CAZyme Information: FOC4_g10002624-t38_1-p1

Basic Information

• Species: Fusarium odoratissimum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium odoratissimum
• CAZyme ID: FOC4_g10002624-t38_1-p1
• CAZy Family: PL3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
258	KB726213|CGC1	28585.81	9.9129

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Fodoratissimumrace4	14596	N/A	137	14459

• Gene Location: location=KB726213:170471-171493(-)

Full Sequence      

MLRAGGRWLALAWWRKTLGREAATQMKQASRANDMGRRGGTAEGQLLPPYPPQPPPSAGK
QHLGKADFTFRLSAGSQRSKTEKYVPEYFLNEKPWQLYHGSMLPLLFHAPNETLVKPIIG
NLPLGSVVDLIIENQINETIPLYKHGDPSWFLGSRGQQRFPGNTVQDAIDSDSKSLNLQD
PALVIVHDLPALGWSVLRFKVTSQQATIIHAAKLRYFALGMSAPILEGITEDTPIKVPES
VVNRPHVEFKPAHDGIFG

Enzyme Prediction     

No EC number prediction in FOC4_g10002624-t38_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.44e-14	125	228	56	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.
177843	PLN02191	1.72e-08	62	239	398	556	L-ascorbate oxidase
259960	CuRO_3_AAO	1.62e-07	117	236	33	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.
215324	PLN02604	1.61e-06	119	241	440	558	oxidoreductase
259870	CuRO_3_LCC_like	3.29e-05	111	225	28	131	Cupredoxin domain 3 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 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. Also included in this family are cupredoxin domains 2, 4, and 6 of the 6-domain MCO ceruloplasmin and similar proteins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD61049.1|AA1	4.87e-155	41	258	422	639
QPC59569.1|AA1	2.80e-110	41	258	422	641
CEI62062.1|AA1	3.13e-109	41	258	422	641
QPC70978.1|AA1	2.48e-108	41	258	422	641
CEF78326.1|AA1	6.98e-108	41	258	422	641

PDB Hits     

FOC4_g10002624-t38_1-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A443HK79|VDTB1_BYSSP	8.53e-08	47	229	408	587	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000024	0.000001

TMHMM  Annotations     

There is no transmembrane helices in FOC4_g10002624-t38_1-p1.