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CAZyme Information: CVL05371.1

You are here: Home > Sequence: CVL05371.1

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 Fusarium mangiferae
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium mangiferae
CAZyme ID CVL05371.1
CAZy Family GH79
CAZyme Description Arabinogalactan endo-beta-1,4-galactanase [Source:UniProtKB/TrEMBL;Acc:A0A1L7UCX8]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
348 FCQH01000016|CGC2 38160.37 9.1990
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FmangiferaeMRC7560 16149 N/A 345 15804
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.89:16

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH53 21 345 2.8e-92 0.9970760233918129

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
311610 Glyco_hydro_53 9.87e-120 21 345 1 333
Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.
226385 GanB 2.56e-60 22 346 41 392
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism].
381626 GH113_mannanase-like 0.001 33 337 2 300
Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins. Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1->4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1->4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.63e-258 1 348 1 348
2.32e-258 1 348 1 348
5.60e-230 5 348 6 350
2.28e-229 5 348 6 350
2.28e-229 5 348 6 350

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.04e-166 18 348 1 332
Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_A Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus]
2.15e-154 18 348 1 332
Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Humicola insolens]
6.82e-134 18 345 18 347
Emericilla nidulans endo-beta-1,4-galactanase [Aspergillus nidulans]
4.97e-127 18 331 1 316
Crystal Structure Of Beta-1,4-galactanase From Aspergillus Aculeatus At 293k [Aspergillus aculeatus],1FOB_A Crystal Structure Of Beta-1,4-galactanase From Aspergillus Aculeatus At 100k [Aspergillus aculeatus],6Q3R_A ASPERGILLUS ACULEATUS GALACTANASE [Aspergillus aculeatus],6Q3R_B ASPERGILLUS ACULEATUS GALACTANASE [Aspergillus aculeatus]
1.76e-37 22 314 9 286
Beta-1,4-galactanase from Bacteroides thetaiotaomicron with galactose [Bacteroides thetaiotaomicron VPI-5482],6GPA_B Beta-1,4-galactanase from Bacteroides thetaiotaomicron with galactose [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.34e-166 18 348 1 332
Arabinogalactan endo-beta-1,4-galactanase OS=Thermothelomyces thermophilus OX=78579 PE=1 SV=1
1.11e-153 18 348 1 332
Arabinogalactan endo-beta-1,4-galactanase OS=Humicola insolens OX=34413 PE=1 SV=1
3.07e-147 2 348 6 356
Probable arabinogalactan endo-beta-1,4-galactanase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=galA PE=3 SV=2
3.55e-146 2 348 6 356
Probable arabinogalactan endo-beta-1,4-galactanase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=galA PE=3 SV=2
2.89e-145 1 348 5 356
Probable arabinogalactan endo-beta-1,4-galactanase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=galA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000399 0.999561 CS pos: 18-19. Pr: 0.9784

TMHMM  Annotations      help

There is no transmembrane helices in CVL05371.1.