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CAZyme Information: Afu2g17540-T-p1

You are here: Home > Sequence: Afu2g17540-T-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 Aspergillus fumigatus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus
CAZyme ID Afu2g17540-T-p1
CAZy Family GH134
CAZyme Description Multicopper oxidase abr1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
664 Chr2_A_fumigatus_Af293|CGC1 73445.39 4.5972
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AfumigatusAf293 10130 330879 290 9840
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in Afu2g17540-T-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 39 384 9.4e-120 0.9851632047477745

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
274555 ascorbase 1.36e-74 22 494 3 517
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.
259966 CuRO_3_Fet3p 3.19e-73 343 502 3 160
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.
225043 SufI 2.12e-65 18 503 32 451
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 4.79e-64 25 508 28 554
L-ascorbate oxidase
215324 PLN02604 1.91e-57 18 494 22 540
oxidoreductase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 664 1 664
0.0 1 664 1 664
0.0 5 653 1 649
4.32e-253 1 527 1 523
2.02e-251 7 524 8 520

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.49e-103 24 520 6 502
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]
4.69e-63 24 521 7 491
Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
1.74e-61 24 521 7 491
Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta]
2.42e-61 24 521 7 491
Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta]
3.21e-61 24 521 7 489
CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 1 664 1 664
Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2
9.72e-146 16 523 18 516
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
1.45e-134 13 524 15 520
Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
1.27e-132 5 524 9 521
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
1.37e-120 4 527 7 516
Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000232 0.999732 CS pos: 18-19. Pr: 0.9677

TMHMM  Annotations      help

There is no transmembrane helices in Afu2g17540-T-p1.