CAZyme Information: CC1G_09609-t26_1-p1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: CC1G_09609-t26_1-p1
• CAZy Family: GH53
• CAZyme Description: laccase 7

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
543	AACS02000003|CGC11	59382.84	5.0658

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=AACS02000003:52732-55069(-)

Full Sequence      

MTSRLLGYLQLAIVLYNSVARGQMILSPSDTMVISNANVSPDGVTRSAVVVNGVHPGPDD
VFAINVVNELTDPTMLRSTSVHWHGLFQRGTNWADGAEGVNQCPISPERSFLYRFSPAGH
AGTFWYHSHFGTQYCDGLRGPMVVYDPDDPYKNEYDVDDVNTIITLADWYHTPAPSIRGP
FFPDSTLINGIGRTPGGPKVDLAVVNVEAGKKYRFRIVSLACDVNFQFSIDKHKLTIIEA
DGQLTDPLEVDRIQIFTGQRYSVILNANQTPDVYRIRAIPNAGVHGLTDTTAGGVNSAIL
RYANAEATELPQEDELPSNLVDLQEWMLHAYAGGDPAAPGRPEAGGADVRIPLRFTFSGG
RFFVNGTAYSSPSVPTLLQIMSGANPGELLPENSIYYLPRNQVIEVEIPSAGISASGPHP
FHLHGHAFSVIRSAGNTSYNYVNPVKRDVVNIGGDSDLVTIRFVTDNPGPWFFHCHIEPH
LVGGLAIVFAEAMKDTMSANPDVPDEWKDLCDIYDKLEPSLTSLSIIRRAEPTDLSAKFR
GLY

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	340	1.1e-131	0.9933993399339934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	7.46e-82	40	493	14	525	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	7.98e-80	348	493	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	7.52e-71	40	502	36	556	L-ascorbate oxidase
259925	CuRO_1_Tv-LCC_like	5.78e-70	28	146	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	1.43e-66	162	309	1	150	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
DAA04512.1|AA1_1|1.10.3.2	0.0	1	543	1	549
AAR01248.1|AA1_1	0.0	1	543	1	549
DAA04516.1|AA1_1|1.10.3.2	0.0	1	542	1	546
DAA04511.1|AA1_1|1.10.3.2	1.68e-294	1	513	1	523
AAR01247.1|AA1_1	1.68e-294	1	513	1	523

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HFU_A	1.82e-240	25	527	2	503	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.89e-240	25	527	2	503	Chain A, Laccase [Coprinopsis cinerea]
3KW7_A	7.87e-198	26	520	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]
2QT6_A	6.40e-196	26	520	2	496	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
1KYA_A	3.31e-191	26	520	2	497	Chain A, Laccase [Trametes versicolor],1KYA_B Chain B, Laccase [Trametes versicolor],1KYA_C Chain C, Laccase [Trametes versicolor],1KYA_D Chain D, Laccase [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q99056|LAC5_TRAVI	9.03e-195	26	520	25	525	Laccase-5 OS=Trametes villosa OX=47662 GN=LCC5 PE=3 SV=2
sp|Q12717|LAC5_TRAVE	1.28e-194	26	520	25	525	Laccase-5 OS=Trametes versicolor OX=5325 GN=LCC5 PE=2 SV=1
sp|Q02497|LAC1_TRAHI	1.64e-193	11	518	8	516	Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1
sp|Q99044|LAC1_TRAVI	3.07e-191	26	520	23	518	Laccase-1 OS=Trametes villosa OX=47662 GN=LCC1 PE=1 SV=1
sp|Q99046|LAC2_TRAVI	9.69e-190	19	517	15	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
0.000746	0.999228	CS pos: 22-23. Pr: 0.9654

TMHMM  Annotations     

There is no transmembrane helices in CC1G_09609-t26_1-p1.