CAZyme Information: MGYG000003613_02032

Basic Information

• Species: SFDP01 sp004558185
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; SFDP01; SFDP01 sp004558185
• CAZyme ID: MGYG000003613_02032
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
358	MGYG000003613_148|CGC1	40581.14	4.141

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003613	2865067	MAG	Fiji	Oceania

• Gene Location: Start: 883; End: 1959 Strand: +

Full Sequence      

MRQTNDYEDNSGGLPLIGMALGVSFFVLLILLLVVSLNKKNSSPSRPQAAAVSSEEEDTA
DYLAGSNLVASDLGFWDMYPPEEETSTVTEEKTQEEETTTEEDPATDGKHVQVTLRDGTT
EWLEINPKWKRNTYDFSNLVSKNNLLKYYADGKQASYLGIDLSRYQKEVNYGALKNEGID
FCMIRVGARGYETGTIQADDMFETHIAGVTQAGIDVGLYFYSQAITEAEAVEEANYLLSR
IGTHKITYPIAFDMEYVENDTARIETLTNSERTKIALAFLKRIEEAGYTGMLYGNKEWLL
KRIDLSQFEEYDIWLAQEADIPDYPYTYSMWQYSRKGEIYGIDGYVDLNISFVDYSAR

Enzyme Prediction     

No EC number prediction in MGYG000003613_02032.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	160	342	2e-42	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.75e-73	159	352	3	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	1.81e-27	159	350	2	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	2.08e-24	160	342	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	9.27e-18	159	349	65	251	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06525	GH25_Lyc-like	2.06e-17	159	349	2	182	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM01196.1	6.99e-107	58	358	71	373
QCT06482.1	6.25e-63	127	355	89	319
QHI72152.1	3.35e-62	132	356	68	292
QYX28904.1	1.91e-60	111	358	45	291
QEK18217.1	2.01e-59	133	352	77	298

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	2.09e-07	161	349	26	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2X8R_A	2.10e-06	159	256	6	100	Thestructure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.86e-07	151	349	2	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000085	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
13	35