CAZyme Information: TRIVIDRAFT_54436-t45_1-p1

Basic Information

• Species: Trichoderma virens
• Lineage: Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma virens
• CAZyme ID: TRIVIDRAFT_54436-t45_1-p1
• CAZy Family: GH47
• CAZyme Description: glycoside hydrolase family 15 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
631		67223.96	5.2360

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=ABDF02000004:786393-788541(+)

Full Sequence      

MHVLSTAVLLGSVAVQKVLGRPGSNGLSDITKRSVDSFISAETPIALNNLLCNVGPDGCR
AFGTSAGAVIASPSTVDPDYYYMWTRDSALVFKNIVDRFTQKYDAGLQRRIEQYISAQVT
LQGISNPSGSLSDGSGLGEPKFELTLNQFTGNWGRPQRDGPALRAIALIGYSKWLINNNY
QSTVSSVIWPIVKNDLNYVAQYWNQTGFDLWEEVNGSSFFTVANQHRALVEGATLATTLG
QSGSTYSSVAPQILCFLQRFWVSGSYIDSNINVNEGRTGKDANSLLASIHTFDPSLGCDA
STFQPCSDKALSNLKVVVDSFRSIYGVNSGISASSAVAIGRYPEDVYFNGNPWYLATFAA
AEQLYDALYVWKQAGSITVTSTSLAFFQQLVPGVAAGTYSSSQSTYTSIINAVSAYADGF
MNEAAKYVPADGSLAEQFDKNSGTPLSAVHLTWSYASFLTAADRRAGIVPSSWASSGANT
VPSSCSGASVVGSYSRPTATSFPPSQTPKPGVPSGTPFTPIPCATPTSVAVTFHELATTQ
FGQTIKVVGSVPELGNWSTNAAVALNAVNYASNHPLWLGSINLAAGEVVQYKYINVGSDG
SVTWESDPNHTYTVPAVACVTQVVKEDTWQS

Enzyme Prediction     

EC	3.2.1.3:94	1.14.99.55:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	63	462	9.6e-78	0.9501385041551247
CBM20	529	616	1.4e-27	0.9333333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	8.53e-144	44	462	1	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	2.05e-46	523	629	1	106	Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
395557	CBM_20	2.19e-35	529	624	1	95	Starch binding domain.
99883	CBM20_alpha_amylase	2.12e-30	529	629	1	94	Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
215006	CBM_2	1.13e-26	529	616	1	88	Starch binding domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ80496.1|CBM20|GH15	0.0	1	631	27	657
UKZ54717.1|CBM20|GH15	0.0	1	631	32	662
QYT01461.1|CBM20|GH15	0.0	1	631	33	663
ACP59398.1|CBM20|GH15	0.0	1	631	1	631
ACJ91348.1|CBM20|GH15	0.0	1	631	1	631

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	0.0	34	631	1	599	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	3.07e-221	34	630	2	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	3.38e-202	38	630	11	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
3EQA_A	8.32e-197	34	503	2	467	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1AGM_A	3.85e-195	34	503	2	466	Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P14804|AMYG_NEUCR	9.41e-274	1	630	1	626	Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
sp|P22832|AMYG_ASPUS	3.27e-223	28	630	19	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
sp|P36914|AMYG_ASPOR	2.10e-222	7	630	10	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P23176|AMYG_ASPKA	2.15e-221	25	630	15	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
sp|P69327|AMYG_ASPAW	1.27e-220	30	630	21	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.070442	0.929527	CS pos: 20-21. Pr: 0.8768

TMHMM  Annotations     

There is no transmembrane helices in TRIVIDRAFT_54436-t45_1-p1.