CAZyme Information: ASPBRDRAFT_190733-t33_1-p1

Basic Information

• Species: Aspergillus brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus brasiliensis
• CAZyme ID: ASPBRDRAFT_190733-t33_1-p1
• CAZy Family: GH132
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
597		67515.74	4.9380

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=KV878679:1799968-1802108(+)

Full Sequence      

MFTQRLLPLGILLWAVWTRASRSDCVHSPQSRDCWLPGFDIHTDYEEKVPPGKLVEYELT
VSNQVIAPDGYLTNGMVVNGQYPGPTIEANWGDTLRITVNNNLTNDNGTSIHWHGLRQLM
TNYLDGVPGVTQCPSKPGSSQVYEFRLMQYGTSWYHSHFSIQYTNGVHGAIKINGPSSMN
YDVDLGPILMSDWYHTDAFALYPTEILTPEAPIPESSVMNGKGVFDCDPSKDSRCTGKKE
RHEIFFSKGTTYRLSLVNTGSLLTYKFWIDGHNFTVIQNDFVPIQPFETDVLIVGIGQRY
DILVKADADFTNGTNFWMHANYCDVDTWESRLGIIRYDPLNTSDPYTPPVSEQHYGFGCQ
DPPPERLVPIVKRQVGKNVNSFDTPDYLRIGLQAWPNVSDPNSRIHTWLLTNRSIYLDWS
DPSLKKLTLDATPDFPPDTTPITLDFQTGDWVYFLILNNYTLSDAATPRTIPRSVHPIHL
HGHDYVILAQGEGPFPDDVVPNLDNPARRDVANCPIGGYLWMAFQINNPGAWLMHCHIAW
HASAGLGLQFIEQPSQIKPLMEQAGVLPDFADRCNEWTNWYENHNVRDNTTQEDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	43	351	5.1e-121	0.9775641025641025

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.05e-70	56	574	3	538	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.
177843	PLN02191	1.12e-68	54	585	23	572	L-ascorbate oxidase
215324	PLN02604	2.90e-68	52	576	22	563	oxidoreductase
259923	CuRO_1_MaLCC_like	9.75e-67	52	174	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.
259968	CuRO_3_MaLCC_like	9.75e-62	397	551	15	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
QIW99253.1|AA1_3	2.73e-308	27	597	47	621
QLI68968.1|AA1_3	3.03e-300	25	597	28	601
QED41496.1|AA1_3	5.56e-287	27	597	38	613
BAA08486.1|AA1_3|1.10.3.-	1.23e-269	23	597	26	605
AEO66253.1|AA1_3	1.25e-225	7	597	11	625

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.71e-143	23	577	37	564	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	3.41e-143	23	577	37	564	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3PPS_A	8.04e-109	12	581	32	592	Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_B Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_C Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_D Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius]
5LWX_A	1.06e-108	27	577	23	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.87e-108	38	577	6	528	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|Q0CCX6|GEDJ_ASPTN	2.69e-271	10	597	11	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q4WQY8|TPCJ_ASPFU	8.59e-264	13	597	15	609	Oxidoreductase tpcJ OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=tpcJ PE=2 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.79e-263	25	597	26	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	7.24e-153	24	597	43	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	6.45e-140	19	577	33	565	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000278	0.999696	CS pos: 22-23. Pr: 0.7933

TMHMM  Annotations     

There is no transmembrane helices in ASPBRDRAFT_190733-t33_1-p1.