CAZyme Information: CC1G_09263-t26_1-p1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: CC1G_09263-t26_1-p1
• CAZy Family: GH5
• CAZyme Description: laccase 6

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
529	AACS02000003|CGC14	57181.06	4.8868

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=AACS02000003:3509205-3511495(-)

Full Sequence      

MTTRLLAYLQLGIALYHSGVRAQATLNPTDTMIISNAQVSPDGFARSAVVVNGVHPGPLL
TGQKDDTFAINVVNELNDPTMLRSTSVHWHGLFQKGTNWADGAEGVNQCPISPASPENTE
NAFEYRFTPAGHAGTFWYHSHFGTQYCDGLRGPMVVYDPQDPYLGDYDASTVITLADWFH
TPAPSLRAPFRPDATLINGIGRTPGGEQVDLAVVNVEAGKKYRFRVVSLACDVNFQFSID
GHKLTIIEADGQLTDRLEVDRIQIFTGQRYSVILNANQEPGNYRIRAIPNAGVPGLVGTV
DEGVNSAILRYAGAPIEEPSSDPPANPVDLREWELHAFSGPGFDPSAPGTPEIGAADVVL
PLQFTFVGGKFQVNGVAYESPDVPTLLQIMSGRNPGELMPEGSVHYLPRNQVVEVQIPSG
SISNSGPHPFHLHGHAFSVVRSAGNSTPNFVNPVKRDVVSIGGASDSVTIRFVTDNPGPW
FFHCHIEPHLVDGLAIVFAEAMEDTVQANPLPEDREYCSVLHAFSGNLC

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	340	5.9e-134	0.976897689768977

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	9.59e-88	40	503	14	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.
259970	CuRO_3_Tv-LCC_like	1.83e-78	357	502	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.
177843	PLN02191	2.30e-76	40	503	36	549	L-ascorbate oxidase
259925	CuRO_1_Tv-LCC_like	1.45e-73	28	158	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	1.56e-71	171	327	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
DAA04511.1|AA1_1|1.10.3.2	0.0	1	529	1	532
AAR01247.1|AA1_1	0.0	1	529	1	532
DAA04516.1|AA1_1|1.10.3.2	1.55e-306	1	528	1	525
DAA04512.1|AA1_1|1.10.3.2	1.92e-296	1	520	1	519
AAR01248.1|AA1_1	3.87e-296	1	520	1	519

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HFU_A	7.82e-236	24	520	1	489	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.32e-235	26	520	3	489	Chain A, Laccase [Coprinopsis cinerea]
3KW7_A	5.48e-187	26	512	2	484	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
6RHH_A	7.78e-186	24	513	1	482	Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RHI_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RHO_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RHP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twenty first structure of the series with 4415 KGy dose (collected after refreezing). [Steccherinum murashkinskyi],6RHR_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RHU_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi],6RHX_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RI0_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RI2_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RI4_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. First structure of the series with 13 KGy dose. [Steccherinum murashkinskyi],6RI6_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Second structure of the series with 400 KGy dose. [Steccherinum murashkinskyi],6RI8_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Third structure of the series with 800 KGy dose. [Steccherinum murashkinskyi],6RII_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourth structure of the series with 1200 KGy dose. [Steccherinum murashkinskyi],6RIK_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Thirteenth structure of the series with 5200 KGy dose. [Steccherinum murashkinskyi],6RIL_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourteenth structure of the series with 5600 KGy dose (data was collected after refreezing). [Steccherinum murashkinskyi]
5MEW_A	8.05e-186	24	513	1	482	The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi. Second structure of the series with total exposition time 33 min. [Steccherinum murashkinskyi],6RGH_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RGP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12719|LAC4_TRAVE	5.64e-188	14	504	12	494	Laccase-4 OS=Trametes versicolor OX=5325 GN=LCC4 PE=3 SV=1
sp|Q99055|LAC4_TRAVI	2.61e-186	14	504	12	494	Laccase-4 OS=Trametes villosa OX=47662 GN=LCC4 PE=3 SV=1
sp|Q02497|LAC1_TRAHI	1.05e-185	22	527	19	518	Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1
sp|Q99056|LAC5_TRAVI	4.38e-184	21	512	20	509	Laccase-5 OS=Trametes villosa OX=47662 GN=LCC5 PE=3 SV=2
sp|Q12717|LAC5_TRAVE	1.77e-183	21	512	20	509	Laccase-5 OS=Trametes versicolor OX=5325 GN=LCC5 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000319	0.999648	CS pos: 22-23. Pr: 0.9810

TMHMM  Annotations     

There is no transmembrane helices in CC1G_09263-t26_1-p1.