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CAZyme Information: TRIVIDRAFT_86342-t45_1-p1

You are here: Home > Sequence: TRIVIDRAFT_86342-t45_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Trichoderma virens
Lineage Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma virens
CAZyme ID TRIVIDRAFT_86342-t45_1-p1
CAZy Family GT32
CAZyme Description glycoside hydrolase family 47 protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
568 ABDF02000002|CGC6 64681.75 5.2939
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

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.113:7

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH47 101 565 2.7e-156 0.9977578475336323

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396217 Glyco_hydro_47 0.0 101 565 1 453
Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
240427 PTZ00470 2.30e-119 68 566 50 519
glycoside hydrolase family 47 protein; Provisional
271200 LanM-like 0.005 184 350 598 749
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 568 1 568
0.0 1 568 1 568
0.0 3 568 6 571
1.08e-303 1 566 1 567
3.11e-280 3 566 4 577

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.92e-74 70 567 16 510
Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes [Penicillium citrinum],1KKT_B Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes [Penicillium citrinum],1KRE_A Structure Of P. Citrinum Alpha 1,2-Mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRE_B Structure Of P. Citrinum Alpha 1,2-Mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRF_A Structure Of P. Citrinum Alpha 1,2-mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRF_B Structure Of P. Citrinum Alpha 1,2-mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum]
6.92e-73 90 567 1 475
Penicillium citrinum alpha-1,2-mannosidase complex with glycerol [Penicillium citrinum],2RI8_B Penicillium citrinum alpha-1,2-mannosidase complex with glycerol [Penicillium citrinum],2RI9_A Penicillium citrinum alpha-1,2-mannosidase in complex with a substrate analog [Penicillium citrinum],2RI9_B Penicillium citrinum alpha-1,2-mannosidase in complex with a substrate analog [Penicillium citrinum]
8.78e-72 85 563 13 465
Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus],5KKB_B Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus]
1.11e-71 85 563 11 463
Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases) [Mus musculus]
1.37e-67 92 562 3 448
Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.16e-75 84 564 35 513
Mannosyl-oligosaccharide alpha-1,2-mannosidase OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CPSG_02648 PE=1 SV=1
7.54e-74 71 564 15 506
Probable mannosyl-oligosaccharide alpha-1,2-mannosidase ARB_00035 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_00035 PE=1 SV=1
3.05e-73 70 567 16 510
Mannosyl-oligosaccharide alpha-1,2-mannosidase OS=Penicillium citrinum OX=5077 GN=MSDC PE=1 SV=2
1.72e-72 86 564 34 509
Probable mannosyl-oligosaccharide alpha-1,2-mannosidase 1B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=mns1B PE=3 SV=1
3.54e-71 83 564 33 509
Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B OS=Aspergillus phoenicis OX=5063 GN=mns1B PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000033 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
13 35