CAZyme Information: CLCR_02807-t43_1-p1

Basic Information

• Species: Cladophialophora carrionii
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora carrionii
• CAZyme ID: CLCR_02807-t43_1-p1
• CAZy Family: GH13
• CAZyme Description: Laccase-2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
636	LGRB01000003|CGC1	71504.84	7.0831

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CcarrioniiKSF	11240	N/A	59	11181

• Gene Location: location=LGRB01000003:1043075-1045154(+)

Full Sequence      

MVSLWARIVAVFHFILLSPPREQWPDQHPLSVSTKATGPAQPSLLADERVPPKPFLPPSA
PRGSDFRCEYPKLKDYKFCSTYGDRSCWLKHSDPAKQSYNITTDYEKVFPEGITRKYYIE
INEKTISPDGVSRAAMLVNGTYPGPWIEACWGDWLEITVNNTLQTNGTTIHWHGIRQLHT
TANDGVNAITQCPIAPNQTFTYKFRAMQYGTSWYHSHYSLQYGDGVLGPLTIHGPSSADF
DEAQPPVLMSDWLHRPWYSAWWDSITTGKRPADPDNILVGGKGSWPASLPSKGFRLDFVR
GRRYLLRLINTSVDTTFVFSIDNHKIQVVGADFVPIVPYMTDHVVVGIGQRYHIIVTANP
MDGNDDASYWIRTIPADGCSPKAMQSIDNRTGIVIYKKKDPVDYPRTFSIECRDEPYGKL
VPVLNWTVGSPSNIAANSEFDIGFDNITAGSLWPASIQKPRWNMYSDTMWLNFSNITLSQ
NLNAKQNEFNSHSVVVKQDSAEDAWVYFLLSGTGIPRSGRQYFPLAHPIHLHGHDFAILQ
QSSQPYQIGGLNLNLKNPPRRDVALLPASGFLVLAFKADNPGHIAVHASGGLAMQVIENG
GKVKLDPFDQKQLWDTCQKWDEWVSKHHFLQDDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	103	407	1e-123	0.9647435897435898

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	2.96e-76	112	233	1	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.
259947	CuRO_2_MaLCC_like	4.40e-57	245	396	2	149	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.
274556	laccase	8.99e-56	112	600	1	522	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.
177843	PLN02191	5.38e-53	115	598	24	546	L-ascorbate oxidase
259926	CuRO_1_Diphenol_Ox	2.64e-48	115	233	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD61993.1|AA1_3	1.76e-184	9	636	15	658
AHZ65141.1|AA1_3	5.63e-184	41	636	30	651
QGI68425.1|AA1_3	2.00e-183	55	636	49	658
QGI99317.1|AA1_3	2.00e-183	55	636	49	658
CCT72796.1|AA1_3	2.83e-183	55	636	49	658

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	4.14e-134	85	636	46	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	8.24e-134	85	636	46	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	1.47e-113	97	624	33	557	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	7.16e-113	97	624	5	529	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	7.37e-113	97	624	6	530	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	6.14e-162	67	636	50	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	9.87e-135	85	636	46	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|A0A067XMP0|PTAE_PESFW	5.05e-120	74	636	22	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|Q12570|LAC1_BOTFU	2.29e-117	73	636	31	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	1.49e-116	85	636	51	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.044571	0.955400	CS pos: 22-23. Pr: 0.7930

TMHMM  Annotations     

There is no transmembrane helices in CLCR_02807-t43_1-p1.