CAZyme Information: MGYG000001571_03392

Basic Information

• Species: Lacrimispora sp000526575
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lacrimispora; Lacrimispora sp000526575
• CAZyme ID: MGYG000001571_03392
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
316	MGYG000001571_33|CGC1	35778.06	4.9204

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001571	4730558	MAG	United States	North America

• Gene Location: Start: 15200; End: 16150 Strand: -

Full Sequence      

MNIRMRVTAGIIAGLVTSIIIATPMNGFSGEAWSQENGQYVDASGKPITGALEKGITVSK
YQNRQNEEGGGINWDKVKESGVSFAMIRLGYLNDKDPYYSVNMTNAAKSGIKTGIFFYTQ
ALDVATAEEEARYVLREIKDYPISYPVAYDVESQYLLDNRMTRQQITDNINAFCKIIEDA
GYRPIVYANNKWLNYHIDMSRIPYDVWYARYGTVNDCTNRTIWQCTDQGRVAGIEGDVTI
EFSFKDYHGLIPADGWKTIDGNRYYMKNFNKQTGWLSLDGAWYYLDQNGVMVHDTDMVVD
GTSYHFESDGTTKGKS

Enzyme Prediction     

No EC number prediction in MGYG000001571_03392.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	56	234	4.7e-42	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.70e-73	54	244	2	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	1.12e-31	54	238	1	181	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	1.12e-24	56	234	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	7.31e-21	54	238	4	184	Uncharacterized bacterial muramidase containing 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	2.12e-19	54	240	64	250	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SET59461.1	5.56e-162	2	310	4	312
ADL03867.1	3.54e-158	2	310	4	312
QRV22095.1	3.54e-158	2	310	4	312
ASN93256.1	2.89e-131	6	297	58	347
QRP42084.1	2.89e-131	6	297	58	347

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	3.23e-13	96	254	59	212	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	3.70e-08	54	238	6	197	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	3.70e-07	54	238	83	274	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.021000	0.973805	0.004225	0.000411	0.000280	0.000241

TMHMM  Annotations     

start	end
7	29