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CAZyme Information: MGYG000000231_02066

You are here: Home > Sequence: MGYG000000231_02066

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 Coprococcus eutactus_A
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus eutactus_A
CAZyme ID MGYG000000231_02066
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
860 95341.39 9.5042
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000231 3050336 Isolate China Asia
Gene Location Start: 17715;  End: 20297  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000231_02066.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 117 306 2.5e-43 0.9943502824858758

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06414 GH25_LytC-like 6.78e-72 114 316 1 191
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599 GH25_muramidase 3.31e-31 115 313 1 184
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.
pfam01183 Glyco_hydro_25 1.17e-26 117 306 1 180
Glycosyl hydrolases family 25.
cd06525 GH25_Lyc-like 1.67e-26 115 314 1 183
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.
COG3757 Acm 7.63e-22 113 313 62 251
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBK82808.1 0.0 1 860 1 860
CBK82807.1 4.81e-117 1 288 1 289
CCO05379.1 5.21e-88 3 788 4 846
QNL98623.1 3.52e-57 101 316 35 251
BAK47549.1 2.20e-49 102 561 191 634

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1JFX_A 6.57e-13 114 313 5 200
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A 2.32e-09 152 314 54 200
Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
5J7K_A 2.95e-06 605 677 2 72
Loopgrafting onto a highly stable FN3 scaffold [synthetic construct],5J7K_B Loop grafting onto a highly stable FN3 scaffold [synthetic construct],5J7K_C Loop grafting onto a highly stable FN3 scaffold [synthetic construct],5J7K_D Loop grafting onto a highly stable FN3 scaffold [synthetic construct],5J7K_E Loop grafting onto a highly stable FN3 scaffold [synthetic construct],5J7K_F Loop grafting onto a highly stable FN3 scaffold [synthetic construct],5J7K_G Loop grafting onto a highly stable FN3 scaffold [synthetic construct],5J7K_H Loop grafting onto a highly stable FN3 scaffold [synthetic construct]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P25310 1.13e-11 114 313 82 277
Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836 3.27e-10 114 313 9 194
Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P50899 6.96e-09 403 720 695 1021
Exoglucanase B OS=Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) OX=590998 GN=cbhB PE=1 SV=1

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
0.000352 0.998881 0.000197 0.000203 0.000173 0.000151

TMHMM  Annotations      download full data without filtering help

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9 31