CAZyme Information: KAG2014958.1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: KAG2014958.1
• CAZy Family: GH24
• CAZyme Description: laccase 5

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
546		58857.91	5.2359

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=JAAGWA010000004:66345-68682(-)

Full Sequence      

MSTRLVAYLQLAISLYHSAARGQAVLNPSDTMVISSANVSPDGVPRSAVVVNGVHPGPVL
VGQKDDNFAINVVNELTDPTMLRSTSVHWHGLFQRGTNWADGAEGVNQCPIAPERSFLYR
FSPAGHAGTFWYHSHFGTQYCDGLRGPMVVYDPEDPYKDEYDVDDVNTIITLADWYHTPA
PSIRGAFRPDATLINGLGRTPGGPPVDLAVVNVQEGQKYRFRIVSLACDVNFQFSIDGHK
LTVIEADGQLTDPLEVDRIQIFTGQRYSVILHANQAPNNYRIRAIPNAGVAGLTGTVDGG
VNSAILRYAGAPVAEPTTEAPSNMIDLSESQLHAYAGGDPAAPGRPEAGGADVTIPLRFT
FSGGRFFVNGTSYTSPSVPTLLQIMNGANPGELLPENSVYYLPRNQVVEVEIPSTGISGS
GPHPFHLHGHAFSVVRSAGNSSYNYVNPVKRDVVSMGGDSDLVTIRFVTDNPGPWFFHCH
IEPHLVGGLAIVFAEAMEDTAAAHPDIPTEWRDLCDIHDDLDPSLTSVSIVRRAEPTGLS
AKFRGL

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	344	2.4e-143	0.9933993399339934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.57e-88	40	510	14	534	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	9.96e-79	352	497	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.
274556	laccase	1.14e-73	31	493	7	517	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.
259925	CuRO_1_Tv-LCC_like	3.71e-73	28	152	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.
177843	PLN02191	2.25e-72	40	498	36	549	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
DAA04516.1|AA1_1|1.10.3.2	0.0	1	546	1	546
DAA04512.1|AA1_1|1.10.3.2	0.0	1	546	1	548
AAR01248.1|AA1_1	0.0	1	546	1	548
DAA04511.1|AA1_1|1.10.3.2	6.56e-309	1	517	1	523
AAR01247.1|AA1_1	6.56e-309	1	517	1	523

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HFU_A	1.74e-253	24	531	1	503	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	7.30e-253	25	531	2	503	Chain A, Laccase [Coprinopsis cinerea]
3KW7_A	9.19e-210	26	524	2	500	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]
1GYC_A	3.38e-204	26	521	2	494	Chain A, LACCASE 2 [Trametes versicolor]
5NQ8_A	3.07e-202	11	524	8	516	Crystal structure of laccases from Pycnoporus sanguineus, izoform II [Trametes coccinea],5NQ9_A Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea],5NQ9_C Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O59896|LAC1_PYCCI	4.81e-203	11	524	8	516	Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1
sp|Q99056|LAC5_TRAVI	7.59e-202	26	524	25	525	Laccase-5 OS=Trametes villosa OX=47662 GN=LCC5 PE=3 SV=2
sp|Q12718|LAC2_TRAVE	1.15e-201	20	521	16	514	Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1
sp|Q12719|LAC4_TRAVE	1.69e-201	17	524	15	518	Laccase-4 OS=Trametes versicolor OX=5325 GN=LCC4 PE=3 SV=1
sp|Q99046|LAC2_TRAVI	2.32e-201	20	521	16	514	Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000802	0.999181	CS pos: 22-23. Pr: 0.9586

TMHMM  Annotations     

There is no transmembrane helices in KAG2014958.1.