CAZyme Information: MGYG000002240_01035

Basic Information

• Species: UBA11963 sp900552975
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; UBA11963; UBA11963 sp900552975
• CAZyme ID: MGYG000002240_01035
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
287	MGYG000002240_6|CGC1	33650.94	4.456

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002240	1580436	MAG	Peru	South America

• Gene Location: Start: 11306; End: 12169 Strand: -

Full Sequence      

MQYNLLDKFKNITLQHRRLTILVLSSIILLIFLSFLGQSFAYKYKEQEEDFDEIQQLINE
IKENDKEIVNQTKVVEIARDVKGVDISGWQGKIDWQALKNSGIDFAMIRVGVRKLNDGEI
VEDSYFKYNIEQANYYDVPVGVYFFSSAKNEYEVIEEATFTLNLIKNYKITYPVAYDFES
FESGRVSKVSDEVINYNALVFLDYMKSHGYNGMLYGNKTAMETRWDLSRFSNYKKWLAHY
MDGVSYKGNYDMWQYTDIGRVNGILADVDLNEAYFAYEIENVNDEIE

Enzyme Prediction     

No EC number prediction in MGYG000002240_01035.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	84	264	1e-42	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	5.20e-68	82	274	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	1.01e-36	82	273	1	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.
cd06525	GH25_Lyc-like	1.07e-28	82	272	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.
pfam01183	Glyco_hydro_25	1.31e-26	84	264	1	180	Glycosyl hydrolases family 25.
cd06524	GH25_YegX-like	1.67e-24	82	271	1	190	YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CUH92515.1	6.02e-50	36	280	61	313
QEK17162.1	5.13e-46	83	271	843	1034
ADL33290.1	1.37e-45	82	274	1033	1225
AOZ95561.1	1.01e-43	83	274	1022	1213
QNM02116.1	1.82e-43	83	277	909	1102

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	3.36e-17	70	274	258	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	8.30e-17	70	274	258	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRU_A	3.26e-15	80	272	19	206	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.22e-14	80	272	19	206	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]
2WAG_A	1.76e-13	80	274	15	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	4.41e-12	78	282	6	203	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.63e-09	81	272	1	179	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
P25310	3.96e-07	81	272	82	278	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

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
0.971767	0.001078	0.000724	0.000009	0.000005	0.026445

TMHMM  Annotations     

start	end
20	42