CAZyme Information: FOZG_16634-t36_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOZG_16634-t36_1-p1
• CAZy Family: GT22
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
589		65874.09	6.0835

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumFo47	18556	660027	365	18191

• Gene Location: location=JH717911.1:354440-356369(-)

Full Sequence      

MTTPRILSFVFLLLLFSCFANCLRRYNFTVTSQWSAADGHGRPVFAINGQTPGPLVTAEE
GEEIEVFVDNQLATETTMHWHGVYQVDRPWNDGVPGVTQYSIQPRDNYTYRFTVQQQYGS
YFYHGHFGPAFADGQRGPIWISPASWRPRPYKSISSSSSDIKGMQRAEANPRHIVISDWN
AEPMDILLIMYRDTNIVPWCSNSIVLNGKGRTYCHSKQDIEDSGGPGRNDLGCLLQDRQD
IYANPQSCKATNGELEVIMAEEGEEWVWINFIHSGAHHELQISIDEHEFYVVAADGEFVH
PQKVHAANCNLGERISILVHLNQKPGDYAIRLTSLRVEQVIQGLGILRYASKAKDQSGFV
VPNTEPWVHLNGTLVSSSLTAMDETKLAPFPERPPPRTADSTLKLFVNMTGPAAWSLGLG
SHQAFRQQLPPLLWEDESRGDTTFGSHGSLLNGSVVDIIFENGANVTTQHPFHKHNHKAW
IIGYGHGGFPWATIEEAIDEGAGKFFNFEDPPIRDGCRLGNATGDWTVIRYQITFPAASM
LHCHMIHHFGAGQQLVLLEGVESMAKIPQEVKNKVHADFVPDLRYGPLD

Enzyme Prediction     

No EC number prediction in FOZG_16634-t36_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	552	2.4e-73	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.05e-61	24	571	2	535	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.
259919	CuRO_1_Abr2_like	3.05e-57	26	141	1	116	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.
259944	CuRO_2_Abr2_like	1.31e-54	172	349	1	137	The second 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 2 of 3-domain MCOs has lost the ability to bind copper.
177843	PLN02191	6.79e-54	23	570	23	557	L-ascorbate oxidase
259965	CuRO_3_Abr2_like	1.32e-53	400	560	1	164	The third 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 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD61048.1|AA1	0.0	1	589	1	589
QPC59570.1|AA1	0.0	8	589	10	590
CEF78328.1|AA1	0.0	1	589	1	590
CEI62063.1|AA1	0.0	1	589	1	591
CZS81623.1|AA1	0.0	8	589	10	590

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	9.33e-45	23	568	3	532	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	1.00e-33	38	565	18	473	Laccase from Antrodiella faginea [Antrodiella faginea]
1HFU_A	3.66e-33	29	559	10	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	3.70e-33	29	559	10	468	Chain A, Laccase [Coprinopsis cinerea]
2HZH_A	8.69e-33	27	565	7	475	Crystal structure of laccase from Coriolus zonatus at 2.6 A resolution [Trametes ochracea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	0.0	12	589	11	592	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	1.34e-88	26	580	22	584	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	1.43e-88	29	568	29	589	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A2G5I8N8|CTB12_CERBT	3.39e-87	25	568	49	621	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1
sp|I1RF62|GIP1_GIBZE	3.36e-86	1	570	2	599	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.001009	0.998983	CS pos: 22-23. Pr: 0.4401

TMHMM  Annotations     

There is no transmembrane helices in FOZG_16634-t36_1-p1.