CAZyme Information: FOYG_17133-t42_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOYG_17133-t42_1-p1
• CAZy Family: GT64
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
686	JH717856.1|CGC1	75058.94	5.2952

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumNRRL32931	17642	660029	362	17280

• Gene Location: location=JH717856.1:124566-127156(-)

Full Sequence      

MHVHAQMLATSVVVLLHAVSTRAALRQFNFTVHSASNSPDGFEREVYLVNGQQPGPLIDV
DEGDDVEIFVQNDLNVETTIHWHGLLQRGTPQMDGVPGVTQDPIPPGGNFTYRFSTESEY
GFFWYHSHLRAYYNDAIRGPLLIRPAASRQRPFASLARNRGDAAALREAERDATNILLND
WTHELSDVVFARYLKTGAFPSCVDSILANGHGRVQCLPKSVLEAGPGLGIEPTNLTAVPT
RPTTTSKMSDMSSMPGMDMVKRSDVHDMTMETAMSSATSGPSSTMPMHRSTSSISSKMPD
MPGMNSLSPRGCMPPMMFKPGFNMSSLPPETCKNTTSPLLTIPADQSRGWLALNLVNSGA
VSALRVSLDAHSMFVYAADGLFIELEEVNVLHMELGQRYSVMIRLDQEPGNYYLRFATFP
SGDMQQVLEGQAIVSYNSTDKSTTDVMEDPAMTWTYVNGSAKANSSVLDPRALSPFEDDI
SPPAGPADRTLSFSISQTDITTWVINRFPFTEPKVPIVYGEDSDGWGSNTTIHLPLNSTI
DIILRISNQSMDVMGHPMHLHGHKFWVLGSGAGSFPFESVTDAPKSLINLQDPPYRDTTG
LPSEGWTALRYVTDNPGAWIFHCHLQWHVVVGMAMVLVEGGDQLPALVGQYNGTADRSRA
PTLIGGNDCRPAVIAAIAVGFIMLWY

Enzyme Prediction     

No EC number prediction in FOYG_17133-t42_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	42	269	4.2e-52	0.5502793296089385
AA1	342	634	6.9e-39	0.5167597765363129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.89e-71	26	640	2	524	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	3.27e-66	8	644	8	551	L-ascorbate oxidase
215324	PLN02604	4.19e-64	12	647	11	554	oxidoreductase
259919	CuRO_1_Abr2_like	4.07e-63	28	144	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	2.93e-52	26	143	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	7	610	1	601
QPG98040.1|AA1	4.87e-309	16	685	16	682
ATY66532.1|AA1	5.05e-309	17	680	11	663
UNI13709.1|AA1	7.08e-289	15	685	15	669
QLI72976.1|AA1	1.14e-284	11	649	16	656

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3KW7_A	6.78e-47	29	639	7	472	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]
1AOZ_A	1.59e-46	25	644	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]
3V9E_A	3.34e-46	19	639	61	542	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
4JHU_A	5.53e-46	29	639	7	466	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
3SQR_A	8.51e-46	19	639	61	542	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	3.83e-102	15	663	12	586	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|Q0UHZ8|ELCG_PHANO	1.17e-84	19	651	35	614	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	8.21e-81	31	651	29	592	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|E9RBR0|ABR2_ASPFU	1.52e-80	18	645	12	577	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A2G5I8N8|CTB12_CERBT	3.72e-76	27	653	51	629	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000496	0.999447	CS pos: 23-24. Pr: 0.9689

TMHMM  Annotations     

There is no transmembrane helices in FOYG_17133-t42_1-p1.