CAZyme Information: ASPCADRAFT_397033-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_397033-t33_1-p1
• CAZy Family: GH76
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
599		66877.61	6.7871

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcarbonariusITEM5010	11735	602072	260	11475

• Gene Location: location=KV907500:850043-852165(-)

Full Sequence      

MRVRHWSWKLVLYPATICGLMFLVFLMQILTPNPLQGLIPSKAYTNQTLSTTHNPDIARP
IIELHPENHVYRNPVAQHFNWEVTADYVRPDGVLKRVYLVNGLFPGPTVEARSGDRLIIN
VTNLLEDESISVHWHGLHTENAMDGAVGVTQHPILPGSTFTYNFTIPADQSGTFWYHAHS
GLIRADGLYGGLIVHAPSPKTTVRGLLARADDNGQDGYSRDILLLVGDWYHRSADQVYSW
YMRAGSFGNEPVPDSLLINGNGRFDCSMAVPARPVDCINRQMNLSYLDANDDTTYRVRIV
NTGSVAGFTLGFQNRDFTLIQVDNIDVEPQDSNSAGILYPGQRMDVILRPGVNNLPSSMA
INLDNEYPNPALSSAQTFAISKSQGDPPQISPSKYTTMFLSDVATKKSLLSTLPEKSQQT
HVVYTKIEKLSRNHNIPYGFFNRTSWKPPIGTPLINLPREEWDENQLVISSGASTSQPNH
DKGIWIDLVVNNLDDSGHPFHLHGHHFYILTTYKAPIGWGAYNPFTDATPPGLAPQTTTS
AKAITPYDLSRAQLRDTVYIPSRGYAVLRFRADNPGIWLFHCHIIWHQASGMAMLLQID

Enzyme Prediction     

No EC number prediction in ASPCADRAFT_397033-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	93	593	7e-94	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	4.06e-72	76	592	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.
177843	PLN02191	1.76e-69	79	596	26	544	L-ascorbate oxidase
215324	PLN02604	3.74e-63	74	597	18	545	oxidoreductase
259977	CuRO_3_MCO_like_4	7.98e-59	422	598	2	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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.
225043	SufI	3.26e-56	81	593	38	443	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
CAK44017.1|AA1	0.0	2	598	8	586
BCS06095.1|AA1	1.31e-271	143	599	1	460
BCR93452.1|AA1	1.31e-271	143	599	1	460
QMW37919.1|AA1	2.03e-268	4	598	18	598
QRD88142.1|AA1	3.75e-268	4	598	35	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	5.48e-57	79	599	5	480	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
3V9E_A	1.70e-54	75	594	66	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	4.49e-54	75	594	66	538	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]
1AOZ_A	5.20e-54	77	595	4	520	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]
5LM8_A	2.84e-49	75	593	22	499	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|Q6CII3|FET3_KLULA	1.45e-63	79	596	30	503	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|I1RMG9|FET3_GIBZE	8.34e-60	79	599	27	497	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
sp|K7NCS2|FETC_EPIFE	2.16e-58	72	593	16	490	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|W3X7K0|PFMAD_PESFW	3.99e-58	80	596	26	487	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1
sp|Q8LPL3|ASO_ARATH	1.66e-57	81	595	28	540	L-ascorbate oxidase OS=Arabidopsis thaliana OX=3702 GN=AAO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000021	0.000000

TMHMM  Annotations     

Start	End
7	29