CAZyme Information: ASPTUDRAFT_168536-t33_1-p1

Basic Information

• Species: Aspergillus tubingensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tubingensis
• CAZyme ID: ASPTUDRAFT_168536-t33_1-p1
• CAZy Family: GH12
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
621	KV878198|CGC11	69405.20	6.7897

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtubingensisCBS134.48	12592	767770	274	12318

• Gene Location: location=KV878198:1435762-1437938(+)

Full Sequence      

MKEQGSILLDSQQSPSLRLRRLPWGIVLYPATICGLILLLFVAQISQPSPLQRLIPSRDS
NSQIHPTVHGPDVSRPFIELHPGDHVYRNPSTQHHDWVVTADHRRPDGVLKRVYAINDLF
PGPTVEARSGDRLIVKVTNHLEEEPISIHWHGVHIENAMDGAVGVTQRPIPPGSTFTYNF
TIPADQSGTFWYHAHSGLLRADGLYGGLIVHEPSPKPTVRGLLARADQQELGSYDKDILL
LVGDWYHRSADQVYSWYMRAGSFGNEPVPDSLLINGVGHFDCSMAVPARPVDCILRHMNV
SYLDAKGDATYRVRVVNTGSVAGFRLGFQNRGFTLIQVDSIDVEQQDSSSAGILYPGQRM
DIILRPSPDETSSSLTIDLDKECFRYPNPALASVQTFDIKNSPNNRSPTISPSNISTSLS
EVATRKSLLSGLPANAHQTYVVYTKIEKLSINHNVPYGFFNRTSWRPHIDTPLIDLPREE
WDENQLVLSTGSTTSRPLSSEQDRDVWIDLVVNNLDDSGHPFHMHGHHFYILRTYQAPVG
WGAYNPFTDAHPPGLAPRPGSSSKTDSPYDLSRAQLRDTVYIPSRGHAVLRFRADNPGIW
LFHCHIIWHQASGMAMLLQIE

Enzyme Prediction     

No EC number prediction in ASPTUDRAFT_168536-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	109	615	2.3e-91	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	9.39e-69	92	614	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.
215324	PLN02604	1.69e-61	92	619	24	545	oxidoreductase
177843	PLN02191	1.79e-60	97	618	28	544	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	2.47e-60	440	620	1	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	8.90e-57	97	615	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	12	620	2	586
BCS06095.1|AA1	0.0	159	621	1	460
BCR93452.1|AA1	0.0	159	621	1	460
QMW37919.1|AA1	2.84e-269	11	620	8	598
QRD88142.1|AA1	1.05e-268	11	620	25	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	4.81e-54	106	616	81	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.26e-53	106	616	81	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]
1ZPU_A	3.48e-51	96	618	6	477	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	5.40e-48	93	617	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]
5LWX_A	1.89e-46	45	615	10	527	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RMG9|FET3_GIBZE	1.84e-60	91	614	23	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	5.17e-60	92	616	73	547	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|K7NCS2|FETC_EPIFE	2.40e-58	91	615	21	490	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|J9VY90|LAC1_CRYNH	4.75e-58	90	621	59	561	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|Q6CII3|FET3_KLULA	2.69e-57	91	618	26	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000018	0.000007

TMHMM  Annotations     

Start	End
21	43