CAZyme Information: CC1G_03940-t26_1-p1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: CC1G_03940-t26_1-p1
• CAZy Family: CBM13
• CAZyme Description: laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
487	AACS02000007|CGC7	53466.38	6.3910

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: location=AACS02000007:468086-470420(+)

Full Sequence      

MILLTFSLLILLSLPAALAGFGSSGDLIVGNRFISPDGFSRSAVLAGSSGGRFHLNVVNE
LIDPAMLRTTSIHWHGLFQRGSQWADGPAGVTQCPIVPGSSFLYQFQVPDQAGTFWYHSH
HQTQYCDGLRGAFVLYDPHDPHHQLYHTPTLSAGALPIFNSTLINGKGRFAGGPPVDLAV
IHVERNRRYRFRLISMSCDPNYIFSIDGHTLTVIEVDGVNVQPHTVDSIQIFAAQRVSFV
LNANRPIDNYWIRADPNFGNTGFAGGINSAVLRYHGAEPADPVTERLPFSSPFREFDLRP
LFPEPVPGRPEVGGADININLEIGFDSQSTRFSVNNATMIQPTVPVLLQILSGARTPQEL
MPPGSIYTLPRNRVVELSIPGGSAGSPHPVHFHGHTFHVIRSAGSSEYNYFDPIQRDVVS
IGEATDNVTIRFVTDNAGPWILHCHIDFHRALGFAVVFAEDAERVAALEPPPAWHELCPK
YEAFGEQ

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	34	308	9.8e-123	0.9933993399339934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259970	CuRO_3_Tv-LCC_like	1.77e-78	316	461	1	146	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.
259949	CuRO_2_Tv-LCC_like	1.23e-68	146	288	9	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.
274555	ascorbase	1.37e-65	57	473	42	535	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.
259925	CuRO_1_Tv-LCC_like	9.12e-62	23	137	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.
177843	PLN02191	1.59e-61	55	468	66	554	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
DAA04517.1|AA1_1	0.0	1	487	1	517
DAA04518.1|AA1_1|1.10.3.2	1.85e-305	6	487	5	516
AAD30965.1|AA1_1	1.98e-237	14	484	13	513
DAA04507.1|AA1_1|1.10.3.2	1.98e-237	14	484	13	513
AAD30966.1|AA1_1|1.10.3.2	9.82e-233	10	484	7	511

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5NQ8_A	2.65e-200	10	484	11	513	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]
5NQ7_A	1.24e-198	10	484	11	513	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
2QT6_A	5.00e-198	22	484	3	493	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
5LDU_A	7.34e-198	22	484	3	494	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
2XYB_A	9.71e-198	22	484	3	492	CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12729|LAC1_PLEOS	9.80e-205	19	486	23	522	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
sp|Q12739|LAC2_PLEOS	6.47e-204	14	486	18	524	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|O59896|LAC1_PYCCI	4.15e-201	10	484	11	513	Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1
sp|Q02497|LAC1_TRAHI	3.62e-200	19	484	21	515	Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1
sp|Q99046|LAC2_TRAVI	8.10e-199	6	486	6	516	Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000259	0.999756	CS pos: 19-20. Pr: 0.9786

TMHMM  Annotations     

There is no transmembrane helices in CC1G_03940-t26_1-p1.