CAZyme Information: MGYG000000494_00657

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-269
• CAZyme ID: MGYG000000494_00657
• CAZy Family: CBM13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1398	MGYG000000494_8|CGC1	159053.77	4.5052

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000494	1504589	MAG	Fiji	Oceania

• Gene Location: Start: 14714; End: 18910 Strand: -

Full Sequence      

MKKGLLKVLSATIIFMVIFTVAFPTINYAYSNINDIEEYTTNENVENEKTEKLTEENVDD
KKEKNIKENENKDENAINEEDTREEVKKEEETVTELEIEETKNEDNVIKEQSNENLKGTG
IGKQDNKQLEDGIYTIASKIDENMVIEVPDKSREDEIKIQLAQKARGINKSQEVKITSIG
NGYYTIAFEHSLKVLDVPGASTESGVKLQQYTSNNTVAQQWIIQEAEDGYYYIISRCNGL
YLDIPGGIATDKAKIQLYEGNKTNAQKFSFTKVEEIKSDKIEDGTYYIASALAENKVVSI
SDGKYNDFANTYIWENEKKEYQKFDIEYNKDVDSYIITAVHSNKSLDVSYGGQDNCSNVA
QYQTHKGNTEQWILKETEEDGYYNIISRCNYLNLDISCGSSSNGANIQMYEDNGTKAQKF
KFIKAEKNKSTNIIEDGIYAIGTKLNEDKVLQIENNGISNNEMAKFGRKPNTLNKSQMFE
IKYLSNGYYEIKQYKSQRVLEVNDGKHFNGTSIVQNSENSESTIQQWIIKDAGEGYFYII
ARCNGLFIDIPAGNVEDNPIGQMYEGNETDAQKFSFTRIEELKTDKIEDGTYYIASALEE
NKVVSISDGEYNDFANTYVWENEKKEYQKFDIEYDENVDSYIITAVHSNKSLDVSYGGQD
NCSNVAQYQTHKGETEQWVLKEVEKGYYNIISRSNYLNLDIEYGGANDGANIQMYEDNGT
KAQKFKFKKAEKNESTQTIEDGIYNVVSKVNDNKVLQIENKSLSNNAKAKFDNKLNVINK
VQAFEISYLSNGYYEIKQYKSQKALEVNDGKHSNGTSIVQNSENNESTIQQWIIKDAGEG
YFYIIARCNGLFIDIPGGDISGNPTIQMYEGNETDAQKFEFIKADQEIVGEQLLEDGVYK
IKSVLSNNKYIDVSAGSYDNGANIQLWTNDNVQQQKFQLTYNKKENYYEIMSVNSGKVLD
VQSNGKDDGANVWQYEGNNTDAQKWVLQSAGDGYYYIVACNSYLYLDIKDGNASNGINVQ
IYEGNETNSQKFKFEKTKMIDSDSYNISIKQDESKVIDIDAGSMDNGANVQIWTFDSVNQ
QIFKIEYVDDTYCKIIAKHSDKVLTVQGDNVVQNDYNGNDRQLWSFEIAGDGYYKVKSKS
TNLYLDVAGNQTVNGTNVKIYEGNTSNAQQFKFKELSLRYGIDVSSHNGNVDWKEVRKSG
KVDYAIIRAGYRGFVTGKIVTDGKFERNVKEATKNGIDIGLYFFTQAVNEQEAVEEANYV
LDLVRKYDVNVRYPIIIDTEYSTSKTNGVLDYEGRADQLDVATRTAVCRAFCDTIRNAGY
IPAVYASKYWFYDNLDVSQLNSYDIWVAHYTGDVKKTTDYKYKYNMWQYTSSGSIPGVYA
PFENGRVNVDMSICYKKY

Enzyme Prediction     

No EC number prediction in MGYG000000494_00657.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	1182	1378	6e-44	0.9943502824858758
CBM13	897	1040	2.1e-24	0.7127659574468085
CBM13	132	299	9.7e-23	0.8563829787234043
CBM13	993	1126	1.2e-20	0.6808510638297872
CBM13	590	761	8.2e-20	0.8776595744680851

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.39e-70	1181	1395	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	3.46e-35	1180	1391	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	2.24e-28	1182	1378	1	180	Glycosyl hydrolases family 25.
pfam14200	RicinB_lectin_2	4.37e-25	935	1022	3	89	Ricin-type beta-trefoil lectin domain-like.
pfam14200	RicinB_lectin_2	1.64e-24	171	258	2	89	Ricin-type beta-trefoil lectin domain-like.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM02113.1	3.64e-50	1169	1392	227	430
QNM02116.1	1.58e-47	1181	1392	909	1098
ADL33290.1	3.33e-46	1181	1395	1034	1225
BCK81546.1	7.92e-46	1176	1396	263	473
ABX43465.1	2.05e-45	1180	1398	424	621

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.78e-22	1182	1391	272	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	4.24e-22	1182	1391	272	466	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
2WAG_A	3.35e-08	1181	1395	18	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
2VSA_A	9.93e-06	737	953	414	612	Structureand mode of action of a mosquitocidal holotoxin [Lysinibacillus sphaericus],2VSE_A Structure and mode of action of a mosquitocidal holotoxin [Lysinibacillus sphaericus],2VSE_B Structure and mode of action of a mosquitocidal holotoxin [Lysinibacillus sphaericus]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.090173	0.907401	0.001349	0.000395	0.000324	0.000320

TMHMM  Annotations     

start	end
5	27