CAZyme Information: FPRO_07604-t41_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRO_07604-t41_1-p1
• CAZy Family: GH139
• CAZyme Description: related to laccase precursor

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
607	FJOF01000007|CGC3	67397.57	5.7882

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FproliferatumET1	16509	1227346	366	16143

• Gene Location: location=FJOF01000007:1759121-1761035(-)

Full Sequence      

MYFTRSSLIFLPLVLQSFIISVTATYWNNTKKFDLTITWENYAPDGFSRKMLLVNGQSPG
PVLEINQDDLVVVKVHNQSPEELTIHYHGLEMKGTPWTDGVPGVTQHPIKPGCSFTYKFH
ATQYGSFWYHSHHRGQIEDGLYGAIIIHPRPHEPNPFHLISDDKETLYEIQKATRHVKPV
VISDFVHLTSTEKWDMTVAAGIEDSCYDSILFNGKGRVECLPKDLVAANLNEIQKSYLEL
VPGGAEFTDKSCLPASALNALAGGLGNEEALLPGTFSGCKETEGQIEVIKVSNKHHASSK
WVAFDIVAAVNFVNGVFSIDGHDIWVYAMDGSYIQPQKVQAIAATNGDRYSVLVKVEKSG
DFKMRFNSNSAPQIITGHAILSVDGFGYTQEAEPWINLVGIPVSKNVVVFNQMVAFPYPP
VPISPTADVTFNLSMEIKGASYLWALNSTGLMSKDLDEQRPTLFNPQPYVHNNVTISTKL
GQWVDLVFVAAMFPQPPHPIHKHGSKMYMLGTGTGLFRWSSVEEAAKEIPDQFNFVNPPR
RDAFLSAPADKEPSWVVVRYHAADPGPWLLHCHINNHMVGGMMMVIQDGVDAWPEVPEEY
AEGGDGE

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	41	582	3.4e-80	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.23e-77	428	589	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.
259919	CuRO_1_Abr2_like	1.07e-56	33	148	1	117	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.
215324	PLN02604	1.42e-53	30	597	24	555	oxidoreductase
274555	ascorbase	6.53e-52	30	599	1	534	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.
259944	CuRO_2_Abr2_like	1.73e-51	178	383	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGI95094.1|AA1	0.0	1	607	1	607
QGI81474.1|AA1	0.0	1	607	1	607
QGI64209.1|AA1	0.0	1	607	1	607
CCT68280.1|AA1	0.0	1	607	1	607
QKD54095.1|AA1	0.0	1	607	1	607

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3PXL_A	2.90e-42	34	602	7	486	Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta]
3FPX_A	5.46e-42	34	602	7	486	Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta]
5LDU_A	7.48e-42	34	602	7	486	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
3DIV_A	7.48e-42	34	602	7	486	Crystal structure of laccase from Cerrena maxima at 1.76A resolution [Cerrena]
3V9E_A	3.22e-41	22	584	66	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1S7IUL2|MCE_TALPI	3.92e-138	30	601	25	593	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|E9RBR0|ABR2_ASPFU	3.29e-129	19	596	8	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|E9E686|MLAC1_METAQ	1.38e-125	27	600	19	610	Laccase 1 OS=Metarhizium acridum (strain CQMa 102) OX=655827 GN=Mlac1 PE=3 SV=2
sp|A0A0B4HQH6|MLAC1_METMF	2.46e-123	27	600	20	611	Laccase 1 OS=Metarhizium majus (strain ARSEF 297) OX=1276143 GN=Mlac1 PE=3 SV=1
sp|A0A0B4F1I0|MLAC1_METAF	6.51e-123	27	600	19	610	Laccase 1 OS=Metarhizium anisopliae (strain ARSEF 549) OX=1276135 GN=Mlac1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000210	0.999781	CS pos: 24-25. Pr: 0.9759

TMHMM  Annotations     

Start	End
7	29