CAZyme Information: ASPVEDRAFT_66491-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_66491-t33_1-p1
• CAZy Family: GH93
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
573		64618.32	4.6531

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AversicolorCBS583.65	13364	1036611	142	13222

• Gene Location: location=KV878140:267292-269193(+)

Full Sequence      

MACRVAELFVYCLAILVFTARSLAQDICENSPTSRGCWGEYNISTDYHSITPDTGVTREY
WLVATNTTLAPDGFERQVLTMNGTLPGPLIEADWGDELVIHVTNGLEHNGTAIHWHGIWQ
RNTNPFDGVPGVTQCPIAPGETFTYRFRATQYGTSWYHSHFSLQMADGLYGPVVIHGPAT
EDYDVDLGPVFLTDWYWKSVFLLWEEHTRYGGFPVRSNAVPPTGLLNGTNVFGCGEQPCT
GEVKRSETSVQKGKKYRIRLIDPSVDGWMKFTIDGHKLTVVAADFVPIEPYETDAVILTS
GQRYDVIVEANQDIGNYWMRAVYQTACNGLDIDNDDIRGILRYEGADIADPTTSQWKISN
SCGDEPYDKLVPYVKKTVGNAAAQKNLNVGWKYDLPELFFHWTLNSKHLTIDWSSPTDYL
AYKNESAFPTESNVYEVPNKNQWTYWVIQDVGLVNAYHPFHLHGHDFFILAEGLGLYTPL
VKLNLDNPPRRDTATMAGSGYLVIAFETDNPGSWLMHCHIAWHASQSLALQFVERESEIG
TLIEPMVDEFESVCDKWGEYHKDSVYHQDDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	45	362	4e-136	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.76e-83	56	542	8	531	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	2.23e-78	56	542	30	554	L-ascorbate oxidase
259923	CuRO_1_MaLCC_like	3.27e-74	55	176	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	1.20e-71	76	533	22	518	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.
225043	SufI	4.05e-70	72	536	48	450	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS23441.1|AA1_3	0.0	4	573	3	565
EAA61461.1|AA1_3	0.0	10	573	10	570
AWI47682.1|AA1_3	5.11e-310	18	511	2	492
CAM12502.1|AA1_3	3.45e-208	28	573	37	581
ABM21605.1|AA1_3	9.43e-204	28	573	43	584

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.14e-199	19	573	30	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	2.28e-199	19	573	30	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	2.60e-155	23	568	16	565	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	2.39e-154	38	568	4	537	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.47e-154	38	568	5	538	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|J5JH35|OPS5_BEAB2	2.92e-204	22	573	38	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	9.22e-201	28	573	39	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	8.07e-179	28	573	37	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q0CCX6|GEDJ_ASPTN	1.33e-150	28	573	28	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.98e-148	17	573	15	610	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 SP

Other	SP_Sec_SPI	CS Position
0.000193	0.999769	CS pos: 24-25. Pr: 0.9748

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_66491-t33_1-p1.