logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000113_00485

You are here: Home > Sequence: MGYG000000113_00485

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 Streptococcus salivarius
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus salivarius
CAZyme ID MGYG000000113_00485
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
967 MGYG000000113_2|CGC6 104818.12 6.8285
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000113 2251845 Isolate Canada North America
Gene Location Start: 251522;  End: 254425  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000113_00485.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 164 350 9.7e-40 0.9717514124293786

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06522 GH25_AtlA-like 1.80e-77 161 364 1 192
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
pfam01183 Glyco_hydro_25 3.45e-37 164 351 1 177
Glycosyl hydrolases family 25.
pfam08481 GBS_Bsp-like 1.45e-32 807 895 1 89
GBS Bsp-like repeat. This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology.
pfam08481 GBS_Bsp-like 1.53e-31 389 477 1 89
GBS Bsp-like repeat. This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology.
cd00599 GH25_muramidase 4.71e-27 163 351 2 174
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ARC22445.1 0.0 1 967 1 967
ALR79927.1 0.0 1 967 1 967
QMI50992.1 0.0 1 967 1 967
ARI57272.1 0.0 1 967 1 967
CCB95385.1 0.0 1 967 1 967

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000294 0.998861 0.000276 0.000185 0.000185 0.000153

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000113_00485.