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CAZyme Information: MGYG000001443_01782

You are here: Home > Sequence: MGYG000001443_01782

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 Streptomyces albus
Lineage Bacteria; Actinobacteriota; Actinomycetia; Streptomycetales; Streptomycetaceae; Streptomyces; Streptomyces albus
CAZyme ID MGYG000001443_01782
CAZy Family GH23
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
269 MGYG000001443_1|CGC21 28257.95 5.9644
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001443 7820353 Isolate not provided not provided
Gene Location Start: 2187445;  End: 2188254  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001443_01782.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd13402 LT_TF-like 7.01e-30 192 268 6 81
lytic transglycosylase-like domain of tail fiber-like proteins and similar domains. These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
COG3953 SLT 6.60e-16 189 267 17 96
SLT domain protein [Mobilome: prophages, transposons].
pfam01464 SLT 1.45e-08 194 264 18 83
Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
cd00118 LysM 1.83e-07 73 121 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.
NF033163 lipo_LipL71 2.69e-07 66 122 399 460
lipoprotein LipL71. Members of this family are lipoprotein LipL71, also known as LruA, as described in Leptospira interrogans but found broadly in the genus Leptospira. Close homologs that are not lipoproteins by sequence are likely defective in their reported coding region.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QID36106.1 8.39e-191 1 269 1 269
AXK34636.1 4.79e-103 1 269 1 274
QNP66800.1 5.89e-86 14 269 9 260
QMU16880.1 7.12e-82 17 269 12 292
ALC20241.1 7.12e-82 17 269 12 292

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54334 5.85e-14 166 267 1093 1191
Phage-like element PBSX protein XkdO OS=Bacillus subtilis (strain 168) OX=224308 GN=xkdO PE=4 SV=2
P45931 1.18e-12 164 267 1343 1443
Uncharacterized protein YqbO OS=Bacillus subtilis (strain 168) OX=224308 GN=yqbO PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.023335 0.950715 0.002231 0.022087 0.001308 0.000298

TMHMM  Annotations      download full data without filtering help

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