CAZyme Information: CC1G_05972-t26_1-p1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: CC1G_05972-t26_1-p1
• CAZy Family: GH11
• CAZyme Description: laccase 4

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
545	AACS02000003|CGC1	59969.77	5.6204

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=AACS02000003:173719-175961(+)

Full Sequence      

MRDSALPVLFLLFGLFPGIQGKVLSSASTLVVHNQFVAPDGFNRSAVLVNGVHPSPLIKA
NKGETYYLNVVNKLHDSTMLRSTSVHWHGLLQHGTAWADGSQSVSQCPISPGHSFEYRFP
GGDQAGTFWYHSHFGTQYCDGLRGPFVIYDENDPYKHLYDVDDENTIITVADWYHTPAPS
LPIPAFADSTLINGKGRYPGGPKVDLAIVNVVKGKRYRFRLLSLACEPNYQFSIDGHRMT
IIEADGYLTEPVVVDRIQIFTGQRYSFILEANRPVANYWIRALPNYGNNGLTLGFEGGIN
SAILRYAGAPKSEPIYSNWPLDRGVQLLESMLHPIYSPPAPGPPVPGAADVNIYLDMGFQ
PESLTYTVNGSVFEPPSVPVLLQIMSGAKNAAELLPKGTLYPLKRNQVVELTVPGGLIGG
PHPFHLHGHSFSVVKSAGSQTYNFDNPVRRDVTNAGEEGEEVVIRFETDNSGPWLFHCHV
EFHLQMGLAIVFAEDIEGMVDRNPVPGAWKELCPIYDALPEDEKTVTILEPTNNTEVSSD
APTTN

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	37	342	1e-147	0.9933993399339934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259970	CuRO_3_Tv-LCC_like	8.13e-80	350	496	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	1.60e-79	32	497	8	526	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	1.63e-77	26	150	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.
259949	CuRO_2_Tv-LCC_like	1.03e-75	166	314	1	151	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	5.68e-70	28	497	26	549	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
DAA04509.1|AA1_1|1.10.3.2	0.0	1	545	1	545
AAR01245.1|AA1_1	0.0	1	545	1	545
ARD69911.1|AA1_1	2.59e-250	3	532	6	537
UES62898.1|AA1_1	1.05e-249	3	532	6	537
UES62896.1|AA1_1	1.09e-241	28	528	32	532

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1A65_A	5.82e-240	22	526	1	500	Chain A, Laccase [Coprinopsis cinerea]
1HFU_A	1.13e-239	23	526	2	500	Chain A, LACCASE 1 [Coprinopsis cinerea]
1GYC_A	1.30e-208	24	521	2	496	Chain A, LACCASE 2 [Trametes versicolor]
6H5Y_A	1.35e-207	24	524	2	496	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]
2QT6_A	8.31e-207	30	519	8	493	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12739|LAC2_PLEOS	4.46e-207	24	524	25	527	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|Q12729|LAC1_PLEOS	7.79e-207	30	524	31	525	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
sp|Q99046|LAC2_TRAVI	4.46e-206	24	521	22	516	Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1
sp|Q02497|LAC1_TRAHI	1.87e-205	24	519	23	515	Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1
sp|Q12718|LAC2_TRAVE	7.28e-205	24	521	22	516	Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000232	0.999747	CS pos: 21-22. Pr: 0.9801

TMHMM  Annotations     

There is no transmembrane helices in CC1G_05972-t26_1-p1.