CAZyme Information: KAG2012203.1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: KAG2012203.1
• CAZy Family: GH16
• CAZyme Description: laccase 2, variant 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
517	JAAGWA010000006|CGC1	55464.97	6.6811

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: location=JAAGWA010000006:2523188-2525510(+)

Full Sequence      

MLLLATALATSLLPFVLGAIGPSTNLVVANKVIAPDGFSRSAVLAGATQPTVQFPGPVIQ
GNKNSFFAINVIDALTDPTMLRTTSIHWHGMFQRGTAWADGPAGVTQCPISPGHSFLYKF
QALNQAGTFWYHSHHESQYCDGLRGAMVVYDPVDPHRNLYDIDNEATIITLADWYHVPAP
SAGLVPTPDSTLINGKGRYAGGPTVPLAVISVTRNRRYRFRLVSLSCDPNYVFSIDGHTM
TVIEVDGVNVQPLVVDSIQIFAGQRYSFVLNANRPVGNYWVRANPNIGTTGFVGGVNSAI
LRYVGASNTDPTTTQTPFSNPLLETNLHPLTNPAAPGLPTPGGVDVAINLNTVFDFSSLT
FSVNGATFHQPPVPVLLQIMSGAQTAQQLLPSGSVYVLPRNKVIELSMPGGSTGSPHPFH
LHGHEFAVVRSAGSSTYNFANPVRRDVVSAGVAGDNVTIRFRTDNPGPWILHCHIDWHLV
LGLAVVFAEDAPTVATMDPPPAWDQLCPIYDALPPNT

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	33	337	3.6e-155	0.9933993399339934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259970	CuRO_3_Tv-LCC_like	4.88e-85	345	490	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	1.65e-83	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.
274555	ascorbase	1.75e-80	53	489	28	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.
177843	PLN02191	1.22e-70	53	489	50	546	L-ascorbate oxidase
259925	CuRO_1_Tv-LCC_like	3.52e-70	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAD30965.1|AA1_1	0.0	1	517	1	517
DAA04507.1|AA1_1|1.10.3.2	0.0	1	517	1	517
DAA04519.1|AA1_1|1.10.3.2	2.39e-307	1	517	1	517
AAD30966.1|AA1_1|1.10.3.2	3.49e-304	1	517	1	515
AAR01244.1|AA1_1	1.42e-303	1	517	1	515

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4JHU_A	4.99e-239	20	516	2	494	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
2HRG_A	9.51e-237	19	516	1	494	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]
4A2D_A	5.47e-236	19	516	1	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]
5ANH_A	5.47e-236	19	516	1	494	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]
4A2F_A	5.67e-236	19	516	1	494	Coriolopsis gallica laccase collected at 12.65 keV [Coriolopsis gallica]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12739|LAC2_PLEOS	1.94e-249	3	516	7	525	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|Q12729|LAC1_PLEOS	5.15e-239	3	513	7	520	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1
sp|Q02497|LAC1_TRAHI	3.14e-233	19	516	22	518	Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1
sp|Q99046|LAC2_TRAVI	4.29e-233	17	513	19	514	Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1
sp|Q01679|LAC1_PHLRA	2.56e-232	17	513	20	515	Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2

SignalP and Lipop Annotations

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     

There is no transmembrane helices in KAG2012203.1.