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CAZyme Information: KAG2012204.1

You are here: Home > Sequence: KAG2012204.1

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 Coprinopsis cinerea
Lineage Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
CAZyme ID KAG2012204.1
CAZy Family GH16
CAZyme Description laccase 2, variant 2
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
436 46832.37 7.8776
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ccinerea326 15250 N/A 238 15012
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.10.3.2:77

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 33 337 2.2e-155 0.9933993399339934

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
259949 CuRO_2_Tv-LCC_like 4.38e-85 167 317 1 157
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Laccase is a multicopper oxidase (MCO) 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 2 of 3-domain MCOs has lost the ability to bind copper.
259925 CuRO_1_Tv-LCC_like 2.06e-71 22 151 1 125
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor. This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
274555 ascorbase 2.01e-59 53 423 28 450
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.
395317 Cu-oxidase 1.88e-54 165 306 1 146
Multicopper oxidase. Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.
177843 PLN02191 1.56e-51 53 423 50 473
L-ascorbate oxidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
7.36e-315 1 423 1 423
7.36e-315 1 423 1 423
8.86e-244 1 423 1 421
9.52e-244 1 423 1 423
3.59e-243 1 423 1 421

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.57e-186 19 423 1 401
Chain A, LACCASE 2 [Trametes versicolor]
6.07e-185 19 423 1 399
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]
2.54e-184 20 423 2 400
T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
4.15e-183 19 423 1 400
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]
1.37e-181 19 423 1 400
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
1.57e-198 3 433 7 440
Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
8.07e-188 3 433 7 438
Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
1.76e-184 17 423 19 421
Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1
5.79e-183 17 423 19 421
Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1
5.61e-181 19 423 22 422
Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.001396 0.998594 CS pos: 18-19. Pr: 0.9690

TMHMM  Annotations      help

There is no transmembrane helices in KAG2012204.1.