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Conserved domains on  [gi|15832453|ref|NP_311226|]
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bifunctional folylpolyglutamate synthase/ dihydrofolate synthase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

bifunctional folylpolyglutamate synthase/dihydrofolate synthase( domain architecture ID 11484987)

bifunctional folylpolyglutamate synthase/dihydrofolate synthase FolC catalyzes two distinct reactions of the de novo folate biosynthetic pathway, the addition of a glutamate to dihydropteroate to form dihydrofolate and the successive additions of glutamate to tetrahydrofolate leading to folylpolyglutamate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 1-416 0e+00

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


:

Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 865.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453    1 MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSQVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGV 80
Cdd:PRK10846   1 MINKQTPQATSPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   81 YSSPHLVCYTERVRVQGQELPESAHTASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160
Cdd:PRK10846  81 YSSPHLVRYTERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSD 240
Cdd:PRK10846 161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFSD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  241 AHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHAAEYLTGRMKTL 320
Cdd:PRK10846 241 GDGTLENLPLPNVPLPNAATALAALRASGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  321 PKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLV 400
Cdd:PRK10846 321 PKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAEHLGNGKSFDSVAQAWDAAMADAKPEDTVLV 400

                        410
                 ....*....|....*.
gi 15832453  401 CGSFHTVAHVMEVIDA 416
Cdd:PRK10846 401 CGSFHTVAHVMEVIDA 416
 
Name Accession Description Interval E-value
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 1-416 0e+00

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 865.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453    1 MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSQVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGV 80
Cdd:PRK10846   1 MINKQTPQATSPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   81 YSSPHLVCYTERVRVQGQELPESAHTASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160
Cdd:PRK10846  81 YSSPHLVRYTERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSD 240
Cdd:PRK10846 161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFSD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  241 AHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHAAEYLTGRMKTL 320
Cdd:PRK10846 241 GDGTLENLPLPNVPLPNAATALAALRASGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  321 PKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLV 400
Cdd:PRK10846 321 PKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAEHLGNGKSFDSVAQAWDAAMADAKPEDTVLV 400

                        410
                 ....*....|....*.
gi 15832453  401 CGSFHTVAHVMEVIDA 416
Cdd:PRK10846 401 CGSFHTVAHVMEVIDA 416
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 11-414 2.15e-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: 481.14  E-value: 2.15e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  11 SPLASWLSYLENLHSKTIDLGLERVSQVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVCYT 90
Cdd:COG0285   2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  91 ERVRVQGQELPESAHTASFAEIESARGDI---SLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVT 167
Cdd:COG0285  82 ERIRINGEPISDEELVEALEEVEPAVEEVdagPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVIT 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 168 SIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGE--PEMPSTIADVAQEKGALLQRRGVEWNYSVTDHD-WAFSDAHGT 244
Cdd:COG0285 162 SIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDqqPEALEVIEERAAELGAPLYRAGRDFSVEEREGAvFSYQGPGGE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 245 LENLPLPL---------------VpqpnaatalAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHA 309
Cdd:COG0285 242 YEDLPLPLlgahqaenaalalaaL---------EALRELGLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAG 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 310 AEYLTGRMKTLPKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHL----GNGKSFDSVAQAW 385
Cdd:COG0285 313 ARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAArelgLRVEVAPDVEEAL 392

                       410       420
                ....*....|....*....|....*....
gi 15832453 386 DAAMADAKAEDTVLVCGSFHTVAHVMEVI 414
Cdd:COG0285 393 EAALELADPDDLILVTGSLYLVGEVRALL 421
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 32-413 6.39e-161

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: 458.67  E-value: 6.39e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453    32 LERVSQVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVCYTERVRVQGQELPESAHTASFAE 111
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   112 IESA--RGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESIGREKA 189
Cdd:TIGR01499  81 VRPIleSLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIAWEKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   190 GIFRSEKPAIVG--EPEMPSTIADVAQEKGALLQRRGVEWNYSVTDH-DWAFSDAHGTLENLPLPL---VPQPNAATALA 263
Cdd:TIGR01499 161 GIIKEGVPIVTGeqEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDEnYLSFSGANLFLEPLALSLlgdHQQENAALALA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   264 ALRASGLEV---SENAIRDGIASAILPGRFQIVSE-SPRVIFDVAHNPHAAEYLTGRMKTlPKNGRVLAVI-GMLHDKDI 338
Cdd:TIGR01499 241 ALEVLGKQNpklSEEAIRQGLANTIWPGRLEILSEdNPNILLDGAHNPHSAEALAEWFKK-RFNGRPITLLfGALADKDA 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832453   339 AGTLAWLKSVVD-DWYCAPLEGPRGATAEQLLEHlgNGKSFDSVAQAWDAAMAD---AKAEDTVLVCGSFHTVAHVMEV 413
Cdd:TIGR01499 320 AAMLAPLKPVVDkEVFVTPFDYPRADDAADLAAF--AEETGKSTVEDWREALEEalnASAEDDILVTGSLYLVGEVRKL 396
Mur_ligase_M pfam08245
Mur ligase middle domain;
54-197 2.18e-09

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 56.93  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453    54 VAGTNGKGTTCRTLESILMAAGYKVGvyssphlvcytervrVQGQELPESAHTasfaeiesargdislTYFEYGTLSALW 133
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIG---------------TIGTYIGKSGNT---------------TNNAIGLPLTLA 50

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832453   134 LFKQAQLDVVILEV---GLG-GRLDatNIVDADVAVVTSIALDHTDWLGpDRESIGREKAGIFRSEKP 197
Cdd:pfam08245  51 EMVEAGAEYAVLEVsshGLGeGRLS--GLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEGLPE 115
 
Name Accession Description Interval E-value
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 1-416 0e+00

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 865.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453    1 MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSQVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGV 80
Cdd:PRK10846   1 MINKQTPQATSPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   81 YSSPHLVCYTERVRVQGQELPESAHTASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160
Cdd:PRK10846  81 YSSPHLVRYTERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSD 240
Cdd:PRK10846 161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFSD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  241 AHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHAAEYLTGRMKTL 320
Cdd:PRK10846 241 GDGTLENLPLPNVPLPNAATALAALRASGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  321 PKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLV 400
Cdd:PRK10846 321 PKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAEHLGNGKSFDSVAQAWDAAMADAKPEDTVLV 400

                        410
                 ....*....|....*.
gi 15832453  401 CGSFHTVAHVMEVIDA 416
Cdd:PRK10846 401 CGSFHTVAHVMEVIDA 416
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 11-414 2.15e-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: 481.14  E-value: 2.15e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  11 SPLASWLSYLENLHSKTIDLGLERVSQVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVCYT 90
Cdd:COG0285   2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  91 ERVRVQGQELPESAHTASFAEIESARGDI---SLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVT 167
Cdd:COG0285  82 ERIRINGEPISDEELVEALEEVEPAVEEVdagPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVIT 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 168 SIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGE--PEMPSTIADVAQEKGALLQRRGVEWNYSVTDHD-WAFSDAHGT 244
Cdd:COG0285 162 SIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDqqPEALEVIEERAAELGAPLYRAGRDFSVEEREGAvFSYQGPGGE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 245 LENLPLPL---------------VpqpnaatalAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHA 309
Cdd:COG0285 242 YEDLPLPLlgahqaenaalalaaL---------EALRELGLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAG 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 310 AEYLTGRMKTLPKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHL----GNGKSFDSVAQAW 385
Cdd:COG0285 313 ARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAArelgLRVEVAPDVEEAL 392

                       410       420
                ....*....|....*....|....*....
gi 15832453 386 DAAMADAKAEDTVLVCGSFHTVAHVMEVI 414
Cdd:COG0285 393 EAALELADPDDLILVTGSLYLVGEVRALL 421
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 32-413 6.39e-161

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: 458.67  E-value: 6.39e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453    32 LERVSQVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVCYTERVRVQGQELPESAHTASFAE 111
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   112 IESA--RGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESIGREKA 189
Cdd:TIGR01499  81 VRPIleSLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIAWEKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   190 GIFRSEKPAIVG--EPEMPSTIADVAQEKGALLQRRGVEWNYSVTDH-DWAFSDAHGTLENLPLPL---VPQPNAATALA 263
Cdd:TIGR01499 161 GIIKEGVPIVTGeqEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDEnYLSFSGANLFLEPLALSLlgdHQQENAALALA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   264 ALRASGLEV---SENAIRDGIASAILPGRFQIVSE-SPRVIFDVAHNPHAAEYLTGRMKTlPKNGRVLAVI-GMLHDKDI 338
Cdd:TIGR01499 241 ALEVLGKQNpklSEEAIRQGLANTIWPGRLEILSEdNPNILLDGAHNPHSAEALAEWFKK-RFNGRPITLLfGALADKDA 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832453   339 AGTLAWLKSVVD-DWYCAPLEGPRGATAEQLLEHlgNGKSFDSVAQAWDAAMAD---AKAEDTVLVCGSFHTVAHVMEV 413
Cdd:TIGR01499 320 AAMLAPLKPVVDkEVFVTPFDYPRADDAADLAAF--AEETGKSTVEDWREALEEalnASAEDDILVTGSLYLVGEVRKL 396
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 54-318 2.87e-39

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 147.88  E-value: 2.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   54 VAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVCYTERVRVQGQELPESAHTASFAEI-----ESARGDISL-TYFEYG 127
Cdd:PLN02881  66 VAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYFWWCwdrlkEKTTEDLPMpAYFRFL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  128 TLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAV-VTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIvgepemp 206
Cdd:PLN02881 146 TLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKPVVCgITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAF------- 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  207 sTIADVAQEKGALLQR-RGVEWNYSVTDHdwafSDAHGtLENLPLPL-------------------VPQPNAATALAALR 266
Cdd:PLN02881 219 -TVPQPDEAMRVLEERaSELGVPLQVVEP----LDSYG-LSGLKLGLagehqylnaglavalcstwLQRTGHEEFEALLQ 292

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832453  267 ASGLEVSenaIRDGIASAILPGRFQIVSES-------PRVIF--DVAHNP----HAAEYLTGRMK 318
Cdd:PLN02881 293 AGTLPEQ---FIKGLSTASLQGRAQVVPDSyinsedsGDLVFylDGAHSPesmeACARWFSSAIK 354
PLN02913 PLN02913
dihydrofolate synthetase
 4-337 2.95e-37

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 141.88  E-value: 2.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453    4 KRTPQAASPLASWLSYLENLH---------------SKTIDLGleRVSQVAARLGVLKPAPFVFTVAGTNGKGTTCRTLE 68
Cdd:PLN02913  17 FSSSTEEPELGDFLRYLDSLKnyeksgvpkdagtdsDDGFDLG--RMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   69 SILMAAGYKVGVYSSPHLVCYTERVRVQGQELPESAHTAS--FAE--------IESARGdiSLTYFEYGTLSALWLFKQA 138
Cdd:PLN02913  95 NILRAQGYSVGCYTSPHLRSIRERISVGKLGKPVSTNTLNdlFHGikpildeaIQLENG--SLTHFEVLTALAFKLFAQE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  139 QLDVVILEVGLGGRLDATNIVDAD---VAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMP--------- 206
Cdd:PLN02913 173 NVDIAVIEAGLGGARDATNVIDSSglaASVITTIGEEHLAALGGSLESIALAKSGIIKQGRPVVLGGPFLPhiesilrdk 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  207 --STIADV--AQEKGALLQRRGVEWN----YSVTDHDWAFSDAHGT---LENLPLPLVPQPNAATALAALRAS------G 269
Cdd:PLN02913 253 asSMNSPVvsASDPGVRSSIKGIITDngkpCQSCDIVIRVEKDDPLfieLSDVNLRMLGSHQLQNAVTAACAAlclrdqG 332

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832453  270 LEVSENAIRDGIASAILPGRFQIVSE---------SPRVIFDVAHNPHAAEYLTGRMKTLPKNGRVLAVIGMLHDKD 337
Cdd:PLN02913 333 WRISDASIRAGLENTNLLGRSQFLTSkeaevlglpGATVLLDGAHTKESAKALVDTIKTAFPEARLALVVAMASDKD 409
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 51-405 1.74e-12

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: 68.88  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453    51 VFTVAGTNGKGTTCRTLESILMAAGYKVGVYSsphlvcyTERVRVQGQELPESahtasfaeiesargDISLTYFEYGTL- 129
Cdd:TIGR01085  87 VIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIG-------TIGYRLGGNDLIKN--------------PAALTTPEALTLq 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   130 SALWLFKQAQLDVVILEV---GLG-GRLDAtniVDADVAVVTSIALDHTDWLGpDRESIGREKAGIFRSE-----KPAIV 200
Cdd:TIGR01085 146 STLAEMVEAGAQYAVMEVsshALAqGRVRG---VRFDAAVFTNLSRDHLDFHG-TMENYFAAKASLFTELglkrfAVINL 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   201 GEPEMPSTIADVAQEKGALLQRRGVEW---NYSVTDHDWAFSDAHGTLEN------LPLPLVPQPNAA--TALAALRASG 269
Cdd:TIGR01085 222 DDEYGAQFVKRLPKDITVSAITQPADGraqDIKITDSGYSFEGQQFTFETpageghLHTPLIGRFNVYnlLAALATLLHL 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   270 LEVSENAIRDGIAS-AILPGRFQIV--SESPRVIFDVAHNPHAAEYLtgrMKTL--PKNGRVLAVIGMLHDKD------- 337
Cdd:TIGR01085 302 GGIDLEDIVAALEKfRGVPGRMELVdgGQKFLVIVDYAHTPDALEKA---LRTLrkHKDGRLIVVFGCGGDRDrgkrplm 378

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832453   338 --IAGTLAWLKSVVDDwycapleGPRGATAEQLLEHLGNGKSFDSV-------AQAWDAAMADAKAEDTVLVCGSFH 405
Cdd:TIGR01085 379 gaIAEQLADLVILTSD-------NPRGEDPEQIIADILAGISEKEKvviiadrRQAIRYAISNAKAGDVVLIAGKGH 448
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 34-405 1.43e-10

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: 63.18  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   34 RVSQVAARLGVLKPAPF--------VFTVAGTNGKGTTCRTLESILMAAGYKVGVYSsphlvcyTERVRVQGQELPesah 105
Cdd:PRK11929  89 PVADLRKALGELAARWYgrpseqlsLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIG-------TLGARLDGRLIP---- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  106 tasfaeiesargdISLTYFEYGTLSA-LWLFKQAQLDVVILEV---GLG-GRLDATNIvdaDVAVVTSIALDHTDWLGpD 180
Cdd:PRK11929 158 -------------GSLTTPDAIILHRiLARMRAAGADAVAMEAsshGLEqGRLDGLRI---AVAGFTNLTRDHLDYHG-T 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  181 RESIGREKAGIFRSEKP---AIVG--EPEMPSTIAD--VAQEKGALLQRRGVEW---NYSVTDHDWAFS--DAHGTLEnL 248
Cdd:PRK11929 221 MQDYEEAKAALFSKLPGlgaAVINadDPAAARLLAAlpRGLKVGYSPQNAGADVqarDLRATAHGQVFTlaTPDGSYQ-L 299

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  249 PLPLVPQPNAA-TALAALRASGLEVSENAIRDGIAS-AILPGRFQIVSES-----PRVIFDVAHNPHAAEYLTGRMKTLP 321
Cdd:PRK11929 300 VTRLLGRFNVSnLLLVAAALKKLGLPLAQIARALAAvSPVPGRMERVGPTagaqgPLVVVDYAHTPDALAKALTALRPVA 379

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  322 --KNGRVLAVIGMLHDKD---------IAGTLAWLKSVVDDwycapleGPRGATAEQLLEHL--GNGKSFDSV-----AQ 383
Cdd:PRK11929 380 qaRNGRLVCVFGCGGDRDkgkrpemgrIAAELADRVVVTSD-------NPRSEAPEAIIDQIlaGIPAGARVFvisdrAE 452

                        410       420
                 ....*....|....*....|..
gi 15832453  384 AWDAAMADAKAEDTVLVCGSFH 405
Cdd:PRK11929 453 AIRQAIWMAAPGDVILIAGKGH 474
Mur_ligase_M pfam08245
Mur ligase middle domain;
54-197 2.18e-09

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 56.93  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453    54 VAGTNGKGTTCRTLESILMAAGYKVGvyssphlvcytervrVQGQELPESAHTasfaeiesargdislTYFEYGTLSALW 133
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIG---------------TIGTYIGKSGNT---------------TNNAIGLPLTLA 50

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832453   134 LFKQAQLDVVILEV---GLG-GRLDatNIVDADVAVVTSIALDHTDWLGpDRESIGREKAGIFRSEKP 197
Cdd:pfam08245  51 EMVEAGAEYAVLEVsshGLGeGRLS--GLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEGLPE 115
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 54-402 2.81e-08

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: 55.47  E-value: 2.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  54 VAGTNGKGTTCRTLESILMAAGYKVGVYSsphlvcyTERVRVQGQELPeSAHTASFAeiesargdISLtyfeYGTLSAlw 133
Cdd:COG0769  85 VTGTNGKTTTTYLLAQILRALGKKTGLIG-------TVGNGIGGELIP-SSLTTPEA--------LDL----QRLLAE-- 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 134 lFKQAQLDVVILEV---GLG-GRLDATNIvdaDVAVVTSIALDHTDWLGpDRESIGREKAGIFRSEKP---AIV------ 200
Cdd:COG0769 143 -MVDAGVTHVVMEVsshALDqGRVDGVRF---DVAVFTNLTRDHLDYHG-TMEAYFAAKARLFDQLGPggaAVInaddpy 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 201 GEP---EMPSTIADVAQEKGALLqrRGVEWNYSVTDHDWAFSDAHGTLE-NLPLP--------------LVpqpnaatal 262
Cdd:COG0769 218 GRRlaaAAPARVITYGLKADADL--RATDIELSADGTRFTLVTPGGEVEvRLPLIgrfnvynalaaiaaAL--------- 286

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 263 aalrasGLEVSENAIRDGIAS-AILPGRFQIVSES--PRVIFDVAHNPHAAEYLtgrMKTLPK--NGRVLAVIGMLHDKD 337
Cdd:COG0769 287 ------ALGIDLEEILAALEKlKGVPGRMERVDGGqgPTVIVDYAHTPDALENV---LEALRPhtKGRLIVVFGCGGDRD 357

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 338 ---------IAGTLAWLksVV--DDWycaplegPRG----ATAEQLLEHLGNGKSFDSV---AQAWDAAMADAKAEDTVL 399
Cdd:COG0769 358 rgkrplmgeIAARLADV--VIvtSDN-------PRSedpaAIIADILAGIPGAGKVLVIpdrAEAIRYAIALAKPGDVVL 428


                ...
gi 15832453 400 VCG 402
Cdd:COG0769 429 IAG 431
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 51-173 1.70e-07

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 53.62  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   51 VFTVAGTNGKGTTCRTLESILMAAGYKVGVYSsphlvcyTERVRVQGQEL-------PESAH------TASFAEIESARG 117
Cdd:PRK14016 482 IVAVTGTNGKTTTTRLIAHILKLSGKRVGMTT-------TDGVYIDGRLIdkgdctgPKSARrvlmnpDVEAAVLETARG 554

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15832453  118 disltyfeygtlsalwlfkqaqldvVILEVGLGGRLdatnivdADVAVVTSIALDH 173
Cdd:PRK14016 555 -------------------------GILREGLAYDR-------CDVGVVTNIGEDH 578
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 35-402 1.19e-04

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 43.97  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453   35 VSQVAARLGVL------KPAPFVFTVA--GTNGKGTTCRTLESILMAAGYKVGVYSsphlvcyTERVRVQGQELPeSAHT 106
Cdd:PRK00139  73 VPDLRKALALLaaafygHPSDKLKLIGvtGTNGKTTTAYLLAQILRLLGEKTALIG-------TLGNGIGGELIP-SGLT 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  107 asfaeiesargdisltyfeygTLSALWLFKQ-AQL-----DVVILEV---GLG-GRLDATNIvdaDVAVVTSIALDHTDW 176
Cdd:PRK00139 145 ---------------------TPDALDLQRLlAELvdagvTYAAMEVsshALDqGRVDGLKF---DVAVFTNLSRDHLDY 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  177 lGPDRESIGREKAGIF-RSEKPAIVGepempstiADvaQEKGALLQRRGVEWNYSVTDHDWAFSDAHGTLE--------- 246
Cdd:PRK00139 201 -HGTMEDYLAAKARLFsELGLAAVIN--------AD--DEVGRRLLALPDAYAVSMAGADLRATDVEYTDSgqtftlvte 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  247 -NLPLPlvpqpnaatalaalrasG----------------LEVSENAIRDGIAS-AILPGRFQIVSES--PRVIFDVAHN 306
Cdd:PRK00139 270 vESPLI-----------------GrfnvsnllaalaallaLGVPLEDALAALAKlQGVPGRMERVDAGqgPLVIVDYAHT 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  307 PHAAEYLtgrMKTLPK--NGRVLAVIGMLHDKD---------IAGTLAwLKSVV--DDwycaplegPRG----ATAEQLL 369
Cdd:PRK00139 333 PDALEKV---LEALRPhaKGRLICVFGCGGDRDkgkrplmgaIAERLA-DVVIVtsDN--------PRSedpaAIIADIL 400

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 15832453  370 EHlgngksFDSV----AQAWDAAMADAKAEDTVLVCG 402
Cdd:PRK00139 401 AG------IYDViedrAEAIRYAIAQAKPGDVVLIAG 431
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 287-339 3.50e-04

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: 39.25  E-value: 3.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15832453   287 PGRFQIVSES--PRVIFDVAHNPHAAEYLTGRMKTLPkNGRVLAVIGMLHDKDIA 339
Cdd:pfam02875   2 PGRLEVVGENngVLVIDDYAHNPDAMEAALRALRNLF-PGRLILVFGGMGDRDAE 55
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
144-341 6.65e-04

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


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 41.95  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  144 ILEVG----LGGRLDAtniVDADVAVVTSIALDHTDWLG-PDRESIGREKAGIFRSEKPAIV-GEPEMPSTIADVAQEKG 217
Cdd:PRK14022 182 IMEVSsqayLVGRVYG---LTFDVGVFLNITPDHIGPIEhPTFEDYFYHKRLLMENSKAVVVnSDMDHFSELLEQVTPQE 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453  218 ALLQrrGVEWNYSVTDHDwAFS-DAHGTLE-NLPLPLVPQPNAATALAALRAS-GLEVSENAIRDGIASAILPGRFQIVS 294
Cdd:PRK14022 259 HDFY--GIDSENQIMASN-AFSfEATGKLAgTYDIQLIGKFNQENAMAAGLAClRLGASLEDIQKGIAQTPVPGRMEVLT 335

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15832453  295 ES--PRVIFDVAHNPHAAEYLTGRMKTLPKnGRVLAVIGMLHDKDIAGT 341
Cdd:PRK14022 336 QSngAKVFIDYAHNGDSLNKLIDVVEEHQK-GKLILLLGAAGNKGESRR 383
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 141-403 6.33e-03

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: 38.54  E-value: 6.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 141 DVVILEVG---LG--GRLdaTNIVDADVAVVTSIALDHTDWLGpDRESIGREKAGIFRSEKP---AIVGE---------P 203
Cdd:COG0770 153 EFAVLEMGmnhPGeiAYL--ARIARPDIAVITNIGPAHLEGFG-SLEGIARAKGEIFEGLPPggvAVLNAddpllaalaE 229

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 204 EMPSTIADVAQEKGALLQRRGVEWNysvtDHDWAFsDAHGTLENLPLPLvPQPnaatalaalrasG-------------- 269
Cdd:COG0770 230 RAKARVLTFGLSEDADVRAEDIELD----EDGTRF-TLHTPGGELEVTL-PLP------------Grhnvsnalaaaava 291

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832453 270 --LEVSENAIRDGIASAIL-PGRFQIV--SESPRVIFDV--AhNPH----AAEYLtgrmKTLPKNGRVLAVIG-ML---- 333
Cdd:COG0770 292 laLGLDLEEIAAGLAAFQPvKGRLEVIegAGGVTLIDDSynA-NPDsmkaALDVL----AQLPGGGRRIAVLGdMLelge 366

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832453 334 -----HdKDIAGTLAwlKSVVDDWYCAplegprGATAEQLLEHLG--NGKSFDSVAQAWDAAMADAKAEDTVLVCGS 403
Cdd:COG0770 367 eseelH-REVGELAA--ELGIDRLFTV------GELARAIAEAAGgeRAEHFEDKEELLAALKALLRPGDVVLVKGS 434
 
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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