|
Name |
Accession |
Description |
Interval |
E-value |
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
25-484 |
8.26e-169 |
|
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440054 [Multi-domain] Cd Length: 423 Bit Score: 482.30 E-value: 8.26e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 25 ASLLQVEHLLDQRWPeTRIDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSP 104
Cdd:COG0285 2 TTYQEALAYLESLHP-FGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 105 VERISIDGKPISPAQYVATYREIEPLVALIDQQSqasagkggpaMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDAT 184
Cdd:COG0285 81 NERIRINGEPISDEELVEALEEVEPAVEEVDAGP----------PTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 185 NVINAPVAVITPISIDHVDYLGADIAGIAGEKAGIITrapdgsPDTVAVIGRQVPKVMEVLLAESVRADASVAREDSEFA 264
Cdd:COG0285 151 NVIDPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIK------PGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 265 VLRRqiavGGQVLQLQGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGaqRQLDGDAVRAGFAAVTSPGRLERMRS 344
Cdd:COG0285 225 VEER----EGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELG--LPISEEAIREGLANARWPGRLEVLSR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 345 APTVFIDAAHNPAGASALAQTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGSPRALDVEALALAAGER 424
Cdd:COG0285 299 GPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAAREL 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 425 fgPDRVRTAENLRDAIDVATSLVDdaaadpdvagdafSRTGIVITGSVVTAGAARTLFGR 484
Cdd:COG0285 379 --GLRVEVAPDVEEALEAALELAD-------------PDDLILVTGSLYLVGEVRALLGR 423
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
47-482 |
2.51e-97 |
|
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273659 [Multi-domain] Cd Length: 397 Bit Score: 298.81 E-value: 2.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 47 LTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYRE 126
Cdd:TIGR01499 1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 127 IEPLVALIDQQSqasagkggpamSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHVDYLG 206
Cdd:TIGR01499 81 VRPILESLSQQP-----------TYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 207 ADIAGIAGEKAGIITRapdGSPdtvAVIGRQVPKVMEVLL--AESVRADASVAREDSEFAVLRRqiavggQVLQLQGLGG 284
Cdd:TIGR01499 150 DTLEEIAWEKAGIIKE---GVP---IVTGEQEPEALNVLKkkAQEKGAPLFVVGRDFNYSETDE------NYLSFSGANL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 285 VYSDIYLPLHGEHQAHNAVLALASVEAFfgAGAQRQLDGDAVRAGFAAVTSPGRLERMR-SAPTVFIDAAHNPAGASALA 363
Cdd:TIGR01499 218 FLEPLALSLLGDHQQENAALALAALEVL--GKQNPKLSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAEALA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 364 QTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGS-PRALDVEALALAAGERFGpdrvRTAENLRDAIDV 442
Cdd:TIGR01499 296 EWFKKRFNGRPITLLFGALADKDAAAMLAPLKPVVDKEVFVTPFDyPRADDAADLAAFAEETGK----STVEDWREALEE 371
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15609584 443 ATSLVddaaadpdvagdafSRTGIVITGSVVTAGAARTLF 482
Cdd:TIGR01499 372 ALNAS--------------AEDDILVTGSLYLVGEVRKLL 397
|
|
| PRK10846 |
PRK10846 |
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional |
43-433 |
7.72e-52 |
|
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
Pssm-ID: 182774 [Multi-domain] Cd Length: 416 Bit Score: 181.04 E-value: 7.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 43 IDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVA 122
Cdd:PRK10846 28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 123 TYREIEplvalidqqsqasAGKGGPAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHV 202
Cdd:PRK10846 108 SFAEIE-------------AARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 203 DYLGADIAGIAGEKAGIITR---APDGSPDTVAVIgrqvpkvmevllaesvradASVAREDSefAVLRR-----QIAVGG 274
Cdd:PRK10846 175 DWLGPDRESIGREKAGIFRAekpAVVGEPDMPSTI-------------------ADVAQEKG--ALLQRrgvdwNYSVTD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 275 QVLQLQGLGGVYSDiyLPLHGEHQAhNAVLALASVEAffgagAQRQLDGDAVRAGFAAVTSPGRLERMRSAPTVFIDAAH 354
Cdd:PRK10846 234 HDWAFSDGDGTLEN--LPLPNVPLP-NAATALAALRA-----SGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 355 NPAGASALAQTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGSPRALDVEALA--LAAGERFgpDRVRT 432
Cdd:PRK10846 306 NPHAAEYLTGRLKALPKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAehLGNGKSF--DSVAQ 383
|
.
gi 15609584 433 A 433
Cdd:PRK10846 384 A 384
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
336-413 |
2.91e-13 |
|
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460731 [Multi-domain] Cd Length: 87 Bit Score: 65.06 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 336 PGRLERMRSA--PTVFIDAAHNPAGASALAQTLAHEFDFRfLVGVLSVLGDKDVD--GILAALEPVFDSVVVTHNGSPRA 411
Cdd:pfam02875 2 PGRLEVVGENngVLVIDDYAHNPDAMEAALRALRNLFPGR-LILVFGGMGDRDAEfhALLGRLAAALADVVILTGDYPRA 80
|
..
gi 15609584 412 LD 413
Cdd:pfam02875 81 ED 82
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
25-484 |
8.26e-169 |
|
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440054 [Multi-domain] Cd Length: 423 Bit Score: 482.30 E-value: 8.26e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 25 ASLLQVEHLLDQRWPeTRIDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSP 104
Cdd:COG0285 2 TTYQEALAYLESLHP-FGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 105 VERISIDGKPISPAQYVATYREIEPLVALIDQQSqasagkggpaMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDAT 184
Cdd:COG0285 81 NERIRINGEPISDEELVEALEEVEPAVEEVDAGP----------PTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 185 NVINAPVAVITPISIDHVDYLGADIAGIAGEKAGIITrapdgsPDTVAVIGRQVPKVMEVLLAESVRADASVAREDSEFA 264
Cdd:COG0285 151 NVIDPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIK------PGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 265 VLRRqiavGGQVLQLQGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGaqRQLDGDAVRAGFAAVTSPGRLERMRS 344
Cdd:COG0285 225 VEER----EGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELG--LPISEEAIREGLANARWPGRLEVLSR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 345 APTVFIDAAHNPAGASALAQTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGSPRALDVEALALAAGER 424
Cdd:COG0285 299 GPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAAREL 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 425 fgPDRVRTAENLRDAIDVATSLVDdaaadpdvagdafSRTGIVITGSVVTAGAARTLFGR 484
Cdd:COG0285 379 --GLRVEVAPDVEEALEAALELAD-------------PDDLILVTGSLYLVGEVRALLGR 423
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
47-482 |
2.51e-97 |
|
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273659 [Multi-domain] Cd Length: 397 Bit Score: 298.81 E-value: 2.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 47 LTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYRE 126
Cdd:TIGR01499 1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 127 IEPLVALIDQQSqasagkggpamSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHVDYLG 206
Cdd:TIGR01499 81 VRPILESLSQQP-----------TYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 207 ADIAGIAGEKAGIITRapdGSPdtvAVIGRQVPKVMEVLL--AESVRADASVAREDSEFAVLRRqiavggQVLQLQGLGG 284
Cdd:TIGR01499 150 DTLEEIAWEKAGIIKE---GVP---IVTGEQEPEALNVLKkkAQEKGAPLFVVGRDFNYSETDE------NYLSFSGANL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 285 VYSDIYLPLHGEHQAHNAVLALASVEAFfgAGAQRQLDGDAVRAGFAAVTSPGRLERMR-SAPTVFIDAAHNPAGASALA 363
Cdd:TIGR01499 218 FLEPLALSLLGDHQQENAALALAALEVL--GKQNPKLSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAEALA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 364 QTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGS-PRALDVEALALAAGERFGpdrvRTAENLRDAIDV 442
Cdd:TIGR01499 296 EWFKKRFNGRPITLLFGALADKDAAAMLAPLKPVVDKEVFVTPFDyPRADDAADLAAFAEETGK----STVEDWREALEE 371
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15609584 443 ATSLVddaaadpdvagdafSRTGIVITGSVVTAGAARTLF 482
Cdd:TIGR01499 372 ALNAS--------------AEDDILVTGSLYLVGEVRKLL 397
|
|
| PRK10846 |
PRK10846 |
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional |
43-433 |
7.72e-52 |
|
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
Pssm-ID: 182774 [Multi-domain] Cd Length: 416 Bit Score: 181.04 E-value: 7.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 43 IDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVA 122
Cdd:PRK10846 28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 123 TYREIEplvalidqqsqasAGKGGPAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHV 202
Cdd:PRK10846 108 SFAEIE-------------AARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 203 DYLGADIAGIAGEKAGIITR---APDGSPDTVAVIgrqvpkvmevllaesvradASVAREDSefAVLRR-----QIAVGG 274
Cdd:PRK10846 175 DWLGPDRESIGREKAGIFRAekpAVVGEPDMPSTI-------------------ADVAQEKG--ALLQRrgvdwNYSVTD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 275 QVLQLQGLGGVYSDiyLPLHGEHQAhNAVLALASVEAffgagAQRQLDGDAVRAGFAAVTSPGRLERMRSAPTVFIDAAH 354
Cdd:PRK10846 234 HDWAFSDGDGTLEN--LPLPNVPLP-NAATALAALRA-----SGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 355 NPAGASALAQTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGSPRALDVEALA--LAAGERFgpDRVRT 432
Cdd:PRK10846 306 NPHAAEYLTGRLKALPKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAehLGNGKSF--DSVAQ 383
|
.
gi 15609584 433 A 433
Cdd:PRK10846 384 A 384
|
|
| PLN02913 |
PLN02913 |
dihydrofolate synthetase |
47-435 |
3.69e-36 |
|
dihydrofolate synthetase
Pssm-ID: 178501 [Multi-domain] Cd Length: 510 Bit Score: 140.34 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 47 LTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISI--DGKPISPAQYVATY 124
Cdd:PLN02913 58 LGRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVgkLGKPVSTNTLNDLF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 125 REIEPLvalIDQQSQASAGkggpAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVI---NAPVAVITPISIDH 201
Cdd:PLN02913 138 HGIKPI---LDEAIQLENG----SLTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIdssGLAASVITTIGEEH 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 202 VDYLGADIAGIAGEKAGIITRapdGSPdtvAVIGRQVPKVMEVLL---AESVRADASVAREDSEFAVLRRQIAVGGQVLQ 278
Cdd:PLN02913 211 LAALGGSLESIALAKSGIIKQ---GRP---VVLGGPFLPHIESILrdkASSMNSPVVSASDPGVRSSIKGIITDNGKPCQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 279 L----------QGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGAqrQLDGDAVRAGFAAVTSPGRLERMRS---- 344
Cdd:PLN02913 285 ScdivirvekdDPLFIELSDVNLRMLGSHQLQNAVTAACAALCLRDQGW--RISDASIRAGLENTNLLGRSQFLTSkeae 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 345 -----APTVFIDAAHNPAGASALAQTLAHEFDFRFLVGVLSVLGDKD----VDGILAALEPvfDSVVVTH----NGSPRA 411
Cdd:PLN02913 363 vlglpGATVLLDGAHTKESAKALVDTIKTAFPEARLALVVAMASDKDhlafASEFLSGLKP--EAVFLTEadiaGGKSRS 440
|
410 420
....*....|....*....|....*..
gi 15609584 412 LDVEALA---LAAGERFGPDRVRTAEN 435
Cdd:PLN02913 441 TSASALKeawIKAAPELGIETLLAENN 467
|
|
| PLN02881 |
PLN02881 |
tetrahydrofolylpolyglutamate synthase |
67-307 |
2.14e-31 |
|
tetrahydrofolylpolyglutamate synthase
Pssm-ID: 215476 Cd Length: 530 Bit Score: 126.70 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 67 IHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYREieplvaLIDQ-QSQASAGKG 145
Cdd:PLN02881 64 IHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYFWW------CWDRlKEKTTEDLP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 146 GPAMSKFevLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAV-ITPISIDHVDYLGADIAGIAGEKAGIITrap 224
Cdd:PLN02881 138 MPAYFRF--LTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKPVVCgITSLGYDHMEILGDTLGKIAGEKAGIFK--- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 225 DGSPD-TVAvigrQVPKVMEVLLAesvRAdasvaredsefavlrRQIAVGGQV---LQLQGLggvySDIYLPLHGEHQAH 300
Cdd:PLN02881 213 PGVPAfTVP----QPDEAMRVLEE---RA---------------SELGVPLQVvepLDSYGL----SGLKLGLAGEHQYL 266
|
....*..
gi 15609584 301 NAVLALA 307
Cdd:PLN02881 267 NAGLAVA 273
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
336-413 |
2.91e-13 |
|
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460731 [Multi-domain] Cd Length: 87 Bit Score: 65.06 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 336 PGRLERMRSA--PTVFIDAAHNPAGASALAQTLAHEFDFRfLVGVLSVLGDKDVD--GILAALEPVFDSVVVTHNGSPRA 411
Cdd:pfam02875 2 PGRLEVVGENngVLVIDDYAHNPDAMEAALRALRNLFPGR-LILVFGGMGDRDAEfhALLGRLAAALADVVILTGDYPRA 80
|
..
gi 15609584 412 LD 413
Cdd:pfam02875 81 ED 82
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
169-384 |
1.50e-11 |
|
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440533 [Multi-domain] Cd Length: 451 Bit Score: 66.28 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 169 DVAVVEVGMggrwdatnviNAP-------------VAVITPISIDHVDYLGaDIAGIAGEKAGIITRAPdgsPDTVAVIG 235
Cdd:COG0770 153 EFAVLEMGM----------NHPgeiaylariarpdIAVITNIGPAHLEGFG-SLEGIARAKGEIFEGLP---PGGVAVLN 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 236 RQVPKVMEvlLAEsvRADASVAR----EDSEFAVLRRQIAVGGQVLQLQGLGGVYsDIYLPLHGEHQAHNAVLALASVEA 311
Cdd:COG0770 219 ADDPLLAA--LAE--RAKARVLTfglsEDADVRAEDIELDEDGTRFTLHTPGGEL-EVTLPLPGRHNVSNALAAAAVALA 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15609584 312 FfgagaqrQLDGDAVRAGFAAVT-SPGRLERMRSAPTV-FIDAAHN--PAGASALAQTLAH--EFDFRFLvgvlsVLGD 384
Cdd:COG0770 294 L-------GLDLEEIAAGLAAFQpVKGRLEVIEGAGGVtLIDDSYNanPDSMKAALDVLAQlpGGGRRIA-----VLGD 360
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
58-367 |
4.79e-11 |
|
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440532 [Multi-domain] Cd Length: 459 Bit Score: 64.71 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 58 GSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTG-----------------RTT--SPHLQspverisidgkpispa 118
Cdd:COG0769 74 GHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGligtvgngiggelipssLTTpeALDLQ---------------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 119 QYVATYREieplvalidqqsqasAGkggpamskfevltamafaafadapVDVAVVEV-GMG---GRWDATNVInapVAVI 194
Cdd:COG0769 138 RLLAEMVD---------------AG------------------------VTHVVMEVsSHAldqGRVDGVRFD---VAVF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 195 TPISIDHVDYLGaDIAGIAGEKAGIITRAPdgsPDTVAVI------GRQvpkvmevlLAEsvRADASV----AREDSEFA 264
Cdd:COG0769 176 TNLTRDHLDYHG-TMEAYFAAKARLFDQLG---PGGAAVInaddpyGRR--------LAA--AAPARVitygLKADADLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 265 VLRRQIAVGGQVLQLQGLGGVYsDIYLPLHGEHQAHNAVLALASVEAffgAGaqrqLDGDAVRAGFAAVTS-PGRLERMR 343
Cdd:COG0769 242 ATDIELSADGTRFTLVTPGGEV-EVRLPLIGRFNVYNALAAIAAALA---LG----IDLEEILAALEKLKGvPGRMERVD 313
|
330 340
....*....|....*....|....*.
gi 15609584 344 SA--PTVFIDAAHNPAgasALAQTLA 367
Cdd:COG0769 314 GGqgPTVIVDYAHTPD---ALENVLE 336
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
69-309 |
3.29e-09 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 56.54 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 69 IAGTNGKTSVARMVDALVTALhrrTGRTTSPhlqspverisidGKPISPAqyVATYREieplvaLID-QQSQASAGKGGp 147
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLA---GGVIGTI------------GTYIGKS--GNTTNN------AIGlPLTLAEMVEAG- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 148 amskfevltamafaafadapVDVAVVEVGMGGRWDA--TNVINAPVAVITPISIDHVDYLGaDIAGIAGEKAGIITRAPD 225
Cdd:pfam08245 57 --------------------AEYAVLEVSSHGLGEGrlSGLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEGLPE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 226 GSpdtVAVIGRQVPkVMEVLLAESVRADASVAR--EDSEFAVLRRQIAV--GGQVLQLQGLGGVYSDIYLPLHGEHQAHN 301
Cdd:pfam08245 116 DG---IAVINADDP-YGAFLIAKLKKAGVRVITygIEGEADLRAANIELssDGTSFDLFTVPGGELEIEIPLLGRHNVYN 191
|
....*...
gi 15609584 302 AVLALASV 309
Cdd:pfam08245 192 ALAAIAAA 199
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
58-367 |
4.65e-09 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 58.22 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 58 GSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGrttsphLQSPVERIsIDGKPISPA----QYVATYREIEPLVAl 133
Cdd:PRK00139 89 GHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTA------LIGTLGNG-IGGELIPSGlttpDALDLQRLLAELVD- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 134 idqqsqasAGkggpamskfevltamafaafadapVDVAVVEV---GMG-GRWDATNVInapVAVITPISIDHVDYLGaDI 209
Cdd:PRK00139 161 --------AG------------------------VTYAAMEVsshALDqGRVDGLKFD---VAVFTNLSRDHLDYHG-TM 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 210 AGIAGEKAGIITRapdgsPDTVAVI------GRQvpkvmevlLAESVRAdASVAREDSEFAVLRRQIAVGGQVLQLQGlg 283
Cdd:PRK00139 205 EDYLAAKARLFSE-----LGLAAVInaddevGRR--------LLALPDA-YAVSMAGADLRATDVEYTDSGQTFTLVT-- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 284 gvysDIYLPLHGEHQAHNAVLALASVEAffgAGaqrqLDGDAVRAGFAAVTS-PGRLERMRSA--PTVFIDAAHNPAgas 360
Cdd:PRK00139 269 ----EVESPLIGRFNVSNLLAALAALLA---LG----VPLEDALAALAKLQGvPGRMERVDAGqgPLVIVDYAHTPD--- 334
|
....*..
gi 15609584 361 ALAQTLA 367
Cdd:PRK00139 335 ALEKVLE 341
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
179-443 |
1.98e-08 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 57.02 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 179 GRWDATNVInapVAVITPISIDHVDYLGaDIAGIAGEKAGIITRAPdgsPDTVAVIGRQVPKVMEVLLAESVRADASVAR 258
Cdd:PRK11929 195 GRLDGLRIA---VAGFTNLTRDHLDYHG-TMQDYEEAKAALFSKLP---GLGAAVINADDPAAARLLAALPRGLKVGYSP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 259 EDSEFAVLRRQIAVG--GQVLQLQGLGGVYSdIYLPLHGEHQAHNAVLALAsveaffgAGAQRQLDGDAVRAGFAAVTS- 335
Cdd:PRK11929 268 QNAGADVQARDLRATahGQVFTLATPDGSYQ-LVTRLLGRFNVSNLLLVAA-------ALKKLGLPLAQIARALAAVSPv 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 336 PGRLERM-----RSAPTVFIDAAHNPagaSALAQTLA-----HEFDFRFLVGVLSVLGDKDVD-----GILAAlePVFDS 400
Cdd:PRK11929 340 PGRMERVgptagAQGPLVVVDYAHTP---DALAKALTalrpvAQARNGRLVCVFGCGGDRDKGkrpemGRIAA--ELADR 414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15609584 401 VVVTHNgSPRALDVEA--LALAAGERfGPDRVRTAENLRDAIDVA 443
Cdd:PRK11929 415 VVVTSD-NPRSEAPEAiiDQILAGIP-AGARVFVISDRAEAIRQA 457
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
169-367 |
1.87e-07 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 53.94 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 169 DVAVVEVGMG--GRWDATNVINAP-VAVITPISIDHVDYLGaDIAGIAGEKAGIITRAPdgsPDTVAVIGRQVP------ 239
Cdd:PRK11929 659 RAAVFELGMNhpGEIAYLAAIAAPtVALVTNAQREHQEFMH-SVEAVARAKGEIIAALP---EDGVAVVNGDDPytaiwa 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 240 ------KVMEVLLAESVRADASVAREDSEFAvlrrqiAVGGQVLQLQGLGGVySDIYLPLHGEHQAHNAVLALASVEAfF 313
Cdd:PRK11929 735 klagarRVLRFGLQPGADVYAEKIAKDISVG------EAGGTRCQVVTPAGS-AEVYLPLIGEHNLRNALAAIACALA-A 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15609584 314 GAGAQrqldgDAVRAGFAAVTSPGRLERMR-SAPTVFIDAAH--NPAGASALAQTLA 367
Cdd:PRK11929 807 GASLK-----QIRAGLERFQPVAGRMQRRRlSCGTRIIDDTYnaNPDSMRAAIDVLA 858
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
58-356 |
4.03e-06 |
|
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273435 [Multi-domain] Cd Length: 464 Bit Score: 49.24 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 58 GSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYREIEPLValidqq 137
Cdd:TIGR01085 79 GHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDLIKNPAALTTPEALTLQSTLAEMV------ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 138 sQASAgkggpamskfevltamafaafadapvDVAVVEV---GMG-GRWDATNVInapVAVITPISIDHVDYLGAdIAGIA 213
Cdd:TIGR01085 153 -EAGA--------------------------QYAVMEVsshALAqGRVRGVRFD---AAVFTNLSRDHLDFHGT-MENYF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 214 GEKAGIITRAPDgspDTVAVI----------GRQVPKVMEVLlAESVRADASVAR-EDSEFAVLRRqiavgGQVLQLQGL 282
Cdd:TIGR01085 202 AAKASLFTELGL---KRFAVInlddeygaqfVKRLPKDITVS-AITQPADGRAQDiKITDSGYSFE-----GQQFTFETP 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15609584 283 GGVYsDIYLPLHGEHQAHNAVLALASVEAFFGagaqrqLDGDAVRAGFAAVTS-PGRLER--MRSAPTVFIDAAHNP 356
Cdd:TIGR01085 273 AGEG-HLHTPLIGRFNVYNLLAALATLLHLGG------IDLEDIVAALEKFRGvPGRMELvdGGQKFLVIVDYAHTP 342
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
65-339 |
3.86e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 43.22 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 65 PSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSphlqspvERISIDGKpispaqyvatyreieplvaLIDqqsqasagK 144
Cdd:PRK14016 481 PIVAVTGTNGKTTTTRLIAHILKLSGKRVGMTTT-------DGVYIDGR-------------------LID--------K 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 145 G---GPAMSKFeVLTAMAfaafadapVDVAVVEVGMGG---------RWDatnvinapVAVITPISIDHvdyLGAD---- 208
Cdd:PRK14016 527 GdctGPKSARR-VLMNPD--------VEAAVLETARGGilreglaydRCD--------VGVVTNIGEDH---LGLGgint 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609584 209 IAGIAGEKAGII-TRAPDGspdtVAVIGRQVPKVMEvlLAEsvRADASVA--REDSEFAVLRRQIAVGGQVLQLQG---- 281
Cdd:PRK14016 587 LEDLAKVKRVVVeAVKPDG----YAVLNADDPMVAA--MAE--RCKGKVIffSMDPDNPVIAEHRAQGGRAVYVEGdyiv 658
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15609584 282 ---------LGGVySDIYLPLHGeHQAHNAVLALASVEAFFGAGaqrqLDGDAVRAGFA-----AVTSPGRL 339
Cdd:PRK14016 659 laeggweirIISL-ADIPLTLGG-KAGFNIENALAAIAAAWALG----IDIELIRAGLRtfvsdAAQAPGRF 724
|
|
| |
