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CAZyme Information: MGYG000000143_02313

You are here: Home > Sequence: MGYG000000143_02313

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 Turicibacter sanguinis
Lineage Bacteria; Firmicutes; Bacilli; Haloplasmatales_A; Turicibacteraceae; Turicibacter; Turicibacter sanguinis
CAZyme ID MGYG000000143_02313
CAZy Family GH25
CAZyme Description Cell division suppressor protein YneA
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
451 49285.98 3.9065
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000143 2958073 Isolate United Kingdom Europe
Gene Location Start: 23454;  End: 24809  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000143_02313.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 36 210 1.1e-48 0.9943502824858758
CBM50 354 397 5.5e-17 0.975
CBM50 246 289 6.7e-17 0.975
CBM50 300 343 8.9e-17 0.975

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06525 GH25_Lyc-like 3.69e-74 34 220 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.
cd00599 GH25_muramidase 2.03e-49 35 220 2 186
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.
pfam01183 Glyco_hydro_25 1.04e-46 36 210 1 180
Glycosyl hydrolases family 25.
cd06414 GH25_LytC-like 5.02e-44 35 220 3 190
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.
COG3757 Acm 2.09e-40 30 225 60 258
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
QJS18123.1 1.12e-317 1 451 1 451
QWT55024.1 3.04e-130 20 448 23 463
QBE96304.1 3.24e-121 24 397 25 403
QIB56830.1 1.19e-118 24 397 25 403
QMW80393.1 1.19e-118 24 397 25 403

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4KRU_A 3.84e-48 35 228 22 215
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A 1.06e-46 35 228 22 215
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]
1JFX_A 1.20e-20 35 220 7 202
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4B8V_A 9.85e-20 290 450 37 216
ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]
2WAG_A 4.13e-15 35 220 18 206
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 3.38e-44 28 224 6 200
Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P39046 1.60e-36 246 448 414 662
Muramidase-2 OS=Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R) OX=768486 GN=EHR_05900 PE=1 SV=1
P34020 3.30e-34 35 234 3 194
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
Q49UX4 1.25e-32 298 448 27 191
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
O07532 3.02e-31 246 451 94 351
Peptidoglycan endopeptidase LytF OS=Bacillus subtilis (strain 168) OX=224308 GN=lytF 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
0.000262 0.999074 0.000182 0.000170 0.000158 0.000149

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000143_02313.