|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
12-243 |
1.80e-29 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 112.85 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 12 PTVGLIGLGRIGMVLLAAL-RRFAPETRVIAAGRDPARVAAATAAWpGVEVMDSERLAV-HANVVVPCLPPEAYRDGVSA 89
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLlKSGVPPEDIIVSDRSPERLEALAERY-GVRVTTDNAEAAaQADVVVLAVKPQDLAEVLEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 90 VAPHMRADAVLMSVTNAVPLPDLGCRC--ARPIVKVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLADP 167
Cdd:COG0345 82 LAPLLDPDKLVISIAAGVTLATLEEALggGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501740221 168 ADGRIASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTESVAALAAILDE-GLSFEDVVARTATPGGTTE 243
Cdd:COG0345 162 ELMDAVTALSGSGPAYVFLFIEAM--ADAGVALGLPRETARELAAQTVLGAAKLLLEsGEHPAELRDRVTSPGGTTI 236
|
|
| PRK07680 |
PRK07680 |
late competence protein ComER; Validated |
14-242 |
1.83e-17 |
|
late competence protein ComER; Validated
Pssm-ID: 181080 [Multi-domain] Cd Length: 273 Bit Score: 80.40 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 14 VGLIGLGRIGMVLLAAL--RRFAPETRVIAAGRDPARVAAATAAWPGVEVMDS-ERLAVHANVVVPCLPPEAYRDGVSAV 90
Cdd:PRK07680 3 IGFIGTGNMGTILIEAFleSGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTiEEVISQSDLIFICVKPLDIYPLLQKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 91 APHMRADAVLMSVTNAVPLPDL----GCRCARpivkVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLAD 166
Cdd:PRK07680 83 APHLTDEHCLVSITSPISVEQLetlvPCQVAR----IIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501740221 167 PADGRIASNLAGSAPAILAAFCSAFLEAnAARARAFGPTELRAMMTESVAALAAILDEGL-SFEDVVARTATPGGTT 242
Cdd:PRK07680 159 EDITRVSSDIVSCGPAFFSYLLQRFIDA-AVEETNISKEEATTLASEMLIGMGKLLEKGLyTLPTLQEKVCVKGGIT 234
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
58-243 |
6.53e-08 |
|
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 272911 [Multi-domain] Cd Length: 245 Bit Score: 52.65 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 58 GVEVM-DSERLAVHANVVVPCLPPEAYRDGVSAVAPHMRADAVLMSVTNAVPLPDLGCR--CARPIVKVILSPAHAAGRG 134
Cdd:TIGR00112 30 GIVASsDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLlgGTRRVVRVMPNTPAKVGAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 135 VCLVTPSPGAGPEQVERICALLQRFCRPVLADPADGRIASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTES 214
Cdd:TIGR00112 110 VTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEAL--ADAGVKQGLPRELALELAAQT 187
|
170 180 190
....*....|....*....|....*....|
gi 501740221 215 VAALAAILDE-GLSFEDVVARTATPGGTTE 243
Cdd:TIGR00112 188 VKGAAKLLEEsGEHPALLKDQVTSPGGTTI 217
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
172-243 |
3.56e-05 |
|
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.
Pssm-ID: 464294 [Multi-domain] Cd Length: 104 Bit Score: 42.00 E-value: 3.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501740221 172 IASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTESVAALAA-ILDEGLSFEDVVARTATPGGTTE 243
Cdd:pfam14748 6 AVTALSGSGPAYVFLFIEAL--ADAGVAMGLPREEARELAAQTVLGAAKlLLTSGEHPAELRDKVTSPGGTTI 76
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
12-243 |
1.80e-29 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 112.85 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 12 PTVGLIGLGRIGMVLLAAL-RRFAPETRVIAAGRDPARVAAATAAWpGVEVMDSERLAV-HANVVVPCLPPEAYRDGVSA 89
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLlKSGVPPEDIIVSDRSPERLEALAERY-GVRVTTDNAEAAaQADVVVLAVKPQDLAEVLEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 90 VAPHMRADAVLMSVTNAVPLPDLGCRC--ARPIVKVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLADP 167
Cdd:COG0345 82 LAPLLDPDKLVISIAAGVTLATLEEALggGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501740221 168 ADGRIASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTESVAALAAILDE-GLSFEDVVARTATPGGTTE 243
Cdd:COG0345 162 ELMDAVTALSGSGPAYVFLFIEAM--ADAGVALGLPRETARELAAQTVLGAAKLLLEsGEHPAELRDRVTSPGGTTI 236
|
|
| PRK07680 |
PRK07680 |
late competence protein ComER; Validated |
14-242 |
1.83e-17 |
|
late competence protein ComER; Validated
Pssm-ID: 181080 [Multi-domain] Cd Length: 273 Bit Score: 80.40 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 14 VGLIGLGRIGMVLLAAL--RRFAPETRVIAAGRDPARVAAATAAWPGVEVMDS-ERLAVHANVVVPCLPPEAYRDGVSAV 90
Cdd:PRK07680 3 IGFIGTGNMGTILIEAFleSGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTiEEVISQSDLIFICVKPLDIYPLLQKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 91 APHMRADAVLMSVTNAVPLPDL----GCRCARpivkVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLAD 166
Cdd:PRK07680 83 APHLTDEHCLVSITSPISVEQLetlvPCQVAR----IIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501740221 167 PADGRIASNLAGSAPAILAAFCSAFLEAnAARARAFGPTELRAMMTESVAALAAILDEGL-SFEDVVARTATPGGTT 242
Cdd:PRK07680 159 EDITRVSSDIVSCGPAFFSYLLQRFIDA-AVEETNISKEEATTLASEMLIGMGKLLEKGLyTLPTLQEKVCVKGGIT 234
|
|
| PRK06928 |
PRK06928 |
pyrroline-5-carboxylate reductase; Reviewed |
13-280 |
6.86e-17 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235888 [Multi-domain] Cd Length: 277 Bit Score: 79.04 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 13 TVGLIGLGRIGMVLLAAL---RRFAPETRVIAAGRDPARVAAATAAWPGVEVMDSE-RLAVHANVVVPCLPPEAYRDGVS 88
Cdd:PRK06928 3 KIGFIGYGSMADMIATKLletEVATPEEIILYSSSKNEHFNQLYDKYPTVELADNEaEIFTKCDHSFICVPPLAVLPLLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 89 AVAPHMRADAVLMSVTNAVPLPDL-GCRCARPIVKVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLADP 167
Cdd:PRK06928 83 DCAPVLTPDRHVVSIAAGVSLDDLlEITPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSHVMTIRE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 168 ADGRIASNLAGSAPAILAAFCSAFLEAnAARARAFGPTELRAMMTESVAALAAIL-DEGLSFEDVVARTATPGGTTEAAI 246
Cdd:PRK06928 163 ENMDIASNLTSSSPGFIAAIFEEFAEA-AVRNSSLSDEEAFQFLNFALAGTGKLLvEEDYTFSGTIERVATKGGITAEGA 241
|
250 260 270
....*....|....*....|....*....|....*
gi 501740221 247 AALNAEAPALCGRLVDATFQREAQLL-AIPPRTRD 280
Cdd:PRK06928 242 EVIQAQLPQFFDELLDRTQKKYASSKkEIQAQKRD 276
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
13-243 |
1.89e-09 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 57.08 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 13 TVGLIGLGRIGMVLLAAL-RRFAPETRVIAAGRDPARVAAATAAWpGVEVM-DSERLAVHANVVVPCLPPEAYRDGVSAV 90
Cdd:PRK11880 4 KIGFIGGGNMASAIIGGLlASGVPAKDIIVSDPSPEKRAALAEEY-GVRAAtDNQEAAQEADVVVLAVKPQVMEEVLSEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 91 APHmrADAVLMSVTNAVPLPDLGCRC--ARPIVKVIlsPAHAA--GRGVCLVTPSPGAGPEQVERICALLQRFCRPV-LA 165
Cdd:PRK11880 83 KGQ--LDKLVVSIAAGVTLARLERLLgaDLPVVRAM--PNTPAlvGAGMTALTANALVSAEDRELVENLLSAFGKVVwVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 166 DPADGRIASNLAGSAPAilaaFCSAFLEANAARARAFG-PTEL-RAMMTESVAALAAILDE-GLSFEDVVARTATPGGTT 242
Cdd:PRK11880 159 DEKQMDAVTAVSGSGPA----YVFLFIEALADAGVKLGlPREQaRKLAAQTVLGAAKLLLEsGEHPAELRDNVTSPGGTT 234
|
.
gi 501740221 243 E 243
Cdd:PRK11880 235 I 235
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
13-169 |
7.08e-09 |
|
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 55.52 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 13 TVGLIGLGRIGMVLLAALRRFAPETRVIAAGRDPARVAAATAAwpGV--EVMDSERLAVH-ANVVVPCLPPEAYRDGVSA 89
Cdd:COG0287 3 RIAIIGLGLIGGSLALALKRAGLAHEVVGVDRSPETLERALEL--GVidRAATDLEEAVAdADLVVLAVPVGATIEVLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 90 VAPHMRADAVLM---SVTNAVplpdlgCRCARPIVKVILS--PAH-AAGR---GV------------CLVTPSPGAGPEQ 148
Cdd:COG0287 81 LAPHLKPGAIVTdvgSVKGAV------VEAAEALLPDGVRfvGGHpMAGTeksGPeaadadlfegapYILTPTEGTDPEA 154
|
170 180
....*....|....*....|..
gi 501740221 149 VERICALLQRF-CRPVLADPAD 169
Cdd:COG0287 155 LERVEELWEALgARVVEMDPEE 176
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
58-243 |
6.53e-08 |
|
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 272911 [Multi-domain] Cd Length: 245 Bit Score: 52.65 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 58 GVEVM-DSERLAVHANVVVPCLPPEAYRDGVSAVAPHMRADAVLMSVTNAVPLPDLGCR--CARPIVKVILSPAHAAGRG 134
Cdd:TIGR00112 30 GIVASsDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLlgGTRRVVRVMPNTPAKVGAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 135 VCLVTPSPGAGPEQVERICALLQRFCRPVLADPADGRIASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTES 214
Cdd:TIGR00112 110 VTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEAL--ADAGVKQGLPRELALELAAQT 187
|
170 180 190
....*....|....*....|....*....|
gi 501740221 215 VAALAAILDE-GLSFEDVVARTATPGGTTE 243
Cdd:TIGR00112 188 VKGAAKLLEEsGEHPALLKDQVTSPGGTTI 217
|
|
| PRK07502 |
PRK07502 |
prephenate/arogenate dehydrogenase family protein; |
12-159 |
3.27e-05 |
|
prephenate/arogenate dehydrogenase family protein;
Pssm-ID: 236034 [Multi-domain] Cd Length: 307 Bit Score: 44.58 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 12 PTVGLIGLGRIGMVLLAALRRFAPETRVIAAGRDPARVAAATAAWPGVEVMDSERLAVH-ANVVVPCLPPEAYRDGVSAV 90
Cdd:PRK07502 7 DRVALIGIGLIGSSLARAIRRLGLAGEIVGADRSAETRARARELGLGDRVTTSAAEAVKgADLVILCVPVGASGAVAAEI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 91 APHMRADAVLM---SVTNAV------PLPDlgcrcarpivKVILSPAHA-AG--------------RGV-CLVTPSPGAG 145
Cdd:PRK07502 87 APHLKPGAIVTdvgSVKASViaamapHLPE----------GVHFIPGHPlAGtehsgpdagfaelfENRwCILTPPEGTD 156
|
170
....*....|....
gi 501740221 146 PEQVERICALLQRF 159
Cdd:PRK07502 157 PAAVARLTAFWRAL 170
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
172-243 |
3.56e-05 |
|
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.
Pssm-ID: 464294 [Multi-domain] Cd Length: 104 Bit Score: 42.00 E-value: 3.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501740221 172 IASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTESVAALAA-ILDEGLSFEDVVARTATPGGTTE 243
Cdd:pfam14748 6 AVTALSGSGPAYVFLFIEAL--ADAGVAMGLPREEARELAAQTVLGAAKlLLTSGEHPAELRDKVTSPGGTTI 76
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
15-105 |
1.71e-03 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 36.83 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 15 GLIGLGRIGMVLLAALRRFAPETRVIAAGRDPARVAAATAAW-PGVEVMDSERLAVHANVVVPCLPPEAYRDGVSAvAPH 93
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAGPHEVVVANSRNPEKAEELAEEYgVGATAVDNEEAAEEADVVFLAVKPEDAPDVLSE-LSD 79
|
90
....*....|..
gi 501740221 94 MRADAVLMSVTN 105
Cdd:pfam03807 80 LLKGKIVISIAA 91
|
|
| PDH_N |
pfam02153 |
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ... |
29-147 |
1.96e-03 |
|
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate dehydrogenases (PDHs) EC:1.3.1.12 involved in tyrosine biosynthesis. This is the N-terminal nucleotide-binding domain of PDHs, which has a modified Rossmann nucleotide-binding fold with an extended beta-sheet sandwiched by three helices on each face.
Pssm-ID: 460467 [Multi-domain] Cd Length: 154 Bit Score: 38.14 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 29 ALRRFAPETRVIAAGRDPARVAAATAAWPGVEVMDSERLAVHANVVVPCLPPEAYRDGVSAVAPHMRADAVLMSVTNavp 108
Cdd:pfam02153 4 ALRRHGFFVTVIGYDINPEAAVAALRLGLGDEATDDIEAVREADIVFLAVPVEQTLPVLKELAPHLKEDALITDVGS--- 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 501740221 109 lpdlgcrcarpiVKVILS-PAHAAGRGVCLVTPSPGAGPE 147
Cdd:pfam02153 81 ------------VKVKIIrELEQHLPDKSFVPGHPMAGTE 108
|
|
|