CAZyme Information: MGYG000004692_00817

Basic Information

• Species: Collinsella aerofaciens_H
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella aerofaciens_H
• CAZyme ID: MGYG000004692_00817
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1659	MGYG000004692_13|CGC1	176785.32	4.8591

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004692	2399484	Isolate	United States	North America

• Gene Location: Start: 41967; End: 46946 Strand: -

Full Sequence      

MVMRKNTRLVSSLLVALGLLCGLGATPVFADDAPLPVDASLEERLAYGEAHPDDDLGTYT
AGSSMEREPLAAALDARAGNGSPYWGGSNASKTFYNGYDEVFASPALKVIDVSEWQGTID
WNKVKNSGVDAVILRFAHSTSHFDKQFERNLSEIRRLGIPFGLYIFSTAQNSNDATSEAY
FTQQIVSKYGLYDLSLPIFYDLEAFYDSNGNPMSPNSASAYEGIVNAYFNTLSGFGINNV
SIYSGRWFTDTYLKAASVRPRVSWIAEYGPKLKTSFSCAGQYGWQYTSSERLDGITANTV
DMSAFSSADFVNVLNLPDFALADGTYYIDSIAKDSSSVTVAEDESLSLYGAQGMANQRFI
LELAGSGAYRIKNEATGRYLSVVDGNAQSGSTVVQAAYAQDEHQLWHVRTADNGFYIQSA
LGNWVLDVSGGSTADGTSVRIWAPNKSAAQRFTFASASTIKTDTAFAIKSVLDPQLVMDI
YGGSSDNRARLQIYNANNSQAQMFTFKQVGNGLYEIVNVNSGKPFEAQGGSVSNGGAISQ
YSSNGTCAQHWSIIDCGNGEYSFINSKSGKAIDVPGGNGVSGSALQIYTYNASDAQKWTL
APARTVRQELDDLAASSKGLVKEGVEYAIGSVSERHVFDIADGSTNSGANLQLYTSNATK
AQRWMFSYDENGYATITNVKSGKVLDVSGGSKKAGANVQQYAPNGSWAQKWILVDCGDGS
VKICSAIRAGFVLDLAGGSTANGANVQVYDDNGTAAQRFRLYTAGEVSKVQTFDSQSAVV
MSSDGRVFDVTGGSMDSGAALQLYSANGTIAQSFGFEFDTEAGLYAIKSAKSYRYLYAQD
GDIVPGAAVKQGNLSPSTPIYNWAIEDAGNGLYRIVNAATGGVLGVGASGKLITVFRGDV
RELSVAFTPSGFKCLRSEQDADAAVHMSDLPDGEYVVSSSMNYSFVLDVSGGSKENSANI
QLYTSNMSNAQRWTVSHDEKGYVTFTNVGSNKVIDVAGGNASSGTNIAQYVSNGTYAQKW
IVAKRSDGSYLIESALRPGFYLGSRGGKASNGANVELSSNQDNSRFVLLSTTPSVAKCDD
ILPEGYFTLSPACSSSGKVTDIAGGSSSNGANVQLYNDNGTLAQLFSFEYHDGYYVIRNV
KSQKVLDVAGGELIPGANVQQWDGDSTNVNQLFAAIDNSDGTFSFVNKATGLVLNVANGS
DSAHANINVSLSNGTAAQKFSLHQVTEFLSEGATSFESTTASKVLDVVGGSMEDGAAIQL
YTPNDTLAQKWYVSKVPGLDNTYEIECIGSAKVLSLTDEGKLVQLTANGTDSQRWHSALS
GGKIALQNAATGQYLCVSGSSSTLGMVDSLELPGVRFNAKSVGVLSEGSFTIQLMSNRSQ
VFDVSGGSTNAGSSVGFYSSNGTAAQIWDVRKNSDGTYEISSAKSCKPLDIRDANQVAGN
GVQIWTRNESTAQKWKLVYNRGEGYAIQSTGGLVLASTNGALALCEDSGSANQRFAFEKA
TYIPPALTGVQWKGCAHYSSTRYGEDWSVIVIHISECTSLSQIDNTFWGTREASAHYGVA
PGQIHQYVGLNDTAWAVGNWEWNKRSVSIEHVGTTANPPSYATLDTSAQLMAALARSKGW
RHLTMGDNVGIHKWYSSTSCPAGTDVNWLVAKANQYLGN

Enzyme Prediction     

No EC number prediction in MGYG000004692_00817.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	110	295	2.4e-35	0.9943502824858758
CBM13	468	603	3e-20	0.675531914893617
CBM13	1029	1175	4.5e-19	0.675531914893617
CBM13	931	1027	5.8e-19	0.4946808510638298
CBM13	624	716	1.2e-18	0.4734042553191489

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	2.38e-48	108	305	2	190	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	2.96e-30	108	305	1	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.
cd06523	GH25_PlyB-like	3.96e-27	108	304	1	176	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
pfam14200	RicinB_lectin_2	1.75e-25	661	749	2	89	Ricin-type beta-trefoil lectin domain-like.
pfam14200	RicinB_lectin_2	2.39e-21	355	442	1	89	Ricin-type beta-trefoil lectin domain-like.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGM63437.1	8.83e-88	84	679	171	785
AXM90834.1	3.68e-87	84	679	167	781
BAQ29887.1	1.33e-86	84	679	171	785
ALE10489.1	1.98e-85	84	679	171	785
AIZ15211.1	3.65e-85	84	679	204	818

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	3.48e-33	85	305	246	467	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	8.47e-33	85	305	246	467	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4JZ5_A	2.84e-12	109	314	25	220	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
1JFX_A	4.76e-09	110	308	8	205	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	2.72e-07	107	315	20	217	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	6.26e-10	69	308	39	282	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P34020	1.48e-07	107	311	1	186	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
P26836	3.89e-07	107	325	9	213	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000377	0.998648	0.000377	0.000214	0.000190	0.000159

TMHMM  Annotations     

start	end
7	29