NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|515567611|ref|WP_017000443|]
View 

MULTISPECIES: Mur ligase family protein [Mammaliicoccus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MurE super family cl34038
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
37-362 2.06e-60

UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis


The actual alignment was detected with superfamily member COG0769:

Pssm-ID: 440532 [Multi-domain]  Cd Length: 459  Bit Score: 202.23  E-value: 2.06e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  37 QDIQDSSIFI-LKSSK-HSKKYAIEAVKKNPVLIITNMPLNSLDDikgNVYVVYIDNYESVAIKLVHLFYDKYIEQLKFI 114
Cdd:COG0769    7 RKVKPGDLFVaLPGARvDGHDFIAQAIARGAVAVVTEAPGALLAA---GVPVIVVPDPRAALALLAAAFYGHPSQKLKLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 115 AVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVYDDDynkiEFLHSTPTTPMHFEFAEIIKHFAERDYDYIVYEATSIA 194
Cdd:COG0769   84 GVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGG----ELIPSSLTTPEALDLQRLLAEMVDAGVTHVVMEVSSHA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 195 LDQRRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL-DQL--SKRSMVNYDT---KEYLKICNDK-YHFSNNNDTY 267
Cdd:COG0769  160 LDQGRVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLfDQLgpGGAAVINADDpygRRLAAAAPARvITYGLKADAD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 268 YKYE-LKNN----KLYISIGKEVYKLDVLFNGTHNYINLATSIFTLHKLNFNIIDILKAVETMKPPAHRFETFEI-NDYQ 341
Cdd:COG0769  240 LRATdIELSadgtRFTLVTPGGEVEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRMERVDGgQGPT 319
                        330       340
                 ....*....|....*....|.
gi 515567611 342 FILDFAHTPLAIkESIEDALR 362
Cdd:COG0769  320 VIVDYAHTPDAL-ENVLEALR 339
Mur_ligase_C super family cl37676
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
330-402 6.73e-05

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.


The actual alignment was detected with superfamily member pfam02875:

Pssm-ID: 460731 [Multi-domain]  Cd Length: 87  Bit Score: 41.18  E-value: 6.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515567611  330 HRFETF-EINDYQFILDFAHTPLAIKESIEDALRYAsniDKQLTVMITGVGLRGYDKIESTMKLIPKYIDQVVL 402
Cdd:pfam02875   3 GRLEVVgENNGVLVIDDYAHNPDAMEAALRALRNLF---PGRLILVFGGMGDRDAEFHALLGRLAAALADVVIL 73
 
Name Accession Description Interval E-value
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
37-362 2.06e-60

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: 202.23  E-value: 2.06e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  37 QDIQDSSIFI-LKSSK-HSKKYAIEAVKKNPVLIITNMPLNSLDDikgNVYVVYIDNYESVAIKLVHLFYDKYIEQLKFI 114
Cdd:COG0769    7 RKVKPGDLFVaLPGARvDGHDFIAQAIARGAVAVVTEAPGALLAA---GVPVIVVPDPRAALALLAAAFYGHPSQKLKLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 115 AVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVYDDDynkiEFLHSTPTTPMHFEFAEIIKHFAERDYDYIVYEATSIA 194
Cdd:COG0769   84 GVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGG----ELIPSSLTTPEALDLQRLLAEMVDAGVTHVVMEVSSHA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 195 LDQRRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL-DQL--SKRSMVNYDT---KEYLKICNDK-YHFSNNNDTY 267
Cdd:COG0769  160 LDQGRVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLfDQLgpGGAAVINADDpygRRLAAAAPARvITYGLKADAD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 268 YKYE-LKNN----KLYISIGKEVYKLDVLFNGTHNYINLATSIFTLHKLNFNIIDILKAVETMKPPAHRFETFEI-NDYQ 341
Cdd:COG0769  240 LRATdIELSadgtRFTLVTPGGEVEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRMERVDGgQGPT 319
                        330       340
                 ....*....|....*....|.
gi 515567611 342 FILDFAHTPLAIkESIEDALR 362
Cdd:COG0769  320 VIVDYAHTPDAL-ENVLEALR 339
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
26-405 8.05e-50

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: 174.43  E-value: 8.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611   26 NKDCSDVTSMYQDIQDSSIFI-LKSSK-HSKKYAIEAVKKNPVLIITNMPLNSLDDikgNVYVVYIDNYESVAIKLVHLF 103
Cdd:TIGR01085   1 DLEVTGLTLDSREVKPGDLFVaIKGTHvDGHDFIHDAIANGAVAVVVERDVDFYVA---PVPVIIVPDLRHALSSLAAAF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  104 YDKYIEQLKFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGvYDDDYNKIEFLHSTPTTPMHFEFAEIIKHFAERDY 183
Cdd:TIGR01085  78 YGHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIG-YRLGGNDLIKNPAALTTPEALTLQSTLAEMVEAGA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  184 DYIVYEATSIALDQRRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL---DQLSKRSMVNYD-------TKEYLKI 253
Cdd:TIGR01085 157 QYAVMEVSSHALAQGRVRGVRFDAAVFTNLSRDHLDFHGTMENYFAAKASLfteLGLKRFAVINLDdeygaqfVKRLPKD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  254 CNdkYHFSNNNDTYYKYELK-NNKLYISIG--------KEVYKLDVLFNGTHNYINLATSIFTLHKL-NFNIIDILKAVE 323
Cdd:TIGR01085 237 IT--VSAITQPADGRAQDIKiTDSGYSFEGqqftfetpAGEGHLHTPLIGRFNVYNLLAALATLLHLgGIDLEDIVAALE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  324 TMKPPAHRFETFEIN-DYQFILDFAHTPlaikESIEDALRYASNIDKQ-LTVMITGVGLRgyDKIESTM--KLIPKYIDQ 399
Cdd:TIGR01085 315 KFRGVPGRMELVDGGqKFLVIVDYAHTP----DALEKALRTLRKHKDGrLIVVFGCGGDR--DRGKRPLmgAIAEQLADL 388

                  ....*.
gi 515567611  400 VVLASE 405
Cdd:TIGR01085 389 VILTSD 394
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
31-362 8.73e-50

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 174.16  E-value: 8.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  31 DVTSMYQD---IQDSSIFI-LKSSK-HSKKYAIEAVKKNPVLIITNmplnSLDDIKGNVYVVYIDNYESVAIKLVHLFYD 105
Cdd:PRK00139  14 EITGLTYDsrkVKPGDLFVaLPGHKvDGRDFIAQAIANGAAAVVAE----ADGEAGTGVPVIIVPDLRKALALLAAAFYG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 106 KYIEQLKFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVYDDDYNKieflHSTPTTPMHFEFAEIIKHFAERDYDY 185
Cdd:PRK00139  90 HPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGTLGNGIGGELI----PSGLTTPDALDLQRLLAELVDAGVTY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 186 IVYEATSIALDQRRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL-DQLSKRSMVNYDTK---EYLKICnDKYHFS 261
Cdd:PRK00139 166 AAMEVSSHALDQGRVDGLKFDVAVFTNLSRDHLDYHGTMEDYLAAKARLfSELGLAAVINADDEvgrRLLALP-DAYAVS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 262 NNNDTYY--KYELKNNKLYISIgkeVYKLDVLFNGTHNYINLATSIFTLHKLNFNIIDILKAVETMKPPAHRFETFEI-N 338
Cdd:PRK00139 245 MAGADLRatDVEYTDSGQTFTL---VTEVESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRMERVDAgQ 321
                        330       340
                 ....*....|....*....|....
gi 515567611 339 DYQFILDFAHTPLAIkESIEDALR 362
Cdd:PRK00139 322 GPLVIVDYAHTPDAL-EKVLEALR 344
Mur_ligase_M pfam08245
Mur ligase middle domain;
116-305 5.53e-31

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 117.41  E-value: 5.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  116 VTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVYdddynkieflhSTPTTPMHFEFAEIIKHFAERDYDYIVYEATSIAL 195
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIGTIGTYIGK-----------SGNTTNNAIGLPLTLAEMVEAGAEYAVLEVSSHGL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  196 DQRRVDFIEN-EIAVFTNFSSEHLEYHHTIENYLESKLKL-DQLSK--RSMVNYDTKEYL-------KICNDKYHFSNNN 264
Cdd:pfam08245  70 GEGRLSGLLKpDIAVFTNISPDHLDFHGTMENYAKAKAELfEGLPEdgIAVINADDPYGAfliaklkKAGVRVITYGIEG 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 515567611  265 -------DTYYKYELKNNKLYISIGKEvYKLDVLFNGTHNYINLATSI 305
Cdd:pfam08245 150 eadlraaNIELSSDGTSFDLFTVPGGE-LEIEIPLLGRHNVYNALAAI 196
F430_CfbE NF033197
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ...
112-378 3.24e-06

coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in synthesizing coenzyme F430, which is used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) MurD, an enzyme of bacterial cell wall biosynthesis.


Pssm-ID: 467992 [Multi-domain]  Cd Length: 419  Bit Score: 48.86  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 112 KFIAVTGTNGKTTTSHMICKLLSKMDVKVATigTLGVYDDDYNKIEFLHS-TPttPMHFEFAEIIKHFAERDYDYIVYE- 189
Cdd:NF033197  93 KFIEITGVKGKTTTAELLAHILSDEYVLLHT--SRGTERYPEGELSNKGSiTP--ASILNALELAEEIGIDDYGFLIFEv 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 190 ---ATSIAldqrrvdfienEIAVFTNFSsehleyhhtiENY-------LESKLKLDQLsKRSMVNYDTKEYLKICNDKYH 259
Cdd:NF033197 169 slgGTGAG-----------DVGIITNIL----------EDYpiaggkrSASAAKLQSL-KNAKVGSINVADLGIYINGKN 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 260 ----FSNNNDTYYKYELKNNKlyisiGKEVYKLDVLFNGTHNYINLATSIFTLHKLNFNIIDILKAVETMKPPAHRFETF 335
Cdd:NF033197 227 klviTVAGVEILSKYPLRFKY-----GNTEFEFNPLLFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMAVK 301
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 515567611 336 EINDYqFILDFAHTPLAIKeSIEDALRYASNIDKQLTVMITGV 378
Cdd:NF033197 302 KEGGV-VIVDNINPGLNVK-AIEYALDDALELLGDGTLVIGGD 342
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
330-402 6.73e-05

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: 41.18  E-value: 6.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515567611  330 HRFETF-EINDYQFILDFAHTPLAIKESIEDALRYAsniDKQLTVMITGVGLRGYDKIESTMKLIPKYIDQVVL 402
Cdd:pfam02875   3 GRLEVVgENNGVLVIDDYAHNPDAMEAALRALRNLF---PGRLILVFGGMGDRDAEFHALLGRLAAALADVVIL 73
 
Name Accession Description Interval E-value
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
37-362 2.06e-60

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: 202.23  E-value: 2.06e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  37 QDIQDSSIFI-LKSSK-HSKKYAIEAVKKNPVLIITNMPLNSLDDikgNVYVVYIDNYESVAIKLVHLFYDKYIEQLKFI 114
Cdd:COG0769    7 RKVKPGDLFVaLPGARvDGHDFIAQAIARGAVAVVTEAPGALLAA---GVPVIVVPDPRAALALLAAAFYGHPSQKLKLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 115 AVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVYDDDynkiEFLHSTPTTPMHFEFAEIIKHFAERDYDYIVYEATSIA 194
Cdd:COG0769   84 GVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGG----ELIPSSLTTPEALDLQRLLAEMVDAGVTHVVMEVSSHA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 195 LDQRRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL-DQL--SKRSMVNYDT---KEYLKICNDK-YHFSNNNDTY 267
Cdd:COG0769  160 LDQGRVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLfDQLgpGGAAVINADDpygRRLAAAAPARvITYGLKADAD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 268 YKYE-LKNN----KLYISIGKEVYKLDVLFNGTHNYINLATSIFTLHKLNFNIIDILKAVETMKPPAHRFETFEI-NDYQ 341
Cdd:COG0769  240 LRATdIELSadgtRFTLVTPGGEVEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRMERVDGgQGPT 319
                        330       340
                 ....*....|....*....|.
gi 515567611 342 FILDFAHTPLAIkESIEDALR 362
Cdd:COG0769  320 VIVDYAHTPDAL-ENVLEALR 339
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
26-405 8.05e-50

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: 174.43  E-value: 8.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611   26 NKDCSDVTSMYQDIQDSSIFI-LKSSK-HSKKYAIEAVKKNPVLIITNMPLNSLDDikgNVYVVYIDNYESVAIKLVHLF 103
Cdd:TIGR01085   1 DLEVTGLTLDSREVKPGDLFVaIKGTHvDGHDFIHDAIANGAVAVVVERDVDFYVA---PVPVIIVPDLRHALSSLAAAF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  104 YDKYIEQLKFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGvYDDDYNKIEFLHSTPTTPMHFEFAEIIKHFAERDY 183
Cdd:TIGR01085  78 YGHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIG-YRLGGNDLIKNPAALTTPEALTLQSTLAEMVEAGA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  184 DYIVYEATSIALDQRRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL---DQLSKRSMVNYD-------TKEYLKI 253
Cdd:TIGR01085 157 QYAVMEVSSHALAQGRVRGVRFDAAVFTNLSRDHLDFHGTMENYFAAKASLfteLGLKRFAVINLDdeygaqfVKRLPKD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  254 CNdkYHFSNNNDTYYKYELK-NNKLYISIG--------KEVYKLDVLFNGTHNYINLATSIFTLHKL-NFNIIDILKAVE 323
Cdd:TIGR01085 237 IT--VSAITQPADGRAQDIKiTDSGYSFEGqqftfetpAGEGHLHTPLIGRFNVYNLLAALATLLHLgGIDLEDIVAALE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  324 TMKPPAHRFETFEIN-DYQFILDFAHTPlaikESIEDALRYASNIDKQ-LTVMITGVGLRgyDKIESTM--KLIPKYIDQ 399
Cdd:TIGR01085 315 KFRGVPGRMELVDGGqKFLVIVDYAHTP----DALEKALRTLRKHKDGrLIVVFGCGGDR--DRGKRPLmgAIAEQLADL 388

                  ....*.
gi 515567611  400 VVLASE 405
Cdd:TIGR01085 389 VILTSD 394
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
31-362 8.73e-50

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 174.16  E-value: 8.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  31 DVTSMYQD---IQDSSIFI-LKSSK-HSKKYAIEAVKKNPVLIITNmplnSLDDIKGNVYVVYIDNYESVAIKLVHLFYD 105
Cdd:PRK00139  14 EITGLTYDsrkVKPGDLFVaLPGHKvDGRDFIAQAIANGAAAVVAE----ADGEAGTGVPVIIVPDLRKALALLAAAFYG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 106 KYIEQLKFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVYDDDYNKieflHSTPTTPMHFEFAEIIKHFAERDYDY 185
Cdd:PRK00139  90 HPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGTLGNGIGGELI----PSGLTTPDALDLQRLLAELVDAGVTY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 186 IVYEATSIALDQRRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL-DQLSKRSMVNYDTK---EYLKICnDKYHFS 261
Cdd:PRK00139 166 AAMEVSSHALDQGRVDGLKFDVAVFTNLSRDHLDYHGTMEDYLAAKARLfSELGLAAVINADDEvgrRLLALP-DAYAVS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 262 NNNDTYY--KYELKNNKLYISIgkeVYKLDVLFNGTHNYINLATSIFTLHKLNFNIIDILKAVETMKPPAHRFETFEI-N 338
Cdd:PRK00139 245 MAGADLRatDVEYTDSGQTFTL---VTEVESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRMERVDAgQ 321
                        330       340
                 ....*....|....*....|....
gi 515567611 339 DYQFILDFAHTPLAIkESIEDALR 362
Cdd:PRK00139 322 GPLVIVDYAHTPDAL-EKVLEALR 344
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
1-362 1.82e-40

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: 153.32  E-value: 1.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611   1 MEITNVLSKIKRDIIFDDHSYKVNFNKDCSDVTSMYQDIQDSSIFILKSSKHS--KKYAIEAVKKNPVLIITNMPLNSlD 78
Cdd:PRK11929   1 MSIGNRLGNVKLEELLQALAWLRGCVAATADLRLDSREVQPGDLFVACRGAASdgRAFIDQALARGAAAVLVEAEGED-Q 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  79 DIKGNVYVVYIDNYESVAIKLVHLFYDKYIEQLKFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGV-YDDDYNKIE 157
Cdd:PRK11929  80 VAAADALVLPVADLRKALGELAARWYGRPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIGTLGArLDGRLIPGS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 158 FlhstpTTPMHFEFAEIIKHFAERDYDYIVYEATSIALDQRRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL-DQ 236
Cdd:PRK11929 160 L-----TTPDAIILHRILARMRAAGADAVAMEASSHGLEQGRLDGLRIAVAGFTNLTRDHLDYHGTMQDYEEAKAALfSK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 237 LSKR--SMVNYDTKEYLKICNDKYH------FSNNNDT-----YYKYELKNNKLYISIGKEVYKLDVLFNGTHNYINLAT 303
Cdd:PRK11929 235 LPGLgaAVINADDPAAARLLAALPRglkvgySPQNAGAdvqarDLRATAHGQVFTLATPDGSYQLVTRLLGRFNVSNLLL 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515567611 304 SIFTLHKLNFNIIDILKAVETMKPPAHRFE----TFEINDYQFILDFAHTPLAIKESIeDALR 362
Cdd:PRK11929 315 VAAALKKLGLPLAQIARALAAVSPVPGRMErvgpTAGAQGPLVVVDYAHTPDALAKAL-TALR 376
Mur_ligase_M pfam08245
Mur ligase middle domain;
116-305 5.53e-31

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 117.41  E-value: 5.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  116 VTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVYdddynkieflhSTPTTPMHFEFAEIIKHFAERDYDYIVYEATSIAL 195
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIGTIGTYIGK-----------SGNTTNNAIGLPLTLAEMVEAGAEYAVLEVSSHGL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  196 DQRRVDFIEN-EIAVFTNFSSEHLEYHHTIENYLESKLKL-DQLSK--RSMVNYDTKEYL-------KICNDKYHFSNNN 264
Cdd:pfam08245  70 GEGRLSGLLKpDIAVFTNISPDHLDFHGTMENYAKAKAELfEGLPEdgIAVINADDPYGAfliaklkKAGVRVITYGIEG 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 515567611  265 -------DTYYKYELKNNKLYISIGKEvYKLDVLFNGTHNYINLATSI 305
Cdd:pfam08245 150 eadlraaNIELSSDGTSFDLFTVPGGE-LEIEIPLLGRHNVYNALAAI 196
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
112-343 1.46e-25

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: 107.47  E-value: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 112 KFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGvydddynkieflhsTPttpmhfeFAEIIKHfaERDYDYIVYEAT 191
Cdd:COG0771  106 PIIAITGTNGKTTTTTLIGHILKAAGLRVAVGGNIG--------------TP-------LLDLLLE--PEPPDVYVLELS 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 192 SIALDqrRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL--DQLSKRSMV-NYD---TKEYLKICNDK-YHFSNNN 264
Cdd:COG0771  163 SFQLE--TTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIfaNQTPDDYAVlNADdplTRALAEEAKARvVPFSLKE 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 265 DTYYKYELKNNKLYISI-GKEVYKLDVL-FNGTHNYINLATSIFTLHKLNFNIIDILKAVETMKPPAHRFETF-EINDYQ 341
Cdd:COG0771  241 PLEGGAGLEDGKLVDRAsGEELLPVDDLrLPGRHNLENALAALAAARALGVPPEAIREALRSFKGLPHRLEFVaEINGVR 320

                 ..
gi 515567611 342 FI 343
Cdd:COG0771  321 FI 322
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
102-379 2.40e-24

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: 103.96  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  102 LFYDkyIEQLKFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGvydddynkieflhstptTPmhfefaeIIKHFAER 181
Cdd:TIGR01087  95 LFLR--LVPLPVVAITGTNGKTTTTSLLYHLLKAAGLKAFLGGNIG-----------------TP-------ALEVLDQE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  182 DYDYIVYEATSIAL-DQRRVDFienEIAVFTNFSSEHLEYHHTIENYLESKLKLdqlskrsMVNYDTKEYLKICNDKYHF 260
Cdd:TIGR01087 149 GAELYVLELSSFQLeTTESLRP---EIALILNISEDHLDWHGSFEDYVAAKLKI-------FARQTEGDVAVLNADDPRF 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  261 SNNND-------TYYKYELKNNKLYISIGKEVYK---LDVLFNGTHNYINL--ATSIFTLHKLNFNiiDILKAVETMKPP 328
Cdd:TIGR01087 219 ARLAQkskaqviWFSVEKDAERGLCIRDGGLYLKpndLEGSLLGLHNAENIlaAIALAKSLGLNLE--AILEALRSFKGL 296
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515567611  329 AHRFETF-EINDYQFILDFAHTplaIKESIEDALryaSNIDKQLTVMITGVG 379
Cdd:TIGR01087 297 PHRLEYVgQKNGVHFYNDSKAT---NVHATLAAL---SAFDNPVILIVGGDD 342
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
1-350 2.29e-23

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


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 101.65  E-value: 2.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611   1 MEITNVLSKIK-----RDIIFDDHSYKVNFNKDCSDVTSMYQDIQDSSIFILKSSKHSKKYAIEAVKKNPVLIITNMpln 75
Cdd:PRK14022   1 ITIETLLDILKkdhnfREIIDQDHYHYNYSGVQFDDISYDSRTADEGTLFFAKGAYFKHKFLQNAITQGLKLYVSEK--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  76 sldDIKGNVYVVYIDNYESVAIKLVHLFYDKYIEQLKFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVYDddyNK 155
Cdd:PRK14022  78 ---DYEVGIPQVIVPDIKKAMSLIAMEFYDNPQHKLKLLAFTGTKGKTTAAYFAYHILKQLHKPAMLSTMNTTLD---GE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 156 iEFLHSTPTTPMHFEFAEIIKHFAERDYDYIVYEATSIALDQRRVDFIENEIAVFTNFSSEHLEY--HHTIENYLESKLK 233
Cdd:PRK14022 152 -TFFKSALTTPESLDLFKMMAEAVDNGMTHLIMEVSSQAYLVGRVYGLTFDVGVFLNITPDHIGPieHPTFEDYFYHKRL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 234 LDQLSKRSMVNYDT---KEYLKICNDKYHFSNNNDTYYKYELKNNKLYISIGKEVYKLDVLFNGTHNYINLATSIFTLHK 310
Cdd:PRK14022 231 LMENSKAVVVNSDMdhfSELLEQVTPQEHDFYGIDSENQIMASNAFSFEATGKLAGTYDIQLIGKFNQENAMAAGLACLR 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 515567611 311 LNFNIIDILKAVETMKPPAhRFETF-EINDYQFILDFAHTP 350
Cdd:PRK14022 311 LGASLEDIQKGIAQTPVPG-RMEVLtQSNGAKVFIDYAHNG 350
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
110-345 1.39e-13

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: 72.06  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 110 QLKFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGTL----GVydddynkieflhstPTTpmhfeFAEIikhfaERDYDY 185
Cdd:COG0770   99 NIPVIAITGSNGKTTTKEMLAAVLSTKGKVLATPGNFnneiGV--------------PLT-----LLRL-----PEDHEF 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 186 IVYEA-TS----IAldqRRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL-DQLSKRSM--VNYDTkEYLKICNDK 257
Cdd:COG0770  155 AVLEMgMNhpgeIA---YLARIARPDIAVITNIGPAHLEGFGSLEGIARAKGEIfEGLPPGGVavLNADD-PLLAALAER 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 258 YH-------FSNNNDTY---YKYELKNNKLYISIGKEVYKLDVLFNGTHNYINLATSIFTLHKLNFNIIDILKAVETMKP 327
Cdd:COG0770  231 AKarvltfgLSEDADVRaedIELDEDGTRFTLHTPGGELEVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQP 310
                        250
                 ....*....|....*....
gi 515567611 328 PAHRFETFE-INDYQFILD 345
Cdd:COG0770  311 VKGRLEVIEgAGGVTLIDD 329
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
114-405 1.58e-13

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 71.93  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 114 IAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVydddynkieflhstpttPMhfeFAEIIKHFAErdyDYIVYEATSI 193
Cdd:PRK14106 111 VAITGTNGKTTTTTLLGEIFKNAGRKTLVAGNIGY-----------------PL---IDAVEEYGED---DIIVAEVSSF 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 194 ALDQrrVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKL---DQLSKRSMVNYD---TKEYLKICNDK-YHFSNNNDT 266
Cdd:PRK14106 168 QLET--IKEFKPKVGCILNITPDHLDRHKTMENYIKAKARIfenQRPSDYTVLNYDdprTRSLAKKAKARvIFFSRKSLL 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 267 YYKYELKNNKLYISIG---KEVYKLDVLF-NGTHNYIN-LATSIFTLhKLNFNIIDILKAVETMKPPAHRFETF-EINDY 340
Cdd:PRK14106 246 EEGVFVKNGKIVISLGgkeEEVIDIDEIFiPGEHNLENaLAATAAAY-LLGISPDVIANTLKTFKGVEHRIEFVaEINGV 324
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515567611 341 QFILDfahtplaIKESIEDALRYASNIDKQLTVMITGvglrGYDKIES---TMKLIPKYIDQVVLASE 405
Cdd:PRK14106 325 KFIND-------SKGTNPDAAIKALEAYETPIVLIAG----GYDKGSDfdeFAKAFKEKVKKLILLGE 381
murF TIGR01143
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ...
110-345 3.40e-11

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273468 [Multi-domain]  Cd Length: 417  Bit Score: 64.59  E-value: 3.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  110 QLKFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGtlgvyddDYNkieflhSTPTTPMhfefaEIIkhFAERDYDYIVYE 189
Cdd:TIGR01143  73 SGKVIGITGSSGKTTTKEMLAAILSHKYKVFATPG-------NFN------NEIGLPL-----TLL--RAPGDHDYAVLE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  190 -ATS----IALdqrRVDFIENEIAVFTNFSSEHLEYHHTIENYLESKLKLDQLSKRS---MVNYDTK--EYLKICN---D 256
Cdd:TIGR01143 133 mGAShpgeIAY---LAEIAKPDIAVITNIGPAHLEGFGSLEGIAEAKGEILQGLKENgiaVINADDPafADLAKRLpnrN 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  257 KYHFSNNN------DTYYKYELKNNKLYISIGKEV-YKLDVLfnGTHNYINLATSIFTLHKLNFNIIDILKAVETMKPPA 329
Cdd:TIGR01143 210 ILSFGFEGgdfvakDISYSALGSTSFTLVAPGGEFeVSLPLL--GRHNVMNALAAAALALELGIPLEEIAEGLAELKLVK 287
                         250
                  ....*....|....*.
gi 515567611  330 HRFETFEINDYQFILD 345
Cdd:TIGR01143 288 GRFEVQTKNGLTLIDD 303
MurC COG0773
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
109-362 2.63e-10

UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440536 [Multi-domain]  Cd Length: 451  Bit Score: 61.62  E-value: 2.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 109 EQLKF---IAVTGTNGKTTTSHMICKLL--SKMDV------KVATIGT---LGvyDDDYNKIE-------FLHSTPTtpm 167
Cdd:COG0773   99 ELMRGkrsIAVAGTHGKTTTTSMLAHILeeAGLDPtfliggILNNFGTnarLG--DGDYFVAEadesdgsFLHYSPD--- 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 168 hfefaeiikhfaerdydyivyeatsialdqrrvdfieneIAVFTNFSSEHLEYHHTIENYLES--KLkLDQLSKRSM--V 243
Cdd:COG0773  174 ---------------------------------------IAVVTNIEADHLDIYGDLEAIKEAfhEF-ARNVPFYGLlvL 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 244 NYDTKEYLKICND------KYHFSNNNDtyykYELKNnklyISIGKEVYKLDVLFNGT------------HNYINLATSI 305
Cdd:COG0773  214 CADDPGLRELLPRcgrpviTYGFSEDAD----YRAEN----IRIDGGGSTFDVLRRGEelgevelnlpgrHNVLNALAAI 285
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515567611 306 FTLHKLNFNIIDILKAVETMKPPAHRFE-TFEINDYQFILDFAHTPLAIKESIEdALR 362
Cdd:COG0773  286 AVALELGVDPEAIAEALASFKGVKRRFElKGEVGGVTVIDDYAHHPTEIAATLA-AAR 342
murC TIGR01082
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ...
114-360 5.44e-10

UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by model TIGR01081. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273433 [Multi-domain]  Cd Length: 448  Bit Score: 60.78  E-value: 5.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  114 IAVTGTNGKTTTSHMICKLLS--KMDVKVATIGTLGVYDDdynkieflhstpttpmhfefaeiikHFAERDYDYIVYEAt 191
Cdd:TIGR01082 102 IAVAGTHGKTTTTAMIAVILKeaGLDPTVVVGGLVKEAGT-------------------------NARLGSGEYLVAEA- 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  192 sialDQRRVDFIE--NEIAVFTNFSSEHLE-YHHTIENYLESKLK-LDQLSKRSMV--NYDTKEYLKICNDK------YH 259
Cdd:TIGR01082 156 ----DESDASFLHlqPNVAIVTNIEPDHLDtYGSSFERLKAAFEKfIHNLPFYGLAviCADDPVLRELVPKAteqvitYG 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611  260 FSNNNDTYY--KYELKNNKLYISI---GKEVYKLDVLFNGTHNYINLATSIFTLHKLNFNIIDILKAVETMKPPAHRFE- 333
Cdd:TIGR01082 232 GSGEDADYRaeNIQQSGAEGKFSVrgkGKLYLEFTLNLPGRHNVLNALAAIAVALELGIDFEAILRALANFQGVKRRFEi 311
                         250       260
                  ....*....|....*....|....*..
gi 515567611  334 TFEINDYQFILDFAHTPLAIKESIEDA 360
Cdd:TIGR01082 312 LGEFGGVLLIDDYAHHPTEIKATLKAA 338
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
109-404 4.29e-07

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: 51.64  E-value: 4.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 109 EQLKFIAVTGTNGKTTTSHMICKLLSKMDVKVatigtlGVY--------------------DDD----YNKIE-----FL 159
Cdd:COG0285   38 RKLPVIHVAGTNGKGSTAAMLESILRAAGYRV------GLYtsphlvrfneriringepisDEElveaLEEVEpaveeVD 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 160 HSTPTTpmhFEF--AEIIKHFAERDYDYIVYE--------ATSIaldqrrvdfIENEIAVFTNFSSEHLEY-HHTIEnyl 228
Cdd:COG0285  112 AGPPTF---FEVttAAAFLYFAEAPVDVAVLEvglggrldATNV---------IDPLVSVITSIGLDHTDFlGDTLE--- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 229 esK--------LKldqlSKRSMVNYDT--------KEYLKICNDKYHFSnNNDTYYKYELKNNKLYISIGKEVYKLDVLF 292
Cdd:COG0285  177 --EiarekagiIK----PGVPVVTGDQqpealeviEERAAELGAPLYRA-GRDFSVEEREGAVFSYQGPGGEYEDLPLPL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 293 NGTHNYINLATSIFT---LHKLNFNI--IDILKAVETMKPPAhRFETFEiNDYQFILDFAHTPLAIKesiedALryASNI 367
Cdd:COG0285  250 LGAHQAENAALALAAleaLRELGLPIseEAIREGLANARWPG-RLEVLS-RGPLVILDGAHNPAGAR-----AL--AETL 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 515567611 368 DKQL----TVMITGVgLRgyDK-IESTMKLIPKYIDQVVLAS 404
Cdd:COG0285  321 KELFpfrkLHLVFGM-LA--DKdIEGMLAALAPLADEVIVTT 359
PRK14016 PRK14016
cyanophycin synthetase; Provisional
114-225 1.19e-06

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 50.54  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 114 IAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVYDDDYnkieFLHSTPTTpmHFEFAEIIkhFAERDYDYIVYEATSI 193
Cdd:PRK14016 483 VAVTGTNGKTTTTRLIAHILKLSGKRVGMTTTDGVYIDGR----LIDKGDCT--GPKSARRV--LMNPDVEAAVLETARG 554
                         90       100       110
                 ....*....|....*....|....*....|....
gi 515567611 194 ALDQRRVDFIENEIAVFTNFSSEHL--EYHHTIE 225
Cdd:PRK14016 555 GILREGLAYDRCDVGVVTNIGEDHLglGGINTLE 588
F430_CfbE NF033197
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ...
112-378 3.24e-06

coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in synthesizing coenzyme F430, which is used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) MurD, an enzyme of bacterial cell wall biosynthesis.


Pssm-ID: 467992 [Multi-domain]  Cd Length: 419  Bit Score: 48.86  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 112 KFIAVTGTNGKTTTSHMICKLLSKMDVKVATigTLGVYDDDYNKIEFLHS-TPttPMHFEFAEIIKHFAERDYDYIVYE- 189
Cdd:NF033197  93 KFIEITGVKGKTTTAELLAHILSDEYVLLHT--SRGTERYPEGELSNKGSiTP--ASILNALELAEEIGIDDYGFLIFEv 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 190 ---ATSIAldqrrvdfienEIAVFTNFSsehleyhhtiENY-------LESKLKLDQLsKRSMVNYDTKEYLKICNDKYH 259
Cdd:NF033197 169 slgGTGAG-----------DVGIITNIL----------EDYpiaggkrSASAAKLQSL-KNAKVGSINVADLGIYINGKN 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 260 ----FSNNNDTYYKYELKNNKlyisiGKEVYKLDVLFNGTHNYINLATSIFTLHKLNFNIIDILKAVETMKPPAHRFETF 335
Cdd:NF033197 227 klviTVAGVEILSKYPLRFKY-----GNTEFEFNPLLFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMAVK 301
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 515567611 336 EINDYqFILDFAHTPLAIKeSIEDALRYASNIDKQLTVMITGV 378
Cdd:NF033197 302 KEGGV-VIVDNINPGLNVK-AIEYALDDALELLGDGTLVIGGD 342
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
111-345 3.77e-06

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: 49.32  E-value: 3.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 111 LKFIAVTGTNGKTTTSHMICKLLSKMDVKVATIGTLGVYDddyNKIeflhSTPTT-----PMHfEFAEI---IKHFAErd 182
Cdd:PRK11929 603 LPVVAITGSNGKTTTKEMIAAILAAWQGEDRVLATEGNFN---NEI----GVPLTllrlrAQH-RAAVFelgMNHPGE-- 672
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 183 ydyIVYEATSIALDqrrvdfieneIAVFTNFSSEHLEYHHTIENYLESKLKL-DQLSKRSM--VNYD---TKEYLK---- 252
Cdd:PRK11929 673 ---IAYLAAIAAPT----------VALVTNAQREHQEFMHSVEAVARAKGEIiAALPEDGVavVNGDdpyTAIWAKlaga 739
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515567611 253 --ICNDKYHFSNNndTYYKYELKNNKLY--------ISIGKEVYKLDVLFNGTHNYINLATSIFTLHKLNFNIIDILKAV 322
Cdd:PRK11929 740 rrVLRFGLQPGAD--VYAEKIAKDISVGeaggtrcqVVTPAGSAEVYLPLIGEHNLRNALAAIACALAAGASLKQIRAGL 817
                        250       260
                 ....*....|....*....|...
gi 515567611 323 ETMKPPAHRFETFEINDYQFILD 345
Cdd:PRK11929 818 ERFQPVAGRMQRRRLSCGTRIID 840
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
330-402 6.73e-05

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: 41.18  E-value: 6.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515567611  330 HRFETF-EINDYQFILDFAHTPLAIKESIEDALRYAsniDKQLTVMITGVGLRGYDKIESTMKLIPKYIDQVVL 402
Cdd:pfam02875   3 GRLEVVgENNGVLVIDDYAHNPDAMEAALRALRNLF---PGRLILVFGGMGDRDAEFHALLGRLAAALADVVIL 73
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH