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CAZyme Information: CPC735_057160-t26_1-p1

You are here: Home > Sequence: CPC735_057160-t26_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 Coccidioides posadasii
Lineage Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides posadasii
CAZyme ID CPC735_057160-t26_1-p1
CAZy Family GT21
CAZyme Description Multicopper oxidase family protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
680 76226.89 8.6984
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CposadasiiC735deltSOWgp 7255 222929 26 7229
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in CPC735_057160-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 155 655 9e-95 0.9804469273743017

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
274555 ascorbase 3.12e-70 141 659 4 522
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.
177843 PLN02191 9.19e-66 137 658 22 544
L-ascorbate oxidase
215324 PLN02604 2.82e-64 143 667 29 553
oxidoreductase
259977 CuRO_3_MCO_like_4 7.49e-63 499 660 1 166
The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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.
274556 laccase 4.14e-57 162 667 27 526
laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.16e-317 269 680 1 412
1.07e-209 207 679 1 483
3.12e-209 87 660 28 598
7.92e-209 87 660 45 615
7.92e-209 87 660 45 615

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.32e-57 138 658 2 477
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]
3.46e-54 152 656 81 538
Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
9.02e-54 152 656 81 538
Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
1.44e-49 144 658 9 467
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]
3.73e-49 144 658 9 467
Type-2 Cu-depleted fungus laccase from 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
1.78e-66 152 654 38 490
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
6.83e-66 124 675 47 573
Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
5.02e-64 124 663 47 563
Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
3.33e-63 124 667 47 567
Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
2.05e-62 138 677 22 508
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 OTHER

Other SP_Sec_SPI CS Position
1.000035 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
82 104