CAZyme Information: ASPWEDRAFT_36463-t33_1-p1

Basic Information

• Species: Aspergillus wentii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus wentii
• CAZyme ID: ASPWEDRAFT_36463-t33_1-p1
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
684	KV878210|CGC10	75042.11	5.0906

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AwentiiDTO134E9	12659	1073089	224	12435

• Gene Location: location=KV878210:1958240-1960702(-)

Full Sequence      

MFAHQTLYAAWLGLAFFVSFTAAALRTYNLTVHSDVRSPDGVSREVYLINGLQPGPLIEA
NEGDSLEIFVKNGLSVDTSLHWHGILQQGTPNMDGVVGVTQYPIPPGGNFTYKFSVHSQY
GFFWYHTHVRAYYNDGIRGPLLIHPSPSRVRSFEKLANSTRERDALLRAEKNATNILLND
WTHEVSDTIYSQYFETGAYPFCVDSILANGLGRVECLPEDVLQSEGGSGMGMSQEAMSMS
MTQNSVSPSSSMTMAMKRQMDMGSMETETATSSQTSTSTMAMDMTMSAMPIPSQPSTGMS
NMGTMTMSGMSPSMTGMTSLSARGCSPPMMFREGYNASSLPPDTCTNTSSPLLTIPADFK
RGWLALNLVNSGAVSKLHVSLDAHSMYVYAADGLYVEMQEVKVLEIEIGQRYSVMIRLNQ
KPGNYYLRFATYPDDDMMKQVLEGQAILSYTMPMMSGRPPMNVTADPSMEWMMINGSAKP
DTSVLNPSLLSPFEPVSPPLGKADQTYAFTINQSDIVTWTMNGTPYMDAEIPIIQGNVSD
GWNANTTIHLPFNSTIDVILRIANDTMDKMGHPMHLHGHNFWVLGSGTGSFPYDSVTEAP
ESLINLRNPPYRDTTNLPQGGWAAIRFVSDNPGAWIFHCHIQWHMLSGMAVVFVEGEDQI
PELIGRSGKGSTATVSAGVCRNSL

Enzyme Prediction     

No EC number prediction in ASPWEDRAFT_36463-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	42	226	3.5e-52	0.44692737430167595
AA1	365	650	1.8e-43	0.49162011173184356

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.26e-72	26	663	2	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	4.81e-68	11	660	7	551	L-ascorbate oxidase
215324	PLN02604	6.52e-64	15	663	14	554	oxidoreductase
259919	CuRO_1_Abr2_like	3.94e-58	28	144	1	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259926	CuRO_1_Diphenol_Ox	4.78e-52	26	144	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOD95012.1|AA1	2.24e-257	23	683	24	662
QPG98040.1|AA1	2.02e-256	23	680	23	664
QLI72976.1|AA1	9.70e-256	19	674	25	665
UPL00042.1|AA1	2.91e-238	21	626	15	601
UNI13709.1|AA1	4.25e-235	21	661	21	631

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	8.55e-49	26	660	68	547	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.19e-48	26	660	68	547	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]
5EHF_A	2.34e-47	39	655	17	467	Laccase from Antrodiella faginea [Antrodiella faginea]
1AOZ_A	1.56e-46	25	660	3	528	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
6RHH_A	6.22e-44	38	655	17	469	Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RHI_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RHO_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RHP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twenty first structure of the series with 4415 KGy dose (collected after refreezing). [Steccherinum murashkinskyi],6RHR_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RHU_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi],6RHX_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RI0_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RI2_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RI4_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. First structure of the series with 13 KGy dose. [Steccherinum murashkinskyi],6RI6_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Second structure of the series with 400 KGy dose. [Steccherinum murashkinskyi],6RI8_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Third structure of the series with 800 KGy dose. [Steccherinum murashkinskyi],6RII_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourth structure of the series with 1200 KGy dose. [Steccherinum murashkinskyi],6RIK_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Thirteenth structure of the series with 5200 KGy dose. [Steccherinum murashkinskyi],6RIL_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourteenth structure of the series with 5600 KGy dose (data was collected after refreezing). [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	1.04e-90	22	663	19	570	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	1.96e-81	23	663	17	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	9.13e-75	9	663	7	588	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	1.40e-74	38	662	35	603	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1
sp|A0A2G5I8N8|CTB12_CERBT	1.91e-72	44	663	67	620	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.478695	0.521295	CS pos: 24-25. Pr: 0.3540

TMHMM  Annotations     

Start	End
7	29