CAZyme Information: MGYG000000364_02104

Basic Information

• Species: Coprococcus sp900767685
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus sp900767685
• CAZyme ID: MGYG000000364_02104
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
336		38368.25	9.8345

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000364	3039243	MAG	Sweden	Europe

• Gene Location: Start: 49967; End: 50977 Strand: -

Full Sequence      

MASNKTPLKGYMDGIDISAWQDTIDITKVPCDFVIVKATEGTDYKNRYFAKHCDQAMKAG
KLLGAFHYANGGDPHSEAEYFLAYSKKYVGKAILVLDWEGQNNPQFGRSDRAWCKEWCDY
VYRKTRVKPLIYIQKSAMDNVKNLGYRLWVAQYPDYEQTGYQKHPWNEGQYDCSIRQYTS
VGRLPGYEGNLDLNKSYIDKATWRKCAAIKTDSDKGKSKGKASDSNSGKSNDKNNKNNKN
RKKKSIDVIAKEVIAGRWGNGEDRKKRLKTAGYDYDKVQEKVNAIVKASQKKSTDEIARE
VIAGDWGNGEDRKNRLKKAGYEYDKIQKRVNELMSG

Enzyme Prediction     

No EC number prediction in MGYG000000364_02104.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	15	186	2.7e-41	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	2.38e-104	12	203	1	195	LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
cd00599	GH25_muramidase	5.15e-38	14	195	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	6.27e-32	15	186	1	179	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	4.18e-25	14	195	2	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.
cd06524	GH25_YegX-like	2.13e-24	14	195	2	191	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
CBK82001.1	3.95e-196	1	278	1	272
QRT50341.1	3.99e-77	12	270	3	245
QRT50187.1	2.71e-75	12	270	3	246
AYZ21718.1	7.71e-58	12	207	3	200
CBK80688.1	6.78e-57	12	278	3	262

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	1.31e-10	12	195	5	201	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	2.85e-09	14	197	18	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	3.16e-09	12	195	20	206	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	7.22e-09	12	195	20	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]
6ZMV_A	1.49e-08	14	186	4	170	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8FFY2	3.72e-13	5	194	60	252	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	6.86e-13	5	194	60	252	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
P00721	6.61e-10	12	136	2	142	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1
P26836	1.53e-09	12	195	9	195	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.57e-09	12	195	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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000364_02104.