CAZyme Information: MGYG000004282_00932

Basic Information

• Species: Ruminococcus_D sp000434695
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_D; Ruminococcus_D sp000434695
• CAZyme ID: MGYG000004282_00932
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
798	MGYG000004282_4|CGC4	86731.49	8.5192

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004282	2340138	MAG	China	Asia

• Gene Location: Start: 162866; End: 165262 Strand: +

Full Sequence      

MLKKAVGFLAALAIAASSSTAAFADRSYDKKAAVAVNTDSQEGADAEKPASQEKTEEQIK
AEEFAEENCDPQLGKYLDSLEKPTTDFSDIAKEAGGGSDDGILTFGYTNNSLIHNSRFDN
MDKVWGIDVSYFQYNIDWNKVKADGIDYAIIRVGYRGYGSGGQLVLDYKFKENIEAAKAA
GLDVGVYFYTQAVNTKEAQEEADFVLSYIKDYTLDLPVYYDIESVDYDTGRLDSAGLTKA
QKTALCTAFCDRIISKGYKAGVYANMSWLTYQIDGAALGKKYPIWLAHYTTQTNYSGDYS
TWQFSSTGKVNGIATSVDMNVDYRDPNGNSNAVGMVTGLSYTTNSDGSVTFKWNKADNAE
KYEIFKYDASSKKYTRIGYSYTTQYKTTASASYGYCVRGTKVESNANVYGAYSDVLYMNS
GKKITDLKAAAGDKSITISWGALLGCDSYEIYRLVETPYTSYYTRIDTTTTNSYTENISS
SLTSVTYKVRPIFKNGSKLVGGEYSDPVTAVTKLPKMSVPTHTASTKSSVSVKWSKVKGA
DGYEISLYNSATKTYTVQKTVNSSTTAATISGLEAAYGYRVAVRAYATVNGSKVYGNWSS
YRTCGTAPEEPSGAYVTQTSGSITLKWNAVSGASSYTVYKKNGGSYTSLGTVSDTTLAVD
NTAGNFSTEYVVAASTVINRKALTSAYSAAACLPENPPATPSIISYMSGSDGILTLRWTV
SKGCSGYRIYKYDEAKKTYVKVKTVYGEGSVTLSLNDLAANSQFKFRVKAFTKTGTGISW
GTSSKTYNARTVSKYVNK

Enzyme Prediction     

No EC number prediction in MGYG000004282_00932.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	127	313	2.8e-47	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	9.87e-81	125	323	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	8.48e-36	125	321	1	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	1.09e-30	127	313	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	1.46e-30	126	320	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.
cd06524	GH25_YegX-like	9.54e-26	126	321	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
CCO05379.1	7.31e-128	58	771	41	742
ADU22705.1	2.12e-102	76	757	59	702
CBK82808.1	1.60e-74	114	785	104	784
CBK79644.1	4.53e-53	101	325	116	343
QNL98623.1	2.83e-52	106	357	35	292

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	3.83e-16	126	320	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.32e-15	126	320	22	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]
1JFX_A	6.75e-12	124	320	5	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4JZ5_A	2.26e-09	127	320	26	210	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	3.92e-11	120	320	5	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.08e-10	124	320	82	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P50899	9.79e-06	337	664	708	1029	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

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
0.000395	0.998831	0.000169	0.000222	0.000187	0.000165

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004282_00932.