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CAZyme Information: MGYG000000102_02991

You are here: Home > Sequence: MGYG000000102_02991

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 Terrisporobacter sp902363255
Lineage Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Terrisporobacter; Terrisporobacter sp902363255
CAZyme ID MGYG000000102_02991
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
446 MGYG000000102_6|CGC2 50717.97 5.1656
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000102 3838773 Isolate Canada North America
Gene Location Start: 71196;  End: 72536  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000102_02991.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 7 184 7.7e-51 0.9943502824858758
CBM50 345 387 4e-16 0.95

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06525 GH25_Lyc-like 2.86e-84 5 193 1 184
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases 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.
pfam01183 Glyco_hydro_25 3.30e-63 7 184 1 180
Glycosyl hydrolases family 25.
cd00599 GH25_muramidase 2.80e-58 5 193 1 186
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.
COG3757 Acm 1.59e-44 4 198 63 258
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06524 GH25_YegX-like 4.91e-42 5 194 1 193
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QBJ75914.1 1.15e-127 5 445 10 442
ATD56705.1 1.15e-127 5 445 10 442
SLK20760.1 1.15e-127 5 445 10 442
ATD55618.1 1.15e-127 5 445 10 442
QAS60493.1 1.27e-117 5 387 10 384

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4KRU_A 6.21e-54 5 200 21 214
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A 1.98e-52 5 200 21 214
X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
5A6S_A 1.65e-19 8 195 26 203
Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A 3.62e-19 5 193 6 202
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A 6.32e-14 3 194 15 207
TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P26836 6.18e-51 5 197 10 200
Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020 8.36e-38 5 199 2 186
Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
Q8CMN2 9.12e-29 223 387 31 190
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q5HRU2 9.12e-29 223 387 31 190
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1
Q49UX4 2.52e-28 221 396 29 200
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 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
1.000051 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000102_02991.