CAZyme Information: ATEG_03000-t26_1-p1

Basic Information

• Species: Aspergillus terreus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus terreus
• CAZyme ID: ATEG_03000-t26_1-p1
• CAZy Family: GH12
• CAZyme Description: predicted protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
621		68532.54	6.5773

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AterreusNIH2624	10551	341663	150	10401

• Gene Location: location=CH476597:585814-588011(+)

Full Sequence      

MKRECCSKGRGIYLPIVSVVLWILLWSWYTAPTGLPSIAVPGEKTHLTDHQLSESPHVES
PDALRPQIRLHPESYMYRESVTQYKHWTVTAEDLRPDGVLKRVYLINGIFPGPTVEARSG
DVVVINVTNHLLDDSFTVHWHGLHIENSMDGVASVTQNAIPPGSSFTYRIVIPSDQSGTF
WYHAHAGLARADGLYGGFVVHPAAAKSTAHGLTSRRGSIDPKSEKDVLLLVGDWYHRSGP
EVMAWYMRAGSFGNEPVPDSLLINGLGQFNCSMAVPARPVDCIHHPMNLSQILPTDGVYK
LRVVNTGSLAGLTLTFNNHNVTVLAVDSMPVEARNGQSVGVLYPGQRMDLHIQQTSEDTP
SLLEAHLDEECFRYPNPALTSTQTFFISSSVHTPDGSPSPDMGSAPGSEPVSIDIHDLPS
AGHILSQLPQTATVNTTEVVYTKIQKLSIRHNVPYGFFNRTSWVAQADPPIPLIDLQREK
WDRNQLSIAVSGPSSNAGAESEAMWVDLVVNNLDDGGHPFHLHGHHFYILAVHKAAIGWG
SYNPFTDDAPPGLDKVKHPYTNGYDLSRAMFRDTVYIPSRAYAVLRFRADNPGIWMFHCH
ILWHLANGMAMLVDVRPTLTS

Enzyme Prediction     

No EC number prediction in ATEG_03000-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	99	610	1.9e-86	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.49e-64	86	609	5	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	3.18e-60	71	612	17	543	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	1.89e-56	439	615	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.
215324	PLN02604	1.21e-55	81	609	24	540	oxidoreductase
225043	SufI	4.18e-54	97	617	48	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW37919.1|AA1	4.44e-244	12	615	25	598
QRD88142.1|AA1	8.10e-244	12	615	42	615
QMW25836.1|AA1	8.10e-244	12	615	42	615
CAK44017.1|AA1	8.80e-215	12	615	18	586
UPX44859.1|AA1	4.05e-212	4	619	12	631

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.83e-51	86	617	6	481	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	7.69e-51	85	611	69	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.00e-50	85	611	69	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	7.83e-45	81	612	3	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	2.63e-44	97	618	38	507	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	5.35e-58	79	617	24	507	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|J9VY90|LAC1_CRYNH	8.71e-57	89	617	68	562	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|I1RMG9|FET3_GIBZE	7.66e-55	96	609	38	490	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|J5JH35|OPS5_BEAB2	8.50e-55	85	617	75	553	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q55P57|LAC1_CRYNB	2.08e-54	96	618	75	563	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999969	0.000049

TMHMM  Annotations     

Start	End
12	31