CAZyme Information: FOMG_13381-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOMG_13381-t38_1-p1
• CAZy Family: GH43|CBM91
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
475		53230.89	6.4261

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum26406	20033	1089452	372	19661

• Gene Location: location=JH659340.1:602513-604167(+)

Full Sequence      

MSATYSIQPRDNYTYRFTVQQQYGSYFYHGHFGPAFADGQRGPIWISPASWRPRPYKPIS
SSSSDIKGMQRAEANPRHIVISDWNAEPMDILLIMYRDTNIVPWCSNSIVLNGKGRTYCH
SKQDIEDSGGPGRNDLGCLLQDRQDIYANPQSCKATNGELEVIMAEEGEEWVWINFIHSG
AHHELQISIDEREFYVVAADGDILVHLNQKPGDYAIRLTSLRVEQVIQGLGILHYSSKVN
GSSGFVVPNTKPWVHLNGTLVSSSLTAMDETKLAPFPERPPPRTTDSTLRLFVNMTGPAA
WSLGLGSHQAFRQQLPPLLWEDESRGDTTFGGHGSLLNRSVVDIIFENGANVTTQHPFHK
HNHKAWIIGYGHGGFPWATIEEAIDEGAGKFFNFEDPPIRDGCRLGNATRDWTVIRYQIT
FPAASMLHCHMIHHFGAGQQLVLLEGVESMAKIPQEVKNKVHADFVPDLRYGPLD

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	5	438	2.1e-29	0.8044692737430168

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	4.09e-53	286	446	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.
259944	CuRO_2_Abr2_like	3.46e-38	77	235	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.
274555	ascorbase	2.08e-26	7	457	81	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.
177843	PLN02191	9.53e-24	6	456	102	557	L-ascorbate oxidase
259960	CuRO_3_AAO	6.89e-21	340	454	47	155	The third cupredoxin domain of plant Ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds 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 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	5	475	100	589
CEI62063.1|AA1	9.26e-298	5	475	102	591
QPC59570.1|AA1	2.09e-296	5	475	102	590
CEF78328.1|AA1	9.86e-295	5	475	102	590
CZS81623.1|AA1	2.31e-293	5	475	102	590

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	8.43e-20	6	454	82	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]
1A65_A	1.89e-10	7	445	87	468	Chain A, Laccase [Coprinopsis cinerea]
1HFU_A	1.89e-10	7	445	87	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
3T6V_A	4.82e-07	11	451	92	475	Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6V_B Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6V_C Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6W_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6W_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6W_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6X_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6X_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6X_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6Z_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T6Z_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T6Z_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T71_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum],3T71_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum],3T71_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum]
3KW7_A	4.54e-06	7	453	87	480	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	2.47e-265	5	475	99	592	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|A0A1S7IUL2|MCE_TALPI	6.85e-57	7	454	102	589	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	1.34e-55	7	455	119	612	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A2G5I8N8|CTB12_CERBT	5.98e-55	7	454	127	621	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	7.21e-55	3	466	94	584	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000045	0.000001

TMHMM  Annotations     

There is no transmembrane helices in FOMG_13381-t38_1-p1.