CAZyme Information: KAG2015100.1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: KAG2015100.1
• CAZy Family: GH3
• CAZyme Description: laccase 5, variant 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
550	JAAGWA010000004|CGC9	59706.51	5.3601

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=JAAGWA010000004:377966-380428(-)

Full Sequence      

MSVDFACEFSIYLKTSAYKSNLLPLAILAVSLRPLIVPVTAQAIPPVATMTVSNINASPD
GFTRPVVAVNGQHPPPPILANKGDDFQITVVNNLDDPTMLRQTSVHWHGIFVHKAAWADG
PDGVTQCPIAQSGDSFTYSFDAGNEAGTFWYHSHYGTQYCDGLRGPLVIYDDNDPYKNLY
DVDDESTIITLADWYHLPTPSIAGIALSDATLINGKGRRPGGPLTDIEIVNVQPGTRYRF
RLISMACEPTYKFSIDGHNMTIIEADGQLTEPHTVQEITIFTGQRYSFILEANQPVGNYW
IRAIPNLGARNLPDFSSGGINSAILRYAGARPRNPTTRAPRNPVVLKEANLRTLLNPGAP
GGSGPADENIVFNLALNAEETGFVMNGVAWANPDIPVMVQLMNGVPAEDIIPQGAYRTLP
RNSVVEVSIPGFEIAGPHPFHLHGHAFDVVRSAGSDTYNYVNPVRRDVVDIGGAGDNVTI
RFRTDNPGPWFFHCHVEFHIITGLAMVFLEAPGDIASNSPPPPSWDALCPKFKSLPANAT
SIQIVPTPTP

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	58	361	1.2e-142	0.9900990099009901

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.68e-78	52	511	8	524	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	1.24e-75	367	512	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.
259925	CuRO_1_Tv-LCC_like	1.53e-74	46	171	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.
274556	laccase	1.91e-69	63	524	21	534	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
215324	PLN02604	9.76e-67	58	510	37	546	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
DAA04515.1|AA1_1	0.0	20	550	3	533
DAA04514.1|AA1_1	1.87e-305	21	548	4	525
DAA04510.1|AA1_1|1.10.3.2	2.14e-252	49	550	31	533
AAR01246.1|AA1_1	2.14e-252	49	550	31	533
DAA04506.1|AA1_1|1.10.3.2	3.82e-223	21	545	4	521

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1A65_A	2.90e-222	42	545	1	503	Chain A, Laccase [Coprinopsis cinerea]
1HFU_A	5.63e-222	47	545	6	503	Chain A, LACCASE 1 [Coprinopsis cinerea]
5A7E_A	2.04e-193	43	535	1	491	Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]
4A2D_A	8.26e-193	43	535	1	491	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	8.55e-193	43	535	1	491	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|Q12719|LAC4_TRAVE	1.29e-189	41	535	21	515	Laccase-4 OS=Trametes versicolor OX=5325 GN=LCC4 PE=3 SV=1
sp|Q99044|LAC1_TRAVI	2.98e-188	39	535	18	515	Laccase-1 OS=Trametes villosa OX=47662 GN=LCC1 PE=1 SV=1
sp|Q99055|LAC4_TRAVI	4.22e-188	41	535	21	515	Laccase-4 OS=Trametes villosa OX=47662 GN=LCC4 PE=3 SV=1
sp|Q12739|LAC2_PLEOS	6.60e-188	43	538	24	525	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|Q01679|LAC1_PHLRA	2.41e-187	43	538	22	518	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
0.055659	0.944320	CS pos: 43-44. Pr: 0.8721

TMHMM  Annotations     

There is no transmembrane helices in KAG2015100.1.