CAZyme Information: EEP77436.1

Basic Information

• Species: Uncinocarpus reesii
• Lineage: Ascomycota; Eurotiomycetes; ; Onygenaceae; Uncinocarpus; Uncinocarpus reesii
• CAZyme ID: EEP77436.1
• CAZy Family: GH16
• CAZyme Description: potential laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
632	CH476615|CGC1	71363.41	6.2426

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ureesii1704	7856	336963	96	7760

• Gene Location: location=CH476615:6029196-6031525(+)

Full Sequence      

MKFLEACFVACFKLLFFLALWADHAAAVSVPRQNLAPGPIFSPPPNVDSPNNVIQCQYPA
MRGWQHDASDKRNWLKWTGPGPAPEPGKYGITTDYEMYTPTGIIRRRLAGEMISVSPFDL
MTVQYFYLTSLEITVTNRLEYNGTAIHMHGLRMLNTNLHDGVPGVTQCPIAPGDSFTYRF
KAIQYGSTWYHSHYSLQYTDGLVGPLTIHGPSSSDYDESIDPLLMTDHIHRSAFAEYHIA
QTGPPPRMSSILLNGIGSYAGLGGNAPTRKYSTLVQKGKKYLLRLINTSTDATFVFSIDN
HNFTVIGADFVPMRPYDTDHIVVGIGQRYHVIVNTLSDVDNGAAFWIRTVPTTGCSRFET
DNPPDERTGILYYGERSSTLPTSTRHQFPLDCRDEPFDRLKPYHPWQVPDPMLDASIFDT
SMDVQRGTWVMPERPSNASKVSFWKAGPSSMYLNYSQPMVKSLDRTSWDDTWVVYPSEDH
TLDSWVYLLVTGFKESGNDGQARVAHPMHFHGHDFALLQQSEVPYQPSAINLTLDNPPRR
DVVLLPSNGFVVIGFRADNPGSWVMHCHIAWHASLGLALQILERKDDFIAHLESRPRDVR
EMERVCTNWDTWFSNPANHWDPDGFFQDDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	130	392	5.3e-102	0.8269230769230769

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259947	CuRO_2_MaLCC_like	2.20e-63	222	391	3	167	The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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 in fungi and plants. Laccase is 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.
259968	CuRO_3_MaLCC_like	1.99e-53	435	582	17	157	The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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 in fungi and plants. 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.
259923	CuRO_1_MaLCC_like	3.34e-50	131	209	44	122	The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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 in fungi and plants. 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	1.69e-49	122	583	55	546	L-ascorbate oxidase
274555	ascorbase	1.71e-47	133	577	44	517	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
QKX62792.1|AA1_3	1.87e-194	28	632	35	661
UPK95500.1|AA1_3	2.26e-190	5	632	5	651
AHZ65141.1|AA1_3	1.34e-186	5	632	5	651
QKD58662.1|AA1_3	3.18e-184	39	632	47	659
CCT71494.1|AA1_3	1.80e-183	39	632	47	659

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	3.15e-119	87	632	50	580	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
3V9E_A	6.25e-119	87	632	50	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	1.21e-98	122	619	83	564	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	6.10e-98	122	619	55	536	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	6.27e-98	122	619	56	537	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4APX3|LAC1_ARTBC	1.21e-234	29	632	27	633	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.23e-115	87	632	50	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	4.08e-115	21	632	13	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	2.01e-110	135	632	107	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q0CCX6|GEDJ_ASPTN	2.53e-106	60	632	34	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000196	0.999771	CS pos: 27-28. Pr: 0.9746

TMHMM  Annotations     

There is no transmembrane helices in EEP77436.1.