logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001436_02397

You are here: Home > Sequence: MGYG000001436_02397

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 Paenibacillus_F sp000411255
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_F; Paenibacillus_F sp000411255
CAZyme ID MGYG000001436_02397
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
121 MGYG000001436_1|CGC27 13447.17 9.7917
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001436 6290841 Isolate not provided not provided
Gene Location Start: 2687394;  End: 2687759  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001436_02397.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM50 4 46 1.5e-16 0.975

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01476 LysM 1.13e-17 4 45 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.
cd00118 LysM 3.41e-16 3 45 2 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 1.81e-14 3 45 1 44
Lysin motif.
COG1388 LysM 2.18e-11 3 43 68 108
LysM repeat [Cell wall/membrane/envelope biogenesis].
PRK10783 mltD 3.09e-09 3 45 345 387
membrane-bound lytic murein transglycosylase D; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QAV16226.1 3.10e-27 1 84 1 88
ALS24302.1 5.37e-11 1 46 1 46
QIZ08316.1 2.05e-10 3 46 8 51
QGP92021.1 3.95e-10 3 46 35 78
QOT00870.1 4.30e-10 4 47 3 47

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4UZ2_A 5.60e-10 3 47 4 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 1.11e-08 3 47 4 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O07532 2.61e-06 3 46 28 71
Peptidoglycan endopeptidase LytF OS=Bacillus subtilis (strain 168) OX=224308 GN=lytF PE=1 SV=2
Q01837 3.60e-06 2 45 196 239
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
1.000048 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001436_02397.