|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-246 |
8.52e-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: 375.20 E-value: 8.52e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIFQ 82
Cdd:COG1116 8 LELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 EHRLFPWLTVEENIAanFNLKQQDV-----RRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:COG1116 88 EPALLPWLTVLDNVA--LGLELRGVpkaerRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 158 FGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQARPGRIHKILPVNLPFPRD---RTSTAFQSLR 234
Cdd:COG1116 166 FGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDrelRTSPEFAALR 245
|
250
....*....|..
gi 637173694 235 QKVLSEFEKTDE 246
Cdd:COG1116 246 AEILDLLREEAE 257
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-219 |
8.42e-117 |
|
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: 333.28 E-value: 8.42e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIFQ 82
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 EHRLFPWLTVEENIAanFNLKQQDV-----RRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:cd03293 81 QDALLPWLTVLDNVA--LGLELQGVpkaeaRERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637173694 158 FGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQARPGRIHKILPVNL 219
Cdd:cd03293 159 FSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-239 |
8.55e-88 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 261.34 E-value: 8.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFI 80
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 81 FQEHRLFPWLTVEENIAanFNLKQQDV-----RRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:COG4525 82 FQKDALLPWLNVLDNVA--FGLRLRGVpkaerRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQARPGRIHKILPvnLPFPRD----------R 225
Cdd:COG4525 160 EPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLE--LDFSRRflagedaraiK 237
|
250
....*....|....
gi 637173694 226 TSTAFQSLRQKVLS 239
Cdd:COG4525 238 SDPAFIALREELLD 251
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-211 |
5.60e-81 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 246.93 E-value: 5.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT-----EPGMkq 77
Cdd:COG3842 6 LELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglppeKRNV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 GFIFQEHRLFPWLTVEENIAanFNLKQQ-----DVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEIL 152
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVA--FGLRMRgvpkaEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 153 LLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRI 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-211 |
3.90e-78 |
|
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: 234.72 E-value: 3.90e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---GF 79
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQEHRLFPWLTVEENIAanFNLKQQ-----DVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLL 154
Cdd:cd03259 77 VFQDYALFPHLTVAENIA--FGLKLRgvpkaEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637173694 155 DEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE--GRI 209
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-225 |
8.61e-77 |
|
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: 231.97 E-value: 8.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIFQEHRLFPWLTVEENIA---- 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIAlavd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 -ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDI 176
Cdd:TIGR01184 81 rVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 637173694 177 WQEKKTTMMLVTHDIDESIYLGNEIVLMQARPG-RIHKILPVNLPFPRDR 225
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAaNIGQILEVPFPRPRDR 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-211 |
1.63e-74 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 230.42 E-value: 1.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGG-----------RR 69
Cdd:COG1118 1 MSIEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlppreRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 70 ItepgmkqGFIFQEHRLFPWLTVEENIAanFNLK-----QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARA 144
Cdd:COG1118 77 V-------GFVFQHYALFPHMTVAENIA--FGLRvrppsKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637173694 145 LLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ--GRI 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-190 |
1.43e-69 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 213.37 E-value: 1.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVD--KSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ- 77
Cdd:COG1136 1 MSPLLELRNltKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 --------GFIFQEHRLFPWLTVEENIA-----ANFNLKqqDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARA 144
Cdd:COG1136 81 arlrrrhiGFVFQFFNLLPELTALENVAlplllAGVSRK--ERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 637173694 145 LLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHD 190
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-223 |
5.38e-68 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 210.71 E-value: 5.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 13 WKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIFQEHRLFPWLTV 92
Cdd:PRK11248 8 YADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIAanFNLKQQDVRR-----KVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRK 167
Cdd:PRK11248 88 QDNVA--FGLQLAGVEKmqrleIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637173694 168 HLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQARPGRIHKILPvnLPFPR 223
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLP--LNFAR 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-214 |
8.31e-67 |
|
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: 206.70 E-value: 8.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkDKQTirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE-PGMKQGF-- 79
Cdd:cd03300 1 IELENVSKFY--GGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKRPVnt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQEHRLFPWLTVEENIAanFNLK-----QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLL 154
Cdd:cd03300 77 VFQNYALFPHLTVFENIA--FGLRlkklpKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 155 DEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKI 214
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK--GKIQQI 212
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-211 |
1.02e-66 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 208.79 E-value: 1.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwKDKQTirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE--P-----GM 75
Cdd:COG1125 2 IEFENVTKRY-PDGTV--AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDldPvelrrRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 76 kqGFIFQEHRLFPWLTVEENIAANFNLKQQD---VRRKVDELIEIVRL--KGFEHAYPHELSGGMSQRVAIARALLRDPE 150
Cdd:COG1125 79 --GYVIQQIGLFPHMTVAENIATVPRLLGWDkerIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637173694 151 ILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRI 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-192 |
2.42e-65 |
|
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: 202.33 E-value: 2.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ----GFIFQEHRLFPWLTVEENIAANFNL---KQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPE 150
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPLLLagvPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 637173694 151 ILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDID 192
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE 202
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-214 |
1.31e-64 |
|
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: 201.41 E-value: 1.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ--- 77
Cdd:cd03296 1 MSIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 GFIFQEHRLFPWLTVEENIAanFNLK---------QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRD 148
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVA--FGLRvkprserppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637173694 149 PEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKI 214
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK--GRIEQV 218
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-214 |
1.30e-63 |
|
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: 202.57 E-value: 1.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE--PGMKQ-GF 79
Cdd:TIGR03265 5 LSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRlpPQKRDyGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQEHRLFPWLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDE 156
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAyglKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 157 PFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKI 214
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNH--GVIEQV 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-211 |
2.18e-63 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 201.84 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 2 TISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT-----EPGMk 76
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdlppkDRNI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 77 qGFIFQEHRLFPWLTVEENIAanFNLK-----QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEI 151
Cdd:COG3839 78 -AMVFQSYALYPHMTVYENIA--FPLKlrkvpKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 152 LLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND--GRI 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-211 |
1.85e-62 |
|
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: 195.98 E-value: 1.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKqtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 GFIFQEHRLFPWLTVEENIAANFNL---KQQDVRRKVDELIEIVRL--KGFEHAYPHELSGGMSQRVAIARALLRDPEIL 152
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLlkwPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 153 LLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN--GEI 214
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
27-211 |
3.14e-59 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 192.24 E-value: 3.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 27 LSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---------GFIFQEHRLFPWLTVEENIA 97
Cdd:COG4175 48 FDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrkkmSMVFQHFALLPHRTVLENVA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 anFNLKQQDV-----RRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDV 172
Cdd:COG4175 128 --FGLEIQGVpkaerRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDE 205
|
170 180 190
....*....|....*....|....*....|....*....
gi 637173694 173 LLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:COG4175 206 LLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDGRI 242
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-204 |
2.42e-58 |
|
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: 185.18 E-value: 2.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkDKQTirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:COG1127 6 IEVRNLTKSF--GDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ---GFIFQEHRLFPWLTVEENIA----ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPE 150
Cdd:COG1127 82 rriGMLFQGGALFDSLTVFENVAfplrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637173694 151 ILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVL 215
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
3-214 |
4.45e-58 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 184.62 E-value: 4.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---GF 79
Cdd:TIGR00968 1 IEIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDrkiGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQEHRLFPWLTVEENIAANFNLKQQD---VRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDE 156
Cdd:TIGR00968 77 VFQHYALFKHLTVRDNIAFGLEIRKHPkakIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 157 PFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKI 214
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSN--GKIEQI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-211 |
4.96e-57 |
|
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: 189.73 E-value: 4.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFW-KDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ--------G 78
Cdd:COG1123 266 LSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrrrvQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQ--EHRLFPWLTVEENIA----ANFNLKQQDVRRKVDELIEIVRL-KGFEHAYPHELSGGMSQRVAIARALLRDPEI 151
Cdd:COG1123 346 MVFQdpYSSLNPRMTVGDIIAeplrLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 152 LLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG1123 426 LILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--GRI 483
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-204 |
5.70e-57 |
|
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: 180.74 E-value: 5.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 7 IVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIF 81
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 82 Q--EHRLFPwLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDE 156
Cdd:cd03225 82 QnpDDQFFG-PTVEEEVAfglENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 637173694 157 PFGALDAFTRKHLQDVLLDIWQEKKTTMMlVTHDIDESIYLGNEIVLM 204
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIII-VTHDLDLLLELADRVIVL 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-238 |
1.26e-56 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 181.41 E-value: 1.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIFQEHRLFPWLTVEENIAan 99
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARLLPWKKVIDNVG-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 100 FNLKQqDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQE 179
Cdd:PRK11247 104 LGLKG-QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQ 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 180 KKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKILPVNLPFPRDRTSTAFQSLRQKVL 238
Cdd:PRK11247 183 HGFTVLLVTHDVSEAVAMADRVLLIEE--GKIGLDLTVDLPRPRRRGSARLAELEAEVL 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-211 |
3.47e-56 |
|
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: 180.92 E-value: 3.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 14 KDKQTIRVlEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---------GFIFQEH 84
Cdd:cd03294 33 KTGQTVGV-NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiSMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 85 RLFPWLTVEENIAanFNLKQQDV-----RRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:cd03294 112 ALLPHRTVLENVA--FGLEVQGVpraerEERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637173694 160 ALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRL 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-206 |
3.55e-56 |
|
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: 177.76 E-value: 3.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 10 KSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM-------KQGFIFQ 82
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelpplrrRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 EHRLFPWLTVEENIAanfnlkqqdvrrkvdelieivrlkgfehaYPheLSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:cd03229 84 DFALFPHLTVLENIA-----------------------------LG--LSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 637173694 163 AFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQA 206
Cdd:cd03229 133 PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-239 |
4.58e-56 |
|
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: 179.61 E-value: 4.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 GFIFQEHR--LFPWLTVEENIAANFNL-KQQDVRRKVDELIEIVRL-KGFEHAYPHELSGGMSQRVAIARALLRDPEILL 153
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDRILAEPLRIhGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 154 LDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKILPVNLPFpRDRTSTAFQSL 233
Cdd:COG1124 162 LDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTVADLL-AGPKHPYTREL 238
|
....*.
gi 637173694 234 RQKVLS 239
Cdd:COG1124 239 LAASLA 244
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-211 |
6.96e-56 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 178.32 E-value: 6.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE------PGMK 76
Cdd:COG2884 2 IRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrreiPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 77 Q--GFIFQEHRLFPWLTVEENIAanFNL-----KQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDP 149
Cdd:COG2884 79 RriGVVFQDFRLLPDRTVYENVA--LPLrvtgkSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637173694 150 EILLLDEPFGALDAFTRKHLQDVLLDIwQEKKTTMMLVTHDIDesiylgneivLMQARPGRI 211
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLE----------LVDRMPKRV 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-204 |
9.64e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 182.21 E-value: 9.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSFWKDKqtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR---RITEPGMKQ 77
Cdd:PRK10851 1 MSIEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsRLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 GFIFQEHRLFPWLTVEENIAanFNLK---------QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRD 148
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIA--FGLTvlprrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637173694 149 PEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVM 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-211 |
1.51e-55 |
|
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: 177.91 E-value: 1.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQ--EHRLF-PwlT 91
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrkvGLVFQnpDDQLFaP--T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 92 VEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKH 168
Cdd:COG1122 93 VEEDVAfgpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 169 LQDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG1122 173 LLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDD--GRI 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-204 |
5.96e-55 |
|
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: 176.54 E-value: 5.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkDKQTirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:cd03261 1 IELRGLTKSF--GGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ---GFIFQEHRLFPWLTVEENIA----ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPE 150
Cdd:cd03261 77 rrmGMLFQSGALFDSLTVFENVAfplrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 637173694 151 ILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVL 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-211 |
8.11e-55 |
|
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: 175.77 E-value: 8.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ---GFIFQE--HRLFPWLTVEENIA-----ANFNLKQQDVRRKVDELIEIVRL-KGFEHAYPHELSGGMSQRVAIARALL 146
Cdd:cd03257 82 keiQMVFQDpmSSLNPRMTIGEQIAeplriHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637173694 147 RDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA--GKI 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-214 |
1.46e-54 |
|
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: 174.75 E-value: 1.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkDKQTirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---GF 79
Cdd:cd03301 1 VELENVTKRF--GNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQEHRLFPWLTVEENIAanFNLK-----QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLL 154
Cdd:cd03301 77 VFQNYALYPHMTVYDNIA--FGLKlrkvpKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 155 DEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKI 214
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND--GQIQQI 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-212 |
1.61e-53 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 172.63 E-value: 1.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 27 LSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT--EPG-----MkqgfIFQEHRLFPWLTVEENIA-- 97
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTalPPAerpvsM----LFQENNLFPHLTVAQNIGlg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 --ANFNLKQQDvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLD 175
Cdd:COG3840 96 lrPGLKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 637173694 176 IWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIH 212
Cdd:COG3840 175 LCRERGLTVLMVTHDPEDAARIADRVLLVAD--GRIA 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-214 |
2.51e-53 |
|
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: 171.71 E-value: 2.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 30 IPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI--TEPGM-------KQGFIFQEHRLFPWLTVEENIAANF 100
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKInlppqqrKIGLVFQQYALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 101 NLKQQDVRR-KVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQE 179
Cdd:cd03297 101 KRKRNREDRiSVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 180 KKTTMMLVTHDIDESIYLGNEIVLMqaRPGRIHKI 214
Cdd:cd03297 181 LNIPVIFVTHDLSEAEYLADRIVVM--EDGRLQYI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-211 |
7.05e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.01 E-value: 7.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE--PGMKQ--G 78
Cdd:COG1131 1 IEVRGLTKRY-GDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARdpAEVRRriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQEHRLFPWLTVEENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:COG1131 77 YVPQEPALYPDLTVRENLrffARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG1131 157 EPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDK--GRI 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-214 |
1.51e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 172.05 E-value: 1.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkDKQTIrvLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFI-- 80
Cdd:PRK09452 15 VELRGISKSF--DGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVnt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 81 -FQEHRLFPWLTVEENIAanFNLKQQ-----DVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLL 154
Cdd:PRK09452 91 vFQSYALFPHMTVFENVA--FGLRMQktpaaEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 155 DEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRIHKI 214
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRIEQD 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-211 |
2.01e-51 |
|
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: 166.55 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPG-------M 75
Cdd:cd03262 1 IEIKNLHKSF-GDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkninelrQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 76 KQGFIFQEHRLFPWLTVEENIAAN----FNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEI 151
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLApikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 152 LLLDEPFGALDAFTRKHLQDVLLDIWQEkKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDD--GRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-211 |
4.27e-51 |
|
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: 173.94 E-value: 4.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL---DTAYDGQILIGGRRITEPGMKQ 77
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 -----GFIFQE--HRLFPwLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLR 147
Cdd:COG1123 81 rgrriGMVFQDpmTQLNP-VTVGDQIAealENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637173694 148 DPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRI 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-192 |
5.30e-51 |
|
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: 166.22 E-value: 5.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ---GFIFQEHRLFPWLTVEENIAANFNL---KQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEI 151
Cdd:cd03258 82 rriGMIFQHFNLLSSRTVFENVALPLEIagvPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 637173694 152 LLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDID 192
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEME 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-191 |
1.76e-50 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 165.17 E-value: 1.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPG-------M 75
Cdd:COG1126 2 IEIENLHKSF-GDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKkdinklrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 76 KQGFIFQEHRLFPWLTVEENIA----ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEI 151
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTlapiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 637173694 152 LLLDEPFGALDAFTRKHLQDVLLDIWQEkKTTMMLVTHDI 191
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEM 196
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-211 |
6.36e-50 |
|
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: 167.20 E-value: 6.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIvdksfwkdKQTirvLEDLRLSI---IPGEFVTVI-GPSGCGKSTLLKIISGLDTAYDGQILIGG--------- 67
Cdd:COG4148 1 MMLEVDF--------RLR---RGGFTLDVdftLPGRGVTALfGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsarg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 68 -------RRItepgmkqGFIFQEHRLFPWLTVEENIaaNFNLKQQDVRRKVDELIEIVRLKGFEH---AYPHELSGGMSQ 137
Cdd:COG4148 70 iflpphrRRI-------GYVFQEARLFPHLSVRGNL--LYGRKRAPRAERRISFDEVVELLGIGHlldRRPATLSGGERQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637173694 138 RVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQ--GRV 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-190 |
2.24e-49 |
|
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: 162.22 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT----EP----- 73
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldeDArarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 74 GMKQGFIFQEHRLFPWLTVEENIAANFNLKQQ-DVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEIL 152
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVMLPLELAGRrDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 637173694 153 LLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHD 190
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHD 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-192 |
5.71e-49 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 164.10 E-value: 5.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ---GFIFQEHRLFPWLTVEENIAanFNLKQQDV-----RRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDP 149
Cdd:COG1135 82 rkiGMIFQHFNLLSSRTVAENVA--LPLEIAGVpkaeiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 150 EILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDID 192
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMD 202
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
21-211 |
1.44e-48 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 164.01 E-value: 1.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTA--YDGQILIGGRRITE-PGMKQGF--IFQEHRLFPWLTVEEN 95
Cdd:TIGR03258 20 VLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHaPPHKRGLalLFQNYALFPHLKVEDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAanFNLKQQ-----DVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQ 170
Cdd:TIGR03258 100 VA--FGLRAQkmpkaDIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRANMR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 637173694 171 DVLLDIWQE-KKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:TIGR03258 178 EEIAALHEElPELTILCVTHDQDDALTLADKAGIM--KDGRL 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-216 |
1.78e-48 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 163.35 E-value: 1.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFWKDkqtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFI---FQEH 84
Cdd:PRK11432 12 ITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIcmvFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 85 RLFPWLTVEENIAanFNLKQQDV-----RRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:PRK11432 88 ALFPHMSLGENVG--YGLKMLGVpkeerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637173694 160 ALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKILP 216
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNK--GKIMQIGS 220
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-214 |
2.39e-48 |
|
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: 162.28 E-value: 2.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 37 VIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE-PGMKQ--GFIFQEHRLFPWLTVEENIAanFNLKQQDVRR---- 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNvPPHLRhiNMVFQSYALFPHMTVEENVA--FGLKMRKVPRaeik 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 110 -KVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVT 188
Cdd:TIGR01187 79 pRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVT 158
|
170 180
....*....|....*....|....*.
gi 637173694 189 HDIDESIYLGNEIVLMqaRPGRIHKI 214
Cdd:TIGR01187 159 HDQEEAMTMSDRIAIM--RKGKIAQI 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-211 |
2.52e-48 |
|
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: 158.81 E-value: 2.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 24 DLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT--EPGMKQ-GFIFQEHRLFPWLTVEENIA--- 97
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaaPPADRPvSMLFQENNLFAHLTVEQNVGlgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 -ANFNLKQQDvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDI 176
Cdd:cd03298 96 sPGLKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 177 WQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDN--GRI 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-211 |
3.00e-47 |
|
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: 156.73 E-value: 3.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 13 WKDKQtirvLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE--PGMKQ-GFIFQEHRLFPW 89
Cdd:cd03299 10 WKEFK----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNlpPEKRDiSYVPQNYALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEENIAanFNLKQQDVRRKVDE--LIEIVRLKGFEHA---YPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:cd03299 86 MTVYKNIA--YGLKKRKVDKKEIErkVLEIAEMLGIDHLlnrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637173694 165 TRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:cd03299 164 TKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKL 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-204 |
2.00e-46 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 158.85 E-value: 2.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 10 KSFwkDKQtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE-PGMKQ--GFIFQEHRL 86
Cdd:PRK11607 27 KSF--DGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPYQRpiNMMFQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 87 FPWLTVEENIAanFNLKQQ-----DVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGAL 161
Cdd:PRK11607 103 FPHMTVEQNIA--FGLKQDklpkaEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 162 DAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:PRK11607 181 DKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
22-211 |
5.58e-46 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 156.77 E-value: 5.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE-PGMKQG--FIFQEHRLFPWLTVEENIAa 98
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNlPPEKRGiaYVYQNYMLFPHKTVFENIA- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 99 nFNLK-----QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVL 173
Cdd:NF040840 95 -FGLKlrkvpKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREM 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 637173694 174 LDIWQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:NF040840 174 KRWHREFGFTAIHVTHNFEEALSLADRVGIM--LNGRL 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-225 |
7.59e-46 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 157.11 E-value: 7.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 24 DLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE-PGMKQ--GFIFQEHRLFPWLTVEENIAanF 100
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvPPAERgvGMVFQSYALYPHLSVAENMS--F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 101 NLK-----QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLD 175
Cdd:PRK11000 99 GLKlagakKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637173694 176 IWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKI-LPVNL-PFPRDR 225
Cdd:PRK11000 179 LHKRLGRTMIYVTHDQVEAMTLADKIVVLDA--GRVAQVgKPLELyHYPANR 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-212 |
1.03e-45 |
|
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: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWLTVEE 94
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElarriAYVPQEPPAPFGLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 NIA--------ANFNLKQQDvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTR 166
Cdd:COG1120 95 LVAlgryphlgLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 637173694 167 KHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIH 212
Cdd:COG1120 174 LEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD--GRIV 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-211 |
1.42e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.51 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM----KQ-GFIFQEHRLFPwLTVEE 94
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpewrRQvAYVPQEPALWG-GTVRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 NIAANFNLKQQDVRR-KVDELIEivRLkGFEHAY----PHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHL 169
Cdd:COG4619 93 NLPFPFQLRERKFDReRALELLE--RL-GLPPDIldkpVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 637173694 170 QDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG4619 170 EELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA--GRL 209
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-190 |
1.60e-45 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 151.71 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 2 TISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---- 77
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ----GFIFQEHRLFPWLTVEENIAANF----NLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDP 149
Cdd:TIGR02982 81 rrriGYIFQAHNLLGFLTARQNVQMALelqpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 637173694 150 EILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHD 190
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD 201
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-204 |
1.68e-45 |
|
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: 151.53 E-value: 1.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIFQEH---RLFPwLTVEENI 96
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRsidRDFP-ISVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 97 AANFNLK-------QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHL 169
Cdd:cd03235 92 LMGLYGHkglfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI 171
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 170 QDvLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:cd03235 172 YE-LLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
10-190 |
3.08e-45 |
|
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: 150.84 E-value: 3.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 10 KSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---------GFI 80
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrreklGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 81 FQEHRLFPWLTVEENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:TIGR03608 82 FQNFALIENETVEENLdlgLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190
....*....|....*....|....*....|...
gi 637173694 158 FGALDAFTRKHLQDVLLDIWQEKKtTMMLVTHD 190
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHD 193
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-192 |
3.70e-45 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 151.75 E-value: 3.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKqtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:COG3638 3 LELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ---GFIFQEHRLFPWLTVEENI-----------AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIAR 143
Cdd:COG3638 80 rriGMIFQQFNLVPRLSVLTNVlagrlgrtstwRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637173694 144 ALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDID 192
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVD 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-204 |
4.20e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.40 E-value: 4.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIFQEH---RLFPwLTVEENIA 97
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAevdWDFP-ITVRDVVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 AN-------FNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQ 170
Cdd:COG1121 100 MGrygrrglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALY 179
|
170 180 190
....*....|....*....|....*....|....
gi 637173694 171 DVLLDiWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:COG1121 180 ELLRE-LRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-213 |
8.05e-45 |
|
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: 151.84 E-value: 8.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ--------GFIFQ--EHRLFPw 89
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrkkvGLVFQfpEHQLFE- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEENIA---ANFNLKQQDVRRKVDELIEIVrlkGFEHAY----PHELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:TIGR04521 98 ETVYKDIAfgpKNLGLSEEEAEERVKEALELV---GLDEEYlersPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637173694 163 AFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHK 213
Cdd:TIGR04521 175 PKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK--GKIVL 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-158 |
5.17e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 145.48 E-value: 5.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWLTVEENI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 97 AAN---FNLKQQDVRRKVDELIEIVRLKGFEH----AYPHELSGGMSQRVAIARALLRDPEILLLDEPF 158
Cdd:pfam00005 81 RLGlllKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-211 |
9.02e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 147.93 E-value: 9.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFWKdkqtIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-------GFI 80
Cdd:PRK09493 7 VSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 81 FQEHRLFPWLTVEENIAanF------NLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLL 154
Cdd:PRK09493 83 FQQFYLFPHLTALENVM--FgplrvrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637173694 155 DEPFGALDAFTRKHLQDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDK--GRI 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-190 |
9.91e-44 |
|
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: 146.86 E-value: 9.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----GFIFQEHRLFPWLTVEEN 95
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrrlAYLGHADGLKPELTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANFNLKQQDV-RRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDvLL 174
Cdd:COG4133 96 LRFWAALYGLRAdREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAE-LI 174
|
170
....*....|....*.
gi 637173694 175 DIWQEKKTTMMLVTHD 190
Cdd:COG4133 175 AAHLARGGAVLLTTHQ 190
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-190 |
1.04e-43 |
|
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: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE------PGMKQ--GFIFQEHRLFPWL 90
Cdd:TIGR02673 15 VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgrqlPLLRRriGVVFQDFRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENIAANFNL---KQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAftrk 167
Cdd:TIGR02673 95 TVYENVALPLEVrgkKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDP---- 170
|
170 180
....*....|....*....|....*.
gi 637173694 168 HLQDVLLDIWQE---KKTTMMLVTHD 190
Cdd:TIGR02673 171 DLSERILDLLKRlnkRGTTVIVATHD 196
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
8-191 |
1.31e-43 |
|
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: 147.11 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI-----TEPG----MKQG 78
Cdd:TIGR02211 7 LGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklssNERAklrnKKLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQEHRLFPWLTVEENIAANF---NLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:TIGR02211 87 FIYQFHHLLPDFTALENVAMPLligKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDI 191
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-205 |
7.72e-43 |
|
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: 145.77 E-value: 7.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPG---MKQ-G 78
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPreaRRQiG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQEHRLFPWLTVEENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:COG4555 78 VLPDERGLYDRLTVRENIryfAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIWQEKKTTmMLVTHDIDESIYLGNEIVLMQ 205
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTV-LFSSHIMQEVEALCDRVVILH 206
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-211 |
1.22e-42 |
|
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: 147.12 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 10 KSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL---DTAYDGQILIGGRRIT---EPGMKQ------ 77
Cdd:COG0444 9 VYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLklsEKELRKirgrei 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 GFIFQE--HRLFPWLTVEENIA----ANFNLKQQDVRRKVDELIEIVRL---KGFEHAYPHELSGGMSQRVAIARALLRD 148
Cdd:COG0444 89 QMIFQDpmTSLNPVMTVGDQIAeplrIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637173694 149 PEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG0444 169 PKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYA--GRI 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-211 |
3.18e-42 |
|
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: 141.77 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----G 78
Cdd:cd03230 1 IEVRNLSKRY-GKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQEHRLFPWLTVEENIaanfnlkqqdvrrkvdelieivrlkgfehayphELSGGMSQRVAIARALLRDPEILLLDEPF 158
Cdd:cd03230 77 YLPEEPSLYENLTVRENL---------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 637173694 159 GALDAFTRKHLQDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:cd03230 124 SGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNN--GRI 173
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-214 |
3.50e-42 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 146.91 E-value: 3.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 2 TISIDIVDKSFWKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT--EP-----G 74
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNelEPadrdiA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 75 MkqgfIFQEHRLFPWLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEI 151
Cdd:PRK11650 80 M----VFQNYALYPHMSVRENMAyglKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 152 LLLDEPFGALDAFTR-------KHLQdvlldiwQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKI 214
Cdd:PRK11650 156 FLFDEPLSNLDAKLRvqmrleiQRLH-------RRLKTTSLYVTHDQVEAMTLADRVVVMNG--GVAEQI 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-192 |
3.99e-42 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 142.62 E-value: 3.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISG-LDTA--YDGQILIGGRRITEPGMKQ---GFIFQEHRLFPWLTVEEN 95
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQrriGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IA----ANFNLKQQdvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQD 171
Cdd:COG4136 97 LAfalpPTIGRAQR--RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRE 174
|
170 180
....*....|....*....|.
gi 637173694 172 VLLDIWQEKKTTMMLVTHDID 192
Cdd:COG4136 175 FVFEQIRQRGIPALLVTHDEE 195
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-194 |
4.40e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 143.57 E-value: 4.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 27 LSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR--RITEPGMKQ-GFIFQEHRLFPWLTVEENIAANFN-- 101
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPvSMLFQENNLFSHLTVAQNIGLGLNpg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 102 LK---QQdvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQ 178
Cdd:PRK10771 100 LKlnaAQ--REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170
....*....|....*.
gi 637173694 179 EKKTTMMLVTHDIDES 194
Cdd:PRK10771 178 ERQLTLLMVSHSLEDA 193
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-190 |
8.29e-42 |
|
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: 142.16 E-value: 8.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 18 TIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGG--------RRITEPGMKQGFIFQEHRLFPW 89
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgRAIPYLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEENIAanFNL-----KQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:cd03292 93 RNVYENVA--FALevtgvPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180
....*....|....*....|....*.
gi 637173694 165 TRKHLQDVLLDIwQEKKTTMMLVTHD 190
Cdd:cd03292 171 TTWEIMNLLKKI-NKAGTTVVVATHA 195
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-204 |
4.70e-41 |
|
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: 138.67 E-value: 4.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPwLTVEEN 95
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkniAYVPQDPFLFS-GTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IaanfnlkqqdvrrkvdelieivrlkgfehaypheLSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLD 175
Cdd:cd03228 96 I----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRA 141
|
170 180
....*....|....*....|....*....
gi 637173694 176 IwqEKKTTMMLVTHDIdESIYLGNEIVLM 204
Cdd:cd03228 142 L--AKGKTVIVIAHRL-STIRDADRIIVL 167
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-204 |
5.75e-41 |
|
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: 141.41 E-value: 5.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM------KQG 78
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlweirkKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQ--EHRlFPWLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILL 153
Cdd:TIGR04520 81 MVFQnpDNQ-FVGATVEDDVAfglENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIII 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637173694 154 LDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIyLGNEIVLM 204
Cdd:TIGR04520 160 LDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVM 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-192 |
9.72e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 137.45 E-value: 9.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKsFWKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI---TEPGMKQ 77
Cdd:COG4161 1 MSIQLKNINC-FYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 --------GFIFQEHRLFPWLTVEEN-IAANFN---LKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARAL 145
Cdd:COG4161 77 irllrqkvGMVFQQYNLWPHLTVMENlIEAPCKvlgLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637173694 146 LRDPEILLLDEPFGALDAFTRKHLQDVLLDIwQEKKTTMMLVTHDID 192
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVE 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-218 |
1.10e-39 |
|
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: 136.93 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFWKDKqtIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAY-----DGQILIGGRRITEPGM---- 75
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVdvle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 76 ---KQGFIFQEHRLFPwLTVEENIAanFNLKQQDVRRKvDELIEIVR--LKGFE-------HAYPHELSGGMSQRVAIAR 143
Cdd:cd03260 79 lrrRVGMVFQKPNPFP-GSIYDNVA--YGLRLHGIKLK-EELDERVEeaLRKAAlwdevkdRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637173694 144 ALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIwqEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKILPVN 218
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLN--GRLVEFGPTE 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-211 |
1.12e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 137.45 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKsFWKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI---TEPGMKQ 77
Cdd:PRK11124 1 MSIQLNGINC-FYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 --------GFIFQEHRLFPWLTVEEN-IAANFN---LKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARAL 145
Cdd:PRK11124 77 irelrrnvGMVFQQYNLWPHLTVQQNlIEAPCRvlgLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637173694 146 LRDPEILLLDEPFGALDAFTRKHLQDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMEN--GHI 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-211 |
1.35e-39 |
|
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: 140.25 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 30 IPGEFVTVI-GPSGCGKSTLLKIISGLDTAYDGQILIGGR-------RITEPGMKQ--GFIFQEHRLFPWLTVEENIaaN 99
Cdd:TIGR02142 20 LPGQGVTAIfGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkGIFLPPEKRriGYVFQEARLFPHLSVRGNL--R 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 100 FNLKQQDVRRKVDELIEIVRLKGFEH---AYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDI 176
Cdd:TIGR02142 98 YGMKRARPSERRISFERVIELLGIGHllgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERL 177
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 177 WQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:TIGR02142 178 HAEFGIPILYVSHSLQEVLRLADRVVVLED--GRV 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-211 |
3.58e-39 |
|
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: 144.21 E-value: 3.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPwLTVEEN 95
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrrqiGVVLQDVFLFS-GTIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IA-ANFNLKQQDVRR-----KVDELIEivRL-KGFEHAYPHE---LSGGMSQRVAIARALLRDPEILLLDEPFGALDAFT 165
Cdd:COG2274 569 ITlGDPDATDEEIIEaarlaGLHDFIE--ALpMGYDTVVGEGgsnLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 637173694 166 RKHLQDVLLDIWQEKktTMMLVTHDiDESIYLGNEIVLMQArpGRI 211
Cdd:COG2274 647 EAIILENLRRLLKGR--TVIIIAHR-LSTIRLADRIIVLDK--GRI 687
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-211 |
1.28e-38 |
|
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: 141.43 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWlTVEE 94
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrrqiAWVPQNPYLFAG-TIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 NIA-ANFNLKQQDVRRkvdeLIEIVRLKGFEHAYPH-------E----LSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:COG4988 430 NLRlGRPDASDEELEA----ALEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637173694 163 AFTRKHLQDVLLDIWQEKktTMMLVTHDIdESIYLGNEIVLMQArpGRI 211
Cdd:COG4988 506 AETEAEILQALRRLAKGR--TVILITHRL-ALLAQADRILVLDD--GRI 549
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-211 |
1.39e-38 |
|
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: 134.62 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ---GFIFQEHRLFPWLTVEENI-----------AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIAR 143
Cdd:cd03256 78 rqiGMIFQQFNLIERLSVLENVlsgrlgrrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 144 ALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRI 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-192 |
1.93e-38 |
|
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: 134.78 E-value: 1.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITepGMK------QGFI--FQEHRLFPWL 90
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT--GLPphriarLGIArtFQNPRLFPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEEN--IAANFNLKQ----------------QDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEIL 152
Cdd:COG0411 95 TVLENvlVAAHARLGRgllaallrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 637173694 153 LLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDID 192
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMD 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-187 |
2.77e-38 |
|
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: 133.33 E-value: 2.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITepGMKQ--------GFIFQEHRLFPWL 90
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPheraragiGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENI-AANFNLKQQDVRRKVDELIEIV-RLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKH 168
Cdd:cd03224 91 TVEENLlLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170
....*....|....*....
gi 637173694 169 LQDVLLDIwQEKKTTMMLV 187
Cdd:cd03224 171 IFEAIREL-RDEGVTILLV 188
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-204 |
3.13e-38 |
|
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: 131.21 E-value: 3.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 7 IVDKSFWKDKQTirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEpgmkqgfifqehrl 86
Cdd:cd00267 2 IENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 87 fpwltveeniaanfnLKQQDVRRKVdelieivrlkgfehAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTR 166
Cdd:cd00267 66 ---------------LPLEELRRRI--------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190
....*....|....*....|....*....|....*...
gi 637173694 167 KHLQDVLLDIWQEKKTTMMlVTHDIDESIYLGNEIVLM 204
Cdd:cd00267 117 ERLLELLRELAEEGRTVII-VTHDPELAELAADRVIVL 153
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-192 |
3.61e-38 |
|
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: 133.58 E-value: 3.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ---GFIFQEHRLFPWLTVEEN-----------IAANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIAR 143
Cdd:TIGR02315 79 rriGMIFQHYNLIERLTVLENvlhgrlgykptWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637173694 144 ALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDID 192
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVD 207
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-204 |
4.47e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 134.76 E-value: 4.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITePGMKQ----------GFIFQ--EHRLF 87
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVIT-AGKKNkklkplrkkvGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 88 PwLTVEENIA---ANFNLKQQDVRRKVDELIEIVrlkGFEHAY----PHELSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:PRK13634 100 E-ETVEKDICfgpMNFGVSEEDAKQKAREMIELV---GLPEELlarsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 637173694 161 LDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-192 |
5.72e-38 |
|
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: 132.95 E-value: 5.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITepGMK------QGFI--FQEHRLFPWL 90
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT--GLPpheiarLGIGrtFQIPRLFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENI-------------AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:cd03219 91 TVLENVmvaaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 158 FGALDAFTRKHLQDVLLDIWqEKKTTMMLVTHDID 192
Cdd:cd03219 171 AAGLNPEETEELAELIRELR-ERGITVLLVEHDMD 204
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-192 |
8.79e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 135.31 E-value: 8.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----- 77
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ---GFIFQEHRLFPWLTVEENIAanFNLK-----QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDP 149
Cdd:PRK11153 82 rqiGMIFQHFNLLSSRTVFDNVA--LPLElagtpKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 150 EILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDID 192
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMD 202
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-211 |
4.88e-37 |
|
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: 129.98 E-value: 4.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 27 LSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---GFIFQEHRLFPWLTVEENIAANFN-- 101
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQrpvSMLFQENNLFAHLTVRQNIGLGLHpg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 102 LKQQDVRR-KVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEK 180
Cdd:TIGR01277 99 LKLNAEQQeKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSER 178
|
170 180 190
....*....|....*....|....*....|.
gi 637173694 181 KTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:TIGR01277 179 QRTLLMVTHHLSDARAIASQIAVVSQ--GKI 207
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-214 |
7.60e-37 |
|
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: 128.32 E-value: 7.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQehrlfpwltvee 94
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElarkiAYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 niaanfnlkqqdvrrkvdeLIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLL 174
Cdd:cd03214 81 -------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 637173694 175 DIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKI 214
Cdd:cd03214 142 RLARERGKTVVMVLHDLNLAARYADRVILLKD--GRIVAQ 179
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
16-204 |
6.57e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 130.38 E-value: 6.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 16 KQTirvLEDLRLSI---IPGEFVTVI-GPSGCGKSTLLKIISGLDTAYDGQILIGGR-------RITEPGMKQ--GFIFQ 82
Cdd:PRK11144 7 KQQ---LGDLCLTVnltLPAQGITAIfGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekGICLPPEKRriGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 EHRLFPWLTVEENIaaNFNLKQQDVrrkvDELIEIVRLKGFEH---AYPHELSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:PRK11144 84 DARLFPHYKVRGNL--RYGMAKSMV----AQFDKIVALLGIEPlldRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 637173694 160 ALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVL 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-212 |
3.62e-35 |
|
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: 125.17 E-value: 3.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI-TEP---GMKQG 78
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEPaeaRRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQEHRLFPWLTVEENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:cd03266 82 FVSDSTGLYDRLTARENLeyfAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIWQEKKtTMMLVTHDIDESIYLGNEIVLMQArpGRIH 212
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHR--GRVV 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-212 |
1.32e-34 |
|
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: 123.46 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkDKQtiRVLEDLRLSIIPGEFVtVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ----G 78
Cdd:cd03264 1 LQLENLTKRY--GKK--RALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLrrriG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQEHRLFPWLTVEE---NIAANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:cd03264 76 YLPQEFGVYPNFTVREfldYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIWQEKktTMMLVTHDIDESIYLGNEIVLMQArpGRIH 212
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNK--GKLV 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-206 |
1.76e-34 |
|
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: 123.38 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEpGMKQ-----GFIFQEHRLFPWLTVEEN 95
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAarqslGYCPQFDALFDELTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 I---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDV 172
Cdd:cd03263 96 LrfyARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDL 175
|
170 180 190
....*....|....*....|....*....|....
gi 637173694 173 LLDIWQEKktTMMLVTHDIDESIYLGNEIVLMQA 206
Cdd:cd03263 176 ILEVRKGR--SIILTTHSMDEAEALCDRIAIMSD 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-191 |
4.48e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 123.32 E-value: 4.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 7 IVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI--TEPGMKQ------- 77
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtARSLSQQkglirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ----GFIFQEHRLFPWLTVEENIAANFNLKQQDVRRKVD----ELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDP 149
Cdd:PRK11264 84 rqhvGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATararELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 637173694 150 EILLLDEPFGALDAftrKHLQDVLLDIWQ--EKKTTMMLVTHDI 191
Cdd:PRK11264 164 EVILFDEPTSALDP---ELVGEVLNTIRQlaQEKRTMVIVTHEM 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-191 |
5.27e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 122.62 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE---------PGMKQGFIFQEHRLFPWLT 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaelRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 92 VEENIAANF---NLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKH 168
Cdd:PRK11629 104 ALENVAMPLligKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|...
gi 637173694 169 LQDVLLDIWQEKKTTMMLVTHDI 191
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDL 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
21-208 |
7.40e-34 |
|
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: 128.35 E-value: 7.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGG---RRITEPGMKQ--GFIFQEHRLFPwLTVEEN 95
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlRDLDEDDLRRriAVVPQRPHLFD-TTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IA-ANFNLKQQDVRrkvdELIEIVRLKGFEHAYPH-----------ELSGGMSQRVAIARALLRDPEILLLDEPFGALDA 163
Cdd:COG4987 429 LRlARPDATDEELW----AALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDA 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637173694 164 FTRKHLQDVLLDIWQEKktTMMLVTHD------IDESIYLGNEIVLMQARP 208
Cdd:COG4987 505 ATEQALLADLLEALAGR--TVLLITHRlaglerMDRILVLEDGRIVEQGTH 553
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-204 |
1.06e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.79 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 2 TISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---- 77
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 -GFIFQE-HRLFPWLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEIL 152
Cdd:PRK13632 85 iGIIFQNpDNQFIGATVEDDIAfglENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637173694 153 LLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIyLGNEIVLM 204
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVF 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-204 |
1.26e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 122.85 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-------GFIFQ--EHRLFPWl 90
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdirkkvGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENIA---ANFNLKQQDVRRKVDELIEIVRLK--GFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFT 165
Cdd:PRK13637 100 TIEKDIAfgpINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 637173694 166 RKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-205 |
1.49e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 125.15 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGG---RRITEPGMKQ------GFIFQEHRLFPWLTV 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREvrrkkiAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIAANFNLK---QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHL 169
Cdd:PRK10070 124 LDNTAFGMELAginAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 637173694 170 QDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQ 205
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-193 |
4.82e-33 |
|
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: 119.24 E-value: 4.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT---EPGMKQGF 79
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkniEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQEHRLFPWLTVEENIAANFNLKQQDvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGIR-KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190
....*....|....*....|....*....|....
gi 637173694 160 ALDAFTRKHLQDVLLDiWQEKKTTMMLVTHDIDE 193
Cdd:cd03268 156 GLDPDGIKELRELILS-LRDQGITVLISSHLLSE 188
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-189 |
6.05e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 125.66 E-value: 6.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEpgMKQ-------GFIFQEHRLFPwLTVE 93
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD--LTLeslrrqiGVVPQDTFLFS-GTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 94 ENIA-ANFNLKQQDVRR-----KVDELIEivrlkGFEHAYPHE-------LSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:COG1132 432 ENIRyGRPDATDEEVEEaakaaQAHEFIE-----ALPDGYDTVvgergvnLSGGQRQRIAIARALLKDPPILILDEATSA 506
|
170 180
....*....|....*....|....*....
gi 637173694 161 LDAFTRKHLQDVLLDIWQEKktTMMLVTH 189
Cdd:COG1132 507 LDTETEALIQEALERLMKGR--TTIVIAH 533
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-193 |
8.37e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.11 E-value: 8.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGldtaydgqIL--IGGRRITEPGMKQGFIFQEHRL---FPwLTVEEN 95
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAG--------VLrpTSGTVRRAGGARVAYVPQRSEVpdsLP-LTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANF--------NLKQQDvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRK 167
Cdd:NF040873 78 VAMGRwarrglwrRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180
....*....|....*....|....*.
gi 637173694 168 HLQDVLLDiWQEKKTTMMLVTHDIDE 193
Cdd:NF040873 157 RIIALLAE-EHARGATVVVVTHDLEL 181
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
12-190 |
1.83e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 120.99 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 12 FWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ--------GFIFQE 83
Cdd:COG4608 24 FGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrrrmQMVFQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 84 HR--LFPWLTVEENIAA----NFNLKQQDVRRKVDELIEIVRLKGfEHA--YPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:COG4608 104 PYasLNPRMTVGDIIAEplriHGLASKAERRERVAELLELVGLRP-EHAdrYPHEFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHD 190
Cdd:COG4608 183 EPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-211 |
2.63e-32 |
|
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: 117.86 E-value: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 7 IVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGG----RRITEPGMKQGFIFQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 EHRLFPWLTVEENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:cd03265 81 DLSVDDELTGWENLyihARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637173694 160 ALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH--GRI 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-204 |
2.72e-32 |
|
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: 117.36 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 16 KQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITePGMKQ---GFIFQE--HRLFPwL 90
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-AKERRksiGYVMQDvdYQLFT-D 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENIAanFNLKQ-QDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHL 169
Cdd:cd03226 88 SVREELL--LGLKElDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 170 QDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:cd03226 166 GELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-157 |
1.13e-31 |
|
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: 116.23 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITepGM------KQGFIF--QEHRLFPWL 90
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLpphriaRLGIGYvpEGRRIFPSL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEEN--IAANFNLKQQDVRRKVDELIEIV-RLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:COG0410 94 TVEENllLGAYARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-212 |
1.17e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 117.42 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM-----KQGF 79
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwdvrrQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQE-HRLFPWLTVEENIAanFNLKQQDVRR-----KVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILL 153
Cdd:PRK13635 86 VFQNpDNQFVGATVQDDVA--FGLENIGVPReemveRVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 154 LDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYlGNEIVLMqaRPGRIH 212
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVM--NKGEIL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-189 |
1.41e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 116.67 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSFW-KDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL-----DTAYDGQILIGGRRITEPG 74
Cdd:COG1117 8 LEPKIEVRNLNVYyGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 75 M-------KQGFIFQEHRLFPwLTVEENIAanFNLKQQDVRRKvDELIEIV---------------RLkgfeHAYPHELS 132
Cdd:COG1117 85 VdvvelrrRVGMVFQKPNPFP-KSIYDNVA--YGLRLHGIKSK-SELDEIVeeslrkaalwdevkdRL----KKSALGLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637173694 133 GGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIwqEKKTTMMLVTH 189
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTH 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-206 |
3.63e-31 |
|
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: 114.30 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 14 KDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT-EPGMKQGFIFQEHRLFPWLTV 92
Cdd:cd03269 8 KRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiAARNRIGYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EEN---IAANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHL 169
Cdd:cd03269 88 IDQlvyLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 637173694 170 QDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLMQA 206
Cdd:cd03269 168 KDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-204 |
3.84e-31 |
|
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: 120.47 E-value: 3.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEhrlfPWLtVEEN 95
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqiAWVPQH----PFL-FAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANFNLKQQDVrrKVDELIEIVRLKG---FEHAYP-----------HELSGGMSQRVAIARALLRDPEILLLDEPFGAL 161
Cdd:TIGR02857 412 IAENIRLARPDA--SDAEIREALERAGldeFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 162 DAFTRKHLQDVLLDIWQEKktTMMLVTHDiDESIYLGNEIVLM 204
Cdd:TIGR02857 490 DAETEAEVLEALRALAQGR--TVLLVTHR-LALAALADRIVVL 529
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-203 |
4.65e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 117.11 E-value: 4.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKS--FWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ--- 77
Cdd:PRK15079 16 VHFDIKDGKqwFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwra 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 -----GFIFQE--HRLFPWLTVEENIAANF-----NLKQQDVRRKVDELIEIVRL-KGFEHAYPHELSGGMSQRVAIARA 144
Cdd:PRK15079 96 vrsdiQMIFQDplASLNPRMTIGEIIAEPLrtyhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 145 LLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHD------IDESI---YLGNEIVL 203
Cdd:PRK15079 176 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDlavvkhISDRVlvmYLGHAVEL 243
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-190 |
4.88e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 114.49 E-value: 4.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---------G 78
Cdd:PRK10584 12 LKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrakhvG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQEHRLFPWLTVEENIAANFNLKQQDVRRKVDELIEIVRLKGFE---HAYPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGkrlDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHD 190
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-211 |
6.34e-30 |
|
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: 112.10 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFWKDKQTIrvLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDT-AYDGQILIGGRR-----ITEpgMKQ- 77
Cdd:COG1119 4 LELRNVTVRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGERrggedVWE--LRKr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 -GFIFQE--HRLFPWLTVEENIAANF--------NLKQQDvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALL 146
Cdd:COG1119 80 iGLVSPAlqLRFPRDETVLDVVLSGFfdsiglyrEPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637173694 147 RDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGRV 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-205 |
8.51e-30 |
|
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: 109.61 E-value: 8.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWlTVEEN 95
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhvGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IaanfnlkqqdvrrkvdelieivrlkgfehaypheLSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLD 175
Cdd:cd03246 96 I----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA 141
|
170 180 190
....*....|....*....|....*....|
gi 637173694 176 IwQEKKTTMMLVTHDIdESIYLGNEIVLMQ 205
Cdd:cd03246 142 L-KAAGATRIVIAHRP-ETLASADRILVLE 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-190 |
8.53e-30 |
|
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: 116.71 E-value: 8.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 11 SFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKS----TLLKIISGLDTAYDGQILIGGR---RITEPGMKQ------ 77
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQdllGLSERELRRirgnri 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 GFIFQE--HRLFPWLTVEENIAANFNLKQ----QDVRRKVDELIEIVRLKGFE---HAYPHELSGGMSQRVAIARALLRD 148
Cdd:COG4172 95 AMIFQEpmTSLNPLHTIGKQIAEVLRLHRglsgAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 637173694 149 PEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHD 190
Cdd:COG4172 175 PDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-211 |
9.33e-30 |
|
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: 116.32 E-value: 9.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 12 FWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdTAYDGQILIGGRRITEPGMKQgfiFQEHR------ 85
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRA---LRPLRrrmqvv 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 86 -------LFPWLTVEENIAANF-----NLKQQDVRRKVDELIEIVRLK-GFEHAYPHELSGGMSQRVAIARALLRDPEIL 152
Cdd:COG4172 368 fqdpfgsLSPRMTVGQIIAEGLrvhgpGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 153 LLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKD--GKV 504
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
1.29e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.14 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSF-WKDKQtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-- 77
Cdd:PRK13647 1 MDNIIEVEDLHFrYKDGT--KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ---GFIFQE--HRLFPwLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDP 149
Cdd:PRK13647 79 skvGLVFQDpdDQVFS-STVWDDVAfgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637173694 150 EILLLDEPFGALDAFTRKHLQDVlLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEI-LDRLHNQGKTVIVATHDVDLAAEWADQVIVLKE--GRV 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-192 |
1.69e-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: 109.87 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSF-WKDKQTIR--VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRitepgmkqGFIF 81
Cdd:cd03250 1 ISVEDASFtWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--------AYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 82 QEhrlfPWL---TVEENI--AANFN-------LK----QQDVRRKVD-ELIEIvrlkgfehaypHE----LSGGMSQRVA 140
Cdd:cd03250 73 QE----PWIqngTIRENIlfGKPFDeeryekvIKacalEPDLEILPDgDLTEI-----------GEkginLSGGQKQRIS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 637173694 141 IARALLRDPEILLLDEPFGALDAFTRKHL-QDVLLDIWQEKKTTmMLVTHDID 192
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLLLNNKTR-ILVTHQLQ 189
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-205 |
2.13e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.75 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSF-WKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM---- 75
Cdd:PRK13650 1 MSNIIEVKNLTFkYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 76 -KQGFIFQE-HRLFPWLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPE 150
Cdd:PRK13650 81 hKIGMVFQNpDNQFVGATVEDDVAfglENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637173694 151 ILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDEsIYLGNEIVLMQ 205
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMK 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-190 |
3.57e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 115.21 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---------G 78
Cdd:PRK10535 10 IRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrehfG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQEHRLFPWLTVEENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVevpAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIwQEKKTTMMLVTHD 190
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-173 |
6.59e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.86 E-value: 6.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT-----EPGMKQGFIFQEHRL-FPWlTVE 93
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspaELARRRAVLPQHSSLsFPF-TVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 94 ENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLR------DPEILLLDEPFGALDAF 164
Cdd:PRK13548 95 EVVAmgrAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLA 174
|
....*....
gi 637173694 165 trkHLQDVL 173
Cdd:PRK13548 175 ---HQHHVL 180
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-211 |
6.80e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.79 E-value: 6.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQT-IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITepGMKQ---- 77
Cdd:COG1101 2 LELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEykra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 GFI---FQEHRL--FPWLTVEEN--IAAN----FNLKQQDVRRKVDELIEIV---------RLK---GFehaypheLSGG 134
Cdd:COG1101 80 KYIgrvFQDPMMgtAPSMTIEENlaLAYRrgkrRGLRRGLTKKRRELFRELLatlglglenRLDtkvGL-------LSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 135 MSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKK-TTMMlVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLM-VTHNMEQALDYGNRLIMMHE--GRI 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-193 |
1.43e-28 |
|
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: 108.19 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 10 KSFWK-DKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRitePGMKQ-------GFIF 81
Cdd:cd03267 24 KSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV---PWKRRkkflrriGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 82 QEHRLFPW-LTVEEN---IAANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:cd03267 101 GQKTQLWWdLPVIDSfylLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 637173694 158 FGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDE 193
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKD 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-212 |
1.49e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.66 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE-------------PgmkqgfifQEHRL 86
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwelarrravlP--------QHSSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 87 -FPWlTVEENIA----ANFNLKQQDVRRkVDELIEIVRLKGFEH-AYPhELSGGMSQRVAIARAL--LRDPE-----ILL 153
Cdd:COG4559 87 aFPF-TVEEVVAlgraPHGSSAAQDRQI-VREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLaqLWEPVdggprWLF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637173694 154 LDEPFGALDAftrKHlQDVLLDI---WQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIH 212
Cdd:COG4559 164 LDEPTSALDL---AH-QHAVLRLarqLARRGGGVVAVLHDLNLAAQYADRILLLHQ--GRLV 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-204 |
1.58e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.44 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPG--------MKQGF 79
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaqkllrQKIQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQE--HRLFPWLTV----EENIAANFNLKQQDVRRKVDELIEIVRLKGfEHA--YPHELSGGMSQRVAIARALLRDPEI 151
Cdd:PRK11308 97 VFQNpyGSLNPRKKVgqilEEPLLINTSLSAAERREKALAMMAKVGLRP-EHYdrYPHMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 637173694 152 LLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:PRK11308 176 VVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-211 |
1.97e-28 |
|
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: 109.79 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT-EP-GMKQ--GFIFQEHRLFPWLTVEE 94
Cdd:TIGR01188 6 FKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVrEPrKVRRsiGIVPQYASVDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 N---IAANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQD 171
Cdd:TIGR01188 86 NlemMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 637173694 172 VLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:TIGR01188 166 YIRAL-KEEGVTILLTTHYMEEADKLCDRIAII--DHGRI 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-193 |
2.06e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.42 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ------GFIFQEHRLFPWLTV 92
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaagiAIIHQELNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIAAN------FNLKQQDVRRKVDELIEivRLkGFE---HAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDA 163
Cdd:COG1129 97 AENIFLGreprrgGLIDWRAMRRRARELLA--RL-GLDidpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
170 180 190
....*....|....*....|....*....|
gi 637173694 164 FTRKHLQDVLLDIwQEKKTTMMLVTHDIDE 193
Cdd:COG1129 174 REVERLFRIIRRL-KAQGVAIIYISHRLDE 202
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-189 |
2.30e-28 |
|
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: 107.29 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 11 SFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHR 85
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrrniGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 86 LFpWLTVEENIAanfnLKQQDVrrKVDELIEIVRLKG---FEHAYPH-----------ELSGGMSQRVAIARALLRDPEI 151
Cdd:cd03245 89 LF-YGTLRDNIT----LGAPLA--DDERILRAAELAGvtdFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPI 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 637173694 152 LLLDEPFGALDAFTRKHLQDVlLDIWQEKKtTMMLVTH 189
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKER-LRQLLGDK-TLIIITH 197
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-191 |
3.15e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 108.00 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQG---- 78
Cdd:COG4167 10 LSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRckhi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 -FIFQ--EHRLFPWLTV----EENIAANFNLKQQDVRRKVdelIEIVRLKGF--EHA--YPHELSGGMSQRVAIARALLR 147
Cdd:COG4167 90 rMIFQdpNTSLNPRLNIgqilEEPLRLNTDLTAEEREERI---FATLRLVGLlpEHAnfYPHMLSSGQKQRVALARALIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 637173694 148 DPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDI 191
Cdd:COG4167 167 QPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHL 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-208 |
3.50e-28 |
|
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: 107.32 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdtaYD---GQILIGGRRITEPGMKQ-----GFIFQEHRLFPwLTV 92
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF---YDvssGSILIDGQDIREVTLDSlrraiGVVPQDTVLFN-DTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIA-ANFNLKQQDVRR-----KVDELIEivrlkGFEHAYPHE-------LSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:cd03253 92 GYNIRyGRPDATDEEVIEaakaaQIHDKIM-----RFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637173694 160 ALDAFTRKHLQDVLLDIwQEKKTTMMlVTH------DIDESIYLGNEIVLMQARP 208
Cdd:cd03253 167 ALDTHTEREIQAALRDV-SKGRTTIV-IAHrlstivNADKIIVLKDGRIVERGTH 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-191 |
4.46e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 106.88 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTirvLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE------PGMK 76
Cdd:PRK10908 2 IRFEHVSKAYLGGRQA---LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrevPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 77 Q--GFIFQEHRLFPWLTVEENIAANFNL---KQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEI 151
Cdd:PRK10908 79 RqiGMIFQDHHLLMDRTVYDNVAIPLIIagaSGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 152 LLLDEPFGALDaftrKHLQDVLLDIWQEKK---TTMMLVTHDI 191
Cdd:PRK10908 159 LLADEPTGNLD----DALSEGILRLFEEFNrvgVTVLMATHDI 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-190 |
6.36e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 6.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFWKDKqtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIggrritEPGMKQGFIFQEHRLF 87
Cdd:COG0488 4 LSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------PKGLRIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 88 PWLTVEENIAANFNLKQQDVRRK----------VDELIEIVRLK----------------------GFEHAYPH----EL 131
Cdd:COG0488 74 DDLTVLDTVLDGDAELRALEAELeeleaklaepDEDLERLAELQeefealggweaearaeeilsglGFPEEDLDrpvsEL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 132 SGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLldiwQEKKTTMMLVTHD 190
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-211 |
1.03e-27 |
|
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: 104.05 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRItepgmkqgfifqehrlfpwltveeniaa 98
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 99 NFNlkqqDVRRKVDELIEIVrlkgfehaypHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIwQ 178
Cdd:cd03216 65 SFA----SPRDARRAGIAMV----------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL-R 129
|
170 180 190
....*....|....*....|....*....|...
gi 637173694 179 EKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:cd03216 130 AQGVAVIFISHRLDEVFEIADRVTVL--RDGRV 160
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1-221 |
1.66e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.02 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIV--DKSFWKDKQT---IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITePGM 75
Cdd:PRK13645 1 FDFSKDIIldNVSYTYAKKTpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP-ANL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 76 KQ-----------GFIFQ--EHRLFPwLTVEENIA---ANFNLKQQDVRRKVDELIEIVRL-KGFEHAYPHELSGGMSQR 138
Cdd:PRK13645 80 KKikevkrlrkeiGLVFQfpEYQLFQ-ETIEKDIAfgpVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 139 VAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpgriHKILPVN 218
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHE-----GKVISIG 233
|
...
gi 637173694 219 LPF 221
Cdd:PRK13645 234 SPF 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-162 |
2.64e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.11 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ------GFIFQEHRLFPWLTVE 93
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKrarlgiGYLPQEASIFRKLTVE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637173694 94 ENIAA---NFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:COG1137 97 DNILAvleLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-204 |
2.90e-27 |
|
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: 103.78 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSFWKdkqtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL--DTAYDGQILIGGRRITEPGMKQ- 77
Cdd:cd03213 9 LTVTVKSSPSKSGK-----QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 -GFIFQEHRLFPWLTVEENI--AANfnlkqqdvrrkvdelieivrLKGfehaypheLSGGMSQRVAIARALLRDPEILLL 154
Cdd:cd03213 84 iGYVPQDDILHPTLTVRETLmfAAK--------------------LRG--------LSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637173694 155 DEPFGALDAFTRKHLQDVLLDIWQEKKTTMMlVTHDIDESIY-LGNEIVLM 204
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTIIC-SIHQPSSEIFeLFDKLLLL 185
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-162 |
3.13e-27 |
|
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: 104.55 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ------GFIFQEHRLFPWLTVE 93
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrarlgiGYLPQEASIFRKLTVE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637173694 94 ENIAA---NFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:cd03218 94 ENILAvleIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-190 |
4.63e-27 |
|
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: 108.99 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGG-----RRITEPGMKQGFIFQEHRLFPwLTVEE 94
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssLDQDEVRRRVSVCAQDAHLFD-TTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 NIA-ANFNLKQQDVRRkvdeLIEIVRLKGFEHAYPH-----------ELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:TIGR02868 428 NLRlARPDATDEELWA----ALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*...
gi 637173694 163 AFTRKHLQDVLLDIWQEKktTMMLVTHD 190
Cdd:TIGR02868 504 AETADELLEDLLAALSGR--TVVLITHH 529
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-192 |
5.71e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.58 E-value: 5.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 2 TISIDIVDKSFwKDKqtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-GFI 80
Cdd:COG4152 1 MLELKGLTKRF-GDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRiGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 81 FQEHRLFPWLTVEENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:COG4152 77 PEERGLYPKMKVGEQLvylARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 158 FGALDAFTRKHLQDVLLDIwQEKKTTMMLVTHDID 192
Cdd:COG4152 157 FSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQME 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
27-193 |
7.87e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.19 E-value: 7.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 27 LSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR--RITEP--------GMkqgfIFQEHRLFPWLTVEENI 96
Cdd:COG3845 26 LTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPrdaialgiGM----VHQHFMLVPNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 97 A------ANFNLKQQDVRRKVDELIEivRLkGFE---HAYPHELSGGMSQRVAIARALLRDPEILLLDEP---------- 157
Cdd:COG3845 102 VlgleptKGGRLDRKAARARIRELSE--RY-GLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPtavltpqead 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 637173694 158 --FGALDAFTrkhlqdvlldiwqEKKTTMMLVTHDIDE 193
Cdd:COG3845 179 elFEILRRLA-------------AEGKSIIFITHKLRE 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-214 |
8.06e-27 |
|
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: 108.35 E-value: 8.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 15 DKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQ--ILIGGRRI--TEPGMKQ--------GFIFQ 82
Cdd:TIGR03269 293 DRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVdmTKPGPDGrgrakryiGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 EHRLFPWLTVEENI--AANFNLKQQDVRRKVdelIEIVRLKGFEH--------AYPHELSGGMSQRVAIARALLRDPEIL 152
Cdd:TIGR03269 373 EYDLYPHRTVLDNLteAIGLELPDELARMKA---VITLKMVGFDEekaeeildKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637173694 153 LLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRIHKI 214
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDGKIVKI 509
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-185 |
8.57e-27 |
|
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: 103.50 E-value: 8.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 14 KDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYD---GQILIGGRRITEPGMKQ--GFIFQEHRLFP 88
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKcvAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WLTVEENI--AANF---NLKQQDVRRKVDE--LIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGAL 161
Cdd:cd03234 95 GLTVRETLtyTAILrlpRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180
....*....|....*....|....
gi 637173694 162 DAFTRKHLQDVLLDIWQEKKTTMM 185
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVIL 198
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-173 |
9.20e-27 |
|
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: 103.46 E-value: 9.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdtaYD---GQILIGGRRITEPGMKQ---- 77
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRF---YDvdsGRILIDGHDVRDYTLASlrrq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 -GFIFQEHRLFPWlTVEENIA-ANFNLKQQDVRR-----KVDELIEivrlkGFEHAYPHE-------LSGGMSQRVAIAR 143
Cdd:cd03251 78 iGLVSQDVFLFND-TVAENIAyGRPGATREEVEEaaraaNAHEFIM-----ELPEGYDTVigergvkLSGGQRQRIAIAR 151
|
170 180 190
....*....|....*....|....*....|
gi 637173694 144 ALLRDPEILLLDEPFGALDAFTRKHLQDVL 173
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAAL 181
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-185 |
1.60e-26 |
|
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: 102.69 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFWKDKQTIrVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GF 79
Cdd:cd03254 3 IEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrsmiGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQEHRLFPWlTVEENIAANFNLKQQDVRRKVDELI----EIVRL-KGFEHAYPHE---LSGGMSQRVAIARALLRDPEI 151
Cdd:cd03254 82 VLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAgahdFIMKLpNGYDTVLGENggnLSQGERQLLAIARAMLRDPKI 160
|
170 180 190
....*....|....*....|....*....|....
gi 637173694 152 LLLDEPFGALDAFTRKHLQDVLLDIwQEKKTTMM 185
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKL-MKGRTSII 193
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-241 |
2.02e-26 |
|
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: 103.35 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 12 FWKdKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQG--------FIFQE 83
Cdd:TIGR02769 18 FGA-KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRrafrrdvqLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 84 --HRLFPWLTVEENIAANF----NLKQQDVRRKVDELIEIVRLKGfEHA--YPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:TIGR02769 97 spSAVNPRMTVRQIIGEPLrhltSLDESEQKARIAELLDMVGLRS-EDAdkLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKILPVNLPFprDRTSTAFQSLRQ 235
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK--GQIVEECDVAQLL--SFKHPAGRNLQS 251
|
....*.
gi 637173694 236 KVLSEF 241
Cdd:TIGR02769 252 AVLPEH 257
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-173 |
2.26e-26 |
|
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: 102.62 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTllkIISGLDTAYD---GQILIGGRRITEPGMKQ-----GFIFQEHRLFPwL 90
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERFYDptsGEILLDGVDIRDLNLRWlrsqiGLVSQEPVLFD-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENIAANFNlkqqdvRRKVDELIEIVRL-------KGFEHAY-----PH--ELSGGMSQRVAIARALLRDPEILLLDE 156
Cdd:cd03249 92 TIAENIRYGKP------DATDEEVEEAAKKanihdfiMSLPDGYdtlvgERgsQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170
....*....|....*..
gi 637173694 157 PFGALDAFTRKHLQDVL 173
Cdd:cd03249 166 ATSALDAESEKLVQEAL 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-190 |
2.45e-26 |
|
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: 106.94 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIggrritEPGMKQGFIFQEHRLFPWLTVEEN----- 95
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP------QPGIKVGYLPQEPQLDPTKTVRENveegv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 ------------IAANFN---------LKQQ-------------DVRRKVDELIEIVRLKGFEhAYPHELSGGMSQRVAI 141
Cdd:TIGR03719 94 aeikdaldrfneISAKYAepdadfdklAAEQaelqeiidaadawDLDSQLEIAMDALRCPPWD-ADVTKLSGGERRRVAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637173694 142 ARALLRDPEILLLDEPFGALDAFTRKHLQDVLldiwQEKKTTMMLVTHD 190
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-204 |
2.66e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 107.06 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 12 FWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTA---YDGQILIGGRRITEPGMKQ--GFIFQEHRL 86
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAisAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 87 FPWLTVEE--NIAANFNLKQQ---DVRR-KVDELIEIVRLKGFEH------AYPHELSGGMSQRVAIARALLRDPEILLL 154
Cdd:TIGR00955 111 IPTLTVREhlMFQAHLRMPRRvtkKEKReRVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637173694 155 DEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVtHDIDESIY-LGNEIVLM 204
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTI-HQPSSELFeLFDKIILM 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-213 |
4.48e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.08 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE-PGM---KQG 78
Cdd:COG4604 2 IEIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRelaKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIF-QEHRLFPWLTVEENIAanF--------NLKQQDvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDP 149
Cdd:COG4604 78 AILrQENHINSRLTVRELVA--FgrfpyskgRLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 150 EILLLDEPFGALDAftrKH---LQDVLLDIWQEKKTTMMLVTHDID-ESIYlGNEIVLMQArpGRIHK 213
Cdd:COG4604 155 DYVLLDEPLNNLDM---KHsvqMMKLLRRLADELGKTVVIVLHDINfASCY-ADHIVAMKD--GRVVA 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-193 |
5.23e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.54 E-value: 5.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFWKDKQTIrvLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGG--------RRITEPGMK 76
Cdd:PRK11831 8 VDMRGVSFTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 77 QGFIFQEHRLFPWLTVEENIA----ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEIL 152
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAyplrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 637173694 153 LLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDE 193
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPE 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-205 |
5.70e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.40 E-value: 5.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKqtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL---DTAYDGQILIGGRRITEPG----- 74
Cdd:PRK09984 5 IRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGrlard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 75 -----MKQGFIFQEHRLFPWLTVEENIAAN-----------FNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQR 138
Cdd:PRK09984 81 irksrANTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637173694 139 VAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQ 205
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALR 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-192 |
5.71e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 103.24 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 10 KSFWK-DKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGG-----------RRItepgmkq 77
Cdd:COG4586 25 KGLFRrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrrkefaRRI------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 GFIF-QEHRLFPWLTVEEN---IAANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILL 153
Cdd:COG4586 98 GVVFgQRSQLWWDLPAIDSfrlLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 637173694 154 LDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDID 192
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-254 |
6.71e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.48 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 13 WKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM-----KQGFIFQE-HRL 86
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnlrrKIGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 87 FPWLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDA 163
Cdd:PRK13642 94 FVGATVEDDVAfgmENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 164 FTRKHLQDVLLDIWQEKKTTMMLVTHDIDES-------IYLGNEIVlMQARPGRIHKI------LPVNLPFP----RDRT 226
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAassdrilVMKAGEII-KEAAPSELFATsedmveIGLDVPFSsnlmKDLR 252
|
250 260
....*....|....*....|....*...
gi 637173694 227 STAFqSLRQKVLSEFEKTDelLLTDGLG 254
Cdd:PRK13642 253 KNGF-DLPEKYLSEDELVE--LLADKLR 277
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-163 |
8.23e-26 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 100.26 E-value: 8.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVL-EDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITepgmKQGFIFQEHRLF--------PWL 90
Cdd:PRK13538 14 RILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEYHQDLLYlghqpgikTEL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637173694 91 TVEENIAANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDA 163
Cdd:PRK13538 90 TALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-222 |
9.86e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.75 E-value: 9.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GF 79
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrkhiGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQE-HRLFPWLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLD 155
Cdd:PRK13648 88 VFQNpDNQFVGSIVKYDVAfglENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 156 EPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQA---RPGRIHKI---------LPVNLPFP 222
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGtvyKEGTPTEIfdhaeeltrIGLDLPFP 246
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-204 |
1.15e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.69 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT-------EPGMKQGFIFQ--EHRLF-Pwl 90
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllEVRKTVGIVFQnpDDQLFaP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRK 167
Cdd:PRK13639 95 TVEEDVAfgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 637173694 168 HLQDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:PRK13639 175 QIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVM 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-192 |
1.51e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.54 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDI--VDKSFW------------------KDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYD 60
Cdd:COG1134 1 MSSMIEVenVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 61 GQILIGGrRIT---EPGMkqGFifqeHrlfPWLTVEENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHA----Yphe 130
Cdd:COG1134 81 GRVEVNG-RVSallELGA--GF----H---PELTGRENIylnGRLLGLSRKEIDEKFDEIVEFAELGDFIDQpvktY--- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637173694 131 lSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWqEKKTTMMLVTHDID 192
Cdd:COG1134 148 -SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMG 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-210 |
2.52e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 101.42 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPG----MKQGFIFQEHRLFPWLTVEENI 96
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRArharQRVGVVPQFDNLDPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 97 ---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRkHLqdvl 173
Cdd:PRK13537 102 lvfGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR-HL---- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 174 ldIWQEKKT------TMMLVTHDIDESIYLGNEIVLMQArpGR 210
Cdd:PRK13537 177 --MWERLRSllargkTILLTTHFMEEAERLCDRLCVIEE--GR 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-194 |
3.34e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISI-DIVDKSFWKDKQtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL-----DTAYDGQILIGGRRITEPG 74
Cdd:PRK14239 1 MTEPIlQVSDLSVYYNKK--KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 75 MKQ-------GFIFQEHRLFPwLTVEENIAANFNLKQQDVRRKVDELIEiVRLKGFE---------HAYPHELSGGMSQR 138
Cdd:PRK14239 79 TDTvdlrkeiGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVE-KSLKGASiwdevkdrlHDSALGLSGGQQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637173694 139 VAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIwqEKKTTMMLVTHDIDES 194
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQA 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-189 |
5.14e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.53 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL-----DTAYDGQILIGGRRITEPGM-------KQGFIFQEHRLFP 88
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVdpievrrEVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WLTVEENIAanFNLKQQDVRRKVDELIEIVR-----------LKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:PRK14267 99 HLTIYDNVA--IGVKLNGLVKSKKELDERVEwalkkaalwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190
....*....|....*....|....*....|..
gi 637173694 158 FGALDAFTRKHLQDVLLDIwqEKKTTMMLVTH 189
Cdd:PRK14267 177 TANIDPVGTAKIEELLFEL--KKEYTIVLVTH 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-203 |
5.43e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 5.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL---DTAYDGQILIGGRRITEPGM-----KQGFIFQE-HRLFPWLT 91
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVwdireKVGIVFQNpDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 92 VEENIAanFNLKQQDVRRKvdELIEIVR-------LKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:PRK13640 102 VGDDVA--FGLENRAVPRP--EMIKIVRdvladvgMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 637173694 165 TRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVL 203
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVL 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-210 |
5.48e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.63 E-value: 5.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT----EPGMKQ-GFIFQEHRLFPwLTVEEN 95
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkpEIYRQQvSYCAQTPTLFG-DTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANFNLKQQ--DVRRKVD-----ELIEIVRLKGFEhayphELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKH 168
Cdd:PRK10247 101 LIFPWQIRNQqpDPAIFLDdlerfALPDTILTKNIA-----ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 637173694 169 LQDVLLDIWQEKKTTMMLVTHDIDEsIYLGNEIVLMQARPGR 210
Cdd:PRK10247 176 VNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGE 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-206 |
6.43e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.06 E-value: 6.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 2 TISIDI--VDKSFwKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGG----RRITEPGM 75
Cdd:PRK13536 39 TVAIDLagVSKSY-GDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 76 KQGFIFQEHRLFPWLTVEENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEIL 152
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLlvfGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 153 LLDEPFGALDAFTRkHLqdvlldIWQEKKT------TMMLVTHDIDESIYLGNEIVLMQA 206
Cdd:PRK13536 195 ILDEPTTGLDPHAR-HL------IWERLRSllargkTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
24-211 |
9.64e-25 |
|
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: 98.21 E-value: 9.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 24 DLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL----DTAYDGQILIGGRRITEP---GMKQGFIFQEHR--LFPWLTVE- 93
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLsirGRHIATIMQNPRtaFNPLFTMGn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 94 ---ENIAANFNLKQQdVRRKVDELIEIVRLKGFE---HAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRK 167
Cdd:TIGR02770 84 haiETLRSLGKLSKQ-ARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 637173694 168 HLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:TIGR02770 163 RVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRI 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-204 |
1.02e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.39 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGG------RRITEPGMKQGFIFQ--EHRLFPWLtV 92
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIRNKAGMVFQnpDNQIVATI-V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHL 169
Cdd:PRK13633 104 EEDVAfgpENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 170 QDVLLDIWQEKKTTMMLVTHDIDESIYlGNEIVLM 204
Cdd:PRK13633 184 VNTIKELNKKYGITIILITHYMEEAVE-ADRIIVM 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-163 |
1.07e-24 |
|
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: 97.04 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE--PGMKQGFIFQEHR--LFPWLTVEEN 95
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqrDEPHENILYLGHLpgLKPELSALEN 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 96 IAAnFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDA 163
Cdd:TIGR01189 94 LHF-WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
35-211 |
1.27e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.11 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 35 VTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQ--EHRLFPwLTVEENIA---ANFNLKQ 104
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkfvGLVFQnpDDQIFS-PTVEQDIAfgpINLGLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 105 QDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTM 184
Cdd:PRK13652 112 ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTV 191
|
170 180
....*....|....*....|....*..
gi 637173694 185 MLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:PRK13652 192 IFSTHQLDLVPEMADYIYVMDK--GRI 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-205 |
1.83e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.75 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT-EPGMKQ--------GFIFQ--EHRLFPwL 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNlkklrkkvSLVFQfpEAQLFE-N 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENI---AANFNLKQQDVRRKVDELIEIVRLKG--FEHAyPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFT 165
Cdd:PRK13641 102 TVLKDVefgPKNFGFSEDEAKEKALKWLKKVGLSEdlISKS-PFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 637173694 166 RKHLQDVLLDiWQEKKTTMMLVTHDIDESIYLGNEIVLMQ 205
Cdd:PRK13641 181 RKEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLE 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-192 |
3.61e-24 |
|
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: 96.45 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 10 KSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIfqehrlfPW 89
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFN-------PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEENIAAN---FNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTR 166
Cdd:cd03220 99 LTGRENIYLNgrlLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180
....*....|....*....|....*.
gi 637173694 167 KHLQDVLLDiWQEKKTTMMLVTHDID 192
Cdd:cd03220 179 EKCQRRLRE-LLKQGKTVILVSHDPS 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-205 |
4.67e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.01 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWLTVEE 94
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlarrlALLPQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 NIAANFN--------LKQQDvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTR 166
Cdd:PRK11231 96 LVAYGRSpwlslwgrLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 637173694 167 KHLQDVLLDIWQEKKtTMMLVTHDIDESIYLGNEIVLMQ 205
Cdd:PRK11231 175 VELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLA 212
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-190 |
6.76e-24 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 99.81 E-value: 6.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFWKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIggrritEPGMKQGFIFQEHRLF 87
Cdd:PRK11819 12 VSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------APGIKVGYLPQEPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 88 PWLTVEENIAANFnlkqQDVRRKVDELIEIVRLKGFEHAYPHE------------------------------------- 130
Cdd:PRK11819 83 PEKTVRENVEEGV----AEVKAALDRFNEIYAAYAEPDADFDAlaaeqgelqeiidaadawdldsqleiamdalrcppwd 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 131 -----LSGGMSQRVAIARALLRDPEILLLDEPFGALDAFT----RKHLQDVlldiwqekKTTMMLVTHD 190
Cdd:PRK11819 159 akvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHDY--------PGTVVAVTHD 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-211 |
6.95e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.92 E-value: 6.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 25 LRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWlTVEENIA-A 98
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrkhlSWVGQNPQLPHG-TLRDNVLlG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 99 NFNLKQQdvrrKVDELIEIVRLKGFEHAYPH-----------ELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRK 167
Cdd:PRK11174 447 NPDASDE----QLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 637173694 168 HLQDVLLDIWQeKKTTMMlVTHDIDEsIYLGNEIVLMQArpGRI 211
Cdd:PRK11174 523 LVMQALNAASR-RQTTLM-VTHQLED-LAQWDQIWVMQD--GQI 561
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-211 |
8.67e-24 |
|
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: 95.63 E-value: 8.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI----TEPGMKQ-GFIFQEHRLFPwLTVEEN 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaladPAWLRRQvGVVLQENVLFN-RSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANfnlkqqDVRRKVDELIEIVRLKGfEHAYPHE---------------LSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:cd03252 96 IALA------DPGMSMERVIEAAKLAG-AHDFISElpegydtivgeqgagLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637173694 161 LDAFTRKHLQDVLLDIWQEKktTMMLVTHDIdESIYLGNEIVLMQArpGRI 211
Cdd:cd03252 169 LDYESEHAIMRNMHDICAGR--TVIIIAHRL-STVKNADRIIVMEK--GRI 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-189 |
1.11e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.51 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 4 SIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISgldTAYD---GQILIGGRRIT---EPGMKQ 77
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT---RAWDpqqGEILLNGQPIAdysEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 GFIFQEHR--LFPwLTVEEN--IAANfnlKQQDvrrkvDELIEIVRLKGFEH---------AYPHE----LSGGMSQRVA 140
Cdd:PRK11160 415 AISVVSQRvhLFS-ATLRDNllLAAP---NASD-----EALIEVLQQVGLEKlleddkglnAWLGEggrqLSGGEQRRLG 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637173694 141 IARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKktTMMLVTH 189
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITH 532
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-205 |
1.51e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.81 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQG------------------FIFQ 82
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadknqlrllrtrltMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 EHRLFPWLTVEENIAAN----FNLKQQDVRRKVDELIEIVRLKGFEHA-YPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:PRK10619 100 HFNLWSHMTVLENVMEApiqvLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637173694 158 FGALDAftrkHLQDVLLDIWQ---EKKTTMMLVTHDIDESIYLGNEIVLMQ 205
Cdd:PRK10619 180 TSALDP----ELVGEVLRIMQqlaEEGKTMVVVTHEMGFARHVSSHVIFLH 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-207 |
2.07e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI--TEPGMKQ-----GFIFQ--EHRLFPwLTV 92
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKlresvGMVFQdpDNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHL 169
Cdd:PRK13636 101 YQDVsfgAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 637173694 170 QDVLLDIWQEKKTTMMLVTHDIDE-SIYLGNEIVLMQAR 207
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGR 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
21-211 |
2.26e-23 |
|
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: 94.51 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT--EP------GMkqGFIFQEHRLFPWLTV 92
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITklPPheraraGI--AYVPQGREIFPRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENI---AANFNLKQQDVRRKVDELIEIvrLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHL 169
Cdd:TIGR03410 93 EENLltgLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 637173694 170 QDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:TIGR03410 171 GRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMER--GRV 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-191 |
2.41e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 16 KQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI-TEPGMKQG-------FIFQE--HR 85
Cdd:PRK10261 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKLQalrrdiqFIFQDpyAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 86 LFPWLTVEENIAANFN----LKQQDVRRKVDELIEIVRLKGfEHA--YPHELSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRvhglLPGKAAAARVAWLLERVGLLP-EHAwrYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190
....*....|....*....|....*....|..
gi 637173694 160 ALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDI 191
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDM 524
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-192 |
3.44e-23 |
|
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: 94.04 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDI--VDKSFW---KDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILI---GG----- 67
Cdd:COG4778 1 MTTLLEVenLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGwvdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 68 ----RRITEpgMKQ---GFIFQEHRLFPWLT----VEENIAANfNLKQQDVRRKVDELIEIVRLKgfE---HAYPHELSG 133
Cdd:COG4778 81 qaspREILA--LRRrtiGYVSQFLRVIPRVSaldvVAEPLLER-GVDREEARARARELLARLNLP--ErlwDLPPATFSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637173694 134 GMSQRVAIARALLRDPEILLLDEPFGALDAFTRkhlqDVLLDIWQEKK---TTMMLVTHDID 192
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANR----AVVVELIEEAKargTAIIGIFHDEE 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-215 |
1.17e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.18 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 4 SIDIVDKSFWKDKQtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdTAYDGQILIGG-----------RRITE 72
Cdd:PRK14258 7 AIKVNNLSFYYDTQ--KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrveffnqniyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 73 PGMKQ--GFIFQEHRLFPwLTVEENIAANFNLKQQDVRRKVDELIEIV--------RLKGFEHAYPHELSGGMSQRVAIA 142
Cdd:PRK14258 84 NRLRRqvSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESAlkdadlwdEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637173694 143 RALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQARPGRIHKIL 215
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLV 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-193 |
1.54e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.27 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM---------KQGFIFQ--EHRLFP 88
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdikqirkKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WlTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKG--FEHAyPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDA 163
Cdd:PRK13649 101 E-TVLKDVAfgpQNFGVSQEEAEALAREKLALVGISEslFEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190
....*....|....*....|....*....|
gi 637173694 164 FTRKHLQDVLLDIwQEKKTTMMLVTHDIDE 193
Cdd:PRK13649 179 KGRKELMTLFKKL-HQSGMTIVLVTHLMDD 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-241 |
1.99e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.83 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 17 QTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQG--------FIFQEH--RL 86
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafrrdiqMVFQDSisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 87 FPWLTVEENIAANF----NLKQQDVRRKVDELIEIVRLKGfEHA--YPHELSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:PRK10419 103 NPRKTVREIIREPLrhllSLDKAERLARASEMLRAVDLDD-SVLdkRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 161 LDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKILPVNlpfPRDR-TSTAFQSLRQKVLS 239
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN--GQIVETQPVG---DKLTfSSPAGRVLQNAVLP 256
|
..
gi 637173694 240 EF 241
Cdd:PRK10419 257 AF 258
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-205 |
2.21e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.26 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ---------GFIFQ--EHRLFP 88
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrkkvGVVFQfpESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WlTVEENIA---ANFNLKQQDVRRKVDELIEIVRL-KGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:PRK13643 100 E-TVLKDVAfgpQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 637173694 165 TRKHLQDVLLDIWQEKKtTMMLVTHDIDESIYLGNEIVLMQ 205
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLE 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-211 |
2.31e-22 |
|
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: 91.76 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPwLTVEEN 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlhskvSLVGQEPVLFA-RSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANFNLKQQDvrrKVDELIEIVRLKGF----EHAYPHE-------LSGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:cd03248 108 IAYGLQSCSFE---CVKEAAQKAHAHSFiselASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637173694 165 TRKHLQDVLLDiWQEkKTTMMLVTHDIdESIYLGNEIVLMQArpGRI 211
Cdd:cd03248 185 SEQQVQQALYD-WPE-RRTVLVIAHRL-STVERADQILVLDG--GRI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-211 |
5.66e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.59 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ------GFIFQE-HRLFPWLTVEE 94
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirklvGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 NIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQD 171
Cdd:PRK13644 98 DLAfgpENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 637173694 172 VLLDIwQEKKTTMMLVTHDIDEsIYLGNEIVLMQArpGRI 211
Cdd:PRK13644 178 RIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDR--GKI 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-205 |
1.11e-21 |
|
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: 88.52 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPG----MKQGFI 80
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEkalsSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 81 FQEHRLFPwLTVEENIAANFnlkqqdvrrkvdelieivrlkgfehayphelSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:cd03247 81 NQRPYLFD-TTLRNNLGRRF-------------------------------SGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637173694 161 LDAFTRKHLQDVLLDIWQEKktTMMLVTHDI------DESIYLGNEIVLMQ 205
Cdd:cd03247 129 LDPITERQLLSLIFEVLKDK--TLIWITHHLtgiehmDKILFLENGKIIMQ 177
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-189 |
1.93e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.86 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPG-----MKQGFIFQEHRLFPWlTVEEN 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANFNLKQQDVRRKV------DELIeivrlKGFEHAYPHE-------LSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAakaanaHDFI-----MEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180
....*....|....*....|....*...
gi 637173694 163 AFTRKHLQDvlldiWQEKKT-TMMLVTH 189
Cdd:TIGR00958 650 AECEQLLQE-----SRSRASrTVLLIAH 672
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-224 |
1.98e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.21 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI-----TEPGM 75
Cdd:PRK09536 2 PMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 76 KQGFIFQEHRLFPWLTVEENIA-------ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRD 148
Cdd:PRK09536 78 RVASVPQDTSLSFEFDVRQVVEmgrtphrSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637173694 149 PEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVtHDIDESIYLGNEIVLMQArpGRIHKILPvnlpfPRD 224
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLAD--GRVRAAGP-----PAD 225
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-182 |
2.54e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 92.64 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 31 PGEFVTVIGPSGCGKSTLLKIISGL--DTAYDGQILIGGRRITEPGMKQ-GFIFQEHRLFPWLTVEENIAanF------- 100
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRETLV--Fcsllrlp 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 101 -NLKQQDVRRKVDELIEIVRLKGFEH-----AYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLL 174
Cdd:PLN03211 171 kSLTKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
....*...
gi 637173694 175 DIWQEKKT 182
Cdd:PLN03211 251 SLAQKGKT 258
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-211 |
2.90e-21 |
|
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: 87.49 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPG----MKQGFIF-----QEHRLFPWL 90
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprdaIRAGIAYvpedrKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENIAAnfnlkqqdvrrkvdelieivrlkgfehayPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQ 170
Cdd:cd03215 94 SVAENIAL-----------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 637173694 171 DVLLDIWQEKKTTmMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:cd03215 145 RLIRELADAGKAV-LLISSELDELLGLCDRILVMYE--GRI 182
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-190 |
3.90e-21 |
|
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: 92.12 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT-----EPGMKQGFIFQEHRLFPWlTVEEN 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdreELGRHIGYLPQDVELFDG-TIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAanfNLKQQDVRR--------KVDELIeiVRL-KGFEH---AYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDA 163
Cdd:COG4618 426 IA---RFGDADPEKvvaaaklaGVHEMI--LRLpDGYDTrigEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180
....*....|....*....|....*..
gi 637173694 164 FTRKHLQDVLLDIwQEKKTTMMLVTHD 190
Cdd:COG4618 501 EGEAALAAAIRAL-KARGATVVVITHR 526
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-189 |
5.93e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAY-----DGQILIGGRRI-----TEPGMKQGFIFQEHRLFP 88
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIfkmdvIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WLTVEENIAANFNLK-----QQDVRRKVDELIEIVRL----KGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:PRK14247 96 NLSIFENVALGLKLNrlvksKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190
....*....|....*....|....*....|
gi 637173694 160 ALDAFTRKHLQDVLLDIwqEKKTTMMLVTH 189
Cdd:PRK14247 176 NLDPENTAKIESLFLEL--KKDMTIVLVTH 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-211 |
9.05e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.50 E-value: 9.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWLTVEEN 95
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarriGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANFNLKQQDVR--RKVDE--LIEIVRLKGFEHAYPHE---LSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKH 168
Cdd:PRK10253 102 VARGRYPHQPLFTrwRKEDEeaVTKAMQATGITHLADQSvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 169 LQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:PRK10253 182 LLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKI 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-211 |
1.01e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.14 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 12 FWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPgmKQGF---------IFQ 82
Cdd:PRK13638 7 LWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS--KRGLlalrqqvatVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 --EHRLFpWLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:PRK13638 85 dpEQQIF-YTDIDSDIAfslRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637173694 158 FGALDAFTRKHLQDVLLDIWQEKKtTMMLVTHDID------ESIY-LGNEIVLMQARPGRI 211
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDliyeisDAVYvLRQGQILTHGAPGEV 223
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
21-182 |
1.05e-20 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 90.91 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIisgLDTAYD---GQILIGGR--RITEPG-MKQGF--IFQEHRLFPwLTV 92
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQL---LLRFYDpqsGRILLDGVdlRQLDPAeLRARMalVPQDPVLFA-ASV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIA-ANFNLKQQDVRR-----KVDELIEivRL-KGFeHAYPHE----LSGGMSQRVAIARALLRDPEILLLDEPFGAL 161
Cdd:TIGR02204 431 MENIRyGRPDATDEEVEAaaraaHAHEFIS--ALpEGY-DTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDEATSAL 507
|
170 180
....*....|....*....|.
gi 637173694 162 DAFTRKHLQDVLLDIWQEKKT 182
Cdd:TIGR02204 508 DAESEQLVQQALETLMKGRTT 528
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-211 |
1.11e-20 |
|
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: 90.55 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPwLTVE 93
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrrqvALVSQDVVLFN-DTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 94 ENIAanFNLKQQDVRRKVDELIEIVRLKGFEHAYPH-----------ELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:TIGR02203 424 NNIA--YGRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637173694 163 AFTRKHLQDVLLDIWQEKktTMMLVTHDIdESIYLGNEIVLMQArpGRI 211
Cdd:TIGR02203 502 NESERLVQAALERLMQGR--TTLVIAHRL-STIEKADRIVVMDD--GRI 545
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-182 |
1.53e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.41 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLlkiISGLDTAYD---GQILIGG---RRITEPGMKQ--GFIFQEHRLFPwLTVE 93
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRVFDpqsGRILIDGtdiRTVTRASLRRniAVVFQDAGLFN-RSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 94 ENI------AANFNLKQQDVRRKVDELIEiVRLKGFEHAYPH---ELSGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:PRK13657 427 DNIrvgrpdATDEEMRAAAERAQAHDFIE-RKPDGYDTVVGErgrQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170
....*....|....*...
gi 637173694 165 TRKHLQDVLLDIWQEKKT 182
Cdd:PRK13657 506 TEAKVKAALDELMKGRTT 523
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-190 |
1.66e-20 |
|
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: 84.42 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkDKQTIrvLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGgrritepgmkqgfifq 82
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 ehrlfpwltveeniaanfnlkqqdvrrkvdelieivrlKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:cd03221 61 --------------------------------------STVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180
....*....|....*....|....*...
gi 637173694 163 AFTRKHLQDVLldiwQEKKTTMMLVTHD 190
Cdd:cd03221 103 LESIEALEEAL----KEYPGTVILVSHD 126
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-163 |
1.73e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIFQEHR--LFPWLTVEENIA- 97
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRnaMKPALTVAENLEf 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637173694 98 -ANFNlkqQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDA 163
Cdd:PRK13539 97 wAAFL---GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-211 |
1.78e-20 |
|
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: 90.26 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdtaYD---GQILIGGRRITEpgMKQ-------GFIFQEHRLFPwL 90
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF---YDvtsGRILIDGQDIRD--VTQaslraaiGIVPQDTVLFN-D 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENIA-ANFNLKQQDVRrkvdELIEIVRLKGFEHAYPH-----------ELSGGMSQRVAIARALLRDPEILLLDEPF 158
Cdd:COG5265 447 TIAYNIAyGRPDASEEEVE----AAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 159 GALDAFTRKHLQDVLLDIWQEKktTMMLVTH------DIDesiylgnEIVLMQArpGRI 211
Cdd:COG5265 523 SALDSRTERAIQAALREVARGR--TTLVIAHrlstivDAD-------EILVLEA--GRI 570
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-163 |
1.80e-20 |
|
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: 86.01 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE--PGMKQGFIFQEHR--LFPWLTVEENI 96
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFqrDSIARGLLYLGHApgIKTTLSVLENL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 97 A--ANFNLKQQdvrrkVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDA 163
Cdd:cd03231 95 RfwHADHSDEQ-----VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-191 |
1.92e-20 |
|
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: 86.62 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIFQEHRLF-----PWL--- 90
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAyaaqkPWLlna 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENI--AANFNlkqqdvRRKVDELIEIVRLKGFEHAYPH-----------ELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:cd03290 94 TVEENItfGSPFN------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 158 FGALDAFTRKHL-QDVLLDIWQEKKTTMMLVTHDI 191
Cdd:cd03290 168 FSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKL 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-206 |
2.28e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKS-TLLKIISGLDT---AY-DGQILIGGRRI---TEP- 73
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvVYpSGDIRFHGESLlhaSEQt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 74 -----GMKQGFIFQEH--RLFPWLTVEENIAANFNLkQQDVRRKV--DELIEIVRLKGFEHA------YPHELSGGMSQR 138
Cdd:PRK15134 86 lrgvrGNKIAMIFQEPmvSLNPLHTLEKQLYEVLSL-HRGMRREAarGEILNCLDRVGIRQAakrltdYPHQLSGGERQR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 139 VAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQA 206
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-161 |
2.50e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 10 KSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE--PGMKQGF----IFQE 83
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltPAKAHQLgiylVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 84 HRLFPWLTVEENIAanFNL-KQQDVRRKVDELIEIVRLkgfeHAYPHELSGGMS----QRVAIARALLRDPEILLLDEPF 158
Cdd:PRK15439 95 PLLFPNLSVKENIL--FGLpKRQASMQKMKQLLAALGC----QLDLDSSAGSLEvadrQIVEILRGLMRDSRILILDEPT 168
|
...
gi 637173694 159 GAL 161
Cdd:PRK15439 169 ASL 171
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-189 |
2.55e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 84.51 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGqiliggrRITEPGMKQGFIFQEHRLFPWLTveeniaanf 100
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG-------RIGMPEGEDLLFLPQRPYLPLGT--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 101 nLKQQdvrrkvdeLIeivrlkgfehaYP--HELSGGMSQRVAIARALLRDPEILLLDEPFGALDAftrkHLQDVLLDIWQ 178
Cdd:cd03223 80 -LREQ--------LI-----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLYQLLK 135
|
170
....*....|.
gi 637173694 179 EKKTTMMLVTH 189
Cdd:cd03223 136 ELGITVISVGH 146
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-190 |
2.58e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFwKDKQtirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGgrritePGMKQGFIFQEHRLF 87
Cdd:COG0488 321 LSKSY-GDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG------ETVKIGYFDQHQEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 88 -PWLTVEENIA---------------ANFNLKQQDVRRKVdelieivrlkgfehaypHELSGGMSQRVAIARALLRDPEI 151
Cdd:COG0488 391 dPDKTVLDELRdgapggteqevrgylGRFLFSGDDAFKPV-----------------GVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190
....*....|....*....|....*....|....*....
gi 637173694 152 LLLDEPFGALDAFTRKHLQDVLLDiWQEkktTMMLVTHD 190
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDD-FPG---TVLLVSHD 488
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-189 |
2.66e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.48 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGgrritePGMKQGFIFQEHRLfPWLTVEE-----N 95
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP------AGARVLFLPQRPYL-PLGTLREallypA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANFNLKQ-QDVRRKV--DELIEivRLkGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDV 172
Cdd:COG4178 451 TAEAFSDAElREALEAVglGHLAE--RL-DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL 527
|
170
....*....|....*..
gi 637173694 173 LLDiwQEKKTTMMLVTH 189
Cdd:COG4178 528 LRE--ELPGTTVISVGH 542
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-212 |
3.38e-20 |
|
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: 89.69 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE--PGMKQ--GFIFQEHRLFPWLTVEENIA 97
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETnlDAVRQslGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 ANFNLK---QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLL 174
Cdd:TIGR01257 1026 FYAQLKgrsWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|....*...
gi 637173694 175 DiWQEKKTTMMlVTHDIDESIYLGNEIVLMQArpGRIH 212
Cdd:TIGR01257 1106 K-YRSGRTIIM-STHHMDEADLLGDRIAIISQ--GRLY 1139
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-229 |
3.77e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 86.29 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 17 QTIRVL-EDLRLSIIPGEFVTVIGPSGCGKS----TLLKIISGLDTAYDGQILIGGRRI---TEPGMKQGFIFQEHR--L 86
Cdd:PRK10418 13 QAAQPLvHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVapcALRGRKIATIMQNPRsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 87 FPWLTVEENiaANFNLKQQDVRRKVDELIEIVRLKGFEHA------YPHELSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:PRK10418 93 NPLHTMHTH--ARETCLALGKPADDATLTAALEAVGLENAarvlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 161 LDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKILPVNLPFPRDRTSTA 229
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH--GRIVEQGDVETLFNAPKHAVT 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-204 |
1.09e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR---------RITEPGMKQ--GFIFQEHRLFPW 89
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIKLRKevGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEENIAanFNLKQQDVR--RKVDELIE--IVRLKGFEHAY------PHELSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:PRK14246 105 LSIYDNIA--YPLKSHGIKekREIKKIVEecLRKVGLWKEVYdrlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 637173694 160 ALDAFTRKHLQDVLLDIwqEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:PRK14246 183 MIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFL 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-199 |
1.90e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.16 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEpgMKQGFIFQE--------HRLFPWL 90
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD--WQTAKIMREavaivpegRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENIA-ANFNLKQQDVRRKVDELIEIV-RLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKH 168
Cdd:PRK11614 96 TVEENLAmGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190
....*....|....*....|....*....|.
gi 637173694 169 LQDVLLDIwQEKKTTMMLVTHDIDESIYLGN 199
Cdd:PRK11614 176 IFDTIEQL-REQGMTIFLVEQNANQALKLAD 205
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-241 |
2.15e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.45 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAY-----DGQILIGGRRITEPGM-------KQGFIFQEHRLFPw 89
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLYAPDVdpvevrrRIGMVFQKPNPFP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEENIA--ANFN--------LKQQDVRRKV--DELIEIVRLKGFEhaypheLSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:PRK14243 105 KSIYDNIAygARINgykgdmdeLVERSLRQAAlwDEVKDKLKQSGLS------LSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 158 FGALDAFTRKHLQDVLLDIwqEKKTTMMLVTHDIDESIYLGNEIVLMQARP----GRIHKILPVnlpfprDRTSTAFQSL 233
Cdd:PRK14243 179 CSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFFNVELteggGRYGYLVEF------DRTEKIFNSP 250
|
....*...
gi 637173694 234 RQKVLSEF 241
Cdd:PRK14243 251 QQQATRDY 258
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
9-192 |
4.48e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.68 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 9 DKSFWKDKQTIRV-----LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----G 78
Cdd:PRK10575 9 DTTFALRNVSFRVpgrtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfarkvA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 FIFQEHRLFPWLTVEENIA--------ANFNLKQQDvRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPE 150
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAigrypwhgALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 637173694 151 ILLLDEPFGALDAftrKHLQDVLLDIW---QEKKTTMMLVTHDID 192
Cdd:PRK10575 168 CLLLDEPTSALDI---AHQVDVLALVHrlsQERGLTVIAVLHDIN 209
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-205 |
4.52e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.06 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPG---------MKQGFIFQ--EHRLFPwL 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyirpvrKRIGMVFQfpESQLFE-D 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENI---AANFNLKQQDVR-RKVDELIEIvrlkGFEH----AYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:PRK13646 102 TVEREIifgPKNFKMNLDEVKnYAHRLLMDL----GFSRdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 163 AFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQ 205
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMK 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-192 |
4.53e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.37 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDIVDKSFwkDKQT---IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQI-------------- 63
Cdd:PRK13651 1 MQIKVKNIVKIF--NKKLpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 64 ---------LIGGRR------ITEPGMKQGFIFQ--EHRLFPwLTVEENI---AANFNLKQQDVRRKVDELIEIVRL-KG 122
Cdd:PRK13651 79 ekekvleklVIQKTRfkkikkIKEIRRRVGVVFQfaEYQLFE-QTIEKDIifgPVSMGVSKEEAKKRAAKYIELVGLdES 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 123 FEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKtTMMLVTHDID 192
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLD 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-191 |
5.44e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.24 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQIliggrrITEPGMKQGFIFQEHRLFPW--LTVEENIA 97
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQKLYLDTTlpLTVNRFLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 ANFNLKQQDV-----RRKVDELIEivrlkgfehAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDV 172
Cdd:PRK09544 92 LRPGTKKEDIlpalkRVQAGHLID---------APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDL 162
|
170
....*....|....*....
gi 637173694 173 LLDIWQEKKTTMMLVTHDI 191
Cdd:PRK09544 163 IDQLRRELDCAVLMVSHDL 181
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
12-206 |
6.91e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 84.02 E-value: 6.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 12 FWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL----------DTAYDGQILiggRRITEPGMKQ---- 77
Cdd:PRK11022 13 FGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypgrvmaeKLEFNGQDL---QRISEKERRNlvga 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 --GFIFQE--HRLFPWLTVEENIAANFNLKQQDVRR-KVDELIEIVRLKGFE------HAYPHELSGGMSQRVAIARALL 146
Cdd:PRK11022 90 evAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKtRRQRAIDLLNQVGIPdpasrlDVYPHQLSGGMSQRVMIAMAIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 147 RDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQA 206
Cdd:PRK11022 170 CRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-189 |
8.68e-19 |
|
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: 85.18 E-value: 8.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT--EPGMKQGFIF---QEHRLFPWlTVEEN 95
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdiDRHTLRQFINylpQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 --IAANFNLKQQDVRRKVdELIEI-VRLKGFEHAYPHEL-------SGGMSQRVAIARALLRDPEILLLDEPFGALDAFT 165
Cdd:TIGR01193 568 llLGAKENVSQDEIWAAC-EIAEIkDDIENMPLGYQTELseegssiSGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180
....*....|....*....|....
gi 637173694 166 RKHLQDVLLDIwQEKktTMMLVTH 189
Cdd:TIGR01193 647 EKKIVNNLLNL-QDK--TIIFVAH 667
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-191 |
9.44e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.14 E-value: 9.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKST----LLKII-SGLDTAYDGQILIG-GRRITEPGMKQ-GFIFQE--HRLFPWLT 91
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInSQGEIWFDGQPLHNlNRRQLLPVRHRiQVVFQDpnSSLNPRLN 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 92 VEENIAANFNLKQQDV--RRKVDELIEIVRLKGFE----HAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFT 165
Cdd:PRK15134 381 VLQIIEEGLRVHQPTLsaAQREQQVIAVMEEVGLDpetrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTV 460
|
170 180
....*....|....*....|....*.
gi 637173694 166 RKHLQDVLLDIWQEKKTTMMLVTHDI 191
Cdd:PRK15134 461 QAQILALLKSLQQKHQLAYLFISHDL 486
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-162 |
3.61e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ------GFIFQEHRLFPWLTVE 93
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArarrgiGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637173694 94 ENIAANF----NLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:PRK10895 97 DNLMAVLqirdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
14-204 |
5.76e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.44 E-value: 5.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 14 KDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIG----------GRRITEPGMKQ------ 77
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKiknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 -----GFIFQ--EHRLFPwLTVEENIA---ANFNLKQQDVRRKVDELIEIVRLK-GFEHAYPHELSGGMSQRVAIARALL 146
Cdd:PRK13631 114 lrrrvSMVFQfpEYQLFK-DTIEKDIMfgpVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 147 RDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMlVTHDIDESIYLGNEIVLM 204
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHVLEVADEVIVM 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-191 |
8.26e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 8.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 11 SFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKS----TLLKII--SGLDTAYDGQIL-------IGGRRITEPGMKQ 77
Cdd:PRK10261 21 AFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLrrrsrqvIELSEQSAAQMRH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 78 ------GFIFQE--HRLFPWLTVEENIAANFNLKQ----QDVRRKVDELIEIVRLKGFEHA---YPHELSGGMSQRVAIA 142
Cdd:PRK10261 101 vrgadmAMIFQEpmTSLNPVFTVGEQIAESIRLHQgasrEEAMVEAKRMLDQVRIPEAQTIlsrYPHQLSGGMRQRVMIA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637173694 143 RALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDI 191
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDM 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-157 |
9.39e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.99 E-value: 9.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR--RITEPG--MKQGFIF-----QEHRLFPWL 90
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRdaIRAGIAYvpedrKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENIA-ANFN-------LKQQDVRRKVDELIEIVRLKgfehaYPH------ELSGGMSQRVAIARALLRDPEILLLDE 156
Cdd:COG1129 346 SIRENITlASLDrlsrgglLDRRRERALAEEYIKRLRIK-----TPSpeqpvgNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
.
gi 637173694 157 P 157
Cdd:COG1129 421 P 421
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
27-208 |
3.24e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.49 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 27 LSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT-EPGMK---QGFI--FQEHRLFPWLTVEEN----- 95
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEgLPGHQiarMGVVrtFQHVRLFREMTVIENllvaq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 ---IAANFN---LKQQDVRRKVDELI-------EIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:PRK11300 106 hqqLKTGLFsglLKTPAFRRAESEALdraatwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLN 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637173694 163 AFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM-QARP 208
Cdd:PRK11300 186 PKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVnQGTP 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-232 |
4.37e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.46 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 60 DGQILIGGRRITEPGMKQ-----GFIFQEHRLFPwLTVEENIA-ANFNLKQQDVRR-----KVDELIEIVRLKGFEHAYP 128
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDlrnlfSIVSQEPMLFN-MSIYENIKfGKEDATREDVKRackfaAIDEFIESLPNKYDTNVGP 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 129 H--ELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIdesiylgneivlmqA 206
Cdd:PTZ00265 1355 YgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI--------------A 1420
|
170 180
....*....|....*....|....*.
gi 637173694 207 RPGRIHKILPVNLPfprDRTSTAFQS 232
Cdd:PTZ00265 1421 SIKRSDKIVVFNNP---DRTGSFVQA 1443
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
13-206 |
1.30e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.14 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 13 WKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT-----EPGMKQGFIFQE---- 83
Cdd:PRK15112 20 WFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysYRSQRIRMIFQDpsts 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 84 ----HRLFPWLTVEenIAANFNLKQQDVRRKVDELIEIVRLKGfEHA--YPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:PRK15112 100 lnprQRISQILDFP--LRLNTDLEPEQREKQIIETLRQVGLLP-DHAsyYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637173694 158 FGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQA 206
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-193 |
1.43e-16 |
|
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: 78.71 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 14 KDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL--DTAYDGQILIGGRRITEPGMKQ------GFIFQEHR 85
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDteragiVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 86 LFPWLTVEENIAANFNLKQQDVR-------RKVDELIEIVRLKGFEHAYP-HELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:TIGR02633 89 LVPELSVAENIFLGNEITLPGGRmaynamyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 637173694 158 FGALdafTRKHLQdVLLDI---WQEKKTTMMLVTHDIDE 193
Cdd:TIGR02633 169 SSSL---TEKETE-ILLDIirdLKAHGVACVYISHKLNE 203
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-191 |
1.66e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.46 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 24 DLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdTAYDGQI----LIGGRRITEPGMKQ---------GFIFQE--HRLFP 88
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIggsaTFNGREILNLPEKElnklraeqiSMIFQDpmTSLNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WLTVEENIAANFNL-----KQQDVRRKVDEL--IEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGAL 161
Cdd:PRK09473 113 YMRVGEQLMEVLMLhkgmsKAEAFEESVRMLdaVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 192
|
170 180 190
....*....|....*....|....*....|
gi 637173694 162 DAFTRKHLQDVLLDIWQEKKTTMMLVTHDI 191
Cdd:PRK09473 193 DVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-193 |
2.93e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.64 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGF------IFQEHRLFPWLTV 92
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALaagvaiIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENI----------AANFNLKQQDVRRKVDEL-IEI---VRLKgfehayphELSGGMSQRVAIARALLRDPEILLLDEPF 158
Cdd:PRK11288 97 AENLylgqlphkggIVNRRLLNYEAREQLEHLgVDIdpdTPLK--------YLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 159 GALDAFTRKHLQDVLLDIWQEKKtTMMLVTHDIDE 193
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGR-VILYVSHRMEE 202
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-203 |
3.69e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.90 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTA-----YDGQILIGGRRI------TEPGMKQGFIFQEHRLFPw 89
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyrdvLEFRRRVGMLFQRPNPFP- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEENIAANFNlKQQDVRRKVDELIEIVRLK--GFEHAY-------PHELSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:PRK14271 115 MSIMDNVLAGVR-AHKLVPRKEFRGVAQARLTevGLWDAVkdrlsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 161 LDAFTRKHLQDVLLDIwqEKKTTMMLVTHDIDESIYLGNEIVL 203
Cdd:PRK14271 194 LDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAAL 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-193 |
3.90e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL--DTAYDGQILIGGRRITEPGMKQ------GFIFQEHRLFPWL 90
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDteragiAIIHQELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENI----------AANFNlkqqDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:PRK13549 98 SVLENIflgneitpggIMDYD----AMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190
....*....|....*....|....*....|...
gi 637173694 161 LDAFTRKHLQDVLLDIwQEKKTTMMLVTHDIDE 193
Cdd:PRK13549 174 LTESETAVLLDIIRDL-KAHGIACIYISHKLNE 205
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-205 |
5.39e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.06 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 2 TISIDIvdKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM------ 75
Cdd:PRK10789 313 ELDVNI--RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdswrsr 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 76 -----KQGFIFQEhrlfpwlTVEENIA-ANFNLKQQDVRR-----KVDEliEIVRL-KGFEHAYPHE---LSGGMSQRVA 140
Cdd:PRK10789 391 lavvsQTPFLFSD-------TVANNIAlGRPDATQQEIEHvarlaSVHD--DILRLpQGYDTEVGERgvmLSGGQKQRIS 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637173694 141 IARALLRDPEILLLDEPFGALDAFTRKH-LQDvlLDIWQEKKtTMMLVTHDIdESIYLGNEIVLMQ 205
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQiLHN--LRQWGEGR-TVIISAHRL-SALTEASEILVMQ 523
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-209 |
6.17e-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: 74.75 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEF-----VTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITepgMKQGFIF--QEHRLFPWLTVEE 94
Cdd:cd03237 10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---YKPQYIKadYEGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 NIAANFNLKQQDVRR--KVDELIE-IVRlkgfehayphELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQD 171
Cdd:cd03237 87 KDFYTHPYFKTEIAKplQIEQILDrEVP----------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 637173694 172 VLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQARPG 209
Cdd:cd03237 157 VIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-175 |
6.30e-16 |
|
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: 76.90 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwKDKQTIrvlEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGgrritePGMKQGFIFQ 82
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLI---DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG------ETVKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 EH-RLFPWLTVEENIA-------------------ANFNLKQQDVRRKVDelieivrlkgfehayphELSGGMSQRVAIA 142
Cdd:TIGR03719 393 SRdALDPNKTVWEEISggldiiklgkreipsrayvGRFNFKGSDQQKKVG-----------------QLSGGERNRVHLA 455
|
170 180 190
....*....|....*....|....*....|...
gi 637173694 143 RALLRDPEILLLDEPFGALDAFTRKHLQDVLLD 175
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALLN 488
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-157 |
6.86e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.70 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILI-GG-------RRITEPG---MKQGFifqEHRLFP 88
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGGdmadarhRRAVCPRiayMPQGL---GKNLYP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637173694 89 WLTVEENI---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:NF033858 92 TLSVFENLdffGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-208 |
8.12e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.38 E-value: 8.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwKDKqtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDT--AYDGQILIG-------GR----- 68
Cdd:TIGR03269 1 IEVKNLTKKF-DGK---EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcGYverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 69 RITEPGMKQGFIFQEHRLFPW---------------------------LTVEENIAANFN---LKQQDVRRKVDELIEIV 118
Cdd:TIGR03269 77 KVGEPCPVCGGTLEPEEVDFWnlsdklrrrirkriaimlqrtfalygdDTVLDNVLEALEeigYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 119 RLkgfEHAYPH---ELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTH------ 189
Cdd:TIGR03269 157 QL---SHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevie 233
|
250 260
....*....|....*....|
gi 637173694 190 DI-DESIYLGNEIVLMQARP 208
Cdd:TIGR03269 234 DLsDKAIWLENGEIKEEGTP 253
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
24-205 |
1.06e-15 |
|
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: 74.10 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 24 DLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR--------RITEPGMKQ------GFIFQEHRLFPW 89
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelelyQLSEAERRRlmrtewGFVHQNPRDGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEE--NIA-----------ANFNLKQQDVRRKVDelIEIVRLKGFehayPHELSGGMSQRVAIARALLRDPEILLLDE 156
Cdd:TIGR02323 101 MRVSAgaNIGerlmaigarhyGNIRATAQDWLEEVE--IDPTRIDDL----PRAFSGGMQQRLQIARNLVTRPRLVFMDE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 637173694 157 PFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQ 205
Cdd:TIGR02323 175 PTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQ 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-175 |
3.24e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdTAYDGQILIGGRRITE-PGMKQGfifqEHRlfPWLTVEENIAANF 100
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwSAAELA----RHR--AYLSQQQTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 101 NLKQ------------QDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLR-DPEI------LLLDEPFGAL 161
Cdd:PRK03695 85 PVFQyltlhqpdktrtEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSL 164
|
170
....*....|....
gi 637173694 162 DAftrkhLQDVLLD 175
Cdd:PRK03695 165 DV-----AQQAALD 173
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-251 |
4.21e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 13 WKDKQTirVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRiTEPGMKQGFIfqehrlfPWLTV 92
Cdd:PRK15056 16 WRNGHT--ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLV-------AYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIAANFNLKQQDV-------------------RRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILL 153
Cdd:PRK15056 86 SEEVDWSFPVLVEDVvmmgryghmgwlrrakkrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 154 LDEPFGALDAFTRKHLQDVLLDIWQEKKtTMMLVTHDIDESIYLGNEIVLMQarpGRIHKILPVNLPFPRDRTSTAFQS- 232
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVK---GTVLASGPTETTFTAENLELAFSGv 241
|
250
....*....|....*....
gi 637173694 233 LRQKVLSEFEktdELLLTD 251
Cdd:PRK15056 242 LRHVALNGSE---ESIITD 257
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-192 |
4.69e-15 |
|
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: 71.76 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWlTVEEN 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrsriSIIPQDPVLFSG-TIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAAnFNLKQQDvrrKVDELIEIVRLKGFEHAYPHEL-----------SGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:cd03244 98 LDP-FGEYSDE---ELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180 190
....*....|....*....|....*....|
gi 637173694 165 TRKHLQDVLldiwQE--KKTTMMLVTHDID 192
Cdd:cd03244 174 TDALIQKTI----REafKDCTVLTIAHRLD 199
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-204 |
5.16e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 73.40 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 1 MTISIDivdksfwKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLD------TA----YDGQILIG---- 66
Cdd:COG4170 9 LTIEID-------TPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwhvTAdrfrWNGIDLLKlspr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 67 -GRRITepGMKQGFIFQEHR--LFPWLTV----EENIAAN-----FNLKQQDVRRKVDELIEIVRLKGFEH---AYPHEL 131
Cdd:COG4170 82 eRRKII--GREIAMIFQEPSscLDPSAKIgdqlIEAIPSWtfkgkWWQRFKWRKKRAIELLHRVGIKDHKDimnSYPHEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637173694 132 SGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-189 |
9.68e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 9.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 27 LSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRItEPG----------MKQGFifqehRLFPWLTVEENI 96
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGdiatrrrvgyMSQAF-----SLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 97 ---AANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVL 173
Cdd:NF033858 361 elhARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170
....*....|....*.
gi 637173694 174 LDIWQEKKTTMMLVTH 189
Cdd:NF033858 441 IELSREDGVTIFISTH 456
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-224 |
1.04e-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: 73.44 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 4 SIDIVDKSFWKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPgmKQGFIFQE 83
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVP--QQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 84 hrlfpwlTVEENIAANFNLKQQDVRRKVDE---LIEIVRLKGFEHAYPHE----LSGGMSQRVAIARALLRDPEILLLDE 156
Cdd:TIGR00957 714 -------SLRENILFGKALNEKYYQQVLEAcalLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637173694 157 PFGALDAFTRKHLQD-VLLDIWQEKKTTMMLVTHDIDesiYLGNEIVLMQARPGRIHKILPVNLPFPRD 224
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGIS---YLPQVDVIIVMSGGKISEMGSYQELLQRD 852
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-189 |
1.18e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.21 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 2 TISIDIVDKSFWKDKqtiRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR---RITEPGMKQG 78
Cdd:PRK10790 340 RIDIDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 79 F-IFQEHrlfPwLTVEENIAANFNLKQQDVRRKVDELIEIVRLKGFEHAYP-----------HELSGGMSQRVAIARALL 146
Cdd:PRK10790 417 VaMVQQD---P-VVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLV 492
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 147 RDPEILLLDEPFGALDAFTRKHLQDVLLDIwqEKKTTMMLVTH 189
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAH 533
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-184 |
1.43e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 72.74 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPwLTVEENI 96
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrnqvALVSQNVHLFN-DTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 97 AanFNLKQQDVRRKVDELIEIVRLKGFEHAYPH-----------ELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFT 165
Cdd:PRK11176 438 A--YARTEQYSREQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
170
....*....|....*....
gi 637173694 166 RKHLQDVlLDIWQEKKTTM 184
Cdd:PRK11176 516 ERAIQAA-LDELQKNRTSL 533
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-162 |
1.77e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.26 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGFIFQEH--RLFPWLTVEENIAA 98
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHlpGLKADLSTLENLHF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637173694 99 NFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:PRK13543 106 LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-162 |
2.40e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.25 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWLTVEENI 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAElarhrAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637173694 97 A--ANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLR-DPEI------LLLDEPFGALD 162
Cdd:COG4138 91 AlhQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvWPTInpegqlLLLDEPMNSLD 165
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-216 |
2.67e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.98 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 14 KDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ------GFIFQE-HR- 85
Cdd:COG3845 266 RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErrrlgvAYIPEDrLGr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 86 -LFPWLTVEENIAA----------NFNLKQQDVRRKVDELIEI--VRLKGfEHAYPHELSGGMSQRVAIARALLRDPEIL 152
Cdd:COG3845 346 gLVPDMSVAENLILgryrrppfsrGGFLDRKAIRAFAEELIEEfdVRTPG-PDTPARSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 153 LLDEPFGALD----AFTRKHLQDVlldiwQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRIHKILP 216
Cdd:COG3845 425 IAAQPTRGLDvgaiEFIHQRLLEL-----RDAGAAVLLISEDLDEILALSDRIAVMYE--GRIVGEVP 485
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-211 |
5.03e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR--------RITEPGMKQ------GFIFQEHR-- 85
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyALSEAERRRllrtewGFVHQHPRdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 86 LFPWLTVEENIAANF---------NLKQQDVR--RKVDelIEIVRLKGFehayPHELSGGMSQRVAIARALLRDPEILLL 154
Cdd:PRK11701 102 LRMQVSAGGNIGERLmavgarhygDIRATAGDwlERVE--IDAARIDDL----PTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 637173694 155 DEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLMQArpGRI 211
Cdd:PRK11701 176 DEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ--GRV 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-205 |
5.08e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 3 ISIDIVDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI--------TEPG 74
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 75 MkqGFIFQEHRLFPWLTVEENIAANFNLKQQ----------DVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARA 144
Cdd:PRK09700 82 I--GIIYQELSVIDELTVLENLYIGRHLTKKvcgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637173694 145 LLRDPEILLLDEPFGALdafTRKHLQDVLLDIWQEKK--TTMMLVTHDIDESIYLGNEIVLMQ 205
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMK 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-192 |
1.15e-13 |
|
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: 69.12 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGmkqgfifqehrlFPWL---TVEENIA 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQ------------FSWImpgTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 anFNLKQQDVRRKvdELIEIVRLKGFEHAYPHE-----------LSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTR 166
Cdd:cd03291 120 --FGVSYDEYRYK--SVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180
....*....|....*....|....*.
gi 637173694 167 KHLQDVLLDIWQEKKTTmMLVTHDID 192
Cdd:cd03291 196 KEIFESCVCKLMANKTR-ILVTSKME 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-191 |
2.14e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 29 IIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPgmkqgfifQEHRLFPWLTVEE---NIAANFNLKQQ 105
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKP--------QYIKPDYDGTVEDllrSITDDLGSSYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 106 DVrrkvdeliEIVRLKGFEHAYPH---ELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKT 182
Cdd:PRK13409 434 KS--------EIIKPLQLERLLDKnvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREA 505
|
....*....
gi 637173694 183 TMMLVTHDI 191
Cdd:PRK13409 506 TALVVDHDI 514
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-189 |
2.28e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 66.78 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGlDTAY---DGQILIGGRRITEPGM----KQG-FI-FQEHRLFPWL 90
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYevtEGEILFKGEDITDLPPeeraRLGiFLaFQYPPEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEeniaanfnlkqqDVRRKVDElieivrlkGFehayphelSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQ 170
Cdd:cd03217 93 KNA------------DFLRYVNE--------GF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170
....*....|....*....
gi 637173694 171 DVlLDIWQEKKTTMMLVTH 189
Cdd:cd03217 145 EV-INKLREEGKSVLIITH 162
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-193 |
2.38e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.05 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTA--YDGQILIGGRRITEPGMKQG------FIFQEHRLFPWL 90
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVCRFKDIRDSealgivIIHQELALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENI------AANFNLKQQDVRRKVDELIEIVRLKgfEHayPHELSG----GMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:NF040905 94 SIAENIflgnerAKRGVIDWNETNRRARELLAKVGLD--ES--PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190
....*....|....*....|....*....|...
gi 637173694 161 LDAFTRKHLQDVLLDIwQEKKTTMMLVTHDIDE 193
Cdd:NF040905 170 LNEEDSAALLDLLLEL-KAQGITSIIISHKLNE 201
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-175 |
2.42e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.99 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVL-EDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGgrritePGMKQGFIFQEH-RLFPWLTVEENIA 97
Cdd:PRK11819 337 RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG------ETVKLAYVDQSRdALDPNKTVWEEIS 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 -------------------ANFNLKQQDVRRKVDelieivrlkgfehayphELSGGMSQRVAIARALLRDPEILLLDEPF 158
Cdd:PRK11819 411 ggldiikvgnreipsrayvGRFNFKGGDQQKKVG-----------------VLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
170
....*....|....*..
gi 637173694 159 GALDAFTRKHLQDVLLD 175
Cdd:PRK11819 474 NDLDVETLRALEEALLE 490
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-189 |
3.07e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.01 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDtAY---DGQILIGGRRITE--P------GMkqGFIFQ---Ehr 85
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHP-KYevtSGSILLDGEDILElsPderaraGI--FLAFQypvE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 86 lFPWLTVEE--NIAAN----FNLKQQDVRRKVDELIEIVRLK----------GFehayphelSGGMSQRVAIARALLRDP 149
Cdd:COG0396 89 -IPGVSVSNflRTALNarrgEELSAREFLKLLKEKMKELGLDedfldryvneGF--------SGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637173694 150 EILLLDEPfgaldaftrkhlqDVLLDIW------------QEKKTTMMLVTH 189
Cdd:COG0396 160 KLAILDET-------------DSGLDIDalrivaegvnklRSPDRGILIITH 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-209 |
3.51e-13 |
|
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: 68.66 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 31 PGEFVTVIGPSGCGKSTLLKIISGldtaydgqILIG--GRRITEPGMKQgfIFQEHR---LFPWLT-------------- 91
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSG--------ELKPnlGDYDEEPSWDE--VLKRFRgteLQDYFKklangeikvahkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 92 -VEeNIAANFN------LKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:COG1245 168 yVD-LIPKVFKgtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 637173694 165 TR----KHLQDVLldiwqEKKTTMMLVTHDI---DesiYLGNEIVLMQARPG 209
Cdd:COG1245 247 QRlnvaRLIRELA-----EEGKYVLVVEHDLailD---YLADYVHILYGEPG 290
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-192 |
5.56e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 15 DKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGldtaydgqiliggrRITEPGMKQGFIFQEHRLFPWLTVEE 94
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------------ALKGTPVAGCVDVPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 NIAANFNlkqqdvrrkVDELIEIVRLKGFEHAY-----PHELSGGMSQRVAIARALLRDPEILLLDEpFGA-LDAFTRKH 168
Cdd:COG2401 105 AIGRKGD---------FKDAVELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDE-FCShLDRQTAKR 174
|
170 180
....*....|....*....|....
gi 637173694 169 LQDVLLDIWQEKKTTMMLVTHDID 192
Cdd:COG2401 175 VARNLQKLARRAGITLVVATHHYD 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-191 |
6.82e-13 |
|
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: 67.89 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPG-----EFVTVIGPSGCGKSTLLKIISGLDTAYDGQIliggrritEPGMKQGFIFQEHRLFPWLTVEENI 96
Cdd:COG1245 351 YGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLKISYKPQYISPDYDGTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 97 AANFNLKQQDVRRKVdELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDI 176
Cdd:COG1245 423 RSANTDDFGSSYYKT-EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170
....*....|....*
gi 637173694 177 WQEKKTTMMLVTHDI 191
Cdd:COG1245 502 AENRGKTAMVVDHDI 516
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-161 |
7.61e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ------GFIF 81
Cdd:PRK10762 10 IDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagiGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 82 QEHRLFPWLTVEENIaanF----------NLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEI 151
Cdd:PRK10762 86 QELNLIPQLTIAENI---FlgrefvnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170
....*....|
gi 637173694 152 LLLDEPFGAL 161
Cdd:PRK10762 163 IIMDEPTDAL 172
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-162 |
1.47e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFwkDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEP--GMKQGFIFQ 82
Cdd:PRK13540 2 LDVIELDF--DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDlcTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 EHR--LFPWLTVEENIAanFNLKQQDVRRKVDELIEIVRLkgfEHA--YP-HELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:PRK13540 80 GHRsgINPYLTLRENCL--YDIHFSPGAVGITELCRLFSL---EHLidYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
....*
gi 637173694 158 FGALD 162
Cdd:PRK13540 155 LVALD 159
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-209 |
1.71e-12 |
|
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: 64.13 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 32 GEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITepgmkqgfifqehrlfpwltveeniaanfnLKQQDVrrkv 111
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------YKPQYI---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 112 delieivrlkgfehayphELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDI 191
Cdd:cd03222 71 ------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDL 132
|
170
....*....|....*...
gi 637173694 192 DESIYLGNEIVLMQARPG 209
Cdd:cd03222 133 AVLDYLSDRIHVFEGEPG 150
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-209 |
1.72e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 31 PGEFVTVIGPSGCGKSTLLKIISGldtaydgqILIG--GRRITEPGMKQgfIFQEHR---LFPWLT-------------- 91
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSG--------ELIPnlGDYEEEPSWDE--VLKRFRgteLQNYFKklyngeikvvhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 92 -VEEnIAANFN------LKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:PRK13409 168 yVDL-IPKVFKgkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 637173694 165 TRKHLQDVLLDIWQEKktTMMLVTHDI---DesiYLGNEIVLMQARPG 209
Cdd:PRK13409 247 QRLNVARLIRELAEGK--YVLVVEHDLavlD---YLADNVHIAYGEPG 289
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-209 |
1.81e-12 |
|
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: 65.08 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 31 PGEFVTVIGPSGCGKSTLLKIISG-----------------LDTAYDGQIL-IGGRRITEPGMKQGFIFQEHRLFPwLTV 92
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeILDEFRGSELqNYFTKLLEGDVKVIVKPQYVDLIP-KAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIAANfnLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDV 172
Cdd:cd03236 104 KGKVGEL--LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARL 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 637173694 173 LLDIWQEKKtTMMLVTHDIDESIYLGNEIVLMQARPG 209
Cdd:cd03236 182 IRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
38-190 |
2.15e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 38 IGPSGCGKSTLLKIISGLDTAYDGQILIggrritEPGMKQG------FIFQEHRLFP---------WLTVEEN--IAANF 100
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSL------DPNERLGklrqdqFAFEEFTVLDtvimghtelWEVKQERdrIYALP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 101 NLKQQDVRRKVDELIEIVRLKGFE-HAYPHEL-----------SGGMSQ-------RVAIARALLRDPEILLLDEPFGAL 161
Cdd:PRK15064 107 EMSEEDGMKVADLEVKFAEMDGYTaEARAGELllgvgipeeqhYGLMSEvapgwklRVLLAQALFSNPDILLLDEPTNNL 186
|
170 180
....*....|....*....|....*....
gi 637173694 162 DAFTRKHLQDVLldiwQEKKTTMMLVTHD 190
Cdd:PRK15064 187 DINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-190 |
2.24e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISG---LDtayDGQILIGGRRITE------PGMKQGFIF----------- 81
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLD---DGRIIYEQDLIVArlqqdpPRNVEGTVYdfvaegieeqa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 82 ----QEHRLFPWLTVEENIAanfNLKQQDvrrKVDELIEIVRLKGFE--------------HAYPHELSGGMSQRVAIAR 143
Cdd:PRK11147 96 eylkRYHDISHLVETDPSEK---NLNELA---KLQEQLDHHNLWQLEnrinevlaqlgldpDAALSSLSGGWLRKAALGR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637173694 144 ALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIwqekKTTMMLVTHD 190
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF----QGSIIFISHD 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-163 |
3.68e-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: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 13 WKD--------KQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTA--YDGQILIGGRRITEPGMKQ-GFIF 81
Cdd:cd03232 6 WKNlnytvpvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNFQRStGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 82 QEHRLFPWLTVEEniAANFnlkqqdvrrkvdelieivrlkgfeHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGAL 161
Cdd:cd03232 86 QQDVHSPNLTVRE--ALRF------------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
..
gi 637173694 162 DA 163
Cdd:cd03232 140 DS 141
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-169 |
3.71e-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: 66.09 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGmkqgfifqehrlFPWL---TVEENIA 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ------------TSWImpgTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 anFNLKQQDVRRKvdELIEIVRLKGFEHAYPHE-----------LSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTR 166
Cdd:TIGR01271 509 --FGLSYDEYRYT--SVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
...
gi 637173694 167 KHL 169
Cdd:TIGR01271 585 KEI 587
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-192 |
5.41e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.35 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM-----KQGFIFQEHRLFpwltvEEN 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLhdlrfKITIIPQDPVLF-----SGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANFNLKQQDVRRKVDELIEIVRLKGFEHAYP----HE-------LSGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:TIGR00957 1376 LRMNLDPFSQYSDEEVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
170 180
....*....|....*....|....*...
gi 637173694 165 TRKHLQDVLLDiwQEKKTTMMLVTHDID 192
Cdd:TIGR00957 1456 TDNLIQSTIRT--QFEDCTVLTIAHRLN 1481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
27-206 |
5.91e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.99 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 27 LSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM---KQGF--IFQEHRLFPWLTVEENIAANFN 101
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPedyRKLFsaVFTDFHLFDQLLGPEGKPANPA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 102 LKQQDVRRKvdELIEIVRLKGFEHAYPhELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKK 181
Cdd:PRK10522 424 LVEKWLERL--KMAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMG 500
|
170 180
....*....|....*....|....*
gi 637173694 182 TTMMLVTHDiDESIYLGNEIVLMQA 206
Cdd:PRK10522 501 KTIFAISHD-DHYFIHADRLLEMRN 524
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-211 |
8.05e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 8.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT----EPGMKQGFIF-QEHR----LFPWLTV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspQDGLANGIVYiSEDRkrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIA---------ANFNLKQQDVRRKVDELIEIVRLKGFEHAYP-HELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:PRK10762 348 KENMSltalryfsrAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 637173694 163 AFTRKHLQDVlldIWQEKKTTM--MLVTHDIDESIYLGNEIVLMqaRPGRI 211
Cdd:PRK10762 428 VGAKKEIYQL---INQFKAEGLsiILVSSEMPEVLGMSDRILVM--HEGRI 473
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-206 |
4.11e-11 |
|
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: 60.50 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM-----KQGFIFQEHRLFPWlTVEE 94
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLedlrsSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 95 NIAAnFNlKQQDVrrkvdELIEIVRLKGfehaYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVll 174
Cdd:cd03369 101 NLDP-FD-EYSDE-----EIYGALRVSE----GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT-- 167
|
170 180 190
....*....|....*....|....*....|...
gi 637173694 175 dIWQE-KKTTMMLVTHDIdESIYLGNEIVLMQA 206
Cdd:cd03369 168 -IREEfTNSTILTIAHRL-RTIIDYDKILVMDA 198
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-204 |
4.17e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGldtAYDGQILIGGRRIT-------EPgMKQGFIFQEHRLFPWLTV 92
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGAPRGARVTgdvtlngEP-LAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIAANFNLKqqdvrrkvdeliEIVRLKGFEHA-----YPHE------------------------LSGGMSQRVAIAR 143
Cdd:PRK13547 91 AAQPAFAFSAR------------EIVLLGRYPHArragaLTHRdgeiawqalalagatalvgrdvttLSGGELARVQFAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 144 AL---------LRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAML 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-165 |
4.64e-11 |
|
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: 60.35 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 14 KDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAY---DGQILIGGrrITEPGMKQGF----IF--QEH 84
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFAEKYpgeiIYvsEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 85 RLFPWLTVEENIAANFNLKQQDVRRKVdelieivrlkgfehayphelSGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:cd03233 93 VHFPTLTVRETLDFALRCKGNEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
.
gi 637173694 165 T 165
Cdd:cd03233 153 T 153
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-207 |
6.15e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 16 KQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIG-GRRITEPGMKQ-----GFIFQEHRLFPw 89
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWwrskiGVVSQDPLLFS- 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEENI--------------------------------------AANFNLKQQDVRRkvDELIEI-------------- 117
Cdd:PTZ00265 474 NSIKNNIkyslyslkdlealsnyynedgndsqenknkrnscrakcAGDLNDMSNTTDS--NELIEMrknyqtikdsevvd 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 118 ----VRLKGFEHAYP-----------HELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKT 182
Cdd:PTZ00265 552 vskkVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250 260
....*....|....*....|....*
gi 637173694 183 TMMLVTHDIdESIYLGNEIVLMQAR 207
Cdd:PTZ00265 632 ITIIIAHRL-STIRYANTIFVLSNR 655
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-204 |
7.26e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.95 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR----RITEPGMKQGFIFQEHRLFPWLTVEENIA 97
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISDVHQNMGYCPQFDAIDDLLTGREHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 98 ANFNLK---QQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLL 174
Cdd:TIGR01257 2035 LYARLRgvpAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170 180 190
....*....|....*....|....*....|
gi 637173694 175 DIWQEKKtTMMLVTHDIDESIYLGNEIVLM 204
Cdd:TIGR01257 2115 SIIREGR-AVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-199 |
9.48e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 15 DKQTIRvleDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR-RITepgmkqgfIFQEHR--LFPWLT 91
Cdd:PRK11147 331 GKQLVK---DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVA--------YFDQHRaeLDPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 92 VEENIAANfnlkQQDV-----RRKV-----DELIEIVRLKGFEHAypheLSGGMSQRVAIARALLRDPEILLLDEPFGAL 161
Cdd:PRK11147 400 VMDNLAEG----KQEVmvngrPRHVlgylqDFLFHPKRAMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 637173694 162 DAFTRKHLQDvLLDIWQekkTTMMLVTHD---IDES-----IYLGN 199
Cdd:PRK11147 472 DVETLELLEE-LLDSYQ---GTVLLVSHDrqfVDNTvtecwIFEGN 513
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-191 |
1.52e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLD------TA----YDGQILI-----GGRRITepGMKQGFIFQE 83
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwrvTAdrmrFDDIDLLrlsprERRKLV--GHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 84 HR--LFPWLTVEENIAAN-------------FNLKqqdvRRKVDELIEIVRLKGFE---HAYPHELSGGMSQRVAIARAL 145
Cdd:PRK15093 98 PQscLDPSERVGRQLMQNipgwtykgrwwqrFGWR----KRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIAL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 637173694 146 LRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDI 191
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDL 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-156 |
1.90e-10 |
|
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: 60.58 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 27 LSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM---KQGF--IFQEHRLFPWLtveeniaanFN 101
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNReayRQLFsaVFSDFHLFDRL---------LG 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637173694 102 LKQQDVRRKVDELIEivRLKgFEHAYPHE--------LSGGMSQRVAIARALLRDPEILLLDE 156
Cdd:COG4615 424 LDGEADPARARELLE--RLE-LDHKVSVEdgrfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-216 |
2.45e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT--EPG--MKQGFIF-QEHR----LFPWL 90
Cdd:PRK11288 267 GLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRdaIRAGIMLcPEDRkaegIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 91 TVEENIA---------ANFNLKQQDVRRKVDELIEIVRLKGFEHAYP-HELSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:PRK11288 347 SVADNINisarrhhlrAGCLINNRWEAENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637173694 161 LDAFTRKHLQDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLMqaRPGRIHKILP 216
Cdd:PRK11288 427 IDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVM--REGRIAGELA 479
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-189 |
2.67e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGlD--TAYDGQILIGGRR------ITEPGMKQGF----IFQEHRLF 87
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DhpQGYSNDLTLFGRRrgsgetIWDIKKHIGYvsssLHLDYRVS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 88 pwLTVEENIAANF----NLKQQ---DVRRKVDELIEIVRLKGFEHAYP-HELSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:PRK10938 353 --TSVRNVILSGFfdsiGIYQAvsdRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQ 430
|
170 180 190
....*....|....*....|....*....|...
gi 637173694 160 ALDAFTRKHLQ---DVLLdiwQEKKTTMMLVTH 189
Cdd:PRK10938 431 GLDPLNRQLVRrfvDVLI---SEGETQLLFVSH 460
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-215 |
2.68e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 24 DLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRIT--------EPGMkqGFIFQEHR---LFPWLTV 92
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavKKGM--AYITESRRdngFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENIAANFNLK------------QQDVRRKVDELIEIVRLKGfeHAYPH---ELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:PRK09700 359 AQNMAISRSLKdggykgamglfhEVDEQRTAENQRELLALKC--HSVNQnitELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 158 FGALDAFTRKHLQDVLLDIWQEKKTTMMlVTHDIDESIYLGNEIVLMqaRPGRIHKIL 215
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGKVILM-VSSELPEIITVCDRIAVF--CEGRLTQIL 491
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-195 |
4.11e-10 |
|
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: 56.61 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 31 PGEFVTVIGPSGCGKSTLLKIISG-LDTAYDGQILIGGRRITEPGMKQgfifqehrlfpwltveeniaanfnlkqqdvrr 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQ-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 110 kvdelieivRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQD-----VLLDIWQEKKTTM 184
Cdd:smart00382 49 ---------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLLLLKSEKNLTV 119
|
170
....*....|.
gi 637173694 185 MLVTHDIDESI 195
Cdd:smart00382 120 ILTTNDEKDLG 130
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-163 |
4.45e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 4 SIDIVDKSF-WKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISG-LDTAYDGQILIGGRRITEPGMkqgfif 81
Cdd:PLN03232 614 AISIKNGYFsWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVAYVPQV------ 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 82 qehrlfPWL---TVEENIAANFNLKQQDVRRKVD--------------ELIEIVRlKGFEhaypheLSGGMSQRVAIARA 144
Cdd:PLN03232 688 ------SWIfnaTVRENILFGSDFESERYWRAIDvtalqhdldllpgrDLTEIGE-RGVN------ISGGQKQRVSMARA 754
|
170
....*....|....*....
gi 637173694 145 LLRDPEILLLDEPFGALDA 163
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDA 773
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
5-193 |
7.38e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.75 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 5 IDIVDKSFWKDKQTI--RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGrritepgmKQGFIFQ 82
Cdd:PRK13545 21 FDKLKDLFFRSKDGEyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------SAALIAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 83 EHRLFPWLTVEENIAAN---FNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFG 159
Cdd:PRK13545 93 SSGLNGQLTGIENIELKglmMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190
....*....|....*....|....*....|....*
gi 637173694 160 ALD-AFTRKHLQDvlLDIWQEKKTTMMLVTHDIDE 193
Cdd:PRK13545 173 VGDqTFTKKCLDK--MNEFKEQGKTIFFISHSLSQ 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-192 |
9.92e-10 |
|
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: 58.77 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdTAYDGQILIGG---RRITEPGMKQGFIFQEHRLFPWL-TVEENI 96
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGvswNSVTLQTWRKAFGVIPQKVFIFSgTFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 97 AANFNLKQQDVRRKVDElieiVRLKGFEHAYPHE-----------LSGGMSQRVAIARALLRDPEILLLDEPFGALDAFT 165
Cdd:TIGR01271 1313 DPYEQWSDEEIWKVAEE----VGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
170 180 190
....*....|....*....|....*....|.
gi 637173694 166 ----RKHLQDVLLDiwqekkTTMMLVTHDID 192
Cdd:TIGR01271 1389 lqiiRKTLKQSFSN------CTVILSEHRVE 1413
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
20-173 |
1.17e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.42 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 20 RVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITE-PGMKQGFIFQEHRLFPWLTVEENIAa 98
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGLKLEMTVFENLK- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637173694 99 nFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVL 173
Cdd:PRK13541 93 -FWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
65-204 |
1.46e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.44 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 65 IGGRRITEPGMKQGFIFQEHRLFpwltveenIAANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARA 144
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYM--------IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 145 LLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEkKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVI 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-204 |
1.83e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 24 DLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPG----MKQGFIF-----QEHRLF-----PW 89
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrLARGLVYlpedrQSSGLYldaplAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 ----LTVEENiaaNFNLKQQDVRRKVDELIEIVRLKgFEHAYP--HELSGGMSQRVAIARALLRDPEILLLDEPFGALDA 163
Cdd:PRK15439 361 nvcaLTHNRR---GFWIKPARENAVLERYRRALNIK-FNHAEQaaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 637173694 164 FTRKHLQDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLM 204
Cdd:PRK15439 437 SARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-178 |
2.06e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 12 FWKD--------KQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISG-LDTAY--DGQILIGGRRITEPGMKQ-GF 79
Cdd:TIGR00956 761 HWRNltyevkikKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErVTTGVitGGDRLVNGRPLDSSFQRSiGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 80 IFQEHRLFPWLTVEENIAANFNLKQ-QDVRRK-----VDELIEIVRLKGFEHAYPHELSGGMS----QRVAIARALLRDP 149
Cdd:TIGR00956 841 VQQQDLHLPTSTVRESLRFSAYLRQpKSVSKSekmeyVEEVIKLLEMESYADAVVGVPGEGLNveqrKRLTIGVELVAKP 920
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 637173694 150 EILL-LDEPFGALDA--------FTRK---HLQDVLLDIWQ 178
Cdd:TIGR00956 921 KLLLfLDEPTSGLDSqtawsickLMRKladHGQAILCTIHQ 961
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-188 |
3.94e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 4 SIDIVDKSF-WKDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISG-LDTAYDGQILIGGRRITEPGMKqgFIF 81
Cdd:PLN03130 614 AISIKNGYFsWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVAYVPQVS--WIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 82 QEhrlfpwlTVEENI--AANFNLKQQDVRRKVDELI-EIVRLKGFEHAYPHE----LSGGMSQRVAIARALLRDPEILLL 154
Cdd:PLN03130 692 NA-------TVRDNIlfGSPFDPERYERAIDVTALQhDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190
....*....|....*....|....*....|....
gi 637173694 155 DEPFGALDAFTRKHLQDVLLDiWQEKKTTMMLVT 188
Cdd:PLN03130 765 DDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVT 797
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-190 |
5.44e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGgrritePGMKQGFiFQEHRLfpwltveENIAANF 100
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------KGIKLGY-FAQHQL-------EFLRADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 101 NLKQQDVRRKVDELIEIVR--LKGFEHA------YPHELSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDV 172
Cdd:PRK10636 393 SPLQHLARLAPQELEQKLRdyLGGFGFQgdkvteETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
170
....*....|....*...
gi 637173694 173 LLDIwqekKTTMMLVTHD 190
Cdd:PRK10636 473 LIDF----EGALVVVSHD 486
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-189 |
6.32e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 18 TIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGlDTAYD---GQILIGGRRIT--EPGM--KQG-FI-FQEHRLFP 88
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAYKileGDILFKGESILdlEPEEraHLGiFLaFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WLTVEE--NIAANFNLKQQDVRRK--------VDELIEIVRLKG-FEHAYPHE-LSGGMSQRVAIARALLRDPEILLLDE 156
Cdd:CHL00131 98 GVSNADflRLAYNSKRKFQGLPELdplefleiINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190
....*....|....*....|....*....|...
gi 637173694 157 PFGALDAFTRKHLQDVlLDIWQEKKTTMMLVTH 189
Cdd:CHL00131 178 TDSGLDIDALKIIAEG-INKLMTSENSIILITH 209
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-193 |
9.09e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 27 LSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQgfifQEHRlfpwltVEENIAANFN----L 102
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQ----LQKL------VSDEWQRNNTdmlsP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 103 KQQDVRRKVDELI-----------EIVRLKGFEHAYPHE---LSGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKH 168
Cdd:PRK10938 94 GEDDTGRTTAEIIqdevkdparceQLAQQFGITALLDRRfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180
....*....|....*....|....*
gi 637173694 169 LQDVLLDIWQeKKTTMMLVTHDIDE 193
Cdd:PRK10938 174 LAELLASLHQ-SGITLVLVLNRFDE 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-243 |
9.28e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 14 KDKQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGldTAYDGQILIGGrRITEPGMKQGFIFQEHRL------- 86
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEG-VITYDGITPEEIKKHYRGdvvynae 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 87 ----FPWLTVEENI--AANF--------NLKQQDVRRKVDELieIVRLKGFEHAYPHE--------LSGGMSQRVAIARA 144
Cdd:TIGR00956 146 tdvhFPHLTVGETLdfAARCktpqnrpdGVSREEYAKHIADV--YMATYGLSHTRNTKvgndfvrgVSGGERKRVSIAEA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 145 LLRDPEILLLDEPFGALDAFTRKHLQDVLLDIWQEKKTTMMLVTHDIDESIY-LGNEIVLMQArpGRIhkilpvnlpfpr 223
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYE--GYQ------------ 289
|
250 260
....*....|....*....|
gi 637173694 224 drtstAFQSLRQKVLSEFEK 243
Cdd:TIGR00956 290 -----IYFGPADKAKQYFEK 304
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-191 |
1.00e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLkiisgldtaydgQILIGGRRITEpgmkqGFIFQEHRLF-----PWL---TV 92
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLL------------QSLLSQFEISE-----GRVWAERSIAyvpqqAWImnaTV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EENI-------AANFnlkqQDVRRkVDELIEIVRL--KGFEHAYPHE---LSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:PTZ00243 738 RGNIlffdeedAARL----ADAVR-VSQLEADLAQlgGGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190
....*....|....*....|....*....|..
gi 637173694 161 LDAFTRKHL-QDVLLDIWQEKktTMMLVTHDI 191
Cdd:PTZ00243 813 LDAHVGERVvEECFLGALAGK--TRVLATHQV 842
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-173 |
1.01e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.48 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLdTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWlTVEEN 95
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKwrkafGVIPQKVFIFSG-TFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANFNLKQQDVRRKVDElieiVRLKGFEHAYPHEL-----------SGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:cd03289 97 LDPYGKWSDEEIWKVAEE----VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
....*....
gi 637173694 165 TRKHLQDVL 173
Cdd:cd03289 173 TYQVIRKTL 181
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-189 |
1.58e-08 |
|
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: 54.75 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYdgqiliGGRRITEPGMKQGFIFQEhrlfPWLTV----EENI 96
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVY------GGRLTKPAKGKLFYVPQR----PYMTLgtlrDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 97 AAN--FNLKQQDVRRKvdELIEIVRLKGFEHAYPHE------------LSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:TIGR00954 537 YPDssEDMKRRGLSDK--DLEQILDNVQLTHILEREggwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|....*..
gi 637173694 163 AftrkHLQDVLLDIWQEKKTTMMLVTH 189
Cdd:TIGR00954 615 V----DVEGYMYRLCREFGITLFSVSH 637
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-219 |
2.72e-08 |
|
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: 53.37 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGM-----KQGFIFQEHRLFpwltvEEN 95
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLhtlrsRLSIILQDPILF-----SGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 IAANFNLKQQDVRRKVDELIEIVRLKGFEHAYPHEL-----------SGGMSQRVAIARALLRDPEILLLDEPFGALDAF 164
Cdd:cd03288 111 IRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 637173694 165 TRKHLQDVLLDIWQEKktTMMLVTHDIdeSIYLGNEIVLMQARPGRIHKILPVNL 219
Cdd:cd03288 191 TENILQKVVMTAFADR--TVVTIAHRV--STILDADLVLVLSRGILVECDTPENL 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-208 |
6.15e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQgfIFQEHRLFPWLTVEENIAANF 100
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD--LRRVLSIIPQSPVLFSGTVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 101 NLKQQDVRRKVD--ELIEIVRLKGFEHAYPHEL-----------SGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRK 167
Cdd:PLN03232 1329 NIDPFSEHNDADlwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 637173694 168 HLQDVLLDiwQEKKTTMMLVTH------DIDESIYLGNEIVLMQARP 208
Cdd:PLN03232 1409 LIQRTIRE--EFKSCTMLVIAHrlntiiDCDKILVLSSGQVLEYDSP 1453
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-195 |
8.10e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLFPWlTVEen 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrkvlGIIPQAPVLFSG-TVR-- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 96 iaanFNLKQQDVRRKVD--ELIEIVRLKGFEHAYPHEL-----------SGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:PLN03130 1331 ----FNLDPFNEHNDADlwESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190
....*....|....*....|....*....|....*.
gi 637173694 163 AFTrkhlqDVLLD--IWQEKKT-TMMLVTHDIDESI 195
Cdd:PLN03130 1407 VRT-----DALIQktIREEFKScTMLIIAHRLNTII 1437
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-163 |
1.04e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTA--YDGQILIGG--------RRITepgmkqGFIFQEHRLFP 88
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGfpkkqetfARIS------GYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WLTVEENIAANFNLK------QQDVRRKVDELIEIVRLKGFEHA---YP--HELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:PLN03140 967 QVTVRESLIYSAFLRlpkevsKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*.
gi 637173694 158 FGALDA 163
Cdd:PLN03140 1047 TSGLDA 1052
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-157 |
1.62e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL-DTAYDGQILIGGRRIT----EPGMKQGFIF-----QEHRLFP 88
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKirnpQQAIAQGIAMvpedrKRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WLTVEENIAANfNLKQQDVRRKVDELIE-------IVRLKgFEHAYPH----ELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:PRK13549 355 VMGVGKNITLA-ALDRFTGGSRIDDAAElktilesIQRLK-VKTASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-191 |
1.75e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 17 QTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGrRITEPGMKQGFIFQehrlfpwLTVEENI 96
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAGLSGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 97 AAN---FNLKQQDVRRKVDELIEIVRLKGFEHAYPHELSGGMSQRVAIARALLRDPEILLLDEPFGALD-AFTRKHLQDV 172
Cdd:PRK13546 107 EFKmlcMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDqTFAQKCLDKI 186
|
170
....*....|....*....
gi 637173694 173 LLdiWQEKKTTMMLVTHDI 191
Cdd:PRK13546 187 YE--FKEQNKTIFFVSHNL 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-162 |
4.74e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.21 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGL-DTAYDGQILIGGRRIT----EPGMKQGFIF-----QEHRLFP 88
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDirnpAQAIRAGIAMvpedrKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WLTVEENIAANfNLKQQDVRRKVDELIE-------IVRLKgFEHAYPH----ELSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:TIGR02633 353 ILGVGKNITLS-VLKSFCFKMRIDAAAElqiigsaIQRLK-VKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
....*
gi 637173694 158 FGALD 162
Cdd:TIGR02633 431 TRGVD 435
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-186 |
1.92e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRI----TEPGMKQGF--IFQEHR---LFPWLTV 92
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhnANEAINHGFalVTEERRstgIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 EEN-IAANFN--------LKQQDVRRKVDELIEIVRLKGFEHAYP-HELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:PRK10982 344 GFNsLISNIRnyknkvglLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180
....*....|....*....|....
gi 637173694 163 AFTRKHLQDVLLDIWQEKKTTMML 186
Cdd:PRK10982 424 VGAKFEIYQLIAELAKKDKGIIII 447
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-162 |
3.16e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 35 VTVIGPSGCGKSTLLKIISGLDTAYDGQILiggrriTEPGMKQGFIFQEH---------------RLFPWLTvEENIAAN 99
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVF------RSAKVRMAVFSQHHvdgldlssnpllymmRCFPGVP-EQKLRAH 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 100 F-------NLKQQDVrrkvdelieivrlkgfehaypHELSGGMSQRVAIARALLRDPEILLLDEPFGALD 162
Cdd:PLN03073 611 LgsfgvtgNLALQPM---------------------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-205 |
3.74e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 8 VDKSFwkdkQTIRVLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQGF------IF 81
Cdd:PRK10982 4 ISKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALengismVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 82 QEHRLFPWLTVEENI-AANFNLK---------QQDVRRKVDEL-IEI-VRLKGfehaypHELSGGMSQRVAIARALLRDP 149
Cdd:PRK10982 80 QELNLVLQRSVMDNMwLGRYPTKgmfvdqdkmYRDTKAIFDELdIDIdPRAKV------ATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 637173694 150 EILLLDEPFGALDAFTRKHLQDVLLDIwQEKKTTMMLVTHDIDESIYLGNEIVLMQ 205
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILR 208
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-192 |
3.80e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 19 IRVLEDLRLSII-PGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGR------RITEPGMKQG---FIFQEHRLFP 88
Cdd:PRK10636 13 VRVLLDNATATInPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvNQETPALPQPaleYVIDGDREYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 89 WLTVEENIAANFN--------------LKQQDVRRKVDELIEIVRLKGFEHAYP-HELSGGMSQRVAIARALLRDPEILL 153
Cdd:PRK10636 93 QLEAQLHDANERNdghaiatihgkldaIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 637173694 154 LDEPFGALDaftrkhlqdvlLD--IWQEK-----KTTMMLVTHDID 192
Cdd:PRK10636 173 LDEPTNHLD-----------LDavIWLEKwlksyQGTLILISHDRD 207
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
90-192 |
5.39e-05 |
|
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: 44.23 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEEniAANFNLKQQDVRRKVDELIEI----VRLKgfEHAYphELSGGMSQRVAIARALLRD---PEILLLDEPFGALd 162
Cdd:TIGR00630 791 MTVEE--AYEFFEAVPSISRKLQTLCDVglgyIRLG--QPAT--TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL- 863
|
90 100 110
....*....|....*....|....*....|....*
gi 637173694 163 aftrkHLQDV--LLDIWQ---EKKTTMMLVTHDID 192
Cdd:TIGR00630 864 -----HFDDIkkLLEVLQrlvDKGNTVVVIEHNLD 893
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
132-189 |
9.22e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 9.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 637173694 132 SGGMSQRVAIARALLRDPEILLLDEPFGALDAFTRKHLQDVLLDiWQEkktTMMLVTH 189
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WPK---TFIVVSH 399
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-190 |
1.08e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQIliggrRITEpGMKQGFIFQEH--------RLFPWLTV 92
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSE-NANIGYYAQDHaydfendlTLFDWMSQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 93 -------EENIAAN-----FNlkQQDVRRKVdelieivrlkgfehaypHELSGGMSQRVAIARALLRDPEILLLDEPFGA 160
Cdd:PRK15064 408 wrqegddEQAVRGTlgrllFS--QDDIKKSV-----------------KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468
|
170 180 190
....*....|....*....|....*....|.
gi 637173694 161 LDAFTRKHLQDVLldiwqEK-KTTMMLVTHD 190
Cdd:PRK15064 469 MDMESIESLNMAL-----EKyEGTLIFVSHD 494
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-210 |
2.13e-04 |
|
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: 40.77 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 22 LEDLRLSIIPGEFVTVIGPSGCGKSTLLK----------IISGLDTAYDGQILIGG--RRITEPGMKqgfifqehrlfpW 89
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNeglyasgkarLISFLPKFSRNKLIFIDqlQFLIDVGLG------------Y 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEENIAAnfnlkqqdvrrkvdelieivrlkgfehaypheLSGGMSQRVAIARALLRDPE--ILLLDEPFGALDAFTRK 167
Cdd:cd03238 79 LTLGQKLST--------------------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 637173694 168 HLQDVLLDIWQEkKTTMMLVTHDiDESIYLGNEIVLMQARPGR 210
Cdd:cd03238 127 QLLEVIKGLIDL-GNTVILIEHN-LDVLSSADWIIDFGPGSGK 167
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-190 |
5.02e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.65 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 31 PGEFVTVIGPSGCGKSTLLKIIsgldtaydgqILIGGRRitepgmkqgfifqehrlFPWLTVEENIAANFNLKQQDVrrk 110
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI----------GLALGGA-----------------QSATRRRSGVKAGCIVAAVSA--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 111 vdELIEIVrlkgfehaypHELSGGMSQRVAIA-----RALLRDPeILLLDEPFGALDAFTRKHLQDVLLDIWQeKKTTMM 185
Cdd:cd03227 70 --ELIFTR----------LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVI 135
|
....*
gi 637173694 186 LVTHD 190
Cdd:cd03227 136 VITHL 140
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-170 |
8.86e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 21 VLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISGLDTAYDGQILIGGRRITEPGMKQ-----GFIFQEHRLF-------- 87
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrrqfSMIPQDPVLFdgtvrqnv 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 88 -PWL--TVEENIAAnfnLKQQDVRRKV---DELIEIVRLKGFEHaypheLSGGMSQRVAIARALL-RDPEILLLDEPFGA 160
Cdd:PTZ00243 1405 dPFLeaSSAEVWAA---LELVGLRERVaseSEGIDSRVLEGGSN-----YSVGQRQLMCMARALLkKGSGFILMDEATAN 1476
|
170
....*....|
gi 637173694 161 LDAFTRKHLQ 170
Cdd:PTZ00243 1477 IDPALDRQIQ 1486
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
90-192 |
1.15e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.52 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 90 LTVEEniAANFNLKQQDVRRKVDELIEiVRLKGFEHAYP-HELSGGMSQRVAIARALLR---DPEILLLDEPFGALdaft 165
Cdd:cd03271 131 MTVEE--ALEFFENIPKIARKLQTLCD-VGLGYIKLGQPaTTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGL---- 203
|
90 100 110
....*....|....*....|....*....|..
gi 637173694 166 rkHLQDV--LLDIWQ---EKKTTMMLVTHDID 192
Cdd:cd03271 204 --HFHDVkkLLEVLQrlvDKGNTVVVIEHNLD 233
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
94-191 |
1.29e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 94 ENIAANFNLKQQDVRRKVDELIEIVRLK--------GFEHayPHELSGGMSQRVAIARALLrdpeiLLLDepFGALDAFT 165
Cdd:COG0419 116 EELKERLKELEEALESALEELAELQKLKqeilaqlsGLDP--IETLSGGERLRLALADLLS-----LILD--FGSLDEER 186
|
90 100
....*....|....*....|....*.
gi 637173694 166 RKHLQDVLLDIwqekkttmMLVTHDI 191
Cdd:COG0419 187 LERLLDALEEL--------AIITHVI 204
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-119 |
6.28e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637173694 14 KDKQTIrvLEDLRLSIIPGEFVTVIGPSGCGKSTLLKIISG-LDTAYD--GQILIGGRRITE--PGMKQGFIFQEHRLFP 88
Cdd:PLN03140 175 KTKLTI--LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDPSLKvsGEITYNGYRLNEfvPRKTSAYISQNDVHVG 252
|
90 100 110
....*....|....*....|....*....|.
gi 637173694 89 WLTVEENIaaNFNLKQQDVRRKVDELIEIVR 119
Cdd:PLN03140 253 VMTVKETL--DFSARCQGVGTRYDLLSELAR 281
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
131-157 |
7.25e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.46 E-value: 7.25e-03
10 20
....*....|....*....|....*..
gi 637173694 131 LSGGMSQRVAIARALLRDPEILLLDEP 157
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| |
