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Conserved domains on  [gi|569001191|ref|XP_006524776|]
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N-acetylmuramoyl-L-alanine amidase isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PGRP super family cl02712
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
360-421 2.67e-17

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


The actual alignment was detected with superfamily member smart00701:

Pssm-ID: 470657  Cd Length: 142  Bit Score: 78.49  E-value: 2.67e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569001191   360 PAIHPRCRWGAAPyRGHPTPLRLPLGFLYVHHTYVPAppCTTFQSCAADMRSMQRFHQDFRG 421
Cdd:smart00701   1 PPIVPRSEWGAKP-RGHTPRLTRPVRYVIIHHTATPN--CYTDAQCAQILRNIQAYHMEELG 59
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
360-421 2.67e-17

Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.


Pssm-ID: 128941  Cd Length: 142  Bit Score: 78.49  E-value: 2.67e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569001191   360 PAIHPRCRWGAAPyRGHPTPLRLPLGFLYVHHTYVPAppCTTFQSCAADMRSMQRFHQDFRG 421
Cdd:smart00701   1 PPIVPRSEWGAKP-RGHTPRLTRPVRYVIIHHTATPN--CYTDAQCAQILRNIQAYHMEELG 59
 
Name Accession Description Interval E-value
PGRP smart00701
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ...
360-421 2.67e-17

Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.


Pssm-ID: 128941  Cd Length: 142  Bit Score: 78.49  E-value: 2.67e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569001191   360 PAIHPRCRWGAAPyRGHPTPLRLPLGFLYVHHTYVPAppCTTFQSCAADMRSMQRFHQDFRG 421
Cdd:smart00701   1 PPIVPRSEWGAKP-RGHTPRLTRPVRYVIIHHTATPN--CYTDAQCAQILRNIQAYHMEELG 59
 
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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