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CAZyme Information: MGYG000001625_01482

You are here: Home > Sequence: MGYG000001625_01482

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 Eikenella corrodens
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Neisseriaceae; Eikenella; Eikenella corrodens
CAZyme ID MGYG000001625_01482
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
221 24016.7 11.6955
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001625 1812730 MAG China Asia
Gene Location Start: 2890;  End: 3555  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001625_01482.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM50 176 218 1.9e-16 0.975

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10783 mltD 3.27e-18 71 215 328 444
membrane-bound lytic murein transglycosylase D; Provisional
pfam01476 LysM 3.47e-16 176 217 1 42
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.
PRK06347 PRK06347 1.58e-15 87 221 332 453
1,4-beta-N-acetylmuramoylhydrolase.
cd00118 LysM 2.95e-15 174 217 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.
PRK06347 PRK06347 1.48e-14 87 221 407 527
1,4-beta-N-acetylmuramoylhydrolase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SNW10682.1 7.88e-119 1 221 532 754
AZR59785.1 3.59e-102 1 221 531 751
QED92057.1 8.50e-95 1 221 533 747
QMT41365.1 4.30e-34 1 220 498 680
QIP50974.1 2.98e-26 23 217 506 689

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4UZ2_A 1.03e-06 174 219 3 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 6.22e-06 174 219 3 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]
2MKX_A 7.24e-06 176 221 7 52
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
Q5HIL2 1.95e-12 86 218 27 135
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain COL) OX=93062 GN=sle1 PE=3 SV=1
Q6GJK9 1.95e-12 86 218 27 135
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=sle1 PE=3 SV=1
Q2FJH7 1.95e-12 86 218 27 135
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain USA300) OX=367830 GN=sle1 PE=3 SV=1
Q6GC24 1.95e-12 86 218 27 135
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=sle1 PE=3 SV=1
Q2G0U9 1.95e-12 86 218 27 135
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=sle1 PE=1 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
1.000058 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001625_01482.