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Conserved domains on  [gi|491214147|ref|WP_005072474|]
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Mur ligase family protein [Mycobacteroides abscessus]

Protein Classification

Mur ligase family protein( domain architecture ID 13558984)

Mur ligase family protein similar to UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (MurE), which catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MurT_C pfam08353
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from ...
 303-408 4.06e-29

MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT.


:

Pssm-ID: 462442  Cd Length: 110  Bit Score: 109.50  E-value: 4.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  303 LAKNPAGWQEALSMVDTDAD--GLVIAVNGQVPDGEDLSWLWDVNFEHFACDNgespVPPVVAAGERGTDLAVRLTYASV 380
Cdd:pfam08353   1 LVKNPVGFNQVLNYIASDPGpkSLLLLLNDNYADGRDVSWIWDVDFEKLNDSN----IKKIIVSGDRAYDMALRLKYAGV 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 491214147  381 TH---TLQHDPVQAIKAC--PPGRVDVIANYTA 408
Cdd:pfam08353  77 PEekiEIEEDLEEALDAIkaPTENVYILPTYTA 109
Mur_ligase_M super family cl37572
Mur ligase middle domain;
60-265 2.42e-15

Mur ligase middle domain;


The actual alignment was detected with superfamily member pfam08245:

Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 74.26  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147   60 ITGTNGKSTTTRMTAAAL-------ATVGPVATNTEGSNMDA-GLVAALAGTR--EADVAVLEVDEMHVP--HVADAVNP 127
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILslaggviGTIGTYIGKSGNTTNNAiGLPLTLAEMVeaGAEYAVLEVSSHGLGegRLSGLLKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  128 AVIVLLNLSRDQLDRVGEINNIERTLRKGLARHR-DAVIVANCDDVLMAsaaydsphvVWVAAGGGWAGDSVSCPRSGEL 206
Cdd:pfam08245  81 DIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPeDGIAVINADDPYGA---------FLIAKLKKAGVRVITYGIEGEA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  207 IMRDGN-RWYSTGTDFarpdpdwwfdddRIYGPSGISLPMSLTLPGTANRGNATLAVAAA 265
Cdd:pfam08245 152 DLRAANiELSSDGTSF------------DLFTVPGGELEIEIPLLGRHNVYNALAAIAAA 199
 
Name Accession Description Interval E-value
MurT_C pfam08353
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from ...
 303-408 4.06e-29

MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT.


Pssm-ID: 462442  Cd Length: 110  Bit Score: 109.50  E-value: 4.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  303 LAKNPAGWQEALSMVDTDAD--GLVIAVNGQVPDGEDLSWLWDVNFEHFACDNgespVPPVVAAGERGTDLAVRLTYASV 380
Cdd:pfam08353   1 LVKNPVGFNQVLNYIASDPGpkSLLLLLNDNYADGRDVSWIWDVDFEKLNDSN----IKKIIVSGDRAYDMALRLKYAGV 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 491214147  381 TH---TLQHDPVQAIKAC--PPGRVDVIANYTA 408
Cdd:pfam08353  77 PEekiEIEEDLEEALDAIkaPTENVYILPTYTA 109
Mur_ligase_M pfam08245
Mur ligase middle domain;
60-265 2.42e-15

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 74.26  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147   60 ITGTNGKSTTTRMTAAAL-------ATVGPVATNTEGSNMDA-GLVAALAGTR--EADVAVLEVDEMHVP--HVADAVNP 127
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILslaggviGTIGTYIGKSGNTTNNAiGLPLTLAEMVeaGAEYAVLEVSSHGLGegRLSGLLKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  128 AVIVLLNLSRDQLDRVGEINNIERTLRKGLARHR-DAVIVANCDDVLMAsaaydsphvVWVAAGGGWAGDSVSCPRSGEL 206
Cdd:pfam08245  81 DIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPeDGIAVINADDPYGA---------FLIAKLKKAGVRVITYGIEGEA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  207 IMRDGN-RWYSTGTDFarpdpdwwfdddRIYGPSGISLPMSLTLPGTANRGNATLAVAAA 265
Cdd:pfam08245 152 DLRAANiELSSDGTSF------------DLFTVPGGELEIEIPLLGRHNVYNALAAIAAA 199
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
 58-186 1.23e-10

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: 62.74  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147   58 VLITGTNGKSTTTRMTAAALATVGPVAtnTEGSNMDAGLVAALAGTReADVAVLEVDEMHVpHVADAVNPAVIVLLNLSR 137
Cdd:TIGR01087 105 VAITGTNGKTTTTSLLYHLLKAAGLKA--FLGGNIGTPALEVLDQEG-AELYVLELSSFQL-ETTESLRPEIALILNISE 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491214147  138 DQLDRVGEINNIERTLRKGLARHR-DAVIVANCDDVLMASAAYDS-PHVVW 186
Cdd:TIGR01087 181 DHLDWHGSFEDYVAAKLKIFARQTeGDVAVLNADDPRFARLAQKSkAQVIW 231
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 56-280 1.76e-10

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: 62.41  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  56 RTVLITGTNGKSTTTRMTAAALATVG-PVATnteGSNMDAGLVAALAGTREADVAVLEV--------DEMHvPHVAdavn 126
Cdd:COG0771  106 PIIAITGTNGKTTTTTLIGHILKAAGlRVAV---GGNIGTPLLDLLLEPEPPDVYVLELssfqlettPSLR-PDVA---- 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 127 paviVLLNLSRDQLDRVGEINN-IERTLRkgLARH--RDAVIVANCDD-VLMASAAYDSPHVVWVaagggwagdSVSCPR 202
Cdd:COG0771  178 ----VILNITPDHLDRHGSMEAyAAAKAR--IFANqtPDDYAVLNADDpLTRALAEEAKARVVPF---------SLKEPL 242

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491214147 203 SGELIMRDGNRWYSTGTDFarpdpdwwfdddriygpsgiSLPMS-LTLPGTANRGNATLAVAAAVELGARPGPAVDAVS 280
Cdd:COG0771  243 EGGAGLEDGKLVDRASGEE--------------------LLPVDdLRLPGRHNLENALAALAAARALGVPPEAIREALR 301
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 13-299 2.98e-08

bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;


Pssm-ID: 237025 [Multi-domain]  Cd Length: 958  Bit Score: 55.87  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  13 ALAAGSAARWASRisGRGAGSMIGgliaLKLDGSVLA--QLGRGRR------TVLITGTNGKSTTTRMTAAALATVGPVA 84
Cdd:PRK11929 559 AFAAGACAAVVER--QVADVDLPQ----IVVDDTRAAlgRLATAWRarfslpVVAITGSNGKTTTKEMIAAILAAWQGED 632

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  85 --TNTEGS-NMDAGLVAALAGTREAD-VAVLEVDEMH---VPHVADAVNPAVIVLLNLSRDQLDRVGEINNIERTLRKGL 157
Cdd:PRK11929 633 rvLATEGNfNNEIGVPLTLLRLRAQHrAAVFELGMNHpgeIAYLAAIAAPTVALVTNAQREHQEFMHSVEAVARAKGEII 712

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 158 ARHR-DAVIVANCDDvlmasaaydsPHVV-WVAAGGG----WAGDSVSCPRSGELIMRDGNRWYSTGTDFarpdpdwwfd 231
Cdd:PRK11929 713 AALPeDGVAVVNGDD----------PYTAiWAKLAGArrvlRFGLQPGADVYAEKIAKDISVGEAGGTRC---------- 772

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491214147 232 ddRIYGPSGiSLPMSLTLPGTANRGNATLAVAAAVELGARPGPAVDAVSAVDQVAGRYRSINLGDHTI 299
Cdd:PRK11929 773 --QVVTPAG-SAEVYLPLIGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRRRLSCGTR 837
 
Name Accession Description Interval E-value
MurT_C pfam08353
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from ...
 303-408 4.06e-29

MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT.


Pssm-ID: 462442  Cd Length: 110  Bit Score: 109.50  E-value: 4.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  303 LAKNPAGWQEALSMVDTDAD--GLVIAVNGQVPDGEDLSWLWDVNFEHFACDNgespVPPVVAAGERGTDLAVRLTYASV 380
Cdd:pfam08353   1 LVKNPVGFNQVLNYIASDPGpkSLLLLLNDNYADGRDVSWIWDVDFEKLNDSN----IKKIIVSGDRAYDMALRLKYAGV 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 491214147  381 TH---TLQHDPVQAIKAC--PPGRVDVIANYTA 408
Cdd:pfam08353  77 PEekiEIEEDLEEALDAIkaPTENVYILPTYTA 109
Mur_ligase_M pfam08245
Mur ligase middle domain;
60-265 2.42e-15

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 74.26  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147   60 ITGTNGKSTTTRMTAAAL-------ATVGPVATNTEGSNMDA-GLVAALAGTR--EADVAVLEVDEMHVP--HVADAVNP 127
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILslaggviGTIGTYIGKSGNTTNNAiGLPLTLAEMVeaGAEYAVLEVSSHGLGegRLSGLLKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  128 AVIVLLNLSRDQLDRVGEINNIERTLRKGLARHR-DAVIVANCDDVLMAsaaydsphvVWVAAGGGWAGDSVSCPRSGEL 206
Cdd:pfam08245  81 DIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPeDGIAVINADDPYGA---------FLIAKLKKAGVRVITYGIEGEA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  207 IMRDGN-RWYSTGTDFarpdpdwwfdddRIYGPSGISLPMSLTLPGTANRGNATLAVAAA 265
Cdd:pfam08245 152 DLRAANiELSSDGTSF------------DLFTVPGGELEIEIPLLGRHNVYNALAAIAAA 199
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
 58-186 1.23e-10

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: 62.74  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147   58 VLITGTNGKSTTTRMTAAALATVGPVAtnTEGSNMDAGLVAALAGTReADVAVLEVDEMHVpHVADAVNPAVIVLLNLSR 137
Cdd:TIGR01087 105 VAITGTNGKTTTTSLLYHLLKAAGLKA--FLGGNIGTPALEVLDQEG-AELYVLELSSFQL-ETTESLRPEIALILNISE 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491214147  138 DQLDRVGEINNIERTLRKGLARHR-DAVIVANCDDVLMASAAYDS-PHVVW 186
Cdd:TIGR01087 181 DHLDWHGSFEDYVAAKLKIFARQTeGDVAVLNADDPRFARLAQKSkAQVIW 231
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 56-280 1.76e-10

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: 62.41  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  56 RTVLITGTNGKSTTTRMTAAALATVG-PVATnteGSNMDAGLVAALAGTREADVAVLEV--------DEMHvPHVAdavn 126
Cdd:COG0771  106 PIIAITGTNGKTTTTTLIGHILKAAGlRVAV---GGNIGTPLLDLLLEPEPPDVYVLELssfqlettPSLR-PDVA---- 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 127 paviVLLNLSRDQLDRVGEINN-IERTLRkgLARH--RDAVIVANCDD-VLMASAAYDSPHVVWVaagggwagdSVSCPR 202
Cdd:COG0771  178 ----VILNITPDHLDRHGSMEAyAAAKAR--IFANqtPDDYAVLNADDpLTRALAEEAKARVVPF---------SLKEPL 242

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491214147 203 SGELIMRDGNRWYSTGTDFarpdpdwwfdddriygpsgiSLPMS-LTLPGTANRGNATLAVAAAVELGARPGPAVDAVS 280
Cdd:COG0771  243 EGGAGLEDGKLVDRASGEE--------------------LLPVDdLRLPGRHNLENALAALAAARALGVPPEAIREALR 301
MurC COG0773
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
 47-280 2.55e-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: 62.01  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  47 VLAQLGRGRRTVLITGTNGKSTTTRMTAAALAT--------VGPVATNTeGSNMDAGlvaalagtrEADVAVLEVDE--- 115
Cdd:COG0773   96 MLAELMRGKRSIAVAGTHGKTTTTSMLAHILEEagldptflIGGILNNF-GTNARLG---------DGDYFVAEADEsdg 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 116 --MHvphvadaVNPAVIVLLNLSRDQLDRVGEINNIERTLRKgLARH--RDAVIVANCDD-VLMASAAYDSPHVVW--VA 188
Cdd:COG0773  166 sfLH-------YSPDIAVVTNIEADHLDIYGDLEAIKEAFHE-FARNvpFYGLLVLCADDpGLRELLPRCGRPVITygFS 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 189 AGGGWAGDSVscprsgelimrdgnRWYSTGTDFarpdpdwwfdddRIYGPSGISLPMSLTLPGTANRGNATLAVAAAVEL 268
Cdd:COG0773  238 EDADYRAENI--------------RIDGGGSTF------------DVLRRGEELGEVELNLPGRHNVLNALAAIAVALEL 291

                        250
                 ....*....|..
gi 491214147 269 GARPGPAVDAVS 280
Cdd:COG0773  292 GVDPEAIAEALA 303
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 48-296 4.81e-10

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: 61.27  E-value: 4.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  48 LAQLGRGRR------TVLITGTNGKSTTTRMTAAALATVGPVATnTEGS-NMDAGL---VAALagTREADVAVLE----- 112
Cdd:COG0770   87 LQQLAAAHRarfnipVIAITGSNGKTTTKEMLAAVLSTKGKVLA-TPGNfNNEIGVpltLLRL--PEDHEFAVLEmgmnh 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 113 VDEMHvpHVADAVNPAVIVLLNLSRDQLDRVGEINNIERTlrKG-LARH--RDAVIVANCDD---VLMASAAydSPHVVW 186
Cdd:COG0770  164 PGEIA--YLARIARPDIAVITNIGPAHLEGFGSLEGIARA--KGeIFEGlpPGGVAVLNADDpllAALAERA--KARVLT 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 187 VaagggwaGDSVSCPRSGELIMRDGNrwystGTDFarpdpdwwfdddRIYGPSGiSLPMSLTLPGTANRGNATLAVAAAV 266
Cdd:COG0770  238 F-------GLSEDADVRAEDIELDED-----GTRF------------TLHTPGG-ELEVTLPLPGRHNVSNALAAAAVAL 292

                        250       260       270
                 ....*....|....*....|....*....|
gi 491214147 267 ELGARPGPAVDAVSAVDQVAGRYRSINLGD 296
Cdd:COG0770  293 ALGLDLEEIAAGLAAFQPVKGRLEVIEGAG 322
murF TIGR01143
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ...
 13-299 9.18e-10

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: 59.97  E-value: 9.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147   13 ALAAGSAARWASRISGRGAGsmiggLIALKLDGSV--LAQLGRGRR------TVLITGTNGKSTTTRMTAAALATVG-PV 83
Cdd:TIGR01143  29 ALAAGAVAVVVDREVGPDNG-----LPQILVDDTLeaLQALARAKRakfsgkVIGITGSSGKTTTKEMLAAILSHKYkVF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147   84 ATNteGS-NMDAGL-VAALAGTREADVAVLEVDEMHV---PHVADAVNPAVIVLLNLSRDQLDRVGEINNIERT---LRK 155
Cdd:TIGR01143 104 ATP--GNfNNEIGLpLTLLRAPGDHDYAVLEMGASHPgeiAYLAEIAKPDIAVITNIGPAHLEGFGSLEGIAEAkgeILQ 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  156 GLARHRDAVIVAncddvlmasaayDSPHVVWVAagggwagdsvSCPRSGELIMRDGNRWYSTGTDFarPDPDWWFDDDRI 235
Cdd:TIGR01143 182 GLKENGIAVINA------------DDPAFADLA----------KRLPNRNILSFGFEGGDFVAKDI--SYSALGSTSFTL 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491214147  236 YGPSG---ISLPmsltLPGTANRGNATLAVAAAVELGARPGPAVDAVSAVDQVAGRYRSINLGDHTI 299
Cdd:TIGR01143 238 VAPGGefeVSLP----LLGRHNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRFEVQTKNGLTL 300
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 60-288 1.25e-09

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: 59.71  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  60 ITGTNGKSTTTRMTAAAL-------ATVGPVATNTEGSNMDAGLV--------AALAGTREADV--AVLEVD----EMH- 117
Cdd:COG0769   85 VTGTNGKTTTTYLLAQILralgkktGLIGTVGNGIGGELIPSSLTtpealdlqRLLAEMVDAGVthVVMEVSshalDQGr 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 118 VphvaDAVNPAVIVLLNLSRDQLDrvgEINNIE------RTLRKGLARHRDAVIvaNCDDVLMASAAYDSPHVVWvaagg 191
Cdd:COG0769  165 V----DGVRFDVAVFTNLTRDHLD---YHGTMEayfaakARLFDQLGPGGAAVI--NADDPYGRRLAAAAPARVI----- 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 192 gwagdSVSCPRSGELIMRDgNRWYSTGTDFarpdpdwwfdddRIYGPSGiSLPMSLTLPGTANRGNATLAVAAAVELGAR 271
Cdd:COG0769  231 -----TYGLKADADLRATD-IELSADGTRF------------TLVTPGG-EVEVRLPLIGRFNVYNALAAIAAALALGID 291

                        250
                 ....*....|....*..
gi 491214147 272 PGPAVDAVSAVDQVAGR 288
Cdd:COG0769  292 LEEILAALEKLKGVPGR 308
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 13-299 2.98e-08

bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;


Pssm-ID: 237025 [Multi-domain]  Cd Length: 958  Bit Score: 55.87  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  13 ALAAGSAARWASRisGRGAGSMIGgliaLKLDGSVLA--QLGRGRR------TVLITGTNGKSTTTRMTAAALATVGPVA 84
Cdd:PRK11929 559 AFAAGACAAVVER--QVADVDLPQ----IVVDDTRAAlgRLATAWRarfslpVVAITGSNGKTTTKEMIAAILAAWQGED 632

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  85 --TNTEGS-NMDAGLVAALAGTREAD-VAVLEVDEMH---VPHVADAVNPAVIVLLNLSRDQLDRVGEINNIERTLRKGL 157
Cdd:PRK11929 633 rvLATEGNfNNEIGVPLTLLRLRAQHrAAVFELGMNHpgeIAYLAAIAAPTVALVTNAQREHQEFMHSVEAVARAKGEII 712

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 158 ARHR-DAVIVANCDDvlmasaaydsPHVV-WVAAGGG----WAGDSVSCPRSGELIMRDGNRWYSTGTDFarpdpdwwfd 231
Cdd:PRK11929 713 AALPeDGVAVVNGDD----------PYTAiWAKLAGArrvlRFGLQPGADVYAEKIAKDISVGEAGGTRC---------- 772

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491214147 232 ddRIYGPSGiSLPMSLTLPGTANRGNATLAVAAAVELGARPGPAVDAVSAVDQVAGRYRSINLGDHTI 299
Cdd:PRK11929 773 --QVVTPAG-SAEVYLPLIGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRRRLSCGTR 837
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 60-296 6.28e-08

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: 54.63  E-value: 6.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147   60 ITGTNGKSTTTRMTAAAL----------ATVG----------PVATNTEGSNMDagLVAALAGTRE--ADVAVLEVDEmH 117
Cdd:TIGR01085  90 VTGTNGKTTTTSLIAQLLrllgkktgliGTIGyrlggndlikNPAALTTPEALT--LQSTLAEMVEagAQYAVMEVSS-H 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  118 --VPHVADAVNPAVIVLLNLSRDQLDRVGEINN---IERTLRKGLARHRDAVIvaNCDDVLMASAAYDSPHVVWVAAGGG 192
Cdd:TIGR01085 167 alAQGRVRGVRFDAAVFTNLSRDHLDFHGTMENyfaAKASLFTELGLKRFAVI--NLDDEYGAQFVKRLPKDITVSAITQ 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  193 WAGDSVSCPRsgelIMRDGNRWYstGTDFarpdpdwwfdddRIYGPSGIsLPMSLTLPGTANRGNATLAVAAAVELGARP 272
Cdd:TIGR01085 245 PADGRAQDIK----ITDSGYSFE--GQQF------------TFETPAGE-GHLHTPLIGRFNVYNLLAALATLLHLGGID 305

                         250       260
                  ....*....|....*....|....*
gi 491214147  273 GPA-VDAVSAVDQVAGRYRSINLGD 296
Cdd:TIGR01085 306 LEDiVAALEKFRGVPGRMELVDGGQ 330
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
 58-178 7.62e-07

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


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 51.12  E-value: 7.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  58 VLITGTNGKSTTTrmtaaalATVGPVATNTEGSNMDAG-----LVAALAGTREADVAVLEVDEMHVPHVADaVNPAVIVL 132
Cdd:PRK14106 111 VAITGTNGKTTTT-------TLLGEIFKNAGRKTLVAGnigypLIDAVEEYGEDDIIVAEVSSFQLETIKE-FKPKVGCI 182

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 491214147 133 LNLSRDQLDRVGEINN-IERTLRKGLARHRDAVIVANCDDVLMASAA 178
Cdd:PRK14106 183 LNITPDHLDRHKTMENyIKAKARIFENQRPSDYTVLNYDDPRTRSLA 229
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 60-288 3.13e-05

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 45.89  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  60 ITGTNGKSTTTRMTAAALA----------TVG-------PVATNTEGSNMDagLVAALAGTREADV--AVLEV-----DE 115
Cdd:PRK00139 100 VTGTNGKTTTAYLLAQILRllgektaligTLGngiggelIPSGLTTPDALD--LQRLLAELVDAGVtyAAMEVsshalDQ 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 116 MHVphvaDAVNPAVIVLLNLSRDQLDRVGEINNIERTLRKGLARHRDAVIVaNCDDVlMASAAYDSPHVVWVAAGGGWag 195
Cdd:PRK00139 178 GRV----DGLKFDVAVFTNLSRDHLDYHGTMEDYLAAKARLFSELGLAAVI-NADDE-VGRRLLALPDAYAVSMAGAD-- 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 196 dsvscprsgelIMRDGNRWYSTGTDFArpdpdwwfdddriygpsgISLPMSLTLPGTANRGNATLAVAAAVELGARPGPA 275
Cdd:PRK00139 250 -----------LRATDVEYTDSGQTFT------------------LVTEVESPLIGRFNVSNLLAALAALLALGVPLEDA 300

                        250
                 ....*....|...
gi 491214147 276 VDAVSAVDQVAGR 288
Cdd:PRK00139 301 LAALAKLQGVPGR 313
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 56-288 4.03e-04

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: 42.77  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147  56 RTVLITGTNGKSTTTRMTAAAL----ATVGPVATN----------TEGSNMDA-GLVAALAGTREA--DVAVLEVDEMH- 117
Cdd:PRK11929 113 SLVAVTGTNGKTSCAQLLAQLLtrlgKPCGSIGTLgarldgrlipGSLTTPDAiILHRILARMRAAgaDAVAMEASSHGl 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 118 VPHVADAVNPAVIVLLNLSRDQLDRVGEINNIERTlRKGLAR--HRDAVIVANCDDVLMASAAYDSPHVVWVAAGGGWAG 195
Cdd:PRK11929 193 EQGRLDGLRIAVAGFTNLTRDHLDYHGTMQDYEEA-KAALFSklPGLGAAVINADDPAAARLLAALPRGLKVGYSPQNAG 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491214147 196 DSVscpRSGELimRDGnrwySTGTDFarpdpdwwfdddRIYGPSGiSLPMSLTLPGTANRGNATLAVAAAVELGARPGPA 275
Cdd:PRK11929 272 ADV---QARDL--RAT----AHGQVF------------TLATPDG-SYQLVTRLLGRFNVSNLLLVAAALKKLGLPLAQI 329

                        250
                 ....*....|...
gi 491214147 276 VDAVSAVDQVAGR 288
Cdd:PRK11929 330 ARALAAVSPVPGR 342
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 58-112 2.79e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 40.14  E-value: 2.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491214147  58 VLITGTNGKSTTTRMTAAALATVGPVA--TNTEG---------SNMDAGLVAA---LAgTREADVAVLE 112
Cdd:PRK14016 483 VAVTGTNGKTTTTRLIAHILKLSGKRVgmTTTDGvyidgrlidKGDCTGPKSArrvLM-NPDVEAAVLE 550
 
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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