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Conserved domains on  [gi|497364595|ref|WP_009678808|]
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folylpolyglutamate synthase/dihydrofolate synthase family protein [Gordonia neofelifaecis]

Protein Classification

bifunctional folylpolyglutamate synthase/dihydrofolate synthase( domain architecture ID 11416298)

bifunctional folylpolyglutamate synthase (FGPS)/dihydrofolate synthase (DHFS) functions in two distinct reactions of the de novo folate biosynthetic pathway, catalyzing the addition of a glutamate residue to dihydropteroate to form dihydrofolate and the successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives

CATH:  3.40.1190.10|3.90.190.20
EC:  6.3.2.-
Gene Ontology:  GO:0004326|GO:0008841|GO:0005524|GO:0006730|GO:0046872
SCOP:  4000353

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 12-465 8.25e-156

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: 448.40  E-value: 8.25e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  12 AELQALEAELDTRWPeTKIEPSLTRITALMELLGNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSPHLQLV 91
Cdd:COG0285    2 TTYQEALAYLESLHP-FGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  92 TERIAIDGEPISARTYVDTYRDIEPYVTMVDDsstagggPRMSKFEVLTAIAYAAFAEAPIEVAVVETGMGGRWDATNVI 171
Cdd:COG0285   81 NERIRINGEPISDEELVEALEEVEPAVEEVDA-------GPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 172 DGQVTVITPIAFDHADYLGDTLTAIAGEKAGIIKPGpsdavIPMdpitVIAPQEPEVADVLLRASVEAGTIVARQDSEFT 251
Cdd:COG0285  154 DPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIKPG-----VPV----VTGDQQPEALEVIEERAAELGAPLYRAGRDFS 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 252 VLEaataVGGQLLSIRGLGGVYDEVFLPLHGAHQAQNAALALAAVEAFFGAGadRQLDVEAVREGFATVDSPGRLERVRS 331
Cdd:COG0285  225 VEE----REGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELG--LPISEEAIREGLANARWPGRLEVLSR 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 332 APSVFVDAAHNPHGARALAQALVSEFDFRRLVGVIGVLGDKDARGLLAELEPVLDVVVLTNNGSPRALDTDALADIANEV 411
Cdd:COG0285  299 GPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAAREL 378

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497364595 412 fgEDRVVVEPFLPEAVEAAVALAEDDDqgsmsgaGVIITGSVVTAGAGRTLFGK 465
Cdd:COG0285  379 --GLRVEVAPDVEEALEAALELADPDD-------LILVTGSLYLVGEVRALLGR 423
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 12-465 8.25e-156

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: 448.40  E-value: 8.25e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  12 AELQALEAELDTRWPeTKIEPSLTRITALMELLGNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSPHLQLV 91
Cdd:COG0285    2 TTYQEALAYLESLHP-FGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  92 TERIAIDGEPISARTYVDTYRDIEPYVTMVDDsstagggPRMSKFEVLTAIAYAAFAEAPIEVAVVETGMGGRWDATNVI 171
Cdd:COG0285   81 NERIRINGEPISDEELVEALEEVEPAVEEVDA-------GPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 172 DGQVTVITPIAFDHADYLGDTLTAIAGEKAGIIKPGpsdavIPMdpitVIAPQEPEVADVLLRASVEAGTIVARQDSEFT 251
Cdd:COG0285  154 DPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIKPG-----VPV----VTGDQQPEALEVIEERAAELGAPLYRAGRDFS 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 252 VLEaataVGGQLLSIRGLGGVYDEVFLPLHGAHQAQNAALALAAVEAFFGAGadRQLDVEAVREGFATVDSPGRLERVRS 331
Cdd:COG0285  225 VEE----REGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELG--LPISEEAIREGLANARWPGRLEVLSR 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 332 APSVFVDAAHNPHGARALAQALVSEFDFRRLVGVIGVLGDKDARGLLAELEPVLDVVVLTNNGSPRALDTDALADIANEV 411
Cdd:COG0285  299 GPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAAREL 378

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497364595 412 fgEDRVVVEPFLPEAVEAAVALAEDDDqgsmsgaGVIITGSVVTAGAGRTLFGK 465
Cdd:COG0285  379 --GLRVEVAPDVEEALEAALELADPDD-------LILVTGSLYLVGEVRALLGR 423
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 34-417 5.24e-93

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: 287.26  E-value: 5.24e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595   34 LTRITALMELLGNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSPHLQLVTERIAIDGEPISARTYVDTYRD 113
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  114 IEPYVTMVDDSSTagggprmsKFEVLTAIAYAAFAEAPIEVAVVETGMGGRWDATNVIDGQVTVITPIAFDHADYLGDTL 193
Cdd:TIGR01499  81 VRPILESLSQQPT--------YFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  194 TAIAGEKAGIIKPGpsdavipmDPItVIAPQEPEVADVLLRASVEAGTIVARQDSEFTVLEAATavggQLLSIRGLGGVY 273
Cdd:TIGR01499 153 EEIAWEKAGIIKEG--------VPI-VTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDE----NYLSFSGANLFL 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  274 DEVFLPLHGAHQAQNAALALAAVEAFFGAGADrqLDVEAVREGFATVDSPGRLERVR-SAPSVFVDAAHNPHGARALAQA 352
Cdd:TIGR01499 220 EPLALSLLGDHQQENAALALAALEVLGKQNPK--LSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAEALAEW 297

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497364595  353 LVSEFDFRRLVGVIGVLGDKDARGLLAELEPVLD-VVVLTNNGSPRALDTDALADiANEVFGEDRV 417
Cdd:TIGR01499 298 FKKRFNGRPITLLFGALADKDAAAMLAPLKPVVDkEVFVTPFDYPRADDAADLAA-FAEETGKSTV 362
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 30-405 2.79e-43

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 157.55  E-value: 2.79e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  30 IEPSLTRITALMELLGNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSPHLQLVTERIAIDGEPISARTYVD 109
Cdd:PRK10846  28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 110 TYRDIEpyvtmvddssTAGGGPRMSKFEVLTAIAYAAFAEAPIEVAVVETGMGGRWDATNVIDGQVTVITPIAFDHADYL 189
Cdd:PRK10846 108 SFAEIE----------AARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 190 GDTLTAIAGEKAGIIKPGPSDAVIPMDPITVIAPQEPEVADVLLRASVEAGTIVARQ-------DSEFTVL--------E 254
Cdd:PRK10846 178 GPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHdwafsdgDGTLENLplpnvplpN 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 255 AATAVGgqllSIRGLGgvydevflplhgahqaqnaalalaaveaffgagadRQLDVEAVREGFATVDSPGRLERVRSAPS 334
Cdd:PRK10846 258 AATALA----ALRASG-----------------------------------LEVSEQAIRDGIASAILPGRFQIVSESPR 298

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497364595 335 VFVDAAHNPHGARALAQALVSEFDFRRLVGVIGVLGDKDARGLLAELEPVLDVVVLTNNGSPRALDTDALA 405
Cdd:PRK10846 299 VILDVAHNPHAAEYLTGRLKALPKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLA 369
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 323-405 1.83e-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: 65.83  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  323 PGRLERVRSA--PSVFVDAAHNPHGARALAQALVSEFDfRRLVGVIGVLGDKDA--RGLLAELEPVLDVVVLTNNGSPRA 398
Cdd:pfam02875   2 PGRLEVVGENngVLVIDDYAHNPDAMEAALRALRNLFP-GRLILVFGGMGDRDAefHALLGRLAAALADVVILTGDYPRA 80


                  ....*..
gi 497364595  399 LDTDALA 405
Cdd:pfam02875  81 EDPGAII 87
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 12-465 8.25e-156

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: 448.40  E-value: 8.25e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  12 AELQALEAELDTRWPeTKIEPSLTRITALMELLGNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSPHLQLV 91
Cdd:COG0285    2 TTYQEALAYLESLHP-FGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  92 TERIAIDGEPISARTYVDTYRDIEPYVTMVDDsstagggPRMSKFEVLTAIAYAAFAEAPIEVAVVETGMGGRWDATNVI 171
Cdd:COG0285   81 NERIRINGEPISDEELVEALEEVEPAVEEVDA-------GPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 172 DGQVTVITPIAFDHADYLGDTLTAIAGEKAGIIKPGpsdavIPMdpitVIAPQEPEVADVLLRASVEAGTIVARQDSEFT 251
Cdd:COG0285  154 DPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIKPG-----VPV----VTGDQQPEALEVIEERAAELGAPLYRAGRDFS 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 252 VLEaataVGGQLLSIRGLGGVYDEVFLPLHGAHQAQNAALALAAVEAFFGAGadRQLDVEAVREGFATVDSPGRLERVRS 331
Cdd:COG0285  225 VEE----REGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELG--LPISEEAIREGLANARWPGRLEVLSR 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 332 APSVFVDAAHNPHGARALAQALVSEFDFRRLVGVIGVLGDKDARGLLAELEPVLDVVVLTNNGSPRALDTDALADIANEV 411
Cdd:COG0285  299 GPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAAREL 378

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497364595 412 fgEDRVVVEPFLPEAVEAAVALAEDDDqgsmsgaGVIITGSVVTAGAGRTLFGK 465
Cdd:COG0285  379 --GLRVEVAPDVEEALEAALELADPDD-------LILVTGSLYLVGEVRALLGR 423
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 34-417 5.24e-93

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: 287.26  E-value: 5.24e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595   34 LTRITALMELLGNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSPHLQLVTERIAIDGEPISARTYVDTYRD 113
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  114 IEPYVTMVDDSSTagggprmsKFEVLTAIAYAAFAEAPIEVAVVETGMGGRWDATNVIDGQVTVITPIAFDHADYLGDTL 193
Cdd:TIGR01499  81 VRPILESLSQQPT--------YFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  194 TAIAGEKAGIIKPGpsdavipmDPItVIAPQEPEVADVLLRASVEAGTIVARQDSEFTVLEAATavggQLLSIRGLGGVY 273
Cdd:TIGR01499 153 EEIAWEKAGIIKEG--------VPI-VTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDE----NYLSFSGANLFL 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  274 DEVFLPLHGAHQAQNAALALAAVEAFFGAGADrqLDVEAVREGFATVDSPGRLERVR-SAPSVFVDAAHNPHGARALAQA 352
Cdd:TIGR01499 220 EPLALSLLGDHQQENAALALAALEVLGKQNPK--LSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAEALAEW 297

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497364595  353 LVSEFDFRRLVGVIGVLGDKDARGLLAELEPVLD-VVVLTNNGSPRALDTDALADiANEVFGEDRV 417
Cdd:TIGR01499 298 FKKRFNGRPITLLFGALADKDAAAMLAPLKPVVDkEVFVTPFDYPRADDAADLAA-FAEETGKSTV 362
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 30-405 2.79e-43

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 157.55  E-value: 2.79e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  30 IEPSLTRITALMELLGNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSPHLQLVTERIAIDGEPISARTYVD 109
Cdd:PRK10846  28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 110 TYRDIEpyvtmvddssTAGGGPRMSKFEVLTAIAYAAFAEAPIEVAVVETGMGGRWDATNVIDGQVTVITPIAFDHADYL 189
Cdd:PRK10846 108 SFAEIE----------AARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 190 GDTLTAIAGEKAGIIKPGPSDAVIPMDPITVIAPQEPEVADVLLRASVEAGTIVARQ-------DSEFTVL--------E 254
Cdd:PRK10846 178 GPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHdwafsdgDGTLENLplpnvplpN 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 255 AATAVGgqllSIRGLGgvydevflplhgahqaqnaalalaaveaffgagadRQLDVEAVREGFATVDSPGRLERVRSAPS 334
Cdd:PRK10846 258 AATALA----ALRASG-----------------------------------LEVSEQAIRDGIASAILPGRFQIVSESPR 298

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497364595 335 VFVDAAHNPHGARALAQALVSEFDFRRLVGVIGVLGDKDARGLLAELEPVLDVVVLTNNGSPRALDTDALA 405
Cdd:PRK10846 299 VILDVAHNPHAAEYLTGRLKALPKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLA 369
PLN02913 PLN02913
dihydrofolate synthetase
 34-452 1.27e-37

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 143.81  E-value: 1.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  34 LTRITALMELLGNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSPHLQLVTERIAI--DGEPISARTYVDTY 111
Cdd:PLN02913  58 LGRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVgkLGKPVSTNTLNDLF 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 112 RDIEPyvtMVDDSSTAGGGpRMSKFEVLTAIAYAAFAEAPIEVAVVETGMGGRWDATNVIDGQ---VTVITPIAFDHADY 188
Cdd:PLN02913 138 HGIKP---ILDEAIQLENG-SLTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIDSSglaASVITTIGEEHLAA 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 189 LGDTLTAIAGEKAGIIKPGpsdavipmDPITVIAPQEPEVADVLL-RASVEAGTIVARQDSEF-TVLEAATAVGG---QL 263
Cdd:PLN02913 214 LGGSLESIALAKSGIIKQG--------RPVVLGGPFLPHIESILRdKASSMNSPVVSASDPGVrSSIKGIITDNGkpcQS 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 264 LSIR-------GLGGVYDEVFLPLHGAHQAQNAALALAAVEAFFGAGADrqLDVEAVREGFATVDSPGRLERVRS----- 331
Cdd:PLN02913 286 CDIVirvekddPLFIELSDVNLRMLGSHQLQNAVTAACAALCLRDQGWR--ISDASIRAGLENTNLLGRSQFLTSkeaev 363

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 332 ----APSVFVDAAHNPHGARALAQALVSEFDFRRLVGVIGVLGDKD----ARGLLAELEPvlDVVVLTN----NGSPRAL 399
Cdd:PLN02913 364 lglpGATVLLDGAHTKESAKALVDTIKTAFPEARLALVVAMASDKDhlafASEFLSGLKP--EAVFLTEadiaGGKSRST 441

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 497364595 400 DTDALADI---ANEVFGEDRVVVEPFLPEAVEAAVALAEDDDQGSMSGAGVIITGS 452
Cdd:PLN02913 442 SASALKEAwikAAPELGIETLLAENNSLLKSLVDASAILRKARTLDPSSVVCVTGS 497
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 54-241 9.32e-33

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 130.55  E-value: 9.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  54 IHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSPHLQLVTERIAIDGEPISARTYV-------DTYRDiepyvtmvddsST 126
Cdd:PLN02881  64 IHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLryfwwcwDRLKE-----------KT 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 127 AGGGPRMSKFEVLTAIAYAAFAEAPIEVAVVETGMGGRWDATNVIDGQVTV-ITPIAFDHADYLGDTLTAIAGEKAGIIK 205
Cdd:PLN02881 133 TEDLPMPAYFRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKPVVCgITSLGYDHMEILGDTLGKIAGEKAGIFK 212

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 497364595 206 PGpsdavIPmdPITViaPQEPEVADVLLRASVEAGT 241
Cdd:PLN02881 213 PG-----VP--AFTV--PQPDEAMRVLEERASELGV 239
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 323-405 1.83e-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: 65.83  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  323 PGRLERVRSA--PSVFVDAAHNPHGARALAQALVSEFDfRRLVGVIGVLGDKDA--RGLLAELEPVLDVVVLTNNGSPRA 398
Cdd:pfam02875   2 PGRLEVVGENngVLVIDDYAHNPDAMEAALRALRNLFP-GRLILVFGGMGDRDAefHALLGRLAAALADVVILTGDYPRA 80


                  ....*..
gi 497364595  399 LDTDALA 405
Cdd:pfam02875  81 EDPGAII 87
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 42-421 2.57e-13

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: 71.58  E-value: 2.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595   42 ELLGNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSPHLQLVTERIAIDGEPISARTYVDTYRDIEpyvTMV 121
Cdd:TIGR01085  76 AFYGHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDLIKNPAALTTPEALTLQSTLA---EMV 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  122 DDSstagggprmskfevltaiayaafaeapIEVAVVET---GMG-GRWDATNVidgQVTVITPIAFDHADYLGdTLTAIA 197
Cdd:TIGR01085 153 EAG---------------------------AQYAVMEVsshALAqGRVRGVRF---DAAVFTNLSRDHLDFHG-TMENYF 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  198 GEKAGIIK--PGPSDAVIPMDpitviAPQEPE-VADVLLRASVEAgtIVARQDSE---FTVLEAATAVGGQLLSIRGLGG 271
Cdd:TIGR01085 202 AAKASLFTelGLKRFAVINLD-----DEYGAQfVKRLPKDITVSA--ITQPADGRaqdIKITDSGYSFEGQQFTFETPAG 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  272 VYdEVFLPLHGAHQAQNAALALAAVEAFFGagadrqLDVEAVREGFATVDS-PGRLERVRSAP--SVFVDAAHNPHgarA 348
Cdd:TIGR01085 275 EG-HLHTPLIGRFNVYNLLAALATLLHLGG------IDLEDIVAALEKFRGvPGRMELVDGGQkfLVIVDYAHTPD---A 344

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497364595  349 LAQAL--VSEFDFRRLVGVIGVLGDKD--ARGLLAELEPVL-DVVVLTNNgSPRALD-TDALADIANEVFGEDRVVVEP 421
Cdd:TIGR01085 345 LEKALrtLRKHKDGRLIVVFGCGGDRDrgKRPLMGAIAEQLaDLVILTSD-NPRGEDpEQIIADILAGISEKEKVVIIA 422
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 45-421 1.18e-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: 66.26  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  45 GNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITsphlqlvTERIAIDGEPI-SART---YVDTYRDIEpyvTM 120
Cdd:COG0769   74 GHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIG-------TVGNGIGGELIpSSLTtpeALDLQRLLA---EM 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 121 VDdsstAGggprmskfevltaiayaafaeapIEVAVVE-TGMG---GRWDATNVidgQVTVITPIAFDHADYLGdTLTAI 196
Cdd:COG0769  144 VD----AG-----------------------VTHVVMEvSSHAldqGRVDGVRF---DVAVFTNLTRDHLDYHG-TMEAY 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 197 AGEKAGIIKPGPSD--AVIPMDpitviapqEPEVADVLLRASVEAGTIVARQDSEFTVLEAATAVGGQLLSIRGLGGVYd 274
Cdd:COG0769  193 FAAKARLFDQLGPGgaAVINAD--------DPYGRRLAAAAPARVITYGLKADADLRATDIELSADGTRFTLVTPGGEV- 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 275 EVFLPLHGAHqaqnaalalaAVE---AFFGAGADRQLDVEAVREGFATVDS-PGRLERVRSA--PSVFVDAAHNPhgaRA 348
Cdd:COG0769  264 EVRLPLIGRF----------NVYnalAAIAAALALGIDLEEILAALEKLKGvPGRMERVDGGqgPTVIVDYAHTP---DA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 349 LAQAL--VSEFDFRRLVGVIGVLGDKDA--RGLLAElepVL----DVVVLTN-NgsPRALDTDA-LADIANEVFGEDRVV 418
Cdd:COG0769  331 LENVLeaLRPHTKGRLIVVFGCGGDRDRgkRPLMGE---IAarlaDVVIVTSdN--PRSEDPAAiIADILAGIPGAGKVL 405


                 ...
gi 497364595 419 VEP 421
Cdd:COG0769  406 VIP 408
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 45-421 1.15e-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: 57.79  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  45 GNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITsphlqlvTERIAIDGEPI-SARTYVDTYRDIEPYVTMVDD 123
Cdd:PRK11929 106 GRPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIG-------TLGARLDGRLIpGSLTTPDAIILHRILARMRAA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 124 SSTAgggprmskfevltaiayaafaeAPIEVAVVETGMGgRWDATNVIdgqVTVITPIAFDHADYLGdTLTAIAGEKAGI 203
Cdd:PRK11929 179 GADA----------------------VAMEASSHGLEQG-RLDGLRIA---VAGFTNLTRDHLDYHG-TMQDYEEAKAAL 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 204 IKPGPSD--AVIPMDpitviAPQEPEVADVLLRAsVEAGTIVARQDSEFTVLEAATAVGGQLLSIRGLGGVYdEVFLPLH 281
Cdd:PRK11929 232 FSKLPGLgaAVINAD-----DPAAARLLAALPRG-LKVGYSPQNAGADVQARDLRATAHGQVFTLATPDGSY-QLVTRLL 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 282 GAHQAQnaalalaavEAFFGAGADRQLDVEA---VREGFATVDSPGRLERV-----RSAPSVFVDAAHNPHgarALAQAL 353
Cdd:PRK11929 305 GRFNVS---------NLLLVAAALKKLGLPLaqiARALAAVSPVPGRMERVgptagAQGPLVVVDYAHTPD---ALAKAL 372

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497364595 354 -----VSEFDFRRLVGVIGVLGDKDA--RGLLAELEPVL-DVVVLTNNgSPRALDTDA-LADIANEVFGEDRVVVEP 421
Cdd:PRK11929 373 talrpVAQARNGRLVCVFGCGGDRDKgkRPEMGRIAAELaDRVVVTSD-NPRSEAPEAiIDQILAGIPAGARVFVIS 448
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 45-391 3.32e-06

UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 49.36  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  45 GNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSphLQLVteriaIDGEPI-SART---YVDTYRDIEpyvTM 120
Cdd:PRK00139  89 GHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGT--LGNG-----IGGELIpSGLTtpdALDLQRLLA---EL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 121 VDDSSTAGGgprmskfevltaiayaafaeapIEV---AVVEtgmgGRWDATNViDGQV-TVITPiafDHADYLGdTLTAI 196
Cdd:PRK00139 159 VDAGVTYAA----------------------MEVsshALDQ----GRVDGLKF-DVAVfTNLSR---DHLDYHG-TMEDY 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 197 AGEKAGIIKPGPSDAVIPMDPitviapqepEVADVLLRASVEAGtiVARQDSEFTVLEAATAVGGQLLSIRGlggvydEV 276
Cdd:PRK00139 208 LAAKARLFSELGLAAVINADD---------EVGRRLLALPDAYA--VSMAGADLRATDVEYTDSGQTFTLVT------EV 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 277 FLPLHGAHqaqnaalalaAVE---AFFGAGADRQLDVEAVREGFATVDS-PGRLERVRSA--PSVFVDAAHNPHgarALA 350
Cdd:PRK00139 271 ESPLIGRF----------NVSnllAALAALLALGVPLEDALAALAKLQGvPGRMERVDAGqgPLVIVDYAHTPD---ALE 337

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 497364595 351 QAL--VSEFDFRRLVGVIGVLGDKDA--RGLLAElepVL----DVVVLT 391
Cdd:PRK00139 338 KVLeaLRPHAKGRLICVFGCGGDRDKgkRPLMGA---IAerlaDVVIVT 383
Mur_ligase_M pfam08245
Mur ligase middle domain;
56-216 4.71e-06

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 47.30  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595   56 VAGTNGKTSVTRMIDSLLRAFHRRTGritsphlqlvTERIAIDGEPISARTYVDTYRDIEpyvTMVDDSstagggprmsk 135
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIG----------TIGTYIGKSGNTTNNAIGLPLTLA---EMVEAG----------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  136 fevltaiayaafaeapIEVAVVETGMGGRwdATNVIDGQVT----VITPIAFDHADYLGdTLTAIAGEKAGIIKPGPSD- 210
Cdd:pfam08245  57 ----------------AEYAVLEVSSHGL--GEGRLSGLLKpdiaVFTNISPDHLDFHG-TMENYAKAKAELFEGLPEDg 117


                  ....*..
gi 497364595  211 -AVIPMD 216
Cdd:pfam08245 118 iAVINAD 124
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
311-416 1.88e-04

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 43.87  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595 311 EAVREGFATVDSPGRLERV-RSAPS-VFVDAAHNPHGARALAQAlVSEFDFRRLVGVIGVLGDKDAR-----GLLAELEP 383
Cdd:PRK14022 316 EDIQKGIAQTPVPGRMEVLtQSNGAkVFIDYAHNGDSLNKLIDV-VEEHQKGKLILLLGAAGNKGESrrpdfGRVANRHP 394

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 497364595 384 VLDvVVLT----NNGSPRALdTDALADIAN---EVFgEDR 416
Cdd:PRK14022 395 YLQ-VILTaddpNNEDPKMI-TQEIASHIThpvEII-DDR 431
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
41-78 3.32e-04

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 43.10  E-value: 3.32e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 497364595  41 MELLGNPQHAYPSIHVAGTNGKTSVTRMIDSLLRAFHR 78
Cdd:PRK14022 100 MEFYDNPQHKLKLLAFTGTKGKTTAAYFAYHILKQLHK 137
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
 51-91 8.75e-04

UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273436 [Multi-domain]  Cd Length: 433  Bit Score: 41.56  E-value: 8.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 497364595   51 YPSIHVAGTNGKTSVTRMIDSLLRAFHRRT---GRITSPHLQLV 91
Cdd:TIGR01087 102 LPVVAITGTNGKTTTTSLLYHLLKAAGLKAflgGNIGTPALEVL 145
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 52-191 8.92e-04

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 41.68  E-value: 8.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497364595  52 PSIHVAGTNGKTSVTRMIDSLLRAFHRRTGRITSphlqlvteriaiDGepisarTYVDTYRdiepyvtmVDDSSTAggGP 131
Cdd:PRK14016 481 PIVAVTGTNGKTTTTRLIAHILKLSGKRVGMTTT------------DG------VYIDGRL--------IDKGDCT--GP 532

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497364595 132 RMSKFeVLTAIAyaafaeapIEVAVVETGMGGRwdatnVIDG------QVTVITPIAFDHadyLGD 191
Cdd:PRK14016 533 KSARR-VLMNPD--------VEAAVLETARGGI-----LREGlaydrcDVGVVTNIGEDH---LGL 581
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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