CAZyme Information: MGYG000000078_01883

Basic Information

• Species: Lachnospira rogosae_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira rogosae_A
• CAZyme ID: MGYG000000078_01883
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
358		40010.89	4.8848

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000078	3032544	Isolate	United Kingdom	Europe

• Gene Location: Start: 28015; End: 29091 Strand: +

Full Sequence      

MDNNFNSQSDNSSDWKSNSRQKNKSRTGSKSKLSVLTIVLLVTAIASIIANIVLLVTDSK
RTADTVARIEDKDIETARNTEKDDMLNLIRSRFESGSSTLSLLKELYPDNIVYVNRSGNY
VFADINPKLAASEYDKSAFARNDKGLMTYSGTNAKTYTGIDLSKHNSDVDFAKVKAAGVD
FAMIRCGYRAYGSGLLVEDTSFNTYTTNAIKNNIDVGVYFYSQALNKEEAIEEANYVLTL
VKPYNITYPIAIDVEAIENDSFRQENLSASELTDVIIAFCDTIKAAGYTPLIYSNLLYFM
DNVELERLEGYDKWFAGYQTASPYYPYKYAMWQYTSTGSINGVSGNVDINIAMKNLKK

Enzyme Prediction     

No EC number prediction in MGYG000000078_01883.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	160	343	2.3e-45	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.66e-81	159	353	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	6.51e-39	159	352	2	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	3.33e-29	159	350	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.
pfam01183	Glyco_hydro_25	7.32e-29	160	343	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	1.53e-23	125	350	38	251	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR72973.1	1.32e-105	65	354	38	332
AOZ96288.1	5.70e-69	77	353	83	359
QEK18217.1	3.70e-63	113	355	57	300
ADL34306.1	4.14e-62	71	353	73	359
QRO38911.1	8.37e-62	104	355	39	287

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	3.50e-09	161	350	26	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	6.83e-07	159	350	7	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
P34020	2.47e-12	159	350	3	178	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	6.54e-06	159	350	84	277	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
0.999892	0.000125	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
33	55