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CAZyme Information: MGYG000001062_00240

You are here: Home > Sequence: MGYG000001062_00240

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 CAG-1427 sp900556585
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; CAG-1427; CAG-1427 sp900556585
CAZyme ID MGYG000001062_00240
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
775 84434.7 4.387
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001062 1871556 MAG Spain Europe
Gene Location Start: 2255;  End: 4582  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001062_00240.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 2 138 5.8e-24 0.7344632768361582
CBM13 658 773 8.4e-23 0.5851063829787234
CBM13 329 418 6e-20 0.4574468085106383
CBM13 477 577 8.5e-19 0.5106382978723404

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06414 GH25_LytC-like 1.78e-45 2 148 53 191
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.
pfam14200 RicinB_lectin_2 1.68e-27 367 455 1 89
Ricin-type beta-trefoil lectin domain-like.
pfam14200 RicinB_lectin_2 6.32e-22 670 759 1 89
Ricin-type beta-trefoil lectin domain-like.
pfam14200 RicinB_lectin_2 4.31e-20 516 605 2 89
Ricin-type beta-trefoil lectin domain-like.
cd00599 GH25_muramidase 8.92e-16 2 146 49 185
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
BAK44097.1 2.69e-152 1 537 677 1212
BAQ29887.1 5.15e-42 4 535 246 785
QTB90054.1 5.73e-42 4 679 236 915
BAR06175.1 2.41e-41 4 371 354 738
AIZ15211.1 2.46e-41 4 379 279 650

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WW5_A 4.60e-09 4 148 321 468
3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A 1.06e-08 4 148 321 468
3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
6IFA_A 2.81e-06 187 289 14 106
Structureof beta-trefoil lectin from Entamoeba histolytica [Entamoeba histolytica HM-1:IMSS],6IFA_B Structure of beta-trefoil lectin from Entamoeba histolytica [Entamoeba histolytica HM-1:IMSS],6IFA_C Structure of beta-trefoil lectin from Entamoeba histolytica [Entamoeba histolytica HM-1:IMSS]
6IFB_A 3.19e-06 187 289 20 112
Structureof rhamnose bound beta-trefoil lectin from Entamoeba histolytica [Entamoeba histolytica HM-1:IMSS],6IFB_B Structure of rhamnose bound beta-trefoil lectin from Entamoeba histolytica [Entamoeba histolytica HM-1:IMSS]

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000074 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001062_00240.