CAZyme Information: FOC4_g10002625-t38_1-p1

Basic Information

• Species: Fusarium odoratissimum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium odoratissimum
• CAZyme ID: FOC4_g10002625-t38_1-p1
• CAZy Family: AA9
• CAZyme Description: Laccase-1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
560		62181.90	6.7798

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=KB726213:172721-174869(-)

Full Sequence      

MFTCNGQTPCPIIYADEGDIVKLSVKSDIYAQSSIHLTVGSWNDGTAGLSQFPTLPRSNW
TNAYDTSGSWGLNWFIDHTATASADGLAGALYVAPSPDRPRPYHLITNDTLELRQISQAE
REIQHLIIQSHQHRDTVWKLLRMRAEGSEYYCYDSILVNGKGRVHCRQPDYDHIKGQKLD
QKGCIQPPGLPDETCKQSLADYEVIETQGRRYMMLNLMNIGFEHSVKVSIDHHKMIVVAN
NAGFIVPEEADVLHIPSASRVTILVRLDAEPRDYAIRISSTSVLQNLHGYAVLRYPVLMY
PNMANLPQAKRLPRYGEPMALPSVAPGLVCVLPDGGTQPNCSTAEGQLLPPYPPQPPPSA
GKQHLGKADFTFRLSAGSQRSKTEKYVPEYFLNEKPWQLYHGSMLPLLFHAPNETLVKPI
IGNLPLGSVVDLIIENQINETIPLYKHGDPSWFLGSRGQQRFPGNTVQDAIDSDSKSLNL
QDPALVIVHDLPALGWSVLRFKVTSQQATIIHAAKLRYFALGMSAPILEGITEDTPIKVP
ESVVNRPHVEFKPAHDGIFG

Enzyme Prediction     

No EC number prediction in FOC4_g10002625-t38_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	2	523	1.3e-38	0.9636871508379888

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259944	CuRO_2_Abr2_like	5.85e-57	124	296	1	138	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.
177843	PLN02191	2.10e-19	1	541	44	556	L-ascorbate oxidase
274555	ascorbase	4.22e-17	3	544	24	536	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.
259951	CuRO_2_tcLCC_insect_like	1.20e-16	126	295	4	150	The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum. This multicopper oxidase (MCO) subfamily includes the majority of insect laccases. One member is laccase 2 from Tribolium castaneum, which is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. 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, plants and insects. 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.
215324	PLN02604	3.32e-16	3	543	47	558	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD61049.1|AA1	0.0	1	560	85	639
CEI62062.1|AA1	0.0	1	560	85	641
QPC59569.1|AA1	0.0	1	560	85	641
QPC70978.1|AA1	0.0	1	560	85	641
CZS81621.1|AA1	0.0	1	560	85	641

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6KLG_A	5.99e-09	5	523	28	524	Crystal Structure of the Zea Mays laccase 3 [Zea mays],6KLI_A Crystal Structure of the Zea Mays laccase 3 complexed with sinapyl [Zea mays],6KLJ_A Crystal Structure of the Zea Mays laccase 3 complexed with coniferyl [Zea mays]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	2.42e-71	1	553	43	584	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|I1RF62|GIP1_GIBZE	1.02e-43	1	531	45	590	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	7.43e-41	1	548	43	610	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	1.04e-40	5	533	65	606	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	1.13e-39	1	531	40	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
0.999955	0.000081

TMHMM  Annotations     

There is no transmembrane helices in FOC4_g10002625-t38_1-p1.