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CAZyme Information: RVD86817.1

You are here: Home > Sequence: RVD86817.1

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 Arthrobotrys flagrans
Lineage Ascomycota; Orbiliomycetes; ; Orbiliaceae; Arthrobotrys; Arthrobotrys flagrans
CAZyme ID RVD86817.1
CAZy Family GH5
CAZyme Description Alpha-galactosidase [Source:UniProtKB/TrEMBL;Acc:A0A437A716]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
466 52959.35 4.7791
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AflagransCBSH-5679 9927 N/A 30 9897
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:58 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 131 415 1e-56 0.9868995633187773

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 3.15e-118 33 337 1 271
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.
177874 PLN02229 8.43e-78 31 430 61 411
alpha-galactosidase
166449 PLN02808 8.87e-73 30 429 29 376
alpha-galactosidase
178295 PLN02692 5.57e-71 30 337 53 319
alpha-galactosidase
374582 Melibiase_2 4.94e-66 33 337 2 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 466 1 466
1.80e-177 30 435 27 443
3.68e-169 30 439 27 447
1.96e-168 30 439 263 736
6.04e-162 30 434 25 426

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.03e-140 30 434 9 408
Chain A, alpha-galactosidase [Trichoderma reesei],1T0O_A Chain A, alpha-galactosidase [Trichoderma reesei]
9.58e-77 33 436 9 390
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
9.57e-66 30 430 6 354
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
1.84e-65 30 337 6 272
Chain A, alpha-galactosidase [Oryza sativa]
9.61e-58 30 347 27 330
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRL_A Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.68e-147 25 434 4 420
Probable alpha-galactosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=aglB PE=3 SV=1
1.30e-146 30 434 26 429
Probable alpha-galactosidase B OS=Penicillium simplicissimum OX=69488 GN=agl1 PE=2 SV=1
1.64e-146 30 434 27 436
Probable alpha-galactosidase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=aglB PE=3 SV=1
3.90e-146 30 434 30 441
Probable alpha-galactosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=aglB PE=3 SV=2
3.90e-146 30 434 30 441
Probable alpha-galactosidase B OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=aglB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000723 0.999230 CS pos: 21-22. Pr: 0.9546

TMHMM  Annotations      help

There is no transmembrane helices in RVD86817.1.