CAZyme Information: RAK79997.1

Basic Information

• Species: Aspergillus fijiensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fijiensis
• CAZyme ID: RAK79997.1
• CAZy Family: GH76
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
554	KZ824631|CGC3	61264.60	6.2359

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfijiensisCBS313.89	12336	1448319	318	12018

• Gene Location: location=KZ824631:545696-547688(+)

Full Sequence      

MVPWLPFFLRGATAISAACNTSEENRPPPDTGVMRHYNFTVMRDIIAPDGYRKSAMLING
QFPGPTIEANWGDTISVTVNNMITTGTEEGLAMHWHGITQKGTPWEDGVPGVTQCPIVPR
SSFTYTFQADQYGTGWYHSHYSAQLTDGVYGPVIIHGPNHVNYDYDLGPIMISEYHHHDY
WSNLLEIFSRPPVIPNVDNNLINGRGIYNCSGTDCSPGASPSRFSFQSGKVHRLRLLNTG
SNANQKISIDGHTMTVIANDFIPVKPYNTDVVTLGAGQRTDVLVKATGRPGDAYWLRASI
DMDCLNSTATHPTVTAAIYYEDADPATWPNTTSTAVWQSNNCAGDPLHQTVPYHPLPPPG
TPSTTETIEINLAQNATGHYLFYMNNTTFRANYNAPLLLLGRTGNFSDPYYANANAYNSG
ANASVRLVFSNIYPMHHPLHLHGHNFWVLAEGRGTWDGVIVNPANPQRRDTQMMQAGTPE
NPAFVVLEWVLDNPGVWPLHCHMSYHVSMGLSLNIIEHPEKIQQLKIPSSLAKTCHEWAV
FSGQEFVNEIDSGV

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	28	336	4.5e-118	0.9615384615384616

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.26e-81	35	530	2	534	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.
215324	PLN02604	2.46e-79	34	531	24	558	oxidoreductase
177843	PLN02191	6.08e-75	31	528	20	555	L-ascorbate oxidase
259923	CuRO_1_MaLCC_like	5.28e-66	32	156	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.
274556	laccase	1.63e-61	35	535	4	539	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS07898.1|AA1_3	4.15e-294	28	554	72	602
BCR95349.1|AA1_3	9.97e-294	28	554	96	626
QGA18227.1|AA1_3	4.96e-236	20	554	50	585
CAK43464.1|AA1_3	1.30e-229	28	516	71	563
QKX63435.1|AA1_3	9.33e-224	28	553	54	583

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	4.76e-101	31	554	64	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	9.42e-101	31	554	64	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	4.40e-100	29	538	18	525	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	4.53e-100	29	538	19	526	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	9.49e-100	29	538	46	553	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	1.37e-175	21	554	49	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	2.62e-113	29	554	68	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.24e-105	29	554	63	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|A0A067XMP0|PTAE_PESFW	6.31e-94	32	538	55	590	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|Q12570|LAC1_BOTFU	2.68e-93	29	554	61	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.027607	0.972389	CS pos: 18-19. Pr: 0.9255

TMHMM  Annotations     

There is no transmembrane helices in RAK79997.1.