CAZyme Information: FOC1_g10003249-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOC1_g10003249-t38_1-p1
• CAZy Family: CE1
• CAZyme Description: Laccase-2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
423		47700.48	6.2755

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=KB730011:225813-228008(-)

Full Sequence      

MWITDACKAVVLSFVAVFHYPSVSDEGPHQDVMTFTHGHSTPEIDYPYFDSPSGPDQDGK
VFTCNYTDLKGWKPCTTADDRSCWLKGPYGQNFTINTDYENFWPIGITREYHLNVTDQSI
NGDGVDNPFGKVFNGKYPGPWIQACWGDLIKVTVHNHLKYNGTTIHWHGLRQLETFEMDG
VNGVTQCPIAPGDSYTYTFRAVQYGTSWYHSHYSLQYADGLAGPITIYGPSSAPFDEGRN
PILITDWSHRSAFQSWQRELVPNPTRPMMNGVLINGMTVTKVGYLTAAADKTVLTINLHL
HGHDFALLAQGTNFSDLDTGKVNLKFNNPPRRDVALLPAGGYLVVAFKADNPGSWLFHCH
IAWHASSGLAIQILEQQTLLNRILDQYPEKMKEVNRVCDNWNKWFKNDTNLWNAHIFQDD
SGI

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	97	283	4.6e-83	0.592948717948718

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	2.13e-69	106	228	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.
400195	Cu-oxidase_3	5.74e-50	114	232	1	119	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259926	CuRO_1_Diphenol_Ox	9.46e-46	109	228	1	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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. 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	1.02e-44	298	374	83	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.
259927	CuRO_1_tcLCC2_insect_like	3.00e-44	132	227	9	104	The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum. This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 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. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD61993.1|AA1_3	5.92e-287	1	423	1	658
AVI02164.1|AA1_3	5.92e-287	1	423	1	658
QGI68425.1|AA1_3	4.36e-282	1	423	1	658
QGI99317.1|AA1_3	4.36e-282	1	423	1	658
CCT72796.1|AA1_3	4.36e-282	1	423	1	658

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	6.95e-72	77	423	42	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	1.36e-71	77	423	42	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	7.25e-56	91	406	5	530	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	7.39e-56	91	406	6	531	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	1.20e-55	91	406	33	558	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|D4APX3|LAC1_ARTBC	1.69e-89	40	423	27	633	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	1.41e-70	77	423	42	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q03966|LAC1_CRYPA	1.28e-62	75	423	36	591	Laccase OS=Cryphonectria parasitica OX=5116 GN=LAC-1 PE=3 SV=1
sp|Q12570|LAC1_BOTFU	3.11e-58	77	423	40	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|A0A067XMP0|PTAE_PESFW	7.53e-58	77	309	29	282	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.085212	0.914760	CS pos: 25-26. Pr: 0.7525

TMHMM  Annotations     

There is no transmembrane helices in FOC1_g10003249-t38_1-p1.