CAZyme Information: FOC1_g10008885-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOC1_g10008885-t38_1-p1
• CAZy Family: PL4
• CAZyme Description: Laccase-1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
458	KB730083|CGC2	50820.22	7.0890

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporumrace1	15626	1229664	188	15438

• Gene Location: location=KB730083:315005-316672(+)

Full Sequence      

MTDISRKGLAGALYVAPSPDRPRPYHLITNDTLELRQISQAEREIQHLIIQSHQHRDTVW
KLLRMRAEGSEYYCYDSILVNGKGRVQCRQPEYDHIKGQKLDQKGCIQPPGLPDETCKQS
LADYEVIETQGRRYMMLNLMNIGFEHSVKVSIDHHKTIVVANNAGFIVPEEADVLHIPSA
SRVTILVRLDAEPARSGVPNMANLPQAKRLPRYGEPMALPSVAPGLVCVLPDGGTQPNCS
TAEGQLLPPYPPQPPPSAGKQHLGKADLTFRLSAGSQPSKTEKYVPEYFLNEKPWQLYHG
SMLPLLFHAPNETLVKPIIGNLPLGSVVDLIIENQINETIPFYKHGDPSWFLGSRGQQRF
PGNTVQDAIDSDSKSLNLQDPALVIVHDLPALGWSVLRFKVTSQQATIIHAAKLRYFALG
MSAPILEGITEDTPIKVPESVVNRPHVEFKPAHDGIFG

Enzyme Prediction     

No EC number prediction in FOC1_g10008885-t38_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259944	CuRO_2_Abr2_like	2.43e-40	46	194	1	114	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.
259965	CuRO_3_Abr2_like	1.48e-14	267	428	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.
177843	PLN02191	1.07e-12	77	439	189	556	L-ascorbate oxidase
259951	CuRO_2_tcLCC_insect_like	2.10e-09	48	193	4	124	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.
259960	CuRO_3_AAO	2.45e-08	317	436	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD61049.1|AA1	2.12e-315	2	458	171	639
QPC59569.1|AA1	2.46e-246	2	458	171	641
QPC70978.1|AA1	8.13e-245	2	458	171	641
CEI62062.1|AA1	3.29e-244	2	458	171	641
CZS81621.1|AA1	1.89e-243	2	458	171	641

PDB Hits     

FOC1_g10008885-t38_1-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	7.76e-45	8	451	133	584	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|Q0UHZ8|ELCG_PHANO	4.99e-25	8	431	150	606	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	4.18e-24	8	446	132	610	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	1.41e-23	8	429	140	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|A0A2G5I8N8|CTB12_CERBT	1.35e-22	8	429	158	614	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000049	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FOC1_g10008885-t38_1-p1.