logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004552_01477

You are here: Home > Sequence: MGYG000004552_01477

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Frisingicoccus sp900757195
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Frisingicoccus; Frisingicoccus sp900757195
CAZyme ID MGYG000004552_01477
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
477 MGYG000004552_10|CGC1 52671.8 8.4823
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004552 2535946 MAG France Europe
Gene Location Start: 62403;  End: 63836  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004552_01477.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam18013 Phage_lysozyme2 2.65e-31 235 395 4 139
Phage tail lysozyme. This domain has a lysozyme like fold. It is found in the tail protein of various phages probably giving them the ability to degrade the host cell wall peptidoglycan layer.
cd06583 PGRP 4.03e-11 29 163 2 110
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.
pfam01510 Amidase_2 6.73e-11 28 178 1 112
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.
smart00644 Ami_2 1.50e-08 29 178 3 119
Ami_2 domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AFB75852.1 8.87e-129 2 244 1 244
QAT50916.1 5.96e-62 15 213 8 191
ABZ85376.1 2.59e-60 15 216 8 188
CDM67796.1 8.54e-60 15 235 8 206
AFB75734.1 1.87e-59 234 420 9 197

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000058 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004552_01477.