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CAZyme Information: MGYG000003528_01584

You are here: Home > Sequence: MGYG000003528_01584

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 CAAGGB01 sp900769285
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; UBA1407; UBA1407; CAAGGB01; CAAGGB01 sp900769285
CAZyme ID MGYG000003528_01584
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
539 MGYG000003528_201|CGC1 54894.1 10.1323
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003528 3662993 MAG Fiji Oceania
Gene Location Start: 8691;  End: 10310  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003528_01584.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM50 290 331 2.6e-16 0.95
CBM50 190 233 5e-16 0.975

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK06347 PRK06347 1.75e-26 171 418 385 592
1,4-beta-N-acetylmuramoylhydrolase.
PRK06347 PRK06347 5.00e-25 188 415 331 521
1,4-beta-N-acetylmuramoylhydrolase.
PRK06347 PRK06347 3.50e-19 254 415 305 447
1,4-beta-N-acetylmuramoylhydrolase.
pfam01476 LysM 2.00e-16 290 332 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 4.45e-16 188 232 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QZN88654.1 7.73e-23 190 538 267 596
ARK32193.1 8.57e-22 177 520 375 696
QQL45181.1 9.83e-20 182 435 160 372
QIB53303.1 1.74e-19 170 417 245 431
AHF89485.1 3.51e-19 183 423 117 301

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4UZ2_A 1.83e-06 290 331 5 46
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]
2MKX_A 4.22e-06 290 332 7 49
Solutionstructure of LysM the peptidoglycan binding domain of autolysin AtlA from Enterococcus faecalis [Enterococcus faecalis V583]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31852 1.90e-15 190 417 90 268
D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlS PE=1 SV=1
O07532 1.13e-14 289 417 241 350
Peptidoglycan endopeptidase LytF OS=Bacillus subtilis (strain 168) OX=224308 GN=lytF PE=1 SV=2
P54421 7.97e-14 290 418 88 193
Probable peptidoglycan endopeptidase LytE OS=Bacillus subtilis (strain 168) OX=224308 GN=lytE PE=1 SV=1
P37710 2.70e-12 190 415 567 734
Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2
P0C2T5 2.75e-12 290 417 245 362
Probable N-acetylmuramidase OS=Lactococcus lactis subsp. cremoris OX=1359 GN=acmA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000002 0.999953 0.000000 0.000097 0.000000

TMHMM  Annotations      download full data without filtering help

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