CAZyme Information: MGYG000002142_00663

Basic Information

• Species: Collinsella sp900545445
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900545445
• CAZyme ID: MGYG000002142_00663
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
430		47089.94	4.5986

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002142	2108482	MAG	United States	North America

• Gene Location: Start: 14204; End: 15496 Strand: +

Full Sequence      

MRQIKRQILFGISLLLFGLAFAHSCYGDTSRSLVENSWRYENGEIVSSLNASEDEGISTL
SITDLPTGATAEGIDVSEHQKKVDWEAVKASGIDFAILRIGFGAPSFGGRLDYQFQRNIS
ECERLGIPYGIYLYSYAWDDSQAEDEASFVIDNLAGHTPQLPVYYDLEDNSIIAEGRQAG
IASRASIFCNRITSAGYSVGIYANLYWFNNVLTDQVFKSSAWDHWIAQYNYQCDYTGNYS
IWQYASDGLVPGVNGYVDMNYSYGSVVAESVKAQRADELASQHAGDLADGTYVIRSAKRP
SSALEAKGGRTANGTAVSLYDVNGTVAQAWTVTHEGDYVVIRNAKSGRAIDPTGPSSDPG
TKLQLWDASGTRPQRWIAIRRDDGGYEFRSAMDPDAAFDLTSGKTSNGTRAQLYTANGTE
AQSWLLSVSK

Enzyme Prediction     

No EC number prediction in MGYG000002142_00663.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	74	253	4.9e-42	0.9943502824858758
CBM13	290	427	9.4e-21	0.6861702127659575

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	9.03e-79	73	263	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	1.24e-29	73	261	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.
cd06413	GH25_muramidase_1	3.76e-24	70	264	2	191	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.
cd06524	GH25_YegX-like	4.81e-22	73	264	2	194	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.
cd06525	GH25_Lyc-like	3.66e-21	73	261	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZH69442.1	4.30e-126	5	266	3	268
ATP53732.1	8.28e-121	5	266	3	268
AWY97591.1	3.51e-63	35	274	47	296
QIA33416.1	1.02e-61	52	263	5	214
QCP36075.1	4.33e-59	35	319	47	336

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	9.85e-19	74	263	272	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	2.37e-18	74	263	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
5A6S_A	6.85e-07	79	261	20	200	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	3.17e-07	65	266	61	258	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.02e-06	65	266	61	258	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	1.02e-06	65	265	61	257	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.012764	0.199301	0.786681	0.000522	0.000390	0.000340

TMHMM  Annotations     

start	end
7	24