CAZyme Information: FOXG_22266-t26_2-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOXG_22266-t26_2-p1
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
680		74193.05	5.3755

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum4287	21354	426428	429	20925

• Gene Location: location=CM000590.1:5260188-5262724(+)

Full Sequence      

MLVSSLVVALYAVGARAALRQFNFTVHSAFKSPDGFEREVYLINGQQPGPLVDVDEGDDV
KIFVQNDLNVETTIHWHGLLQRGTPHMDGVPGVTQDPIPPGGNYTYRFSTASEYGFFWYH
SHFRAYYNDAIRGPLLIRPAASRQRPFATLAQDQDELAALLAAERNATNVLLNDWTHELS
DVVFARYMKTGAFPSCVDSILANGQGKVQCLPKSALESGPGLRIEPKKTTTALGTSATTS
EMQHMSDMPSMDMLKGRDMHNMPMESPVSPVTSRPSATMSMDHSPSPASSGMPDMPGMDS
LSPRGCMPPMMFKPGFNISSLPPETCTNTTSHLLVISTDQSRGWLALNLVNSGAVSALRV
SLDGHSMFVYAADGLYTKLQEVNVLHMELGQRYSVMVKLDQSPGNYYLRFTTFPSGDMQQ
VLEGQAIVSYNADNSSTTDVMEDPAKSWMYINGSAKADAALLDPSALSPFDGHNSPPSGR
PDKALSFVVSQTDIVTWVIDRAPFSEPDVPIIYGENSSGWNSNTTMHLPINSTIDIIMSI
SNQSMDMMGHPIHLHGHKFWVLGSGEGSFPYAAVTDAPADLINLRDPPYRDTMGLPSQGW
AAIRYVTDNPGAWMFHCHLQWHIVVGMAMVLVEGGDQLPALVGQYNKTADRSGATELIAS
RYGPSATLVAIVVVAITLWY

Enzyme Prediction     

No EC number prediction in FOXG_22266-t26_2-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	36	229	5.9e-51	0.48324022346368717
AA1	335	628	1.9e-42	0.5195530726256983

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.68e-66	20	655	2	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.
177843	PLN02191	1.98e-65	6	638	10	551	L-ascorbate oxidase
215324	PLN02604	2.58e-62	2	641	7	554	oxidoreductase
259919	CuRO_1_Abr2_like	2.13e-60	22	138	1	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase 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.
259926	CuRO_1_Diphenol_Ox	2.11e-52	20	137	1	118	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats 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
UPL00042.1|AA1	0.0	1	604	1	601
ATY66532.1|AA1	3.38e-315	1	672	1	661
QPG98040.1|AA1	1.32e-314	6	663	12	665
UNI13709.1|AA1	8.32e-279	12	639	18	631
QLI72976.1|AA1	3.51e-277	17	643	29	656

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3X1B_A	4.72e-47	23	640	28	498	Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus],3X1B_B Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus]
1AOZ_A	2.03e-46	19	638	3	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]
5EHF_A	6.53e-45	12	633	1	467	Laccase from Antrodiella faginea [Antrodiella faginea]
1HFU_A	1.36e-44	23	633	8	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.38e-44	23	633	8	468	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	3.95e-104	19	664	22	590	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	3.36e-82	15	639	15	577	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	2.01e-79	23	649	27	596	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	6.55e-77	32	647	32	599	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	2.51e-76	38	645	59	614	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000444	0.999524	CS pos: 17-18. Pr: 0.9615

TMHMM  Annotations     

There is no transmembrane helices in FOXG_22266-t26_2-p1.