peptidoglycan recognition protein LA, isoform E [Drosophila melanogaster]
peptidoglycan recognition protein( domain architecture ID 11274790)
peptidoglycan recognition protein (PGRP) is a pattern recognition receptor that binds and may also hydrolyze peptidoglycans (PGNs) of bacterial cell walls
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PGRP | smart00701 | Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ... |
181-322 | 5.68e-53 | |||
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: 172.09 E-value: 5.68e-53
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Name | Accession | Description | Interval | E-value | |||
PGRP | smart00701 | Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ... |
181-322 | 5.68e-53 | |||
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: 172.09 E-value: 5.68e-53
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PGRP | cd06583 | Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ... |
205-331 | 7.48e-22 | |||
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. Pssm-ID: 133475 [Multi-domain] Cd Length: 126 Bit Score: 89.66 E-value: 7.48e-22
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Amidase_2 | pfam01510 | N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ... |
246-329 | 2.29e-07 | |||
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding. Pssm-ID: 460236 [Multi-domain] Cd Length: 122 Bit Score: 48.89 E-value: 2.29e-07
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Name | Accession | Description | Interval | E-value | |||
PGRP | smart00701 | Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme; The ... |
181-322 | 5.68e-53 | |||
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: 172.09 E-value: 5.68e-53
|
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PGRP | cd06583 | Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ... |
205-331 | 7.48e-22 | |||
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. Pssm-ID: 133475 [Multi-domain] Cd Length: 126 Bit Score: 89.66 E-value: 7.48e-22
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Amidase_2 | pfam01510 | N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ... |
246-329 | 2.29e-07 | |||
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding. Pssm-ID: 460236 [Multi-domain] Cd Length: 122 Bit Score: 48.89 E-value: 2.29e-07
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Ami_2 | smart00644 | Ami_2 domain; |
204-328 | 8.88e-06 | |||
Ami_2 domain; Pssm-ID: 214760 [Multi-domain] Cd Length: 126 Bit Score: 44.66 E-value: 8.88e-06
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Blast search parameters | ||||
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