CAZyme Information: FOYG_05732-t42_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOYG_05732-t42_1-p1
• CAZy Family: GH1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
587	JH717842.1|CGC17	65241.12	6.1631

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumNRRL32931	17642	660029	362	17280

• Gene Location: location=JH717842.1:22754-24667(+)

Full Sequence      

MGSTSSLHPFHLGGLGGQLSQHQTNGLSLLGTFDSPVLPSFLTDNPTPNGYPWSTLNPST
NYYNDYPNTGVIRRYDFSISRGTIAPDGYELGVILVNGQFPGPTIEANWGDTIQVTVSND
IENEGLAIHWHGFQQKTTPWEDGVPGITQCPIPPGKKFTYQFVAELYGTTWYHSHYSAQY
SAGLFGPIVIYGPREKKNYDIDIGPILLNDWYHQEYFDLVEAVMKPGSPGFVFSDSNLIN
GKMNFNCSSVSPGDNTPCTSNAGVSKFHFKRGKTYRLRLINAGAEGLQRFSIDGHSMTVI
ANDFVPVEPYETKVVTLGIGQRSDILVKAKGDLDSYWMRSNISSKCSLSRAPDALAAIYY
DHADQNKEPESEPWDIPDPGTCANDDLSLTKPIMKLSLPYADLTMDLEVNSFKNESDVTL
WSLGNVSFRANYNSPTLLLSKLGNHSFEEQWNVRNTGNAKSVRINVINNTPVAHPMHLHG
FNMYVLHEGPGTWDGTIINRNNPERRDVVMIRGNGHLVVQFDAANNPGVWPFHCHIAWHV
SAGLLTQFLTNPDKVERLRIPNIVAETCRQWGRWTSTNIPAQIDSGL

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	60	377	6.1e-128	0.9839743589743589

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.42e-85	72	558	1	531	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.
215324	PLN02604	8.55e-79	72	558	24	554	oxidoreductase
177843	PLN02191	3.69e-77	69	571	20	567	L-ascorbate oxidase
259923	CuRO_1_MaLCC_like	1.02e-71	70	191	1	122	The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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. It 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. 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.
259968	CuRO_3_MaLCC_like	1.46e-65	396	549	1	157	The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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. It 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. 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 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
QKD46407.1|AA1_3	0.0	1	587	1	587
UPL01463.1|AA1_3	0.0	9	587	11	588
AGT80114.1|AA1_3	0.0	10	587	7	583
AHD26939.1|AA1_3	0.0	10	587	12	588
QKD53289.1|AA1_3	0.0	1	587	1	585

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.21e-115	53	587	49	580	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	2.41e-115	53	587	49	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	3.71e-112	52	578	3	532	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.82e-112	52	578	4	533	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	4.19e-112	52	578	31	560	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	2.36e-177	46	587	38	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q96WM9|LAC2_BOTFU	1.37e-120	53	587	49	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	2.20e-118	53	587	54	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	3.37e-105	56	587	40	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|Q4WQY8|TPCJ_ASPFU	2.54e-104	70	580	57	599	Oxidoreductase tpcJ OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=tpcJ PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000066	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FOYG_05732-t42_1-p1.