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Conserved domains on  [gi|2414964148|ref|WP_268959339|]
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Mur ligase family protein, partial [Pseudomonas amygdali]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10846 super family cl32591
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 3-254 2.42e-119

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


The actual alignment was detected with superfamily member PRK10846:

Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 347.45  E-value: 2.42e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148   3 STSLSDWLAYLEQLHPSAIDMGLDRSRQVAQQLGLTRPAPRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRY 82
Cdd:PRK10846   10 TSPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  83 NERVKVQGVEATDLELCDAFAAVEAARGDVTLTYFEMGTLAAFWLFEQARLDAVVLEVGLGGRLDAVNLVDADFALVTSI 162
Cdd:PRK10846   90 TERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148 163 GVDHAEYLGNTRESVAFEKAGIFRAGCPALCGDPEPPEPLLAKARELGCPLLMRGRDFDLSIGKDSWDWRgvahGEQVEL 242
Cdd:PRK10846  170 ALDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFS----DGDGTL 245

                         250
                  ....*....|..
gi 2414964148 243 RGLPLLDLPMQN 254
Cdd:PRK10846  246 ENLPLPNVPLPN 257
 
Name Accession Description Interval E-value
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 3-254 2.42e-119

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 347.45  E-value: 2.42e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148   3 STSLSDWLAYLEQLHPSAIDMGLDRSRQVAQQLGLTRPAPRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRY 82
Cdd:PRK10846   10 TSPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  83 NERVKVQGVEATDLELCDAFAAVEAARGDVTLTYFEMGTLAAFWLFEQARLDAVVLEVGLGGRLDAVNLVDADFALVTSI 162
Cdd:PRK10846   90 TERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148 163 GVDHAEYLGNTRESVAFEKAGIFRAGCPALCGDPEPPEPLLAKARELGCPLLMRGRDFDLSIGKDSWDWRgvahGEQVEL 242
Cdd:PRK10846  170 ALDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFS----DGDGTL 245

                         250
                  ....*....|..
gi 2414964148 243 RGLPLLDLPMQN 254
Cdd:PRK10846  246 ENLPLPNVPLPN 257
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 4-248 5.35e-115

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: 336.31  E-value: 5.35e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148   4 TSLSDWLAYLEQLHPSAIDMGLDRSRQVAQQLGLTRPAPRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYN 83
Cdd:COG0285     2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  84 ERVKVQGVEATDLELCDAFAAVEAARGDV---TLTYFEMGTLAAFWLFEQARLDAVVLEVGLGGRLDAVNLVDADFALVT 160
Cdd:COG0285    82 ERIRINGEPISDEELVEALEEVEPAVEEVdagPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVIT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148 161 SIGVDHAEYLGNTRESVAFEKAGIFRAGCPALCGDPEPP--EPLLAKARELGCPLLMRGRDFDLS-IGKDSWDWRGvAHG 237
Cdd:COG0285   162 SIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEalEVIEERAAELGAPLYRAGRDFSVEeREGAVFSYQG-PGG 240

                         250
                  ....*....|.
gi 2414964148 238 EQVELRgLPLL 248
Cdd:COG0285   241 EYEDLP-LPLL 250
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 25-233 7.78e-84

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: 256.06  E-value: 7.78e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  25 LDRSRQVAQQLGLTRPAPRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYNERVKVQGVEATDLELCDAFAA 104
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148 105 VEAA--RGDVTLTYFEMGTLAAFWLFEQARLDAVVLEVGLGGRLDAVNLVDADFALVTSIGVDHAEYLGNTRESVAFEKA 182
Cdd:TIGR01499  81 VRPIleSLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIAWEKA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2414964148 183 GIFRAGCPALCGD--PEPPEPLLAKARELGCPLLMRGRDFDLSIGK-DSWDWRG 233
Cdd:TIGR01499 161 GIIKEGVPIVTGEqePEALNVLKKKAQEKGAPLFVVGRDFNYSETDeNYLSFSG 214
Mur_ligase_M pfam08245
Mur ligase middle domain;
47-185 4.97e-12

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 63.09  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  47 VTGTNGKGSTCAFVAALLQAQGLK---VGVYSSPHLIRYNERVKVQgveatdlelcdafaaveaargdvtLTYFEMgtla 123
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVigtIGTYIGKSGNTTNNAIGLP------------------------LTLAEM---- 52

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2414964148 124 afwlfEQARLDAVVLEV---GLG-GRLDavNLVDADFALVTSIGVDHAEYLGnTRESVAFEKAGIF 185
Cdd:pfam08245  53 -----VEAGAEYAVLEVsshGLGeGRLS--GLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELF 110
 
Name Accession Description Interval E-value
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 3-254 2.42e-119

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 347.45  E-value: 2.42e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148   3 STSLSDWLAYLEQLHPSAIDMGLDRSRQVAQQLGLTRPAPRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRY 82
Cdd:PRK10846   10 TSPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  83 NERVKVQGVEATDLELCDAFAAVEAARGDVTLTYFEMGTLAAFWLFEQARLDAVVLEVGLGGRLDAVNLVDADFALVTSI 162
Cdd:PRK10846   90 TERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148 163 GVDHAEYLGNTRESVAFEKAGIFRAGCPALCGDPEPPEPLLAKARELGCPLLMRGRDFDLSIGKDSWDWRgvahGEQVEL 242
Cdd:PRK10846  170 ALDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFS----DGDGTL 245

                         250
                  ....*....|..
gi 2414964148 243 RGLPLLDLPMQN 254
Cdd:PRK10846  246 ENLPLPNVPLPN 257
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 4-248 5.35e-115

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: 336.31  E-value: 5.35e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148   4 TSLSDWLAYLEQLHPSAIDMGLDRSRQVAQQLGLTRPAPRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYN 83
Cdd:COG0285     2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  84 ERVKVQGVEATDLELCDAFAAVEAARGDV---TLTYFEMGTLAAFWLFEQARLDAVVLEVGLGGRLDAVNLVDADFALVT 160
Cdd:COG0285    82 ERIRINGEPISDEELVEALEEVEPAVEEVdagPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVIT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148 161 SIGVDHAEYLGNTRESVAFEKAGIFRAGCPALCGDPEPP--EPLLAKARELGCPLLMRGRDFDLS-IGKDSWDWRGvAHG 237
Cdd:COG0285   162 SIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEalEVIEERAAELGAPLYRAGRDFSVEeREGAVFSYQG-PGG 240

                         250
                  ....*....|.
gi 2414964148 238 EQVELRgLPLL 248
Cdd:COG0285   241 EYEDLP-LPLL 250
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 25-233 7.78e-84

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: 256.06  E-value: 7.78e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  25 LDRSRQVAQQLGLTRPAPRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYNERVKVQGVEATDLELCDAFAA 104
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148 105 VEAA--RGDVTLTYFEMGTLAAFWLFEQARLDAVVLEVGLGGRLDAVNLVDADFALVTSIGVDHAEYLGNTRESVAFEKA 182
Cdd:TIGR01499  81 VRPIleSLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIAWEKA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2414964148 183 GIFRAGCPALCGD--PEPPEPLLAKARELGCPLLMRGRDFDLSIGK-DSWDWRG 233
Cdd:TIGR01499 161 GIIKEGVPIVTGEqePEALNVLKKKAQEKGAPLFVVGRDFNYSETDeNYLSFSG 214
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 17-213 4.33e-50

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 172.15  E-value: 4.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  17 HPSAIDMGLDRSRQVAQQLGLTRPAPR--VITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYNERVKVQGVEAT 94
Cdd:PLN02881   34 DPSNPGDQFDLLFDYLKILELEEAISRlkVIHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDIS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  95 DlelcDAFAAV---------EAARGDVTL-TYFEMGTLAAFWLFEQARLDAVVLEVGLGGRLDAVNLVDADFAL-VTSIG 163
Cdd:PLN02881  114 E----EKFLRYfwwcwdrlkEKTTEDLPMpAYFRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKPVVCgITSLG 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2414964148 164 VDHAEYLGNTRESVAFEKAGIFRAGCPALCGdPEPPEP---LLAKARELGCPL 213
Cdd:PLN02881  190 YDHMEILGDTLGKIAGEKAGIFKPGVPAFTV-PQPDEAmrvLEERASELGVPL 241
PLN02913 PLN02913
dihydrofolate synthetase
 6-199 2.02e-34

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 129.55  E-value: 2.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148   6 LSDWLAYLEQLH-------PSAI----DMGLD--RSRQVAQQLGLTRPAPRVITVTGTNGKGSTCAFVAALLQAQGLKVG 72
Cdd:PLN02913   26 LGDFLRYLDSLKnyeksgvPKDAgtdsDDGFDlgRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  73 VYSSPHLIRYNERVKV--QGVEATDLELCDAF--------AAVEAARGdvTLTYFEMGTLAAFWLFEQARLDAVVLEVGL 142
Cdd:PLN02913  106 CYTSPHLRSIRERISVgkLGKPVSTNTLNDLFhgikpildEAIQLENG--SLTHFEVLTALAFKLFAQENVDIAVIEAGL 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148 143 GGRLDAVNLVDAD---FALVTSIGVDHAEYLGNTRESVAFEKAGIFRAGCPALCGDPEPP 199
Cdd:PLN02913  184 GGARDATNVIDSSglaASVITTIGEEHLAALGGSLESIALAKSGIIKQGRPVVLGGPFLP 243
Mur_ligase_M pfam08245
Mur ligase middle domain;
47-185 4.97e-12

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 63.09  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  47 VTGTNGKGSTCAFVAALLQAQGLK---VGVYSSPHLIRYNERVKVQgveatdlelcdafaaveaargdvtLTYFEMgtla 123
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVigtIGTYIGKSGNTTNNAIGLP------------------------LTLAEM---- 52

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2414964148 124 afwlfEQARLDAVVLEV---GLG-GRLDavNLVDADFALVTSIGVDHAEYLGnTRESVAFEKAGIF 185
Cdd:pfam08245  53 -----VEAGAEYAVLEVsshGLGeGRLS--GLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELF 110
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 44-235 3.42e-07

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: 50.78  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  44 VITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSphliRYNErvkvqgveatdlelcdaFAAVEAARGDVTLTYFEMGTL- 122
Cdd:TIGR01085  87 VIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGT----IGYR-----------------LGGNDLIKNPAALTTPEALTLq 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148 123 AAFWLFEQARLDAVVLEV---GLG-GRLDAVNLvdaDFALVTSIGVDHAEYLGnTRESVAFEKAGIFRA-GCPA---LCG 194
Cdd:TIGR01085 146 STLAEMVEAGAQYAVMEVsshALAqGRVRGVRF---DAAVFTNLSRDHLDFHG-TMENYFAAKASLFTElGLKRfavINL 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2414964148 195 DpEPPEPLLAKARELGCPLLMRGRDF-----DLSIGKDSWDWRGVA 235
Cdd:TIGR01085 222 D-DEYGAQFVKRLPKDITVSAITQPAdgraqDIKITDSGYSFEGQQ 266
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 43-73 1.29e-05

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: 45.84  E-value: 1.29e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2414964148  43 RVITVTGTNGKGSTCAFVAALLQAQGLKVGV 73
Cdd:COG0769    81 KLIGVTGTNGKTTTTYLLAQILRALGKKTGL 111
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 40-73 4.03e-05

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 44.30  E-value: 4.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2414964148  40 PAPRVITVTGTNGKGSTCAFVAALLQAQGLKVGV 73
Cdd:COG0771   103 SPAPIIAITGTNGKTTTTTLIGHILKAAGLRVAV 136
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 44-182 6.36e-05

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 43.99  E-value: 6.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  44 VITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSphlirynERVKVQG--VEATDlelCDAFAA---------VEAArgdv 112
Cdd:PRK14016  482 IVAVTGTNGKTTTTRLIAHILKLSGKRVGMTTT-------DGVYIDGrlIDKGD---CTGPKSarrvlmnpdVEAA---- 547

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414964148 113 tltyfemgtlaafwLFEQARldAVVLEVGLGGRLdavnlvdADFALVTSIGVDHaeyLG----NTRESVAFEKA 182
Cdd:PRK14016  548 --------------VLETAR--GGILREGLAYDR-------CDVGVVTNIGEDH---LGlggiNTLEDLAKVKR 595
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 43-73 1.50e-04

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 42.43  E-value: 1.50e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2414964148  43 RVITVTGTNGKGSTCAFVAALLQAQGLKVGV 73
Cdd:PRK00139   96 KLIGVTGTNGKTTTAYLLAQILRLLGEKTAL 126
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
 34-73 4.57e-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: 41.17  E-value: 4.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2414964148  34 QLGLTRPAPRVITVTGTNGKGSTCAFVAALLQAQGLKVGV 73
Cdd:TIGR01087  94 ELFLRLVPLPVVAITGTNGKTTTTSLLYHLLKAAGLKAFL 133
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 42-209 2.26e-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: 38.93  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  42 PRVITVTGTNGKGSTCAFVAALLQAQGlkvGVYSSP-----HLirynervkvqgveatdlelcdafaaveaarGdVTLTY 116
Cdd:COG0770   100 IPVIAITGSNGKTTTKEMLAAVLSTKG---KVLATPgnfnnEI------------------------------G-VPLTL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148 117 FEMgtlaafwlfeQARLDAVVLEVG---LG--GRLdaVNLVDADFALVTSIGVDHAEYLGnTRESVAFEKAGIFrAGCPA 191
Cdd:COG0770   146 LRL----------PEDHEFAVLEMGmnhPGeiAYL--ARIARPDIAVITNIGPAHLEGFG-SLEGIARAKGEIF-EGLPP 211

                         170       180
                  ....*....|....*....|...
gi 2414964148 192 -----LCGDpeppEPLLAKAREL 209
Cdd:COG0770   212 ggvavLNAD----DPLLAALAER 230
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 43-186 5.59e-03

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: 38.15  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414964148  43 RVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYNERVKVQGVEATDLELCDAFAAVEAargdvtltyfemgtl 122
Cdd:PRK11929  113 SLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIGTLGARLDGRLIPGSLTTPDAIILHRILARMRA--------------- 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2414964148 123 aafwlfeqARLDAVVLEV---GLG-GRLDAVNLVDADFalvTSIGVDHAEYLGnTRESVAFEKAGIFR 186
Cdd:PRK11929  178 --------AGADAVAMEAsshGLEqGRLDGLRIAVAGF---TNLTRDHLDYHG-TMQDYEEAKAALFS 233
 
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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