CAZyme Information: MGYG000003619_01040

Basic Information

• Species: SFDP01 sp900770785
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; SFDP01; SFDP01 sp900770785
• CAZyme ID: MGYG000003619_01040
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
417	MGYG000003619_101|CGC1	46678.4	4.1348

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003619	2720357	MAG	Fiji	Oceania

• Gene Location: Start: 62943; End: 64196 Strand: -

Full Sequence      

MDSRFLRNTILISILFMITIFGVVLYSNGLGPGQQKEAAATPQETEKILLEGQVGDDLYG
WMEDETFFDDADMDQKEQEGESLSLIATSVEKDLRVQIVDKDGKTVEGQFFKILINGEDE
YKDLDRDGIIYVGELSAGEYQVKLMEKEGFIVPREAMPVKVKSRVEYVAIGDISLLIKTE
KEVDALAEDGGRIEETEEGSGPSQILTREDAAFGIDVSRWNETIDWAKVKDAGVSYAIIR
VGYRGSVTGSLVEDYYFRKNIEGATEAGIPVGVYFFTQAINQVEAVEEASMVLELCRDYK
LTYPVFIDTEGAGGEGRADGLDVKTRTAVCEAFCETIRNSGYQAGIYASKNWYNNKLDTS
RLPDNIVIWLAEYADAPTYDKKYHMWQYSSSGRILGIEGRVDLNLSFLDMEEMQNNP

Enzyme Prediction     

No EC number prediction in MGYG000003619_01040.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	215	397	2.3e-46	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	2.19e-87	213	407	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	1.79e-38	214	405	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	1.20e-34	215	397	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	2.33e-28	214	404	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.
COG3757	Acm	1.98e-25	214	404	65	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
QNM02113.1	1.75e-142	1	407	1	431
QNM02116.1	1.38e-71	213	408	908	1100
ADL33290.1	5.34e-67	201	407	1021	1225
AOZ95561.1	3.34e-66	206	407	1014	1213
ADL34064.1	7.16e-65	77	405	82	484

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	4.23e-21	209	405	266	466	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	1.03e-20	209	405	266	466	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRU_A	6.29e-18	214	404	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.51e-17	214	404	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	1.80e-13	214	404	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
P25310	2.05e-12	199	404	66	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	4.15e-12	214	416	11	206	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P76421	5.33e-12	214	414	69	262	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	7.18e-12	214	414	69	262	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	9.69e-12	214	414	69	262	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.981669	0.017476	0.000299	0.000065	0.000043	0.000461

TMHMM  Annotations     

start	end
5	27