CAZyme Information: KAF6524966.1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: KAF6524966.1
• CAZy Family: GH51
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
862	CM024363|CGC10	95576.13	4.8109

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumFo5176	17912	660025	0	17912

• Gene Location: location=CM024363:930575-934625(+)

Full Sequence      

MVAYDEEADALLEEFELREEVKVRDDRTPPSVYEFPGPLIEARSGDRLVIHVHNGVQDEG
VSLHWHGLRMKDKNSVDGAVGFTQCPIAPGRSFTYNFTIGAEEHGTFWWHSHSDVQRADG
LWGGLIVHSPDEIDLQREEYLLMVGDWFHQNQTEVLRWYADASSRGNEPVPDSLLVNGQG
RFNCSMAVPARPVACSQVQFSNLKPLMMSRSQKKARLRVVNTGSVAGLSLRAGGAIIRPV
RVDGGFAVKAEATETVGILYPGERVDLEAEWKGNHAGDHRLTVYLDDENFGYPNPALNPT
QSFPMFSSSTKGSSNEPVPQPLEQDEIQVLDSQNLKTATKVSDLPAKAEQTILLYAKVEK
LAHMDYAPVGFINHTSWTAQTPPLLAQNRTSWDENQLIPFIGISGSKPKRVDIVINNLDD
GAHPFHLHGHSFYVLSSYRNPGRGSWGSYNPYTDEAPPNGLNLEFPVRRDTWKQAMSETP
EPTRQASAAPEAPATTEASPAPATTESAASPPAATSGPILDPQHWAQVNEEQAQAEAEGA
GDDNADADSTLDPDNASSTASITSSILEYRTIHGRTYHSEQGNAQYWASNDEQQNDLMDL
THHILTLGLGDKLHLAPLKEEKLHQAIDIGTGTGIWAIDFADQYPGAEIIGTDLSPIQPS
WVPPNVQFEIEDCTREWTFKSDFADYIHVRWLMGSVRDWDAFFSEAYRVCKPGAWIESHE
ASCNVSSDDGTVAPNSAMGHWGEFFKEGGKKIGTSFSVVEDGTQRKAMEKAGFINIQEFD
FRNPVGTWPKDPVEKRMGAYSKYGLETDSEGFILFMAHTLGWTREEILVYIAQFRREIRS
GKHHGYFAQKVVWGQKPETTAA

Enzyme Prediction     

No EC number prediction in KAF6524966.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	34	440	1.3e-65	0.8212290502793296

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
177843	PLN02191	2.82e-50	34	471	50	505	L-ascorbate oxidase
274555	ascorbase	3.40e-49	34	471	28	482	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.
259869	CuRO_1_LCC_like	2.45e-44	35	128	28	120	Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.
259926	CuRO_1_Diphenol_Ox	2.07e-43	34	128	27	119	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.
259927	CuRO_1_tcLCC2_insect_like	1.02e-39	34	128	13	105	The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum. This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. 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, plants and insects. 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
QKD61545.1|AA1	0.0	1	471	1	555
AVI02163.1|AA1	0.0	1	471	1	555
QPC80252.1|AA1	2.40e-238	34	471	126	559
QPC62885.1|AA1	5.70e-237	34	471	126	559
CZS85875.1|AA1	1.97e-230	26	471	114	552

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	2.69e-36	34	471	30	482	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]
3SQR_A	2.88e-35	36	470	96	500	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]
3V9E_A	2.88e-35	36	470	96	500	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
1ZPU_A	3.48e-32	34	471	30	438	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]
5LM8_A	1.37e-28	34	471	50	456	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|S0EG57|ME178_GIBF5	5.48e-123	548	858	42	351	Methyltransferase FFUJ_09178 OS=Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) OX=1279085 GN=FFUJ_09178 PE=2 SV=1
sp|P9WEZ3|PYTC_ASPTE	1.86e-58	554	857	23	323	Methyltransferase pytC OS=Aspergillus terreus OX=33178 GN=pytC PE=2 SV=1
sp|Q0CZH2|PYTC_ASPTN	9.25e-58	554	857	23	323	Methyltransferase pytC OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pytC PE=2 SV=2
sp|I1RMG9|FET3_GIBZE	4.79e-46	34	471	52	455	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|K7NCS2|FETC_EPIFE	8.75e-46	34	471	50	454	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000043	0.000000

TMHMM  Annotations     

There is no transmembrane helices in KAF6524966.1.