CAZyme Information: MGYG000000515_00192

Basic Information

• Species: UBA2882 sp900549665
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA2882; UBA2882 sp900549665
• CAZyme ID: MGYG000000515_00192
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
450		48692.83	4.0653

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000515	2818145	MAG	Fiji	Oceania

• Gene Location: Start: 232995; End: 234347 Strand: -

Full Sequence      

MDSKLKGKVVAVAIVMVLLVVATVFGADYYKKQQSRTAREQAVDELTDSTNAGAANVAAN
GTATAETSAITAADNAAGGNDLYSRYKLDPTKDPYAYLKDDDFFDPVNEENDPATELTLL
VSSVEKDLRVNVIDGLGRLVSGQDFSISVKDSNGRTHNYKDGDKDGSIYIAPVEPGDYQV
SLKGADQYVLTDASDVAISVKEQLDYTVIDDISFMIKSESQVDASKEDTAINEAELDSDG
TESNERLDDEDALFGIDVSKWNKEIDWEKVAASGVEFAVIRCGYRGASTGALVEDPYFKK
NIEGAQAAGIKVGIYFFTQAVNPVEAVEEASMVLALSGEYKLALPIFIDTEGAGGNGRAD
GLDVETRTAVCEAFCRTIDNAGFNSGIYASKNWLEHNLSMSSLSDYTVWLAQYSKSATYK
GDYALWQYTSAGTVDGIGTRVDLNMCYMDY

Enzyme Prediction     

No EC number prediction in MGYG000000515_00192.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	256	437	5.8e-47	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.96e-84	254	447	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	6.04e-38	255	445	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	5.30e-30	256	437	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	5.82e-28	248	445	56	252	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06524	GH25_YegX-like	7.98e-27	254	444	1	190	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
QNM02113.1	5.19e-119	1	447	1	431
ADL34064.1	1.87e-73	107	445	80	484
QNM02116.1	9.57e-71	254	450	908	1102
AOZ95561.1	7.30e-67	254	447	1021	1213
CBK74089.1	2.63e-66	254	445	325	515

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	4.82e-15	253	444	20	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.16e-14	253	444	20	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]
5A6S_A	1.30e-07	283	444	43	199	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
Q8X7H0	4.93e-11	253	445	67	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421	1.20e-10	253	445	67	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.62e-10	253	445	67	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P26836	3.86e-09	253	444	9	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

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
0.733360	0.234787	0.006239	0.002476	0.001069	0.022067

TMHMM  Annotations     

start	end
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