CAZyme Information: FOIG_10428-t36_1-p1

Basic Information

• Species: Fusarium odoratissimum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium odoratissimum
• CAZyme ID: FOIG_10428-t36_1-p1
• CAZy Family: GH3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
664	KK036127.1|CGC8	75544.65	5.4927

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FodoratissimumNRRL54006	16975	1089451	341	16634

• Gene Location: location=KK036127.1:339030-341270(-)

Full Sequence      

MALIERVWHACVSIVAWLTMWPTSPSTSYQHPLRPNHPHTHIEDPSPGFPIFHPPPGDHE
FLCEYPEMTGFVQCSIPENRECWLRHPDGREFNIHTNYENFAPKGIMRHYTLNITESWYN
ADGQNFTEAKLFNGEYPGPWLEACWGDTFNITVINSMKRNGTSIHWHGIRQNQTMDMDGV
NGITQCPIAPGDSFSYIFNTTQYGTSWYHSHYSVQYADGLQGPITIHGPQSAPYDATKRP
LLMTDWSHESAFRLLFPGSQFSNKTILLNGAGNVSHYGYTPTLPVPDNYELYFNKTPTDK
PSRPKRYLLRLINTSFDSTLVFSIDNHWLQIVTSDFVPIEPYFNTSVLIGIGQRYNVIVE
ANPLAGDVNGIPEDGNFWIRTWVADACGIAPGGDGYEKTGILRYNHTDKALPSSQPWVNI
SKACSDETYTSLRPKIPWYIGPAANAQAADQTGERFNVTFDPNAKNTPEFQEEYPVATFG
LQRPGQNFRPLQINYSDPVMFHLDEPRDTYPPKWVVIPEDYTEKEWVYFVLTIEGISART
GAHPIHLHGHDFALLQQEENQTYDPSRLNLKLDNPPRRDVVLLPRNGFVVIAFKADNPGI
WLMHCHIARHASEGLAMQVLERQGDANELFPVGSPNMIEAERVCKDWKTWMDGEKDFFEG
DSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	96	424	1.2e-119	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	4.70e-64	105	227	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.
274556	laccase	1.33e-63	105	617	1	515	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.
274555	ascorbase	2.14e-54	133	610	26	512	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.
259968	CuRO_3_MaLCC_like	2.76e-52	490	620	32	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.
225043	SufI	6.34e-52	127	619	52	446	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD61499.1|AA1_3	0.0	1	664	1	664
AVI02162.1|AA1_3	0.0	1	664	1	645
UPK95743.1|AA1_3	0.0	1	664	1	669
UQC83994.1|AA1_3	8.51e-225	39	663	40	680
QLI67119.1|AA1_3	2.30e-217	1	650	1	650

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	4.71e-121	66	664	31	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	9.35e-121	66	664	31	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
6F5K_A	8.84e-99	74	664	4	559	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
5LWX_A	1.55e-97	92	650	35	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	7.78e-97	92	650	7	528	Crystal structure of a laccase-like multicopper oxidase McoG from 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	3.08e-161	45	664	29	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	1.39e-119	66	664	31	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	8.57e-117	77	664	48	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q0CCX6|GEDJ_ASPTN	9.37e-117	77	664	32	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	8.41e-116	75	664	28	610	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
0.114961	0.885017	CS pos: 25-26. Pr: 0.8709

TMHMM  Annotations     

There is no transmembrane helices in FOIG_10428-t36_1-p1.