CAZyme Information: P175DRAFT_0440866-t39_1-p1

Basic Information

• Species: Aspergillus ochraceoroseus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus ochraceoroseus
• CAZyme ID: P175DRAFT_0440866-t39_1-p1
• CAZy Family: CE2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
540	MSFN02000006|CGC9	61268.48	5.5495

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AochraceoroseusIBT24754	9070	1392256	153	8917

• Gene Location: location=MSFN02000006:133142-134855(+)

Full Sequence      

MNWLLFALCLLWHSELVFCKDVYLNWKLTWVNAGPDGFQRPVIGINGEWPCPQVDLHLGD
RLIADVYNGLGNQSTGIHWHGMHQFGSPEMDGANGVTQCPIEPGQHMRYDFQVNQTGTFW
YHSHQMGQYPDGLRGPLILHDTKPLPFQYDEEITVTVSDWYHKQMGELVDEMEEVGVEPT
PDAILFNEATNTRLKVDPGKTYLIRLICMGNWAGHSVTFEDHDITIVEVDGVLTNPHYLP
PQLMRIAPGQRMSVLITTKDDTSRNYGILDAMDIVEMFVHENRSIPAGFNPNGTAWLVYD
EQKPLPPAPTIHVTDASVDFFNDLNLVSYEPKRRLEPVDRQIILNISQASQGRIAAFTIN
DQVYEEPTVPTLYTAMLATPEQAPDPSIYGSTNPYVVKYGEVVEIVINNFHSNLHAWHFH
GHTPQIIQRGTTYGGYFEGYFPNISSTPLRRDTIMVEPKSHLVFRFRAKNIDKCSLPPYS
DLLLRIWLLHCHTEFHVAAHLTATIIEAPERLHQFRVPEDHWRICPSSVLGATGSIGALN

Enzyme Prediction     

No EC number prediction in P175DRAFT_0440866-t39_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	377	1.4e-117	0.9851632047477745

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	8.89e-69	24	496	4	512	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.
225043	SufI	4.88e-67	36	510	48	451	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].
215324	PLN02604	9.39e-61	5	531	4	560	oxidoreductase
177843	PLN02191	6.29e-59	3	520	7	557	L-ascorbate oxidase
259920	CuRO_1_Fet3p	1.31e-58	22	140	1	121	The first Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK42098.1|AA1_2	5.61e-227	20	525	20	532
BCS11789.1|AA1_2	7.01e-222	20	525	20	518
QKX61289.1|AA1_2	1.34e-217	8	525	8	514
ACJ13061.1|AA1_2	1.72e-216	7	527	2	516
AHA42447.1|AA1	2.87e-216	7	527	6	520

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.12e-102	25	538	6	513	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]
4JHU_A	1.06e-52	33	527	15	487	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
5ANH_A	3.90e-51	33	527	15	487	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]
1AOZ_A	4.11e-51	23	512	5	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]
6H5Y_A	7.50e-51	33	527	15	487	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4WZB4|ABR1_ASPFU	1.02e-216	7	527	6	520	Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2
sp|E9R598|FETC_ASPFU	3.15e-133	22	528	23	514	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	4.34e-132	25	538	28	528	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	3.85e-130	25	535	26	524	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|W3X7K0|PFMAD_PESFW	9.10e-115	22	519	23	501	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000206	0.999779	CS pos: 19-20. Pr: 0.9797

TMHMM  Annotations     

There is no transmembrane helices in P175DRAFT_0440866-t39_1-p1.