CAZyme Information: ACLA_062550-t26_1-p1

Basic Information

• Species: Aspergillus clavatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus
• CAZyme ID: ACLA_062550-t26_1-p1
• CAZy Family: GH47
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
549	DS027050|CGC1	61480.58	5.3262

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AclavatusNRRL1	9428	344612	287	9141

• Gene Location: location=DS027050:596931-598822(+)

Full Sequence      

MFRLCHLLLLFLLRTVLCATLTYDFNITWVRSNPDGAYERPTIGINGQWPLPAITAHVGD
RIVVNVWNQLGNQSTSLHFHGLFMKGSPHMDGPEQVTQCAIPPGSQFVYNFTVEQPGTYW
YHSHTQSQYPDGLRGPLIIHDDASPFHDQYDEELTLTISDWYHDPMADLLPGYMKKGSRM
AREPFPNANLLNDSQHVRIDVQPGKTYLIHLINMGAFMGQYFWIEGHEMTIVEVDGVYTR
PTVAENVYLATGQRYAVLLTTKEGRDANYPMVASMDPLSILGHGKTMRSVTGWLVYDSNS
PMPPPERVDWYEAIDDMSLVPYDSAPLLLEPSHQITLDMNMHRLQDGVMHWLLNDISYAA
PKRPTLYTAMTSGEAALEDVSTYERSTNPFILDEGAVVEIIVNNKHMGRHPFHLHGHSFQ
AVYRSNHWAGSFAESNVTEADFLAVPLRRDTLTVNPGGSMVIRFRADNPGVWIFHCHMEW
HAHSGLIATMIEAPLALQSLGIPTDHIDACAAGGISLNGTMPIQPVADADAHSEEDKPAE
VTPMDGPKE

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	374	3.8e-134	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.47e-85	23	486	4	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.
225043	SufI	2.89e-79	25	494	40	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].
177843	PLN02191	4.73e-72	19	492	22	546	L-ascorbate oxidase
215324	PLN02604	5.44e-70	23	486	27	540	oxidoreductase
259966	CuRO_3_Fet3p	7.55e-68	333	494	2	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
AHZ65140.1|AA1_2	1.74e-221	17	519	6	506
AEO71107.1|AA1_2	6.41e-221	19	519	33	535
QOX58957.1|AA1_2	1.02e-219	12	539	17	543
UPL01783.1|AA1_2	1.68e-219	17	519	17	517
CCT72117.1|AA1_2	3.90e-219	12	519	8	512

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	4.06e-145	20	519	2	509	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	4.48e-69	39	514	21	540	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]
3KW7_A	5.36e-69	24	510	7	491	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
2QT6_A	1.33e-68	24	510	7	487	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
1V10_A	1.64e-68	17	492	20	489	Chain A, Laccase [Rigidoporus microporus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	3.92e-211	13	519	15	523	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	2.75e-206	19	543	23	547	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|E9R598|FETC_ASPFU	9.62e-192	15	514	17	515	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|P78591|FET3_CANAX	8.50e-150	11	519	14	526	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|P38993|FET3_YEAST	5.01e-143	20	519	23	530	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000212	0.999765	CS pos: 18-19. Pr: 0.9828

TMHMM  Annotations     

There is no transmembrane helices in ACLA_062550-t26_1-p1.