CAZyme Information: P170DRAFT_511049-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_511049-t37_1-p1
• CAZy Family: GT69
• CAZyme Description: conidial pigment biosynthesis oxidase Arb2/brown2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
612	MSFO01000005|CGC13	68564.15	5.0649

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000005:2966553-2968671(+)

Full Sequence      

MAQSRTMNLSVLLLALAGFVSAKVVKEELTLTWEQGAPNGQAREMILMNGQFPGPTFTWD
EDDDVEVLVHNQMPFNTTIHWHGLMMQDTPWSDGVPGLTQKPIEVNQSFIYRFKASPPGT
HWWHSHSRTTLLDGLYGALYIRPKPTNPAPWALISDNPRDIEAMQKAVANPHVIVVSDWT
QFKSWEYMDAQEASGYAVFCVDSLLINGKGSVYCPGEDFLVSHTSTYMKWAIYPGHVNDK
GCLPFVKSTENKYLANGRPEAIPLHLQRGCVPATGDQEVIEVDPAAEWVSLNFVDAATFK
TPVFSIDEHQMWVYEADGHFIEPQRVDTVEFYAGERYSVMVKLDKKPQDYTIRVTDTGLT
QIIASYATLRYKGGREGAETTGVINYGGLNTTAVVTLDRDHLPPYPPNAPAAHSDAQHVL
NTHRWHNAWQYTMTGGGMYGEDRSAYAPLLYHPNSADAMNESLVIRTKNGTWVDLVIQVG
SLPEQPQEFPHIMHKHTGRTWQIGAGEGIWNYTSVDEAIQAEPSKFNLKNPNFRDTFITS
FDGPSWIVLRYQVTNPGPWLMHCHFEIHLGGGMAVAILDGVDAWPEVPPEYAPDQKGFYL
DADKDAPGDREL

Enzyme Prediction     

No EC number prediction in P170DRAFT_511049-t37_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	41	574	1.8e-82	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.07e-76	415	580	1	164	The third 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 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.
259944	CuRO_2_Abr2_like	1.62e-64	172	372	1	138	The second 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 2 of 3-domain MCOs has lost the ability to bind copper.
259919	CuRO_1_Abr2_like	2.43e-55	29	142	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.
274555	ascorbase	3.23e-49	33	590	10	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	1.70e-47	5	588	3	555	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKG86291.1|AA1	0.0	10	605	10	574
QKX57114.1|AA1	0.0	9	598	9	602
CEI66207.1|AA1	0.0	20	598	20	602
CZS77880.1|AA1	0.0	8	598	6	607
CEF74605.1|AA1	0.0	8	598	6	607

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z1X_A	1.83e-44	37	582	16	468	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
1AOZ_A	1.28e-41	37	588	16	532	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]
2XYB_A	2.43e-40	28	591	7	489	CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]
2HRG_A	3.28e-40	28	591	7	488	Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii]
5ANH_A	2.92e-39	28	591	7	488	Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_B Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_C Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RF62|GIP1_GIBZE	0.0	8	598	6	607	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	3.73e-251	25	608	20	611	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	2.60e-248	16	599	15	600	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	1.32e-223	8	592	6	606	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1
sp|A0A0B4F1I0|MLAC1_METAF	3.15e-209	22	591	20	610	Laccase 1 OS=Metarhizium anisopliae (strain ARSEF 549) OX=1276135 GN=Mlac1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000216	0.999746	CS pos: 22-23. Pr: 0.9798

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_511049-t37_1-p1.