CAZyme Information: TRIVIDRAFT_46494-t45_1-p1

Basic Information

• Species: Trichoderma virens
• Lineage: Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma virens
• CAZyme ID: TRIVIDRAFT_46494-t45_1-p1
• CAZy Family: GH20
• CAZyme Description: glycoside hydrolase family 27 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
624		67874.03	6.0502

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=ABDF02000083:184926-186800(-)

Full Sequence      

MAPPTAAVLVSLAGIFLLRPVAAQTQCGGNLYTPGTLNFTTECYNAFMDCAARFEANASL
VDCNDGNGNLFMQQQANLGASPGSQNNDAVIAFQDIRDLCLLSGSTTATWGYSDNQWYWA
AAEDACYTNDPTRTDVVKTHPAPYCIQNRDSGLPECYPQPDATPGGPLKVLKTAKTRNGF
KSSARGWNTYGVQALQNGSQVVPSFAGQSGLYYTQKFVETQCGVLARPEFKAAGYDLCSL
DSGWQAFSEVDEHGRIIYNTTRFNLPQLASWLHSRDLKLGVYITPGVPCVAHNQTIVGTK
IKVGDILNGNNDQINCDFDFSKDGVQQWHDSVVAQWASWGVDMLKLDFVTPGSPSNGANL
ACDSSAAVKAYQKAIEKSGRKIRLDISWKLCRNETWLPVWSDLAESMRTDQDLDNYGTNT
LMAWQVGQRAIENYRQYIGLQAQRNVPITIYPDMDALFTVNPEHLAGVNDSIRTTVQNHW
LGAAANLVIGGDMQQIDALGLKLTTSKQSIAAADFFAQYPMQPRNPGTGSNAAKQLQAWI
GGPSNNHEAYVLLVNYGPDLGNGGFGTKLYGSQKVTVSLKDLGISGSTWTFTDIWTGKST
RVTGSYSVSLTEGASQLLRVTKSH

Enzyme Prediction     

EC	3.2.1.22:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	328	599	5.3e-34	0.9563318777292577

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269893	GH27	4.46e-56	184	511	2	267	glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
374582	Melibiase_2	3.25e-12	224	390	37	167	Alpha galactosidase A.
407673	Melibiase_C	1.17e-08	535	620	3	74	Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ58316.1|GH27	0.0	1	624	1	624
UKZ84001.1|GH27	0.0	1	624	1	624
QYT06340.1|GH27	0.0	4	623	3	622
CAA93246.1|GH27|3.2.1.22	0.0	4	624	3	624
UKZ69640.1|GH27	0.0	1	622	1	622

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	3.99e-12	249	387	86	231	Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4NXK_A	3.80e-11	249	387	86	231	Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus]
1R46_A	3.88e-09	214	511	34	287	Structure of human alpha-galactosidase [Homo sapiens],1R46_B Structure of human alpha-galactosidase [Homo sapiens],1R47_A Structure of human alpha-galactosidase [Homo sapiens],1R47_B Structure of human alpha-galactosidase [Homo sapiens],3GXN_A Crystal structure of apo alpha-galactosidase A at pH 4.5 [Homo sapiens],3GXN_B Crystal structure of apo alpha-galactosidase A at pH 4.5 [Homo sapiens],3GXP_A Crystal structure of acid-alpha-galactosidase A complexed with galactose at pH 4.5 [Homo sapiens],3GXP_B Crystal structure of acid-alpha-galactosidase A complexed with galactose at pH 4.5 [Homo sapiens],3GXT_A Crystal structure of alpha-galactosidase A at pH 4.5 complexed with 1-deoxygalactonijirimycin [Homo sapiens],3GXT_B Crystal structure of alpha-galactosidase A at pH 4.5 complexed with 1-deoxygalactonijirimycin [Homo sapiens],3HG2_A Human alpha-galactosidase catalytic mechanism 1. Empty active site [Homo sapiens],3HG2_B Human alpha-galactosidase catalytic mechanism 1. Empty active site [Homo sapiens],3HG4_A Human alpha-galactosidase catalytic mechanism 3. Covalent intermediate [Homo sapiens],3HG4_B Human alpha-galactosidase catalytic mechanism 3. Covalent intermediate [Homo sapiens],3HG5_A Human alpha-galactosidase catalytic mechanism 4. Product bound [Homo sapiens],3HG5_B Human alpha-galactosidase catalytic mechanism 4. Product bound [Homo sapiens],3S5Y_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Y_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Z_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Z_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],4NXS_A Crystal structure of human alpha-galactosidase A in complex with 1-deoxygalactonojirimycin-pFPhT [Homo sapiens],4NXS_B Crystal structure of human alpha-galactosidase A in complex with 1-deoxygalactonojirimycin-pFPhT [Homo sapiens],6IBK_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfamidate ME763 [Homo sapiens],6IBK_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfamidate ME763 [Homo sapiens],6IBM_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfate ME776 [Homo sapiens],6IBM_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfate ME776 [Homo sapiens],6IBR_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol epoxide LWA481 [Homo sapiens],6IBR_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol epoxide LWA481 [Homo sapiens],6IBT_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol aziridine ME737 [Homo sapiens],6IBT_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol aziridine ME737 [Homo sapiens]
3LX9_A	5.25e-09	214	511	34	287	Chain A, Alpha-galactosidase A [Homo sapiens],3LX9_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXA_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXA_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXB_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXB_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXC_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXC_B Chain B, Alpha-galactosidase A [Homo sapiens]
3HG3_A	1.22e-08	214	511	34	287	Chain A, Alpha-galactosidase A [Homo sapiens],3HG3_B Chain B, Alpha-galactosidase A [Homo sapiens],3TV8_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3TV8_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q92451|AGAL3_HYPJE	0.0	4	624	3	624	Alpha-galactosidase 3 OS=Hypocrea jecorina OX=51453 GN=agl3 PE=1 SV=1
sp|C8VJZ7|AGAL8_EMENI	5.84e-113	171	587	69	481	Putative alpha-galactosidase 8 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agl8 PE=5 SV=2
sp|P51569|AGAL_MOUSE	5.48e-10	187	511	24	318	Alpha-galactosidase A OS=Mus musculus OX=10090 GN=Gla PE=1 SV=1
sp|P06280|AGAL_HUMAN	5.40e-09	187	511	24	318	Alpha-galactosidase A OS=Homo sapiens OX=9606 GN=GLA PE=1 SV=1
sp|P14749|AGAL_CYATE	2.62e-07	210	621	67	408	Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000227	0.999767	CS pos: 23-24. Pr: 0.9782

TMHMM  Annotations     

There is no transmembrane helices in TRIVIDRAFT_46494-t45_1-p1.