CAZyme Information: MGYG000000364_01417

Basic Information

• Species: Coprococcus sp900767685
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus sp900767685
• CAZyme ID: MGYG000000364_01417
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
832		91653.47	9.9671

Genome Property

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

• Gene Location: Start: 134071; End: 136569 Strand: -

Full Sequence      

MFRKKLIRTMLGGAVSLALLSAVAIPSKTSYAAGTDTIQSMVSVSQTADDSQDFISAASF
NSTNNLPVSPSKYTHAAQFKGAKIQKGIDVSQWNGPINWKKVKASGVTFAFIRVGGRYYG
SGKYYIDENYRENLKGAIAAGLDVGVYFYSQAISVTEARTEAAYTMNLISGFNINLPIVM
DYEYAWEDGLTGRLYDAHLSKSAATKVINTFCATVEARGYVGMLYASKTVLTDDMNVSSI
SKHYPVWSALYSDTDTDTLTAKHSYWQYSDNGTVAGIPKATDMNFRYIKAPVAPATVIQQ
NSTDSSITLKWTKVPEVYGYQIVRYDESQNKYVSVGTTKGANTLTFTDKNLRDGKRYTYK
VRGYYKLNSGNVYGAYTDACTGVTIADNIENFKVAAVSDQAIKLSWSPITAATGYRIYRL
NNSTGKYESVRTLSSSTITSYTDSNLNSGTDYSYKIRAYTTTESGTIWHVVSDKVTGTTT
PGLVSGLKVKLSTSDSISIKWNKEKNVSGYLVYTWDKQTATWTKLANVKGGDETTYTHTK
LKSSTQYSYSVRAYYQKNGSMRYTDLCSAISVYSGPAAPSKIVTKTRSENSLDFSWSRVP
AATGYLIYQYDNVKKAYVLLKKTTDNTSCTYTATKLKATTPYIFAVRAYVQKDGVSGGSA
YKVLKTVTTPAAPSTVKYTSLGGHRCTRWSKVSGASGYVVYKYDKRSKKFAAVKKLAGES
STSYIGKEVDARYYTYVVRTYITYNGHTYYGALSKLPVSGTLNIIGVVSDTAVRVRRGPS
TNNSIITELYYGQKVAIIGGVKRNGETWYKVSFKKGSSRITGYMHSAYIKIQ

Enzyme Prediction     

No EC number prediction in MGYG000000364_01417.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	88	277	3.9e-45	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.02e-70	85	287	1	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	1.69e-33	86	284	1	184	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	1.10e-27	88	277	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	8.62e-23	86	285	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.
cd06413	GH25_muramidase_1	4.84e-21	86	284	4	187	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK82808.1	2.65e-309	1	832	1	860
CBK82807.1	4.35e-92	68	256	100	288
CCO05379.1	2.10e-87	74	758	93	845
QNL98623.1	5.26e-62	73	287	36	251
ADU22705.1	1.91e-51	72	701	94	677

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.27e-13	86	284	21	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
2WW5_A	2.86e-13	85	287	269	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]
4KRT_A	6.14e-13	86	284	21	205	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]
2WWC_A	6.64e-13	85	287	269	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
1JFX_A	3.22e-11	86	284	6	200	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
P50899	1.11e-10	235	553	643	963	Exoglucanase B OS=Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) OX=590998 GN=cbhB PE=1 SV=1
P25310	4.92e-10	86	284	83	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	4.15e-09	86	284	10	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q02388	4.60e-09	305	698	429	805	Collagen alpha-1(VII) chain OS=Homo sapiens OX=9606 GN=COL7A1 PE=1 SV=2
Q63870	1.36e-08	305	698	430	806	Collagen alpha-1(VII) chain OS=Mus musculus OX=10090 GN=Col7a1 PE=1 SV=3

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
0.000299	0.998933	0.000217	0.000211	0.000183	0.000152

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000364_01417.