CAZyme Information: ASPBRDRAFT_150862-t33_1-p1

Basic Information

• Species: Aspergillus brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus brasiliensis
• CAZyme ID: ASPBRDRAFT_150862-t33_1-p1
• CAZy Family: CE5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
595		65807.08	4.8620

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AbrasiliensisCBS101740	13263	767769	274	12989

• Gene Location: location=KV878683:974899-976858(+)

Full Sequence      

MFGVLPVWVVLTGLATALSQNKTNGQSKWGTLSSPILPKFLGHDQNDDTPPWGNTWPGGD
PPNTGVTRHYNFSVTRAYKAPDGYNKSVILINDQFPGPLIEANWGDMVEVTVTNNIDTLD
EGVTLHWHGLTMKKSPWYDGVPGLSQCPIAPGTSFTYKFQADQFGSSWYHSHYSAQYNDG
LYGPMVIYGPVQSDIGDYDYDLGPVLLSDYLHDNYYDVLVQGFKQPPVIVGFDNNLINGK
GQYDCNATASGSAGCLPGAGLSQFRFHSGKSHRLRLVNAGSLANQKFSIDNHEMTVFAND
FVPVEPYTTDVITLGPGQRTDVIVHANGSAHDLVWMRSEIDTACLFDTITYDTALAAVYY
EAASTSETPNTTSRATWESNNCRNDPLHQTIPYYSMTPPATPATVETVTITLGYNETGYV
VFFVDGSSFRSDYNDPILLGTHANVSQVYPAERNIYNFGSHNSSVRMVLVNTYIMQHPIH
LHGHNFWVLAEGTGTWDGTTIVNPSNPQRRDTHILQPGTVDEPSYIVLEWMQNNPGVWPM
HCHMSNHASAGLVISIMEHPEQFANMSIPNTLSQTCRSWDDFSNTNFVNEIDSGV

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	62	376	1.5e-113	0.9519230769230769

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	7.49e-74	67	552	1	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.
215324	PLN02604	9.73e-69	67	566	24	554	oxidoreductase
259923	CuRO_1_MaLCC_like	4.01e-68	65	188	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.
177843	PLN02191	5.27e-67	64	558	20	546	L-ascorbate oxidase
259968	CuRO_3_MaLCC_like	4.78e-62	397	557	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX63435.1|AA1_3	5.49e-277	32	595	25	584
CAK48652.1|AA1_3	1.92e-264	30	595	84	648
BCS07898.1|AA1_3	2.46e-263	8	595	8	602
BCR95349.1|AA1_3	4.73e-262	25	595	52	626
QGA18227.1|AA1_3	3.68e-239	11	595	12	585

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.62e-111	16	595	36	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	3.22e-111	16	595	36	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	6.12e-99	33	586	13	560	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	3.10e-98	62	586	18	532	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.18e-98	62	586	19	533	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|A0A067XMP2|PTAK_PESFW	9.13e-166	11	595	6	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q96WM9|LAC2_BOTFU	1.79e-113	62	595	63	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	1.29e-112	62	595	68	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	3.38e-96	82	595	77	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q0CCX6|GEDJ_ASPTN	1.55e-90	70	584	62	590	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
0.000265	0.999725	CS pos: 19-20. Pr: 0.6261

TMHMM  Annotations     

There is no transmembrane helices in ASPBRDRAFT_150862-t33_1-p1.