CAZyme Information: FOIG_16769-t36_2-p1

Basic Information

• Species: Fusarium odoratissimum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium odoratissimum
• CAZyme ID: FOIG_16769-t36_2-p1
• CAZy Family: GT62
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
594		64607.12	5.1291

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FodoratissimumNRRL54006	16975	1089451	341	16634

• Gene Location: location=KK036195.1:1972-4117(-)

Full Sequence      

MDGVPGVTQDPIPPGGNYTYRFSTASEYGFFWYHSHFRAYYNDAIRGPLLIRPAASRQRP
FATLAQDQDELAALLAAERNATNVLLNDWTHELSDVVFARYMKTGAFPSCVDSILANGQG
RVQCLPKSALESGPGLGIEPKKTTTALGTSATTSEMQHMSDMPSMDMLKGRDMHDMPMES
PVSPVTSRPSATMSMDHSTSPASSGMPDMPGMDSLNPRGCMPPMMFKPGFNISSLPPETC
TNTTSHLLVISTDQSRGWLALNLVNSGAVSALRVSLDGHSMFVYAADGLYTKLQEVNVLH
MELGQRYSVMVKLDQSPGNYYLRFTTFPSGDMQQVLEGQAIVSYNADNSSTTDVIEDPAK
SWMYINGSAKADAALLDPSALSPFDGHNSPPSGRPDKALSFVVSQTDIVTWVIDRAPFSE
PDVPIIYGENSSGWNSNTTMHLPINSTIDIIMSISNQSMDMMGHPIHLHGHKFWVLGSGE
GSFPYAAVTDAPADLINLRDPPYRDTMGLPSQGWAAIRYVTDNPGAWMFHCHLQWHIVVG
MAMVLVEGGDQLPALVGQYNKTADRSGATELIASRYGPSATLVAIVVVAITLWY

Enzyme Prediction     

No EC number prediction in FOIG_16769-t36_2-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	249	542	1.4e-42	0.5195530726256983

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.93e-41	2	569	71	541	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	3.05e-41	2	552	93	551	L-ascorbate oxidase
215324	PLN02604	1.85e-39	2	555	94	554	oxidoreductase
259977	CuRO_3_MCO_like_4	1.55e-38	428	547	49	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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.
259870	CuRO_3_LCC_like	2.29e-38	396	546	5	132	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
UPL00042.1|AA1	2.42e-296	1	518	87	601
ATY66532.1|AA1	1.36e-265	1	586	104	661
QPG98040.1|AA1	1.07e-264	1	577	93	665
QLI72976.1|AA1	4.70e-235	1	557	99	656
UNI13709.1|AA1	1.49e-229	1	553	93	631

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F5K_A	2.67e-30	230	579	200	549	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
3X1B_A	5.11e-29	2	554	98	498	Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus],3X1B_B Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus]
5EHF_A	7.43e-29	2	547	77	467	Laccase from Antrodiella faginea [Antrodiella faginea]
1HFU_A	2.58e-28	2	547	77	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.61e-28	2	547	77	468	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	7.21e-73	2	578	91	590	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	2.06e-61	2	553	88	577	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	7.95e-61	2	559	109	614	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	2.31e-56	2	561	117	626	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1
sp|A0A443HK79|VDTB1_BYSSP	2.42e-55	2	561	88	599	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
1.000038	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FOIG_16769-t36_2-p1.