CAZyme Information: TRIVIDRAFT_68354-t45_1-p1

Basic Information

• Species: Trichoderma virens
• Lineage: Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma virens
• CAZyme ID: TRIVIDRAFT_68354-t45_1-p1
• CAZy Family: GH76
• CAZyme Description: glycoside hydrolase family 64 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
444	ABDF02000086|CGC2	48581.59	6.0047

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TvirensGv29-8	12405	413071	0	12405

• Gene Location: location=ABDF02000086:188526-189860(+)

Full Sequence      

MHFTRLILMAGMAFAELSRGINLIEHGATIASPGGIQDFIITRDNTLNGTYHHRVALTKS
SNALTLPVKLVNQFDDGQINAYIQGLDKNGAIVFVTADGGLIYPSSGGSRVPVEVRQDLA
IPLPALHESITINIPIPLNSGRIYFCQGNLTFAILDRGNGEALVQPSINPGDSNASLNWG
FIELTFPQDGSIYANISYVDFVGLVLSMVLTTTNRGGTQITRGLHADAVSRLCQGLRAQS
LKDDHHWLGMCVTNESGRPIRIISPNYYHRIHEEAFKYYWTGYVDEVWEHYSRTPLIIDT
QSESGNVTCQVTGDVLRCGNDPFTYSKPSAADIWGCNSGPFARHEDETGIHLAVIPRLCA
GFVRSTLLLEGGHVQPSLNSNYHYTVSPTHHYSRLVHELQIDGRGYAFSYDDVNPRGDEN
ASGTVAAPNPDLLTIYVGSPPTDV

Enzyme Prediction     

No EC number prediction in TRIVIDRAFT_68354-t45_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH64	65	438	7.6e-86	0.9918256130790191

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185759	GH64-GluB-like	1.02e-165	66	438	1	369	glycoside hydrolase family 64: beta-1,3-glucanase B (GluB)-like. This subfamily is represented by GluB, beta-1,3-glucanase B , from Lysobacter enzymogenes Strain N4-7 and related bacterial and ascomycete proteins. GluB is a member of the glycoside hydrolase family 64 (GH64) involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. GluB possesses the conserved Glu and Asp residues required to cleave substrate beta-1,3-glucans. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Based on the structure of laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis, which belongs to the same family as GluB but to a different subfamily, this cd is a two-domain model. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain.
406796	Glyco_hydro_64	1.41e-164	65	437	2	370	Beta-1,3-glucanase. Family 64 glycoside hydrolases have beta-1,3-glucanase activity.
185755	GH64-LPHase-like	8.08e-68	66	435	1	350	glycoside hydrolase family 64: laminaripentaose-producing, beta-1,3-glucanase (LPHase)-like. This subfamily is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB , the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain.
185753	GH64-like	2.72e-31	66	438	1	319	glycosyl hydrolase 64 family. This family is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB , the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain, and in the Salinispora tropica CNB-440, coagulation factor 5/8 C-terminal domain (FA58C) protein, they are positioned C-terminal of two FA58C domains which are proposed to function as cell surface-attached, carbohydrate-binding domain. This FA58C-containing protein has an internal peptide deletion (of approx. 44 residues) in the LPHase domain II.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ52544.1|GH64	0.0	1	444	1	436
UKZ78351.1|GH64	2.85e-302	1	444	1	412
QYS99657.1|GH64	6.80e-242	1	444	1	444
UKZ69195.1|GH64	2.03e-179	25	441	30	453
UKZ72110.1|GH64	1.12e-167	29	442	29	448

PDB Hits     

TRIVIDRAFT_68354-t45_1-p1 has no PDB hit.

Swiss-Prot Hits     

TRIVIDRAFT_68354-t45_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000279	0.999680	CS pos: 20-21. Pr: 0.8153

TMHMM  Annotations     

There is no transmembrane helices in TRIVIDRAFT_68354-t45_1-p1.