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CAZyme Information: Z517_02953-t43_1-p1

You are here: Home > Sequence: Z517_02953-t43_1-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 Fonsecaea pedrosoi
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Fonsecaea; Fonsecaea pedrosoi
CAZyme ID Z517_02953-t43_1-p1
CAZy Family AA7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
550 61214.06 5.4549
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FpedrosoiCBS271-37 12573 1442368 46 12527
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 47 378 4.7e-124 0.9881305637982196

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
274555 ascorbase 1.00e-83 31 490 4 517
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 6.48e-77 26 498 33 450
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].
259966 CuRO_3_Fet3p 5.10e-72 339 498 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.
177843 PLN02191 9.82e-71 13 496 8 546
L-ascorbate oxidase
215324 PLN02604 1.03e-69 13 490 7 540
oxidoreductase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
7.87e-213 26 502 7 484
2.13e-209 26 502 23 501
1.41e-208 26 502 18 495
1.53e-206 1 508 1 511
4.61e-206 26 502 32 513

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.01e-134 27 505 1 488
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]
1.23e-73 32 496 28 488
Crystal structure of laccases from Pycnoporus sanguineus, izoform II [Trametes coccinea],5NQ9_A Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea],5NQ9_C Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea]
1.06e-72 32 496 7 466
Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii]
1.61e-71 32 496 7 467
CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]
3.07e-71 32 496 7 466
Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_B Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_C Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.00e-202 13 502 7 501
Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
3.18e-195 26 502 22 502
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
1.18e-182 21 502 15 498
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
2.88e-136 26 502 21 504
Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
1.17e-133 24 501 16 505
Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000204 0.999791 CS pos: 26-27. Pr: 0.9767

TMHMM  Annotations      help

There is no transmembrane helices in Z517_02953-t43_1-p1.