CAZyme Information: KAG2014983.1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: KAG2014983.1
• CAZy Family: GH24
• CAZyme Description: laccase 7

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
398		43149.29	4.5899

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=JAAGWA010000004:137545-138991(-)

Full Sequence      

MVVYDDNDPHAALYDEDDENTIITLADWYHIPAPSIQGAAQPDATLINGKGRYVGGPAAE
LSIVNVEQGKKYRMRLISLSCDPNWQFSIDGHELTIIEVDGQLTEPHTVDRLQIFTGQRY
SFVLDANQPVDNYWIRAQPNKGRNGLAGTFANGVNSAILRYAGAANADPTTSANPNPVQL
NEADLHALIDPAAPGIPTPGAADVNLRFQLGFSGGRFTINGTAYESPSVPTLLQIMSGAQ
SVNDLLPAGSVYELPRNQVVELVVPAGVLGGPHPFHLHGHAFSVVRSAGSSTYNFVNPVK
RDVVSLGVTGDEVTIRFVTDNPGPWFFHCHIEFHLMNGLAIVFAEDMANTVDANNPPVEW
AQLCEIYDDLPPEATSIQTVVRRAEPTGFSAKFRREGL

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	1	195	9.5e-88	0.6336633663366337

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259970	CuRO_3_Tv-LCC_like	2.53e-91	203	347	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.
259949	CuRO_2_Tv-LCC_like	4.77e-75	21	177	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.
395317	Cu-oxidase	2.59e-53	19	164	1	146	Multicopper oxidase. Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.
274555	ascorbase	6.81e-49	17	345	132	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	3.82e-44	25	345	161	546	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAS38574.1|AA1_1	1.19e-297	1	398	142	539
DAA04506.1|AA1_1|1.10.3.2	6.85e-297	1	398	142	539
AAD30964.1|AA1_1|1.10.3.2	6.85e-297	1	398	142	539
AAR01242.1|AA1_1	3.13e-224	1	309	138	446
DAA04516.1|AA1_1|1.10.3.2	2.23e-181	1	394	148	544

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1A65_A	6.65e-285	1	381	124	504	Chain A, Laccase [Coprinopsis cinerea]
1HFU_A	2.60e-284	1	380	124	503	Chain A, LACCASE 1 [Coprinopsis cinerea]
4A2D_A	8.35e-158	1	373	124	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]
4A2F_A	8.64e-158	1	373	124	494	Coriolopsis gallica laccase collected at 12.65 keV [Coriolopsis gallica]
5A7E_A	1.36e-156	1	373	124	494	Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12739|LAC2_PLEOS	2.66e-149	1	370	158	522	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|Q99046|LAC2_TRAVI	1.93e-148	1	370	144	514	Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1
sp|Q99044|LAC1_TRAVI	2.29e-147	1	372	145	517	Laccase-1 OS=Trametes villosa OX=47662 GN=LCC1 PE=1 SV=1
sp|Q12718|LAC2_TRAVE	4.44e-147	1	370	144	514	Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1
sp|Q12729|LAC1_PLEOS	8.68e-147	1	370	156	520	Laccase-1 OS=Pleurotus ostreatus OX=5322 GN=POX1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000036	0.000001

TMHMM  Annotations     

There is no transmembrane helices in KAG2014983.1.