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CAZyme Information: CC1G_09614-t26_1-p1

You are here: Home > Sequence: CC1G_09614-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 Coprinopsis cinerea
Lineage Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
CAZyme ID CC1G_09614-t26_1-p1
CAZy Family GH5|GH5
CAZyme Description laccase 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
530 AACS02000003|CGC10 57222.16 4.9359
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ccinereaokay7-130 13657 240176 301 13356
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 34 327 5.3e-134 0.9933993399339934

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
259970 CuRO_3_Tv-LCC_like 3.61e-90 335 479 1 147
The third 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. 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 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.
274555 ascorbase 2.45e-79 35 477 14 523
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.
259949 CuRO_2_Tv-LCC_like 1.05e-73 153 309 1 159
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.
177843 PLN02191 1.76e-73 5 477 8 546
L-ascorbate oxidase
215324 PLN02604 1.26e-62 5 477 9 546
oxidoreductase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 530 1 539
0.0 1 530 1 539
0.0 1 530 1 539
0.0 5 441 1 446
4.08e-248 1 526 1 544

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 19 513 1 504
Chain A, Laccase [Coprinopsis cinerea]
0.0 20 512 2 503
Chain A, LACCASE 1 [Coprinopsis cinerea]
2.52e-211 21 505 2 494
Coriolopsis gallica Laccase T2 Copper Depleted at pH 4.5 [Coriolopsis gallica],4A2E_A Crystal Structure of a Coriolopsis gallica Laccase at 1.7 A Resolution pH 5.5 [Coriolopsis gallica],4A2G_A Coriolopsis gallica laccase collected at 8.98 keV [Coriolopsis gallica],4A2H_A Crystal Structure of Laccase from Coriolopsis gallica pH 7.0 [Coriolopsis gallica]
2.61e-211 21 505 2 494
Coriolopsis gallica laccase collected at 12.65 keV [Coriolopsis gallica]
4.12e-210 21 505 2 494
Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.53e-204 21 502 24 515
Laccase-4 OS=Trametes versicolor OX=5325 GN=LCC4 PE=3 SV=1
2.03e-203 2 504 4 517
Laccase-1 OS=Trametes villosa OX=47662 GN=LCC1 PE=1 SV=1
4.07e-203 21 502 24 515
Laccase-4 OS=Trametes villosa OX=47662 GN=LCC4 PE=3 SV=1
1.65e-202 2 502 4 515
Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1
3.09e-202 2 504 4 515
Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000255 0.999714 CS pos: 18-19. Pr: 0.9413

TMHMM  Annotations      help

There is no transmembrane helices in CC1G_09614-t26_1-p1.