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CAZyme Information: MGYG000004279_00145

You are here: Home > Sequence: MGYG000004279_00145

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 UMGS1484 sp900552285
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1484; UMGS1484 sp900552285
CAZyme ID MGYG000004279_00145
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
315 MGYG000004279_6|CGC1 34775.88 9.8534
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004279 1699873 MAG China Asia
Gene Location Start: 5258;  End: 6205  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004279_00145.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK11198 PRK11198 1.99e-13 256 313 86 146
LysM domain/BON superfamily protein; Provisional
pfam01476 LysM 1.19e-12 268 313 1 43
LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
pfam01510 Amidase_2 4.07e-12 26 162 2 121
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.
cd00118 LysM 1.33e-09 266 312 1 45
Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
smart00257 LysM 2.43e-08 267 312 1 44
Lysin motif.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUO22979.1 6.11e-106 1 314 184 505
AFB75734.1 2.76e-104 1 314 184 505
ADB89215.1 7.45e-97 1 182 11 192
CBL18646.1 5.72e-92 1 181 3 183
AFB76124.1 6.14e-72 4 313 7 241

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
1.000028 0.000003 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004279_00145.