CAZyme Information: ASPBRDRAFT_654468-t33_1-p1

Basic Information

• Species: Aspergillus brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus brasiliensis
• CAZyme ID: ASPBRDRAFT_654468-t33_1-p1
• CAZy Family: GT32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
542		61526.81	4.8225

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AbrasiliensisCBS101740	13263	767769	274	12989

• Gene Location: location=KV878679:1336828-1338548(+)

Full Sequence      

MIRTLITLGLYGFVRQALSKNVYLDWNITWVTAAPDGYARPVIGINGHWPCPQIDVNVGD
NLIVDVYNGLGNESTGIHWHGLHQNYNGYMDGVPGVTQCELHPQQRMRYIVPMNQTGTYW
YHSHEPGQYPDGLRGPIIVHDNVPAPYHYDEEMTLTLSDWYHVQIPILLDEFIVPSDHAP
YGGQEPLPDAILFNDMHNTKISVKPDTTYLIHVVCMGNFPGHALVIDDHDMTIVGMDGIA
IEPHFLPPQLLRMAVGQRVDLLLTTKNDTSKNYAIWDGLDIDEMFVQEGRSPPAGYNPNG
TAWLMYNEDAPLPPPPVIHVNNASLEFLDDVTLTPRDHLPLIDPIQHQFIFDVYPTTVDG
KPAYSINNMTYNAPDSPTLYTAIYSDPEACMDPDLYGDVNPFVVNYGDVVEIVLNNHHDN
LHPWHLHGHDFQVLQRTYPYGGFFDGYRNVSATPMRRDTLMVEPMGHFVIRFRAMNPDKL
TLIVLLRVWMFHCHIEWHVEVRLMAIIIEAPDQLQNMTIPNDHLQMCGNTQPSNWAPLAP
SP

Enzyme Prediction     

No EC number prediction in ASPBRDRAFT_654468-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	385	2.9e-120	0.9851632047477745

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.95e-63	24	530	4	541	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	4.48e-62	22	511	36	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].
259945	CuRO_2_Fet3p_like	2.32e-58	151	308	1	148	The second Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic 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 2 of 3-domain MCOs has lost the ability to bind copper.
177843	PLN02191	8.08e-56	26	531	28	565	L-ascorbate oxidase
259966	CuRO_3_Fet3p	4.05e-55	344	511	3	160	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic 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 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK42098.1|AA1_2	0.0	1	542	1	547
BCS11789.1|AA1_2	0.0	1	542	1	533
BCR99488.1|AA1_2	0.0	1	479	1	479
QQK43508.1|AA1_2	3.67e-218	9	527	8	513
QKX61289.1|AA1_2	1.02e-217	12	527	12	514

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.17e-109	25	527	6	500	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]
1AOZ_A	4.27e-51	19	533	1	544	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]
5EHF_A	3.59e-46	25	527	7	486	Laccase from Antrodiella faginea [Antrodiella faginea]
1HFU_A	3.99e-46	28	538	11	486	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	4.06e-46	28	538	11	486	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4WZB4|ABR1_ASPFU	1.09e-211	3	527	5	518	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	9.38e-139	10	527	8	511	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|K7NCS2|FETC_EPIFE	1.47e-133	6	527	7	514	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	1.14e-126	8	527	14	515	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|W3X7K0|PFMAD_PESFW	3.55e-118	19	527	20	507	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
0.000300	0.999663	CS pos: 19-20. Pr: 0.9658

TMHMM  Annotations     

There is no transmembrane helices in ASPBRDRAFT_654468-t33_1-p1.