CAZyme Information: AKAW_04680-t41_1-p1

Basic Information

• Species: Aspergillus luchuensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis
• CAZyme ID: AKAW_04680-t41_1-p1
• CAZy Family: GH13
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
672	DF126456|CGC3	76570.77	6.2513

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AluchuensisIFO4308	11755	1033177	267	11488

• Gene Location: location=DF126456:800158-802667(+)

Full Sequence      

MLLESCWTALVHFFSFQSLFASQQSPLPPKGGLEYPLPPGGEVNYPSPTTSTAQQPTPTK
ILKFKPIDASIECEYEGLSDTHVALPRGDQRTWLKPKPNVNGTTYDIHTNYETTWPKGRV
RDYSFTVTESGELEPDGVKKEAGKYFDGKYPGRRIEACWGDTVRVHVKNSLPYNGTAIHM
HGIRMFETGFSDGVPGVTQCPIAKNDTYTYEFTATQYGTTWYHSHYSLQYTDGLLGPLTI
YGPASVVDYDDALEPLMLADRIHQGAFGRWTWVTVENHNPPIPMDTILINDHGSAAGKFQ
NLRYRTKKVTKGKKYLLRLINASTDTAFIFSIDQHKMTVIGTDLVPITPYLKDTLYIGIG
QRYHVIVEADAIDECRNYWIRTQPATGCHNFNFEPNERQGIFVYNEDNHDDPISTPYVPP
YNGDCRDEEHKVLRPVVEWQVPPPTPDQLRKVQSPWMVLKQDNFTMPPEEGHDGTNDPKW
SAWQIHDDPAWVNYKDLTINHLNGSHTWPANAALFEIRRNESNWAYMVIDGAHQPKESGT
PLGEKTVPAAHPMHLHGHDFALLKQSYTKLDDKLFDGNHTADLQKFIETELEYNNPARRD
VVLLPKGGYIVIAFKILEDREKFQEIMKRKNADNQTAEDRKNNGCKNWATWYDNKANRWE
NGTGRFQDDSGV

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	109	421	6.9e-117	0.9807692307692307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259947	CuRO_2_MaLCC_like	1.71e-70	253	419	1	165	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.
259923	CuRO_1_MaLCC_like	1.25e-67	118	241	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.
400195	Cu-oxidase_3	4.32e-43	126	245	1	119	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259926	CuRO_1_Diphenol_Ox	2.80e-42	121	241	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.
274555	ascorbase	3.43e-39	135	563	15	456	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
BCS14352.1|AA1_3	0.0	128	672	10	554
BCS02695.1|AA1_3	0.0	180	616	1	437
CAK46289.1|AA1_3	2.00e-280	1	672	1	672
QKX62792.1|AA1_3	2.16e-159	68	672	57	661
BCS03291.1|AA1_3	4.66e-155	60	672	44	671

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	3.60e-88	105	616	52	516	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	3.60e-88	105	616	52	516	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	1.05e-75	85	614	16	504	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LWW_A	1.11e-74	98	614	1	477	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LM8_A	7.96e-74	105	614	7	476	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4APX3|LAC1_ARTBC	1.29e-120	71	672	49	633	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1
sp|Q0CCX6|GEDJ_ASPTN	8.16e-90	105	616	42	534	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	4.94e-88	105	616	52	517	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	5.40e-84	98	615	48	524	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	6.28e-84	105	616	40	539	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.741563	0.258440

TMHMM  Annotations     

There is no transmembrane helices in AKAW_04680-t41_1-p1.