logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004691_01979

You are here: Home > Sequence: MGYG000004691_01979

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 UBA9502 sp900555625
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA9502; UBA9502 sp900555625
CAZyme ID MGYG000004691_01979
CAZy Family GH0
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
445 MGYG000004691_142|CGC1 49523.54 4.8092
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004691 2701187 MAG China Asia
Gene Location Start: 448;  End: 1785  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004691_01979.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01471 PG_binding_1 4.62e-12 369 430 1 57
Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.
COG3409 PGRP 1.99e-07 364 430 39 102
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis].
pfam13620 CarboxypepD_reg 1.96e-06 44 136 6 81
Carboxypeptidase regulatory-like domain.
COG3409 PGRP 3.87e-06 360 432 117 185
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis].
cd11308 Peptidase_M14NE-CP-C_like 0.003 44 132 6 71
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain. This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASN94441.1 1.29e-227 29 443 3 415
QRP40879.1 1.29e-227 29 443 3 415
QJU21247.1 3.69e-227 29 443 3 415
QIX92999.1 6.08e-226 29 443 3 415
ANU48790.1 1.74e-225 29 443 3 415

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1LBU_A 3.99e-06 358 430 5 73
HydrolaseMetallo (zn) Dd-peptidase [Streptomyces albus G]

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
1.000046 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004691_01979.