logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: RAK73805.1

You are here: Home > Sequence: RAK73805.1

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 Aspergillus fijiensis
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fijiensis
CAZyme ID RAK73805.1
CAZy Family AA8
CAZyme Description glycoside hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
442 KZ824675|CGC1 48694.70 4.9955
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AfijiensisCBS313.89 12336 1448319 318 12018
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 125 418 4.4e-65 0.9912663755458515

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 2.63e-121 28 331 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 2.77e-91 24 333 59 327
alpha-galactosidase
166449 PLN02808 4.27e-91 1 431 8 376
alpha-galactosidase
178295 PLN02692 1.51e-83 24 391 52 367
alpha-galactosidase
374582 Melibiase_2 1.88e-67 28 331 2 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.89e-268 15 442 14 442
1.89e-268 15 442 14 442
1.61e-267 6 442 5 443
1.61e-267 6 442 5 443
1.87e-266 6 442 5 443

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.39e-173 18 442 1 414
Chain A, alpha-galactosidase [Trichoderma reesei],1T0O_A Chain A, alpha-galactosidase [Trichoderma reesei]
6.01e-85 24 438 5 360
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
8.08e-82 21 438 2 359
Chain A, alpha-galactosidase [Oryza sativa]
2.19e-78 28 441 9 393
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
3.62e-70 24 375 26 359
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
2.86e-268 6 442 5 443
Probable alpha-galactosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglB PE=3 SV=1
3.32e-267 6 442 5 443
Probable alpha-galactosidase B OS=Aspergillus niger OX=5061 GN=aglB PE=2 SV=1
2.17e-258 9 442 11 442
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
3.09e-258 9 442 11 442
Probable alpha-galactosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglB PE=3 SV=1
1.18e-254 2 442 7 447
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
0.000292 0.999661 CS pos: 17-18. Pr: 0.9789

TMHMM  Annotations      help

There is no transmembrane helices in RAK73805.1.