPWLNVLdnVMLGLADEkLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDE 159
Cdd:NF000106 94 R*GRRESFSGRENL--YMIGR*LD-LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695804877 160 PFGALDALTRHTLQQELLQIhQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVI 217
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-208 |
2.97e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.26 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESAtQGDICINGEPVTGVGKE-----RGIVFQEPRLFPWLNVLDNV 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAelarhRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 MLGLADeKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIAR-------GLVARPQILMLDEPFGALDALTR 169
Cdd:COG4138 91 ALHQPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAvllqvwpTINPEGQLLLLDEPMNSLDVAQQ 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 695804877 170 HTLQQELLQIHQrAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:COG4138 170 AALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLK 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-216 |
4.25e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.32 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 15 SWQQVTA---LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVG-LESATQGDICIngepvtgvgkeRGIVFQEPRLfPWL 90
Cdd:PLN03232 623 SWDSKTSkptLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVI-----------RGSVAYVPQV-SWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 91 ---NVLDNVMLG--LADEKLSRA---AKRQRALEMLERVQLSEfVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:PLN03232 691 fnaTVRENILFGsdFESERYWRAidvTALQHDLDLLPGRDLTE-IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 163 ALDALTRHTLQQELLQiHQRAGTTTLLVTHDVeEAVALADRVVVLSprPGRIRE 216
Cdd:PLN03232 770 ALDAHVAHQVFDSCMK-DELKGKTRVLVTNQL-HFLPLMDRIILVS--EGMIKE 819
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-212 |
6.60e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 74.37 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 25 FSLDIAAG-----ELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGvgKERGIVFQEPrlfpwlNVLDNVMLG 99
Cdd:cd03237 13 FTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY--KPQYIKADYE------GTVRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 100 LADEKLSRAakrQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQI 179
Cdd:cd03237 85 ITKDFYTHP---YFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
|
170 180 190
....*....|....*....|....*....|...
gi 695804877 180 HQRAGTTTLLVTHDVEEAVALADRVVVLSPRPG 212
Cdd:cd03237 162 AENNEKTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-207 |
7.71e-16 |
|
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: 74.89 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGlesatqgdiciNGEPVTGVGKERGIVFQEPRlFPWL---NVLDNVML 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILG-----------ELEPSEGKIKHSGRISFSSQ-FSWImpgTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 99 GLA-DEklsraakrQRALEMLERVQLSEFVNALPAQ-----------LSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:cd03291 121 GVSyDE--------YRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695804877 167 LTRHTLQQELLqIHQRAGTTTLLVTHDVEEaVALADRVVVL 207
Cdd:cd03291 193 FTEKEIFESCV-CKLMANKTRILVTSKMEH-LKKADKILIL 231
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-207 |
7.84e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKE--RG---IVF 81
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSrlaVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRLFPwLNVLDNVMLGLAD---EKLSRAAKRQRALEMLERVQ---LSEfVNALPAQLSGGMAQRVAIARGLVARPQIL 155
Cdd:PRK10789 396 QTPFLFS-DTVANNIALGRPDatqQEIEHVARLASVHDDILRLPqgyDTE-VGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695804877 156 MLDEPFGALDALTRHTLQQELLQihQRAGTTTLLVTHDVeEAVALADRVVVL 207
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQ--WGEGRTVIISAHRL-SALTEASEILVM 522
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-216 |
1.50e-15 |
|
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: 72.83 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER-----GIVFQEPRLFpwlnvldn 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrsslTIIPQDPTLF-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 96 vmLGLADEKLSRaAKRQRALEMLERVQLSEFVNalpaQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQe 175
Cdd:cd03369 95 --SGTIRSNLDP-FDEYSDEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 176 llQIHQR-AGTTTLLVTHDVeEAVALADRVVVLSprPGRIRE 216
Cdd:cd03369 167 --TIREEfTNSTILTIAHRL-RTIIDYDKILVMD--AGEVKE 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-207 |
1.65e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 24 NFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGK----ERGIVF-----QEPRLFpwlnvLD 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpedrQSSGLY-----LD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 95 -----NVMlGLADEKLSRAAKRQRALEMLER------VQLSEfVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:PRK15439 356 aplawNVC-ALTHNRRGFWIKPARENAVLERyrralnIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695804877 164 LDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVM 476
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-207 |
1.66e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.82 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV-TGVGKergiVFQEPRLFPWLNVLDNVMLG 99
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISD----VHQNMGYCPQFDAIDDLLTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 100 laDEKLSRAAK-RQRALEMLERVQ--------LSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRH 170
Cdd:TIGR01257 2030 --REHLYLYARlRGVPAEEIEKVAnwsiqslgLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190
....*....|....*....|....*....|....*..
gi 695804877 171 TLQQELLQIhQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:TIGR01257 2108 MLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-208 |
3.30e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 14 KSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGL--ESATQGDICING-EPVTGVGKERGIVFQEPRLFPWL 90
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNrKPTKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 91 NVLDNVMLgLADEKLSRAAKRQRALEMLERVqLSEFV----------NALPAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:PLN03211 156 TVRETLVF-CSLLRLPKSLTKQEKILVAESV-ISELGltkcentiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695804877 161 FGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLS 281
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-222 |
4.58e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTG-----VGKERGIVFQEPRLFPWLNVLD 94
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaskeVARRIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 95 NVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQ----LSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRH 170
Cdd:PRK10253 101 LVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 171 TLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLspRPGRI------REVVSLAL 222
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKIvaqgapKEIVTAEL 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
79-213 |
7.69e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRLFPwLNVLDNVMLGLAD---EKLSRAAKRqralemlerVQLSEFVNALPAQ-----------LSGGMAQRVAI 144
Cdd:PTZ00265 1300 IVSQEPMLFN-MSIYENIKFGKEDatrEDVKRACKF---------AAIDEFIESLPNKydtnvgpygksLSGGQKQRIAI 1369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 145 ARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVeEAVALADRVVVLSpRPGR 213
Cdd:PTZ00265 1370 ARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFN-NPDR 1436
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-207 |
9.02e-15 |
|
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: 73.41 E-value: 9.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDIcingepvtgvgKERGIVFQEPRlFPWL---NVLDNVML 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGRISFSPQ-TSWImpgTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 99 GLA-DEklsraakrQRALEMLERVQLSEFVNALPAQ-----------LSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:TIGR01271 510 GLSyDE--------YRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695804877 167 LTRHTLQQELLqIHQRAGTTTLLVTHDVEEaVALADRVVVL 207
Cdd:TIGR01271 582 VTEKEIFESCL-CKLMSNKTRILVTSKLEH-LKKADKILLL 620
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-237 |
1.07e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVG--------LESATQGDICINGEPVTGV-----GKERGIVFQEPR-LF 87
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAAIdaprlARLRAVLPQAAQpAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 88 PWlNVLDNVMLGLADEKLSRAAKRQR----ALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGL---------VARPQI 154
Cdd:PRK13547 97 AF-SAREIVLLGRYPHARRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 155 LMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSprPGRIrevvsLALPHPRQRDDAAFI 234
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA--DGAI-----VAHGAPADVLTPAHI 248
|
...
gi 695804877 235 AAC 237
Cdd:PRK13547 249 ARC 251
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-231 |
1.29e-14 |
|
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: 73.06 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEpVTGVGKERGIvfQEPRLfpwlnvLDNVMLGLA 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQAWI--QNDSL------RENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 102 -DEKLSRAAKRQRA----LEML---ERVQLSEF-VNalpaqLSGGMAQRVAIARGLVARPQILMLDEPFGALDA-LTRHT 171
Cdd:TIGR00957 725 lNEKYYQQVLEACAllpdLEILpsgDRTEIGEKgVN-----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHI 799
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 172 LQQELLQIHQRAGTTTLLVTHDVeEAVALADRVVVLSprPGRIREVVSlaLPHPRQRDDA 231
Cdd:TIGR00957 800 FEHVIGPEGVLKNKTRILVTHGI-SYLPQVDVIIVMS--GGKISEMGS--YQELLQRDGA 854
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
3-208 |
1.29e-14 |
|
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: 69.98 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRhVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLES---ATQGDICINGEPVTGVGK--ER 77
Cdd:cd03233 5 SWRNISFT-TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEkyPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 GIVF--QEPRLFPWLNVldnvmlgladeklsraakrQRALEMLERVQLSEFVNAlpaqLSGGMAQRVAIARGLVARPQIL 155
Cdd:cd03233 84 EIIYvsEEDVHFPTLTV-------------------RETLDFALRCKGNEFVRG----ISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695804877 156 MLDEPFGALDALTRHTLQQELLQIHQRAGTTTLL-VTHDVEEAVALADRVVVLS 208
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLY 194
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-216 |
1.65e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.31 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQvtalQNFS-----LDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER---- 77
Cdd:PRK10522 323 LELRNVTFAYQD----NGFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrkl 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 78 -GIVFQEPRLFPWLnvldnvmlgLADEKlsRAAKRQRALEMLERVQLSEFVN-----ALPAQLSGGMAQRVAIARGLVAR 151
Cdd:PRK10522 399 fSAVFTDFHLFDQL---------LGPEG--KPANPALVEKWLERLKMAHKLEledgrISNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 152 PQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDvEEAVALADRvvVLSPRPGRIRE 216
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADR--LLEMRNGQLSE 529
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-207 |
1.68e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 71.76 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 19 VTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLesaTQGDICING----------------EPVTGVGKERGIVFQ 82
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTAdrmrfddidllrlsprERRKLVGHNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPR--LFPWLNVLDNVMLGLADEKLS-RAAKR-----QRALEMLERVQLSE---FVNALPAQLSGGMAQRVAIARGLVAR 151
Cdd:PRK15093 97 EPQscLDPSERVGRQLMQNIPGWTYKgRWWQRfgwrkRRAIELLHRVGIKDhkdAMRSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 152 PQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-208 |
3.61e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESAtQGDICINGEPV-----TGVGKERGIVFQEPRLFPWLNVLD 94
Cdd:PRK03695 10 TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLeawsaAELARHRAYLSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 95 NVMLGLADekLSRAAKRQRALEML-ERVQLSEFVNALPAQLSGGMAQRVAIA-------RGLVARPQILMLDEPFGALDA 166
Cdd:PRK03695 89 YLTLHQPD--KTRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 167 LTRHTLQQeLLQIHQRAGTTTLLVTHDVEEAVALADRVVVLS 208
Cdd:PRK03695 167 AQQAALDR-LLSELCQQGIAVVMSSHDLNHTLRHADRVWLLK 207
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-214 |
3.70e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.71 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLES--ATQGDICINGEPVTGVG-KER---GI--VFQEPRLFPWLNVL 93
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSpDERaraGIflAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 94 DnvMLGLA-----DEKLSRAAKRQRALEMLERVQLSE-----FVNAlpaQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:COG0396 96 N--FLRTAlnarrGEELSAREFLKLLKEKMKELGLDEdfldrYVNE---GFSGGEKKRNEILQMLLLEPKLAILDETDSG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 164 LD--ALTrhTLQQELLQIHQRaGTTTLLVTH------DVEeavalADRVVVLSprPGRI 214
Cdd:COG0396 171 LDidALR--IVAEGVNKLRSP-DRGILIITHyqrildYIK-----PDFVHVLV--DGRI 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-209 |
6.90e-14 |
|
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: 67.18 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING---------EPVTGVGKERGIVfqeprLFPWLNV 92
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEgedllflpqRPYLPLGTLREQL-----IYPWDDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 93 LdnvmlgladeklsraakrqralemlervqlsefvnalpaqlSGGMAQRVAIARGLVARPQILMLDEPFGALDaltrHTL 172
Cdd:cd03223 92 L-----------------------------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALD----EES 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 695804877 173 QQELLQIHQRAGTTTLLVTHDvEEAVALADRVVVLSP 209
Cdd:cd03223 127 EDRLYQLLKELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-207 |
1.13e-13 |
|
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: 69.85 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 24 NFSLDIAAGELVALVGSSGCGKSTLLRMLVGL-ESATQGDICINGEPVT----------GVG------KERGIVfqeprl 86
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDirnpaqairaGIAmvpedrKRHGIV------ 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 fPWLNVLDNVMLGLADE-----KLSRAAKRQRALEMLERVQLSEFVNALP-AQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:TIGR02633 352 -PILGVGKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695804877 161 FGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-219 |
1.69e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 23 QNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGE------PVTGVGKERGIVFQEPR---LFPWLNVL 93
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDAVKKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 94 DNV-------------MLGLADEKLS-RAAKRQRALEMLERVQLSEFVNalpaQLSGGMAQRVAIARGLVARPQILMLDE 159
Cdd:PRK09700 360 QNMaisrslkdggykgAMGLFHEVDEqRTAENQRELLALKCHSVNQNIT----ELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 160 PFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLspRPGRIREVVS 219
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVF--CEGRLTQILT 492
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-207 |
3.02e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDicingepvtgVGKERGIVF--QEPrlfpWL---NVLDNV 96
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR----------VWAERSIAYvpQQA----WImnaTVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 MLglADEKlsRAAKRQRALemleRV-QLSEFVNALPA-----------QLSGGMAQRVAIARGLVARPQILMLDEPFGAL 164
Cdd:PTZ00243 742 LF--FDEE--DAARLADAV----RVsQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695804877 165 DALTRHTLQQELLQIHQrAGTTTLLVTHDVeEAVALADRVVVL 207
Cdd:PTZ00243 814 DAHVGERVVEECFLGAL-AGKTRVLATHQV-HVVPRADYVVAL 854
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-227 |
3.36e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 25 FSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV----TGVGKERGIVF-QEPR----LFPWLNVLDN 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirsPRDAIRAGIMLcPEDRkaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 96 VMLGlADEKLSRAA---KRQRalemlERVQLSEFVNAL------PAQ----LSGGMAQRVAIARGLVARPQILMLDEPFG 162
Cdd:PRK11288 352 INIS-ARRHHLRAGcliNNRW-----EAENADRFIRSLniktpsREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 163 ALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLspRPGRI-----------REVVSLALPHPRQ 227
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVM--REGRIagelareqateRQALSLALPRTSA 498
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
16-192 |
3.97e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.13 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 16 WQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEpvtGVGKERGiVFQEPRLF-------- 87
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ---SIKKDLC-TYQKQLCFvghrsgin 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 88 PWLNVLDNVMLgladeKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDAL 167
Cdd:PRK13540 87 PYLTLRENCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 695804877 168 TRHTLQQElLQIHQRAGTTTLLVTH 192
Cdd:PRK13540 162 SLLTIITK-IQEHRAKGGAVLLTSH 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-197 |
4.69e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVT--------------- 71
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdarhrravcpriaym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 72 --GVGKErgivfqeprLFPWLNVLDNV-----MLGladekLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAI 144
Cdd:NF033858 82 pqGLGKN---------LYPTLSVFENLdffgrLFG-----QDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695804877 145 ARGLVARPQILMLDEPFGALDALTRhtlQQ--ELL-QI-HQRAGTTTLLVTHDVEEA 197
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSR---RQfwELIdRIrAERPGMSVLVATAYMEEA 201
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-216 |
5.88e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 5.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVG-LESATQGDICIngepvtgvgkeRGIVFQEPRLfPWL---NVLDNVM 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI-----------RGTVAYVPQV-SWIfnaTVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 98 LGLA-----DEKLSRAAKRQRALEMLERVQLSEF----VNalpaqLSGGMAQRVAIARGLVARPQILMLDEPFGALDAlt 168
Cdd:PLN03130 701 FGSPfdperYERAIDVTALQHDLDLLPGGDLTEIgergVN-----ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA-- 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695804877 169 rHTLQQELLQIHQRA--GTTTLLVTHDVeEAVALADRVVVLSprPGRIRE 216
Cdd:PLN03130 774 -HVGRQVFDKCIKDElrGKTRVLVTNQL-HFLSQVDRIILVH--EGMIKE 819
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-177 |
6.03e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVtgVGK--------ERGIVF---------QEP 84
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI--VARlqqdpprnVEGTVYdfvaegieeQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 85 RLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQ-----------LSGGMAQRVAIARGLVARPQ 153
Cdd:PRK11147 97 YLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQlgldpdaalssLSGGWLRKAALGRALVSNPD 176
|
170 180
....*....|....*....|....
gi 695804877 154 ILMLDEPFGALDALTRHTLQQELL 177
Cdd:PRK11147 177 VLLLDEPTNHLDIETIEWLEGFLK 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-216 |
6.51e-13 |
|
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: 68.05 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-----KERGIVFQEPRLFPW-LNVLDN 95
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlrFKITIIPQDPVLFSGsLRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 96 VMLGLADEKLSRAakrqralemLERVQLSEFVNALPAQ-----------LSGGMAQRVAIARGLVARPQILMLDEPFGAL 164
Cdd:TIGR00957 1382 PFSQYSDEEVWWA---------LELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695804877 165 DALTRHTLQQELLQihQRAGTTTLLVTHDVEEAVALAdRVVVLSprPGRIRE 216
Cdd:TIGR00957 1453 DLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYT-RVIVLD--KGEVAE 1499
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-195 |
1.44e-12 |
|
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: 66.86 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 11 HVRKSW--------QQVTA---------LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESaTQGDICINGEPVTGV 73
Cdd:TIGR01271 1207 HAQKCWpsggqmdvQGLTAkyteagravLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSV 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 74 G-----KERGIVFQEPRLFP--WLNVLDNVMlGLADEKLSRAAkrqralemlERVQLSEFVNALPAQ-----------LS 135
Cdd:TIGR01271 1286 TlqtwrKAFGVIPQKVFIFSgtFRKNLDPYE-QWSDEEIWKVA---------EEVGLKSVIEQFPDKldfvlvdggyvLS 1355
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 136 GGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHqrAGTTTLLVTHDVE 195
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF--SNCTVILSEHRVE 1413
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-195 |
1.58e-12 |
|
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: 65.65 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESaTQGDICINGE-----PVTGVGKERGIVFQEPRLF--PWLNV 92
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVswnsvPLQKWRKAFGVIPQKVFIFsgTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 93 LDNVMlGLADEKLSRAAkrqralemlERVQLSEFVNALPAQL-----------SGGMAQRVAIARGLVARPQILMLDEPF 161
Cdd:cd03289 97 LDPYG-KWSDEEIWKVA---------EEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190
....*....|....*....|....*....|....
gi 695804877 162 GALDALTRHTLQQELLqiHQRAGTTTLLVTHDVE 195
Cdd:cd03289 167 AHLDPITYQVIRKTLK--QAFADCTVILSEHRIE 198
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-214 |
2.18e-12 |
|
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: 64.09 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLES--ATQGDICINGEPVTGVG-KER-----GIVFQEPRLFPwlnvl 93
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPpEERarlgiFLAFQYPPEIP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 94 dnvmlGladeklsraakrqralemlerVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQ 173
Cdd:cd03217 91 -----G---------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695804877 174 QELLQIHqRAGTTTLLVTH--DVEEAVAlADRVVVLspRPGRI 214
Cdd:cd03217 145 EVINKLR-EEGKSVLIITHyqRLLDYIK-PDRVHVL--YDGRI 183
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-166 |
3.10e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 63.42 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESA--TQGDICINGEPVT-GVGKERGIVFQEPRLFPWLNVLdnvml 98
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDkNFQRSTGYVEQQDVHSPNLTVR----- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 99 gladEKLSRAAKrQRALEMLERvqlsefvnalpaqlsggmaQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:cd03232 98 ----EALRFSAL-LRGLSVEQR-------------------KRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-207 |
6.58e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 10 RHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV----TGVGKERGI--VFQE 83
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALENGIsmVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PRLFPWLNVLDNVMLG--------LADEKLSRAAKR---QRALEMLERVQLsefvnalpAQLSGGMAQRVAIARGLVARP 152
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGryptkgmfVDQDKMYRDTKAifdELDIDIDPRAKV--------ATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 153 QILMLDEPFGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITIL 207
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-212 |
1.18e-11 |
|
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: 62.77 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 32 GELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGIVFQE-----------PRLFP-WLNVLDNVMLG 99
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNyftkllegdvkVIVKPqYVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 100 LADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHT---LQQEL 176
Cdd:cd03236 106 KVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNaarLIREL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 695804877 177 LQiHQRAgttTLLVTHDVEEAVALADRVVVLSPRPG 212
Cdd:cd03236 186 AE-DDNY---VLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-212 |
2.10e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 60.66 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 28 DIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGepVTGVGKERGIvfqeprlfpwlnvldnvmlgladeklsr 107
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG--ITPVYKPQYI---------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 108 aakrqralemlervqlsefvnalpaQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTT 187
Cdd:cd03222 71 -------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
170 180
....*....|....*....|....*
gi 695804877 188 LLVTHDVEEAVALADRVVVLSPRPG 212
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-196 |
6.16e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.99 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEpVTGVGKERGIVFQeprlfpwLNVLDNVMLGL 100
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIAISAGLSGQ-------LTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 101 ADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEpfgALDALTRHTLQQELLQIH 180
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQKCLDKIY 187
|
170
....*....|....*...
gi 695804877 181 Q--RAGTTTLLVTHDVEE 196
Cdd:PRK13546 188 EfkEQNKTIFFVSHNLGQ 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-215 |
7.45e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 24 NFSLDiaAGELVALVGSSGCGKSTLLRMLVGL-ESATQGDICINGEPVT----------GVG------KERGIVfqeprl 86
Cdd:PRK13549 282 SFSLR--RGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKirnpqqaiaqGIAmvpedrKRDGIV------ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 87 fPWLNVLDNVMLGLADE-----KLSRAAKRQRALEMLERVQLSEFVNALP-AQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:PRK13549 354 -PVMGVGKNITLAALDRftggsRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 161 FGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLSprPGRIR 215
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMH--EGKLK 484
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-207 |
1.16e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 26 SLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKER--GIVFQEprlfpWLNvLDNVMLGLADE 103
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQlqKLVSDE-----WQR-NNTDMLSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 104 KLSRAA---------KRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQ 174
Cdd:PRK10938 97 DTGRTTaeiiqdevkDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190
....*....|....*....|....*....|...
gi 695804877 175 ELLQIHQrAGTTTLLVTHDVEEAVALADRVVVL 207
Cdd:PRK10938 177 LLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-213 |
4.71e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 2 TSSTLVSFRHVRKSwqqvtaLQNFSLDIAAGEL-----VALVGSSGCGKSTLLRMLVGLESATQG----DICINGEPvtg 72
Cdd:COG1245 337 EEETLVEYPDLTKS------YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGevdeDLKISYKP--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 73 vgkergivfQEprlfpwlnvLDNVMLGLADEKLSRAAKRQRA-----LEMLERVQLSEFVNALPAQLSGGMAQRVAIARG 147
Cdd:COG1245 408 ---------QY---------ISPDYDGTVEEFLRSANTDDFGssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAAC 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695804877 148 LVARPQILMLDEPFGALD---------ALTRHTLQQellqihqraGTTTLLVTHDVEEAVALADRVVVLSPRPGR 213
Cdd:COG1245 470 LSRDADLYLLDEPSAHLDveqrlavakAIRRFAENR---------GKTAMVVDHDIYLIDYISDRLMVFEGEPGV 535
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-213 |
8.53e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 8.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 2 TSSTLVSFRHVRKSwqqvtaLQNFSLD-----IAAGELVALVGSSGCGKSTLLRMLVGLESATQGDicingepvtgVGKE 76
Cdd:PRK13409 336 ERETLVEYPDLTKK------LGDFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE----------VDPE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 77 RGIVFQEPRLFPWLNvldnvmlGLADEKLSRAAKRQRA----LEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARP 152
Cdd:PRK13409 400 LKISYKPQYIKPDYD-------GTVEDLLRSITDDLGSsyykSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695804877 153 QILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEAVALADRVVVLSPRPGR 213
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-193 |
1.07e-09 |
|
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: 58.02 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICInGEPV--TGVGKERG------ 78
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVklAYVDQSRDaldpnk 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEPRlfpwlNVLDNVMLGladeklsraaKRqralEMLERVQLSEFvN-------ALPAQLSGGMAQRVAIARGLVAR 151
Cdd:TIGR03719 402 TVWEEIS-----GGLDIIKLG----------KR----EIPSRAYVGRF-NfkgsdqqKKVGQLSGGERNRVHLAKTLKSG 461
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 152 PQILMLDEPFGALDALTRHTLQQELLQIhqrAGtTTLLVTHD 193
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNF---AG-CAVVISHD 499
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-233 |
3.58e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFR--HVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-----K 75
Cdd:PLN03232 1231 SRGSIKFEdvHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGltdlrR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 76 ERGIVFQEPRLFPwlnvldnvmlGLADEKLSRAAKRQRA--LEMLERVQLSEFVN----ALPAQL-------SGGMAQRV 142
Cdd:PLN03232 1311 VLSIIPQSPVLFS----------GTVRFNIDPFSEHNDAdlWEALERAHIKDVIDrnpfGLDAEVseggenfSVGQRQLL 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 143 AIARGLVARPQILMLDEPFGAL----DALTRHTLQQELlqihqrAGTTTLLVTHDVEEAVAlADRVVVLSprPGRIREVV 218
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVdvrtDSLIQRTIREEF------KSCTMLVIAHRLNTIID-CDKILVLS--SGQVLEYD 1451
|
250
....*....|....*...
gi 695804877 219 SlalphPRQ---RDDAAF 233
Cdd:PLN03232 1452 S-----PQEllsRDTSAF 1464
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-166 |
3.67e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 32 GELVALVGSSGCGKSTLLRMLVGLESA--TQGDICINGEP--------VTGVGKERGIvfQEPRLFPWLNVLDNVMLGLA 101
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPkkqetfarISGYCEQNDI--HSPQVTVRESLIYSAFLRLP 983
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 102 DEkLSRAAKRQRALEMLERVQLSEFVNA---LPA--QLSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:PLN03140 984 KE-VSKEEKMMFVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-193 |
3.72e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 20 TALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDIcingepvtGVGKERGIV-FQEPR--LFPWLNVLDNv 96
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTKLEVAyFDQHRaeLDPEKTVMDN- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 mlgLADEK--LSRAAKRQRALEMLERVQLSEFVNALPAQ-LSGGMAQRVAIARgLVARP-QILMLDEPFGALDALTRHTL 172
Cdd:PRK11147 404 ---LAEGKqeVMVNGRPRHVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELL 479
|
170 180
....*....|....*....|.
gi 695804877 173 qQELLQIHQragTTTLLVTHD 193
Cdd:PRK11147 480 -EELLDSYQ---GTVLLVSHD 496
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-193 |
5.16e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 23 QNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICIngEPVTGVGKERgivfQEPRLFPWLNVLDNVMLG--- 99
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL--DPNERLGKLR----QDQFAFEEFTVLDTVIMGhte 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 100 ----------------LADEKLSRAAKRQ-------------RALEMLERVQLS-EFVNALPAQLSGGMAQRVAIARGLV 149
Cdd:PRK15064 92 lwevkqerdriyalpeMSEEDGMKVADLEvkfaemdgytaeaRAGELLLGVGIPeEQHYGLMSEVAPGWKLRVLLAQALF 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695804877 150 ARPQILMLDEPFGALDALTRHTLQQELlqiHQRaGTTTLLVTHD 193
Cdd:PRK15064 172 SNPDILLLDEPTNNLDINTIRWLEDVL---NER-NSTMIIISHD 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-196 |
5.29e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPV-----TGV-GKERGIVFQEprlfpwlnvLD 94
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaisSGLnGQLTGIENIE---------LK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 95 NVMLGLADEKLsraakRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALD-ALTRHTLQ 173
Cdd:PRK13545 110 GLMMGLTKEKI-----KEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCLD 184
|
170 180
....*....|....*....|...
gi 695804877 174 QelLQIHQRAGTTTLLVTHDVEE 196
Cdd:PRK13545 185 K--MNEFKEQGKTIFFISHSLSQ 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-218 |
5.60e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 21 ALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVGKERGI------VFQEPR---LFPWLN 91
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhgfalVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 92 VLDNVMLG-----------LADEKLSraAKRQRALEMLeRVQLSEFVNALpAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:PRK10982 343 IGFNSLISnirnyknkvglLDNSRMK--SDTQWVIDSM-RVKTPGHRTQI-GSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 161 FGALDALTRHTLQQELLQIHQRaGTTTLLVTHDVEEAVALADRVVVLSprPGRIREVV 218
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMS--NGLVAGIV 473
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
29-208 |
7.98e-09 |
|
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: 54.53 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 29 IAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICING-----EPVTGVGKERGIVFQEPRLFPwlnvlDNVMLGLADE 103
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRLSIILQDPILFS-----GSIRFNLDPE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 104 klsRAAKRQRALEMLERVQLSEFVNALPAQL-----------SGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTL 172
Cdd:cd03288 119 ---CKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENIL 195
|
170 180 190
....*....|....*....|....*....|....*.
gi 695804877 173 QQELLQIHqrAGTTTLLVTHDVeEAVALADRVVVLS 208
Cdd:cd03288 196 QKVVMTAF--ADRTVVTIAHRV-STILDADLVLVLS 228
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-213 |
1.72e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.71 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 19 VTALQNFSLDIAAGELVALVGSSGCGKSTLLrmLVGLESATQGDIcINGEPVTGvgkERGIVFqeprlfpwLNVLDNVM- 97
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARL-ISFLPKFS---RNKLIF--------IDQLQFLId 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 98 LGLADEKLSRAAkrqralemlervqlsefvnalpAQLSGGMAQRVAIARGLVARPQ--ILMLDEPFGALDALTRHTLQQE 175
Cdd:cd03238 74 VGLGYLTLGQKL----------------------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190
....*....|....*....|....*....|....*...
gi 695804877 176 LLQIHQRaGTTTLLVTHDvEEAVALADRVVVLSPRPGR 213
Cdd:cd03238 132 IKGLIDL-GNTVILIEHN-LDVLSSADWIIDFGPGSGK 167
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
39-192 |
2.76e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 39 GSSGCGKSTLLRMLVGLESATQGDICINGEPV--------TGVGKERGIVFQeprlfpwLNVLDNvmLGLADEKLSRAAK 110
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniakpycTYIGHNLGLKLE-------MTVFEN--LKFWSEIYNSAET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 111 RQRALEMLervQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQeLLQIHQRAGTTTLLV 190
Cdd:PRK13541 104 LYAAIHYF---KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKANSGGIVLLS 179
|
..
gi 695804877 191 TH 192
Cdd:PRK13541 180 SH 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-203 |
3.50e-08 |
|
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: 51.22 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 32 GELVALVGSSGCGKSTLLRMLVGLESATQGDIC-INGEpvtgvgkergivfqeprlfpwlnvldnvmlgladeklsraak 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGE------------------------------------------ 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 111 rqRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQE-----LLQIHQRAGT 185
Cdd:smart00382 40 --DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNL 117
|
170
....*....|....*...
gi 695804877 186 TTLLVTHDVEEAVALADR 203
Cdd:smart00382 118 TVILTTNDEKDLGPALLR 135
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-197 |
8.61e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGleSATQG---DICI------NGEPVTGVGKE 76
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLfgrrrgSGETIWDIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 77 RGIV----FQEPRLFpwLNVLDNVMLGLADE-KLSRA---AKRQRALEMLERVQLSEFVNALPAQ-LSGGMAQRVAIARG 147
Cdd:PRK10938 338 IGYVssslHLDYRVS--TSVRNVILSGFFDSiGIYQAvsdRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRA 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695804877 148 LVARPQILMLDEPFGALDALTRHTLQQELLQIHQRAGTTTLLVTHDVEEA 197
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-192 |
1.06e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.06 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGE---------PVTGVGKERGIVfqeprLFPwLNV 92
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgklfyvpqrPYMTLGTLRDQI-----IYP-DSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 93 LDNVMLGLADEKLsraakrqraLEMLERVQLS---------EFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGA 163
Cdd:TIGR00954 542 EDMKRRGLSDKDL---------EQILDNVQLThilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180
....*....|....*....|....*....
gi 695804877 164 LDAltrhTLQQELLQIHQRAGTTTLLVTH 192
Cdd:TIGR00954 613 VSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-165 |
1.10e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 1 MTSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLES--ATQGDICINGEPVTGVGKE-- 76
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEer 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 77 --RGI--VFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLERV-QLSEFVNALPAQL--------SGGMAQRVA 143
Cdd:CHL00131 82 ahLGIflAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIInEKLKLVGMDPSFLsrnvnegfSGGEKKRNE 161
|
170 180
....*....|....*....|..
gi 695804877 144 IARGLVARPQILMLDEPFGALD 165
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLD 183
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-213 |
1.25e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 50.72 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTL----------LRMLVGLESATQGDICINGEP----VTGVGKERGI----VFQE 83
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQFLGQMDKPdvdsIEGLSPAIAIdqktTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 84 PR--------LFPWLNVLdnvmlgladekLSRAAKRQRaLEMLERVQLSEF-VNALPAQLSGGMAQRVAIAR----GLVA 150
Cdd:cd03270 91 PRstvgtvteIYDYLRLL-----------FARVGIRER-LGFLVDVGLGYLtLSRSAPTLSGGEAQRIRLATqigsGLTG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695804877 151 rpQILMLDEPFGALDALTRHTLQqELLQIHQRAGTTTLLVTHDvEEAVALADRVVVLSPRPGR 213
Cdd:cd03270 159 --VLYVLDEPSIGLHPRDNDRLI-ETLKRLRDLGNTVLVVEHD-EDTIRAADHVIDIGPGAGV 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-216 |
1.39e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 3 SSTLVSFRHV--RKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-----K 75
Cdd:PLN03130 1234 SSGSIKFEDVvlRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlmdlrK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 76 ERGIVFQEPRLFPwlnvldnvmlGLADEKLSRAAKRQRA--LEMLERVQLSEFVNALPAQL-----------SGGMAQRV 142
Cdd:PLN03130 1314 VLGIIPQAPVLFS----------GTVRFNLDPFNEHNDAdlWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLL 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695804877 143 AIARGLVARPQILMLDEPFGAL----DALTRHTLQQELlqihqrAGTTTLLVTHDVEEAVAlADRVVVLSprPGRIRE 216
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVdvrtDALIQKTIREEF------KSCTMLIIAHRLNTIID-CDRILVLD--AGRVVE 1452
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-212 |
3.41e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 32 GELVALVGSSGCGKSTLLRMLVGLESATQGDIciNGEPvtgvGKERgiVFQEPR---LFPWLNVLDN------------- 95
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEP----SWDE--VLKRFRgteLQDYFKKLANgeikvahkpqyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 96 ----VMLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHT 171
Cdd:COG1245 171 lipkVFKGTVRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLN 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695804877 172 ---LQQELLqihqRAGTTTLLVTHDVeeAV--ALADRVVVLSPRPG 212
Cdd:COG1245 251 varLIRELA----EEGKYVLVVEHDL--AIldYLADYVHILYGEPG 290
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-210 |
3.43e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 12 VRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVglesatqGDIcingEPVTGVGK--ERGIV--------- 80
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GEL----EPDSGTVKwsENANIgyyaqdhay 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 81 -FQEPR-LFPWlnvLDNVMLGLADEKLSRAakrqraleMLERVQLS-EFVNALPAQLSGGMAQRVAIARGLVARPQILML 157
Cdd:PRK15064 394 dFENDLtLFDW---MSQWRQEGDDEQAVRG--------TLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695804877 158 DEPFGALDALTRHTLQQELlqiHQRAGtTTLLVTHDVEEAVALADRVVVLSPR 210
Cdd:PRK15064 463 DEPTNHMDMESIESLNMAL---EKYEG-TLIFVSHDREFVSSLATRIIEITPD 511
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-193 |
3.59e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 7 VSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICInGEPV--TGVGKERG------ 78
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVklAYVDQSRDaldpnk 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 79 IVFQEprlfpwlnV---LDNVMLGladeklsraaKRqralEMLERVQLSEFVNALPAQ------LSGGMAQRVAIARGLV 149
Cdd:PRK11819 404 TVWEE--------IsggLDIIKVG----------NR----EIPSRAYVGRFNFKGGDQqkkvgvLSGGERNRLHLAKTLK 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695804877 150 ARPQILMLDEPFGALDALTRHTLQQELLQIhqrAGtTTLLVTHD 193
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVETLRALEEALLEF---PG-CAVVISHD 501
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-177 |
7.30e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDIcingepvtgvGKERGI---VFQ 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI----------GLAKGIklgYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 83 EPRLfPWLNvldnvmlglADEK----LSRAAKRQraLEMLERVQLSEF------VNALPAQLSGGMAQRVAIARGLVARP 152
Cdd:PRK10636 382 QHQL-EFLR---------ADESplqhLARLAPQE--LEQKLRDYLGGFgfqgdkVTEETRRFSGGEKARLVLALIVWQRP 449
|
170 180
....*....|....*....|....*
gi 695804877 153 QILMLDEPFGALDALTRHTLQQELL 177
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRQALTEALI 474
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-165 |
9.41e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 6 LVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLE--SATQGDICINGEPVTGVGKE----RGI 79
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEdragEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 80 --VFQEPRLFPwlNVLDNVMLGLAdeklSRAAKRQRALEMLERVQLSEFVNA------LPAQL---------SGGMAQRV 142
Cdd:PRK09580 81 fmAFQYPVEIP--GVSNQFFLQTA----LNAVRSYRGQEPLDRFDFQDLMEEkiallkMPEDLltrsvnvgfSGGEKKRN 154
|
170 180
....*....|....*....|...
gi 695804877 143 AIARGLVARPQILMLDEPFGALD 165
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLD 177
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
132-212 |
1.01e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 132 AQLSGGMAQRVAIARGLVARPQILM--LDEPFGALDALTRHTLQQeLLQIHQRAGTTTLLVTHDvEEAVALADRVVVLSP 209
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGITyiLDEPSIGLHPQDTHKLIN-VIKKLRDQGNTVLLVEHD-EQMISLADRIIDIGP 552
|
...
gi 695804877 210 RPG 212
Cdd:PRK00635 553 GAG 555
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-168 |
1.91e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 32 GELVALVGSSGCGKSTLLRMLVGLESA---TQGDICINGEPV-TGVGKERGIVFQEPRLFPWLNVLDNVMLGLA---DEK 104
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLdSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYlrqPKS 868
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695804877 105 LSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMA----QRVAIARGLVARPQ-ILMLDEPFGALDALT 168
Cdd:TIGR00956 869 VSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNveqrKRLTIGVELVAKPKlLLFLDEPTSGLDSQT 937
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-212 |
2.18e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 32 GELVALVGSSGCGKSTLLRMLVGLesaTQGDICINGEPVT--GV-----GKERGIVFQE-------PRLFP-WLNVLDNV 96
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGE---LIPNLGDYEEEPSwdEVlkrfrGTELQNYFKKlyngeikVVHKPqYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 97 MLGLADEKLSRAAKRQRALEMLERVQLSEFVNALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHT---LQ 173
Cdd:PRK13409 176 FKGKVRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNvarLI 255
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695804877 174 QELLQihqraGTTTLLVTHDVeeAV--ALADRVVVLSPRPG 212
Cdd:PRK13409 256 RELAE-----GKYVLVVEHDL--AVldYLADNVHIAYGEPG 289
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-208 |
3.38e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 9 FRHVRKSWQQ--VTALQNFSLDIAAGELVALVGSSGCGKSTLLRML----VGLESATQGDICINGEPVTGVGKE-RGIVF 81
Cdd:TIGR00956 62 FRKLKKFRDTktFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHyRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 82 QEPRL---FPWLNV---LDNVML----GLADEKLSRA--AKRQRALEM----LERVQLSEFVNALPAQLSGGMAQRVAIA 145
Cdd:TIGR00956 142 YNAETdvhFPHLTVgetLDFAARcktpQNRPDGVSREeyAKHIADVYMatygLSHTRNTKVGNDFVRGVSGGERKRVSIA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 146 RGLVARPQILMLDEPFGALDALTrhTLQ-QELLQIHQRAGTTTLLVT--HDVEEAVALADRVVVLS 208
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSAT--ALEfIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLY 285
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-193 |
4.15e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 24 NFSLDIAAgeLVALVGSSGCGKSTLLRMLVGlesatqgdiciNGEPVTGV----GKERGIVFQEPRLfPWLNVLDNVML- 98
Cdd:PLN03073 529 NFGIDLDS--RIAMVGPNGIGKSTILKLISG-----------ELQPSSGTvfrsAKVRMAVFSQHHV-DGLDLSSNPLLy 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 99 ------GLADEKLsraakrqralemleRVQLSEF--VNALPAQ----LSGGMAQRVAIARGLVARPQILMLDEPFGALDA 166
Cdd:PLN03073 595 mmrcfpGVPEQKL--------------RAHLGSFgvTGNLALQpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
170 180
....*....|....*....|....*..
gi 695804877 167 LTRHTLQQELLQIHqragTTTLLVTHD 193
Cdd:PLN03073 661 DAVEALIQGLVLFQ----GGVLMVSHD 683
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-213 |
9.61e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 134 LSGGMAQRVAIAR----GLVArpQILMLDEPFGALDALTRHTLQQELLQIhQRAGTTTLLVTHDvEEAVALADRVVVLSP 209
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsGLTG--VLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDIGP 564
|
....
gi 695804877 210 RPGR 213
Cdd:TIGR00630 565 GAGE 568
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-211 |
1.27e-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: 41.82 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 34 LVALVGSSGCGKSTLLRML-VGL--ESATQGDICINGEPVTGVGKERGIVfqepRLFPWLNvldnvmlglADEKLsraaK 110
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALkYALtgELPPNSKGGAHDPKLIREGEVRAQV----KLAFENA---------NGKKY----T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 111 RQRALEMLERV------QLSEFVNALPAQLSGG------MAQRVAIARGLVARPQILMLDEPFGALDA---------LTR 169
Cdd:cd03240 87 ITRSLAILENVifchqgESNWPLLDMRGRCSGGekvlasLIIRLALAETFGSNCGILALDEPTTNLDEenieeslaeIIE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695804877 170 HTLQQELLQIhqragtttLLVTHDvEEAVALADRVVVLSPRP 211
Cdd:cd03240 167 ERKSQKNFQL--------IVITHD-EELVDAADHIYRVEKDG 199
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-165 |
1.40e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEpvtgvgKERGIVFQEPrlfPWLNV--LDNVM-- 97
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN------WQLAWVNQET---PALPQpaLEYVIdg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 98 ----------LGLADEKLSRAA---------------KRQRALEML-----ERVQLSEFVNAlpaqLSGGMAQRVAIARG 147
Cdd:PRK10636 88 dreyrqleaqLHDANERNDGHAiatihgkldaidawtIRSRAASLLhglgfSNEQLERPVSD----FSGGWRMRLNLAQA 163
|
170
....*....|....*...
gi 695804877 148 LVARPQILMLDEPFGALD 165
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLD 181
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
31-63 |
2.08e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.23 E-value: 2.08e-04
10 20 30
....*....|....*....|....*....|...
gi 695804877 31 AGELVALVGSSGCGKSTLLRMLVGLESATQGDI 63
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
22-193 |
2.83e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.76 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNF-------SLDIAAGeLVALVGSSGCGKSTLLRML-------VGLESATQGDICINGEPVTGV-------------- 73
Cdd:COG0419 7 LENFrsyrdteTIDFDDG-LNLIVGPNGAGKSTILEAIryalygkARSRSKLRSDLINVGSEEASVelefehggkryrie 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 74 -------------GKERGIVFQepRLFPwLNVLDNVM--LGLADEKLSRAAKRQRALEMLERVQLSEFVNALPA-QLSGG 137
Cdd:COG0419 86 rrqgefaefleakPSERKEALK--RLLG-LEIYEELKerLKELEEALESALEELAELQKLKQEILAQLSGLDPIeTLSGG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 138 MAQRVAIARGLVarpqiLMLDepFGALDALTRHTLQQELLQIHqragtttlLVTHD 193
Cdd:COG0419 163 ERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
134-220 |
5.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 134 LSGG------MAQRVAIARGLVARPQILMLDEPFGALDALTRHTL----QQELLQIHQragttTLLVTHDvEEAVALADR 203
Cdd:PRK03918 789 LSGGerialgLAFRLALSLYLAGNIPLLILDEPTPFLDEERRRKLvdimERYLRKIPQ-----VIIVSHD-EELKDAADY 862
|
90
....*....|....*...
gi 695804877 204 VVVLSPRPGRIR-EVVSL 220
Cdd:PRK03918 863 VIRVSLEGGVSKvEVVSL 880
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-212 |
8.66e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 134 LSGGMAQRVAIARGLVAR---PQILMLDEPFGALdaltrHTLQ-QELLQIHQR---AGTTTLLVTH--DVeeaVALADRV 204
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL-----HFDDiKKLLEVLQRlvdKGNTVVVIEHnlDV---IKTADYI 901
|
....*...
gi 695804877 205 VVLSPRPG 212
Cdd:TIGR00630 902 IDLGPEGG 909
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-160 |
1.86e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLE--SATQGDICINGEPVT--GVGK--ERGIVF-QEPRLFPWLNVLD 94
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDvsTVSDaiDAGLAYvTEDRKGYGLNLID 355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695804877 95 NVMLGLADEKLSRAAKRQRALEMLERVQLSEF----------VNALPAQLSGGMAQRVAIARGLVARPQILMLDEP 160
Cdd:NF040905 356 DIKRNITLANLGKVSRRGVIDENEEIKVAEEYrkkmniktpsVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-87 |
2.72e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.99 E-value: 2.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695804877 22 LQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQGDICINGEPVTGVG-----KERGIVFQEPRLF 87
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGlrelrRQFSMIPQDPVLF 1396
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
19-63 |
2.95e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.38 E-value: 2.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 695804877 19 VTALQNFSLDIAA-----GELVALVGSSGCGKSTLLRMLVGLESATQGDI 63
Cdd:PRK01889 177 VSALDGEGLDVLAawlsgGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
133-165 |
3.73e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 3.73e-03
10 20 30
....*....|....*....|....*....|...
gi 695804877 133 QLSGGMAQRVAIARGLVARPQILMLDEPFGALD 165
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
134-212 |
4.56e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.59 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695804877 134 LSGGMAQRVAIARGLVAR---PQILMLDEPFGALdaltrHTLQ-QELLQIHQR---AGTTTLLVTHDVeEAVALADRVVV 206
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGL-----HFHDvKKLLEVLQRlvdKGNTVVVIEHNL-DVIKCADWIID 243
|
....*.
gi 695804877 207 LSPRPG 212
Cdd:cd03271 244 LGPEGG 249
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
34-83 |
7.50e-03 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 36.55 E-value: 7.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 695804877 34 LVALVGSSGCGKSTLLRMLVglESATQGDIC-INGePVTGV-GKERGIVFQE 83
Cdd:cd01882 41 VVVVVGPPGVGKSTLIRSLI--KRYTKQNLSdIKG-PITIVtGKKRRLTFIE 89
|
|
| |
