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CAZyme Information: MGYG000004678_01273

You are here: Home > Sequence: MGYG000004678_01273

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 Finegoldia magna
Lineage Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Finegoldia; Finegoldia magna
CAZyme ID MGYG000004678_01273
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
780 87027.13 9.6892
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004678 1841606 Isolate United States North America
Gene Location Start: 71609;  End: 73951  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004678_01273.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 578 751 3.9e-44 0.9887005649717514

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06414 GH25_LytC-like 2.01e-75 574 765 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 8.52e-38 575 763 1 185
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.
pfam01183 Glyco_hydro_25 1.01e-31 578 751 2 180
Glycosyl hydrolases family 25.
cd06525 GH25_Lyc-like 3.59e-28 575 763 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.
pfam04122 CW_binding_2 9.71e-23 375 460 1 80
Putative cell wall binding repeat 2. This repeat is found in multiple tandem copies in proteins including amidase enhancers and adhesins.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAG07790.1 0.0 1 780 1 780
QKH79509.1 0.0 1 780 1 785
QQK08229.1 8.37e-51 576 780 5 217
QAR21437.1 8.79e-44 575 780 5 206
QQO42089.1 1.20e-43 575 780 5 206

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5J72_A 5.84e-28 177 452 134 419
ChainA, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630],5J72_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630]
5J6Q_A 2.06e-21 178 426 289 551
ChainA, Cell wall binding protein cwp8 [Clostridioides difficile 630]
7ACZ_B 1.11e-20 140 429 3 341
ChainB, SLPH (HMW SLP) [Clostridioides difficile R20291],7ACZ_D Chain D, SLPH (HMW SLP) [Clostridioides difficile R20291]
7ACX_B 4.08e-20 178 426 43 329
ChainB, S-layer protein [Clostridioides difficile],7ACX_D Chain D, S-layer protein [Clostridioides difficile]
7ACY_B 7.36e-20 178 426 43 329
ChainB, S-layer protein [Clostridioides difficile 630],7ACY_D Chain D, S-layer protein [Clostridioides difficile 630],7QGQ_B Chain B, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_D Chain D, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_J Chain J, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_K Chain K, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_L Chain L, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_M Chain M, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_N Chain N, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_T Chain T, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_U Chain U, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_V Chain V, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_W Chain W, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_X Chain X, Precursor of the S-layer proteins [Clostridioides difficile 630]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q02114 2.80e-32 177 467 30 315
N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
Q02113 2.85e-25 174 423 61 302
Amidase enhancer OS=Bacillus subtilis (strain 168) OX=224308 GN=lytB PE=1 SV=1
P26836 8.20e-15 575 779 10 211
Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8X7H0 1.84e-11 535 762 30 252
Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421 4.49e-11 535 762 30 252
Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 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
0.000402 0.998832 0.000270 0.000160 0.000162 0.000153

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004678_01273.