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Conserved domains on  [gi|16130250|ref|NP_416818|]
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bifunctional folylpolyglutamate synthetase/dihydrofolate synthetase [Escherichia coli str. K-12 substr. MG1655]

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: 865.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250    1 MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGV 80
Cdd:PRK10846   1 MINKQTPQATSPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   81 YSSPHLVRYTERVRVQGQELPESAHTASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160
Cdd:PRK10846  81 YSSPHLVRYTERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSD 240
Cdd:PRK10846 161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFSD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  241 AHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHAAEYLTGRMKAL 320
Cdd:PRK10846 241 GDGTLENLPLPNVPLPNAATALAALRASGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  321 PKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLV 400
Cdd:PRK10846 321 PKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAEHLGNGKSFDSVAQAWDAAMADAKPEDTVLV 400

                        410
                 ....*....|....*.
gi 16130250  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: 865.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250    1 MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGV 80
Cdd:PRK10846   1 MINKQTPQATSPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   81 YSSPHLVRYTERVRVQGQELPESAHTASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160
Cdd:PRK10846  81 YSSPHLVRYTERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSD 240
Cdd:PRK10846 161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFSD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  241 AHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHAAEYLTGRMKAL 320
Cdd:PRK10846 241 GDGTLENLPLPNVPLPNAATALAALRASGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  321 PKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLV 400
Cdd:PRK10846 321 PKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAEHLGNGKSFDSVAQAWDAAMADAKPEDTVLV 400

                        410
                 ....*....|....*.
gi 16130250  401 CGSFHTVAHVMEVIDA 416
Cdd:PRK10846 401 CGSFHTVAHVMEVIDA 416
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 11-414 1.22e-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: 481.91  E-value: 1.22e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  11 SPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVRYT 90
Cdd:COG0285   2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  91 ERVRVQGQELPESAHTASFAEIESARGDI---SLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVT 167
Cdd:COG0285  82 ERIRINGEPISDEELVEALEEVEPAVEEVdagPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVIT 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 168 SIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGE--PEMPSTIADVAQEKGALLQRRGVEWNYSVTDHD-WAFSDAHGT 244
Cdd:COG0285 162 SIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDqqPEALEVIEERAAELGAPLYRAGRDFSVEEREGAvFSYQGPGGE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 245 LENLPLPL---------------VpqpnaatalAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHA 309
Cdd:COG0285 242 YEDLPLPLlgahqaenaalalaaL---------EALRELGLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAG 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 310 AEYLTGRMKALPKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHL----GNGKSFDSVAQAW 385
Cdd:COG0285 313 ARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAArelgLRVEVAPDVEEAL 392

                       410       420
                ....*....|....*....|....*....
gi 16130250 386 DAAMADAKAEDTVLVCGSFHTVAHVMEVI 414
Cdd:COG0285 393 EAALELADPDDLILVTGSLYLVGEVRALL 421
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 32-413 3.01e-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: 459.44  E-value: 3.01e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250    32 LERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTASFAE 111
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   112 IESA--RGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESIGREKA 189
Cdd:TIGR01499  81 VRPIleSLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIAWEKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   190 GIFRSEKPAIVG--EPEMPSTIADVAQEKGALLQRRGVEWNYSVTDH-DWAFSDAHGTLENLPLPL---VPQPNAATALA 263
Cdd:TIGR01499 161 GIIKEGVPIVTGeqEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDEnYLSFSGANLFLEPLALSLlgdHQQENAALALA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   264 ALRASGLEV---SENAIRDGIASAILPGRFQIVSE-SPRVIFDVAHNPHAAEYLTGRMKaLPKNGRVLAVI-GMLHDKDI 338
Cdd:TIGR01499 241 ALEVLGKQNpklSEEAIRQGLANTIWPGRLEILSEdNPNILLDGAHNPHSAEALAEWFK-KRFNGRPITLLfGALADKDA 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130250   339 AGTLAWLKSVVD-DWYCAPLEGPRGATAEQLLEHlgNGKSFDSVAQAWDAAMAD---AKAEDTVLVCGSFHTVAHVMEV 413
Cdd:TIGR01499 320 AAMLAPLKPVVDkEVFVTPFDYPRADDAADLAAF--AEETGKSTVEDWREALEEalnASAEDDILVTGSLYLVGEVRKL 396
Mur_ligase_M pfam08245
Mur ligase middle domain;
54-197 2.63e-09

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 56.54  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250    54 VAGTNGKGTTCRTLESILMAAGYKVGvyssphlvrytervrVQGQELPESAHTasfaeiesargdislTYFEYGTLSALW 133
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIG---------------TIGTYIGKSGNT---------------TNNAIGLPLTLA 50

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130250   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: 865.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250    1 MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGV 80
Cdd:PRK10846   1 MINKQTPQATSPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   81 YSSPHLVRYTERVRVQGQELPESAHTASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160
Cdd:PRK10846  81 YSSPHLVRYTERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSD 240
Cdd:PRK10846 161 ADVAVVTSIALDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFSD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  241 AHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHAAEYLTGRMKAL 320
Cdd:PRK10846 241 GDGTLENLPLPNVPLPNAATALAALRASGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  321 PKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLV 400
Cdd:PRK10846 321 PKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAEHLGNGKSFDSVAQAWDAAMADAKPEDTVLV 400

                        410
                 ....*....|....*.
gi 16130250  401 CGSFHTVAHVMEVIDA 416
Cdd:PRK10846 401 CGSFHTVAHVMEVIDA 416
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 11-414 1.22e-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: 481.91  E-value: 1.22e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  11 SPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVRYT 90
Cdd:COG0285   2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  91 ERVRVQGQELPESAHTASFAEIESARGDI---SLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVT 167
Cdd:COG0285  82 ERIRINGEPISDEELVEALEEVEPAVEEVdagPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVIT 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 168 SIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGE--PEMPSTIADVAQEKGALLQRRGVEWNYSVTDHD-WAFSDAHGT 244
Cdd:COG0285 162 SIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDqqPEALEVIEERAAELGAPLYRAGRDFSVEEREGAvFSYQGPGGE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 245 LENLPLPL---------------VpqpnaatalAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHA 309
Cdd:COG0285 242 YEDLPLPLlgahqaenaalalaaL---------EALRELGLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAG 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 310 AEYLTGRMKALPKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHL----GNGKSFDSVAQAW 385
Cdd:COG0285 313 ARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAArelgLRVEVAPDVEEAL 392

                       410       420
                ....*....|....*....|....*....
gi 16130250 386 DAAMADAKAEDTVLVCGSFHTVAHVMEVI 414
Cdd:COG0285 393 EAALELADPDDLILVTGSLYLVGEVRALL 421
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 32-413 3.01e-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: 459.44  E-value: 3.01e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250    32 LERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTASFAE 111
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   112 IESA--RGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESIGREKA 189
Cdd:TIGR01499  81 VRPIleSLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIAWEKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   190 GIFRSEKPAIVG--EPEMPSTIADVAQEKGALLQRRGVEWNYSVTDH-DWAFSDAHGTLENLPLPL---VPQPNAATALA 263
Cdd:TIGR01499 161 GIIKEGVPIVTGeqEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDEnYLSFSGANLFLEPLALSLlgdHQQENAALALA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   264 ALRASGLEV---SENAIRDGIASAILPGRFQIVSE-SPRVIFDVAHNPHAAEYLTGRMKaLPKNGRVLAVI-GMLHDKDI 338
Cdd:TIGR01499 241 ALEVLGKQNpklSEEAIRQGLANTIWPGRLEILSEdNPNILLDGAHNPHSAEALAEWFK-KRFNGRPITLLfGALADKDA 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130250   339 AGTLAWLKSVVD-DWYCAPLEGPRGATAEQLLEHlgNGKSFDSVAQAWDAAMAD---AKAEDTVLVCGSFHTVAHVMEV 413
Cdd:TIGR01499 320 AAMLAPLKPVVDkEVFVTPFDYPRADDAADLAAF--AEETGKSTVEDWREALEEalnASAEDDILVTGSLYLVGEVRKL 396
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 54-319 1.74e-39

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 148.27  E-value: 1.74e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   54 VAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTASFAEI-----ESARGDISL-TYFEYG 127
Cdd:PLN02881  66 VAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYFWWCwdrlkEKTTEDLPMpAYFRFL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  128 TLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAV-VTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIvgepemp 206
Cdd:PLN02881 146 TLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKPVVCgITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAF------- 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  207 sTIADVAQEKGALLQR-RGVEWNYSVTDHdwafSDAHGtLENLPLPL-------------------VPQPNAATALAALR 266
Cdd:PLN02881 219 -TVPQPDEAMRVLEERaSELGVPLQVVEP----LDSYG-LSGLKLGLagehqylnaglavalcstwLQRTGHEEFEALLQ 292

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130250  267 ASGLEVSenaIRDGIASAILPGRFQIVSES-------PRVIF--DVAHNP----HAAEYLTGRMKA 319
Cdd:PLN02881 293 AGTLPEQ---FIKGLSTASLQGRAQVVPDSyinsedsGDLVFylDGAHSPesmeACARWFSSAIKG 355
PLN02913 PLN02913
dihydrofolate synthetase
 4-337 6.40e-36

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 138.03  E-value: 6.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250    4 KRTPQAASPLASWLSYLENLH---------------SKTIDLGleRVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLE 68
Cdd:PLN02913  17 FSSSTEEPELGDFLRYLDSLKnyeksgvpkdagtdsDDGFDLG--RMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   69 SILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTAS--FAE--------IESARGdiSLTYFEYGTLSALWLFKQA 138
Cdd:PLN02913  95 NILRAQGYSVGCYTSPHLRSIRERISVGKLGKPVSTNTLNdlFHGikpildeaIQLENG--SLTHFEVLTALAFKLFAQE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  139 QLDVVILEVGLGGRLDATNIVDAD---VAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMP--------- 206
Cdd:PLN02913 173 NVDIAVIEAGLGGARDATNVIDSSglaASVITTIGEEHLAALGGSLESIALAKSGIIKQGRPVVLGGPFLPhiesilrdk 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  207 --STIADV--AQEKGALLQRRGVEWN----YSVTDHDWAFSDAHGT---LENLPLPLVPQPNAATALAALRAS------G 269
Cdd:PLN02913 253 asSMNSPVvsASDPGVRSSIKGIITDngkpCQSCDIVIRVEKDDPLfieLSDVNLRMLGSHQLQNAVTAACAAlclrdqG 332

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130250  270 LEVSENAIRDGIASAILPGRFQIVSE---------SPRVIFDVAHNPHAAEYLTGRMKALPKNGRVLAVIGMLHDKD 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 8.59e-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: 69.65  E-value: 8.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250    51 VFTVAGTNGKGTTCRTLESILMAAGYKVGVYSsphlvryTERVRVQGQELPESahtasfaeiesargDISLTYFEYGTL- 129
Cdd:TIGR01085  87 VIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIG-------TIGYRLGGNDLIKN--------------PAALTTPEALTLq 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   130 SALWLFKQAQLDVVILEV---GLG-GRLDAtniVDADVAVVTSIALDHTDWLGpDRESIGREKAGIFRSE-----KPAIV 200
Cdd:TIGR01085 146 STLAEMVEAGAQYAVMEVsshALAqGRVRG---VRFDAAVFTNLSRDHLDFHG-TMENYFAAKASLFTELglkrfAVINL 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   201 GEPEMPSTIADVAQEKGALLQRRGVEW---NYSVTDHDWAFSDAHGTLEN------LPLPLVPQPNAA--TALAALRASG 269
Cdd:TIGR01085 222 DDEYGAQFVKRLPKDITVSAITQPADGraqDIKITDSGYSFEGQQFTFETpageghLHTPLIGRFNVYnlLAALATLLHL 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   270 LEVSENAIRDGIAS-AILPGRFQIV--SESPRVIFDVAHNPHAAEYLTGRMKALPKnGRVLAVIGMLHDKD--------- 337
Cdd:TIGR01085 302 GGIDLEDIVAALEKfRGVPGRMELVdgGQKFLVIVDYAHTPDALEKALRTLRKHKD-GRLIVVFGCGGDRDrgkrplmga 380

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130250   338 IAGTLAWLKSVVDDwycapleGPRGATAEQLLEHLGNGKSFDSV-------AQAWDAAMADAKAEDTVLVCGSFH 405
Cdd:TIGR01085 381 IAEQLADLVILTSD-------NPRGEDPEQIIADILAGISEKEKvviiadrRQAIRYAISNAKAGDVVLIAGKGH 448
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 51-405 3.58e-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: 62.03  E-value: 3.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   51 VFTVAGTNGKGTTCRTLESILMAAGYKVGVYSsphlvryTERVRVQGQELPesahtasfaeiesargdISLTYFEYGTLS 130
Cdd:PRK11929 114 LVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIG-------TLGARLDGRLIP-----------------GSLTTPDAIILH 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  131 A-LWLFKQAQLDVVILEV---GLG-GRLDATNIvdaDVAVVTSIALDHTDWLGpDRESIGREKAGIFRSEKP---AIVG- 201
Cdd:PRK11929 170 RiLARMRAAGADAVAMEAsshGLEqGRLDGLRI---AVAGFTNLTRDHLDYHG-TMQDYEEAKAALFSKLPGlgaAVINa 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  202 -EPEMPSTIAD--VAQEKGALLQRRGVEW---NYSVTDHDWAFS--DAHGTLEnLPLPLVPQPNAA-TALAALRASGLEV 272
Cdd:PRK11929 246 dDPAAARLLAAlpRGLKVGYSPQNAGADVqarDLRATAHGQVFTlaTPDGSYQ-LVTRLLGRFNVSnLLLVAAALKKLGL 324

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  273 SENAIRDGIAS-AILPGRFQIVSES-----PRVIFDVAHNPHAAEYLTGRMKALP--KNGRVLAVIGMLHDKD------- 337
Cdd:PRK11929 325 PLAQIARALAAvSPVPGRMERVGPTagaqgPLVVVDYAHTPDALAKALTALRPVAqaRNGRLVCVFGCGGDRDkgkrpem 404

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130250  338 --IAGTLAWLKSVVDDwycapleGPRGATAEQLLEHL--GNGKSFDSV-----AQAWDAAMADAKAEDTVLVCGSFH 405
Cdd:PRK11929 405 grIAAELADRVVVTSD-------NPRSEAPEAIIDQIlaGIPAGARVFvisdrAEAIRQAIWMAAPGDVILIAGKGH 474
Mur_ligase_M pfam08245
Mur ligase middle domain;
54-197 2.63e-09

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 56.54  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250    54 VAGTNGKGTTCRTLESILMAAGYKVGvyssphlvrytervrVQGQELPESAHTasfaeiesargdislTYFEYGTLSALW 133
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIG---------------TIGTYIGKSGNT---------------TNNAIGLPLTLA 50

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130250   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 2.12e-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: 55.86  E-value: 2.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  54 VAGTNGKGTTCRTLESILMAAGYKVGVYSsphlvryTERVRVQGQELPeSAHTASFAeiesargdISLtyfeYGTLSAlw 133
Cdd:COG0769  85 VTGTNGKTTTTYLLAQILRALGKKTGLIG-------TVGNGIGGELIP-SSLTTPEA--------LDL----QRLLAE-- 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 134 lFKQAQLDVVILEV---GLG-GRLDATNIvdaDVAVVTSIALDHTDWLGpDRESIGREKAGIFRSEKP---AIV------ 200
Cdd:COG0769 143 -MVDAGVTHVVMEVsshALDqGRVDGVRF---DVAVFTNLTRDHLDYHG-TMEAYFAAKARLFDQLGPggaAVInaddpy 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 201 GEP---EMPSTIADVAQEKGALLqrRGVEWNYSVTDHDWAFSDAHGTLE-NLPLP--------------LVpqpnaatal 262
Cdd:COG0769 218 GRRlaaAAPARVITYGLKADADL--RATDIELSADGTRFTLVTPGGEVEvRLPLIgrfnvynalaaiaaAL--------- 286

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 263 aalrasGLEVSENAIRDGIAS-AILPGRFQIVSES--PRVIFDVAHNPHAAEyltgrmKALP-----KNGRVLAVIGMLH 334
Cdd:COG0769 287 ------ALGIDLEEILAALEKlKGVPGRMERVDGGqgPTVIVDYAHTPDALE------NVLEalrphTKGRLIVVFGCGG 354

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 335 DKD---------IAGTLAWLksVV--DDWycaplegPRG----ATAEQLLEHLGNGKSFDSV---AQAWDAAMADAKAED 396
Cdd:COG0769 355 DRDrgkrplmgeIAARLADV--VIvtSDN-------PRSedpaAIIADILAGIPGAGKVLVIpdrAEAIRYAIALAKPGD 425


                ....*.
gi 16130250 397 TVLVCG 402
Cdd:COG0769 426 VVLIAG 431
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 51-173 2.18e-07

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 53.24  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   51 VFTVAGTNGKGTTCRTLESILMAAGYKVGVYSsphlvryTERVRVQGQEL-------PESAH------TASFAEIESARG 117
Cdd:PRK14016 482 IVAVTGTNGKTTTTRLIAHILKLSGKRVGMTT-------TDGVYIDGRLIdkgdctgPKSARrvlmnpDVEAAVLETARG 554

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130250  118 disltyfeygtlsalwlfkqaqldvVILEVGLGGRLdatnivdADVAVVTSIALDH 173
Cdd:PRK14016 555 -------------------------GILREGLAYDR-------CDVGVVTNIGEDH 578
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 287-339 2.69e-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: 39.63  E-value: 2.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16130250   287 PGRFQIVSES--PRVIFDVAHNPHAAEyLTGRMKALPKNGRVLAVIGMLHDKDIA 339
Cdd:pfam02875   2 PGRLEVVGENngVLVIDDYAHNPDAME-AALRALRNLFPGRLILVFGGMGDRDAE 55
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 54-402 2.84e-04

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 42.81  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250   54 VAGTNGKGTTCRTLESILMAAGYKVGVYSsphlvryTERVRVQGQELPeSAHTasfaeiesargdisltyfeygTLSALW 133
Cdd:PRK00139 100 VTGTNGKTTTAYLLAQILRLLGEKTALIG-------TLGNGIGGELIP-SGLT---------------------TPDALD 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  134 LFKQ-AQL-----DVVILEV---GLG-GRLDATNIvdaDVAVVTSIALDHTDWlGPDRESIGREKAGIF-RSEKPAIVGe 202
Cdd:PRK00139 151 LQRLlAELvdagvTYAAMEVsshALDqGRVDGLKF---DVAVFTNLSRDHLDY-HGTMEDYLAAKARLFsELGLAAVIN- 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  203 pempstiADvaQEKGALLQRRGVEWNYSVTDHDWAFSDAHGTLE----------NLPLPlvpqpnaatalaalrasG--- 269
Cdd:PRK00139 226 -------AD--DEVGRRLLALPDAYAVSMAGADLRATDVEYTDSgqtftlvtevESPLI-----------------Grfn 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  270 -------------LEVSENAIRDGIAS-AILPGRFQIVSES--PRVIFDVAHNPHAAEYLtgrMKALPK--NGRVLAVIG 331
Cdd:PRK00139 280 vsnllaalaallaLGVPLEDALAALAKlQGVPGRMERVDAGqgPLVIVDYAHTPDALEKV---LEALRPhaKGRLICVFG 356

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  332 MLHDKD---------IAGTLAwLKSVV--DDwycaplegPRG----ATAEQLLEHlgngksFDSV----AQAWDAAMADA 392
Cdd:PRK00139 357 CGGDRDkgkrplmgaIAERLA-DVVIVtsDN--------PRSedpaAIIADILAG------IYDViedrAEAIRYAIAQA 421

                        410
                 ....*....|
gi 16130250  393 KAEDTVLVCG 402
Cdd:PRK00139 422 KPGDVVLIAG 431
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
144-341 1.74e-03

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


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 40.41  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  144 ILEVG----LGGRLDAtniVDADVAVVTSIALDHTDWLG-PDRESIGREKAGIFRSEKPAIV-GEPEMPSTIADVAQEKG 217
Cdd:PRK14022 182 IMEVSsqayLVGRVYG---LTFDVGVFLNITPDHIGPIEhPTFEDYFYHKRLLMENSKAVVVnSDMDHFSELLEQVTPQE 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250  218 ALLQrrGVEWNYSVTDHDwAFS-DAHGTLE-NLPLPLVPQPNAATALAALRAS-GLEVSENAIRDGIASAILPGRFQIVS 294
Cdd:PRK14022 259 HDFY--GIDSENQIMASN-AFSfEATGKLAgTYDIQLIGKFNQENAMAAGLAClRLGASLEDIQKGIAQTPVPGRMEVLT 335

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 16130250  295 ES--PRVIFDVAHNPHAAEYLTGRMKALPKnGRVLAVIGMLHDKDIAGT 341
Cdd:PRK14022 336 QSngAKVFIDYAHNGDSLNKLIDVVEEHQK-GKLILLLGAAGNKGESRR 383
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 141-403 4.09e-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: 39.31  E-value: 4.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 141 DVVILEVG---LG--GRLdaTNIVDADVAVVTSIALDHTDWLGpDRESIGREKAGIFRSEKP---AIVGE---------P 203
Cdd:COG0770 153 EFAVLEMGmnhPGeiAYL--ARIARPDIAVITNIGPAHLEGFG-SLEGIARAKGEIFEGLPPggvAVLNAddpllaalaE 229

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 204 EMPSTIADVAQEKGALLQRRGVEWNysvtDHDWAFsDAHGTLENLPLPLvPQPnaatalaalrasG-------------- 269
Cdd:COG0770 230 RAKARVLTFGLSEDADVRAEDIELD----EDGTRF-TLHTPGGELEVTL-PLP------------Grhnvsnalaaaava 291

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 270 --LEVSENAIRDGIASAIL-PGRFQIV--SESPRVIFDV--AhNPHAaeyltgrMKA-------LPKNGRVLAVIG-ML- 333
Cdd:COG0770 292 laLGLDLEEIAAGLAAFQPvKGRLEVIegAGGVTLIDDSynA-NPDS-------MKAaldvlaqLPGGGRRIAVLGdMLe 363

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130250 334 --------HdKDIAGTLAwlKSVVDDWYCAplegprGATAEQLLEHLG--NGKSFDSVAQAWDAAMADAKAEDTVLVCGS 403
Cdd:COG0770 364 lgeeseelH-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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