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CAZyme Information: RAK79179.1

You are here: Home > Sequence: RAK79179.1

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 RAK79179.1
CAZy Family GH51|GH51
CAZyme Description multicopper like protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
566 KZ824634|CGC2 62553.82 4.7656
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 1.10.3.2:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 41 374 1.6e-122 0.9881305637982196

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
274555 ascorbase 3.56e-85 21 486 1 517
L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
225043 SufI 8.72e-72 10 494 24 450
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
177843 PLN02191 3.41e-70 10 492 8 546
L-ascorbate oxidase
215324 PLN02604 7.43e-68 5 486 2 540
oxidoreductase
259966 CuRO_3_Fet3p 2.35e-62 333 494 1 160
The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.35e-197 10 516 16 521
1.36e-191 19 516 32 527
2.72e-191 19 524 23 523
2.23e-189 21 524 21 521
4.50e-187 19 524 20 522

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.65e-133 20 515 1 500
Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
3.68e-66 8 492 10 489
Chain A, Laccase [Rigidoporus microporus]
7.90e-65 35 492 17 465
Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
3.44e-60 25 492 7 467
CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]
1.35e-59 25 492 7 469
Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.47e-183 19 524 20 523
Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
2.27e-181 19 516 22 516
Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
3.40e-165 14 524 15 520
Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
6.09e-131 19 515 21 521
Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
5.33e-129 19 515 21 517
Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000269 0.999712 CS pos: 19-20. Pr: 0.9805

TMHMM  Annotations      help

There is no transmembrane helices in RAK79179.1.