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CAZyme Information: MGYG000000661_00212

You are here: Home > Sequence: MGYG000000661_00212

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
Lineage Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-302;
CAZyme ID MGYG000000661_00212
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
247 28078.81 4.4604
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000661 1287314 MAG Kazakhstan Asia
Gene Location Start: 39499;  End: 40242  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000661_00212.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM50 174 216 8.5e-17 0.975

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3409 PGRP 1.86e-25 13 153 40 183
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis].
pfam01471 PG_binding_1 1.89e-18 97 153 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.
pfam01476 LysM 2.15e-16 174 216 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.
cd00118 LysM 9.21e-15 174 215 3 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.
COG3409 PGRP 3.87e-14 57 155 12 104
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUH19058.1 2.92e-23 90 216 69 195
CCC57680.1 9.90e-22 15 218 31 223
ABW20078.1 1.70e-21 90 217 69 198
AUS95891.1 1.70e-20 95 230 7 135
ADI02383.1 3.13e-20 14 217 48 223

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4UZ2_A 1.17e-12 174 217 5 48
Crystalstructure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_D Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ3_A Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8]
4XCM_A 1.59e-11 174 217 5 48
Crystalstructure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4XCM_B Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8]
3BKH_A 2.74e-11 91 159 11 79
ChainA, lytic transglycosylase [Pseudomonas phage phiKZ],3BKV_A Chain A, lytic transglycosylase [Pseudomonas phage phiKZ]
5TV7_A 1.12e-10 81 159 98 175
ChainA, Putative peptidoglycan-binding/hydrolysing protein [Clostridioides difficile 630],5TV7_B Chain B, Putative peptidoglycan-binding/hydrolysing protein [Clostridioides difficile 630]
4LPQ_A 1.19e-07 95 159 14 78
Crystalstructure of the L,D-transpeptidase (residues 123-326) from Xylanimonas cellulosilytica DSM 15894 [Xylanimonas cellulosilytica DSM 15894]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54421 2.52e-09 174 220 88 134
Probable peptidoglycan endopeptidase LytE OS=Bacillus subtilis (strain 168) OX=224308 GN=lytE PE=1 SV=1
Q01838 4.94e-08 174 215 320 361
Probable endopeptidase p60 OS=Listeria seeligeri OX=1640 GN=iap PE=3 SV=1
O07532 6.44e-08 173 220 93 140
Peptidoglycan endopeptidase LytF OS=Bacillus subtilis (strain 168) OX=224308 GN=lytF PE=1 SV=2
L7N653 1.06e-07 11 166 11 179
N-acetylmuramoyl-L-alanine amidase CwlM OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=cwlM PE=1 SV=1
Q01837 2.90e-07 174 215 314 355
Probable endopeptidase p60 OS=Listeria ivanovii OX=1638 GN=iap PE=3 SV=1

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
0.965262 0.034444 0.000124 0.000071 0.000039 0.000075

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000661_00212.