CAZyme Information: CC1G_00686-t26_1-p1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: CC1G_00686-t26_1-p1
• CAZy Family: AA1
• CAZyme Description: bilirubin oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
434	AACS02000001|CGC11	47821.24	6.6413

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=AACS02000001:3584850-3586656(+)

Full Sequence      

MHPHLRPLLVALTSSFALQNFAAAALTTPRAIHSKDTMFISNIRASPDGFERPVIAVNGH
HPALLIKAKKGDEFELTVANHLTEETMLRQTSIHGIFQHKSSWADGPEGVTQCPVAQFGN
SFTYKFNAGNETGTYWYHSHFAPLILSVTAETQYCDGLRGPLVIYDDNDPYRNDYDGGHI
LICSIISVQPVFPAVDNEDTIITLADWYHLQAPSINTTIAPPVNATLINGKGRQPVKPDS
PLAIVNVKQGKRYRFRILSLSCDPNYNFSIDGHDLTVIEADGQLTRKLVVQRLQIPMTRG
ELLTLLVFSIRSICAGHAFSVIQSAGSPNKNYIDPVRRDVVSIGDPDRKENVTIRFVTDN
PGPWFFHCHIEFHLSGGLGAVFVEDQKDIKSSDRAPPPSWSELCPTFDALPTNATFVSTV
ATPTAPTAPTNIPF

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	46	295	2.8e-90	0.7326732673267327

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259925	CuRO_1_Tv-LCC_like	1.17e-71	34	166	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.
259970	CuRO_3_Tv-LCC_like	1.75e-46	199	386	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	7.01e-43	200	332	1	118	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.
259926	CuRO_1_Diphenol_Ox	9.01e-39	40	165	7	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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.
274555	ascorbase	1.91e-37	40	332	8	275	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABP81837.1|AA1_1	5.24e-244	1	434	1	562
DAA04514.1|AA1_1	1.18e-134	37	420	28	522
DAA04515.1|AA1_1	1.43e-129	28	420	23	528
DAA04510.1|AA1_1|1.10.3.2	4.72e-125	32	420	26	528
AAR01246.1|AA1_1	4.72e-125	32	420	26	528

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HFU_A	2.03e-108	32	420	3	503	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.09e-108	32	420	3	503	Chain A, Laccase [Coprinopsis cinerea]
1GYC_A	2.83e-101	31	410	1	494	Chain A, LACCASE 2 [Trametes versicolor]
2QT6_A	6.11e-100	40	413	10	497	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
5NQ8_A	6.04e-99	16	410	10	513	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|Q02497|LAC1_TRAHI	1.88e-100	15	413	9	518	Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1
sp|Q12718|LAC2_TRAVE	5.72e-99	31	410	21	514	Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1
sp|Q99046|LAC2_TRAVI	1.14e-98	31	410	21	514	Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1
sp|Q99044|LAC1_TRAVI	2.33e-98	17	410	6	515	Laccase-1 OS=Trametes villosa OX=47662 GN=LCC1 PE=1 SV=1
sp|O59896|LAC1_PYCCI	6.88e-97	15	410	9	513	Laccase OS=Pycnoporus cinnabarinus OX=5643 GN=LCC3-1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.093942	0.906029	CS pos: 22-23. Pr: 0.8561

TMHMM  Annotations     

There is no transmembrane helices in CC1G_00686-t26_1-p1.