CAZyme Information: FOMG_13380-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOMG_13380-t38_1-p1
• CAZy Family: GH43|CBM91
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
551		61136.52	6.5696

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum26406	20033	1089452	372	19661

• Gene Location: location=JH659340.1:598529-600664(-)

Full Sequence      

MAKHHVQLIYADEGDIVKLSVTSDIYAQSSIHLFGIGHKQTVGSWNDGTVGLSQFPTLPR
SNWTNAYDTSGSWGLNWFIDHTTTASADGLAGALYIAPSPDRPRPYHLITNDTLELRQIN
QAEREIQHLIIQSHQHRDTVWKLLRMRAEGLEYYCYDSILVNGNGRVHCRQPEYDHIKGQ
KLDQKGCIQPSGLPDETCKQSLADYEVIETQGRRYMMLNLMNIGFEHSVKVSIDHHKMIV
VANNAGFIVPEEADVVHIPSASRVTILVRLEAEPGDYAIRISSTSVLQNLHGYAVLRYPA
KRLPQYGEPMALPSVAPGLVCVVPDGGTQPNCSTAEGQLLPPYPPQPPPSAGKQHLGKAD
FTFRLSAGSQRSKTEKYVPEYFLNEKPWQLYHGSMLPLLFHAPNETLVKPIIGNLPLGSV
VDLIIENQINETIPLYKHGDPSWFLGSCGQQRFPGNTVQDAIDSDSKSLNLQDPALVIVH
DLPALGWSVLRFKVTSQQATIIHAAKLRYFALGMSAPILEGITEDTPIQVPESVLNRPHV
EFKPAHDGIFG

Enzyme Prediction     

No EC number prediction in FOMG_13380-t38_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	8	514	1.9e-36	0.9357541899441341

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259944	CuRO_2_Abr2_like	3.39e-56	127	299	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	5.06e-17	9	535	56	559	L-ascorbate oxidase
259951	CuRO_2_tcLCC_insect_like	6.30e-15	129	298	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.
259965	CuRO_3_Abr2_like	9.43e-14	418	521	56	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.
259868	CuRO_2_LCC_like	1.45e-12	155	298	30	152	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) are able to 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 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
QKD61049.1|AA1	0.0	8	551	96	639
CEI62062.1|AA1	0.0	9	551	97	641
QPC59569.1|AA1	8.92e-318	9	551	97	641
CZS81621.1|AA1	3.39e-316	9	551	97	641
QPC70978.1|AA1	4.73e-316	9	551	97	641

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	6.18e-06	9	280	84	307	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|W3X732|PFMAY_PESFW	1.43e-70	8	544	54	584	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	3.00e-45	7	539	54	610	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	4.95e-42	9	531	57	597	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|Q0UHZ8|ELCG_PHANO	1.91e-41	14	524	78	606	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|E9RBR0|ABR2_ASPFU	3.48e-39	9	522	52	573	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000068	0.000002

TMHMM  Annotations     

There is no transmembrane helices in FOMG_13380-t38_1-p1.