CAZyme Information: Z517_06970-t43_1-p1

Basic Information

• Species: Fonsecaea pedrosoi
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Fonsecaea; Fonsecaea pedrosoi
• CAZyme ID: Z517_06970-t43_1-p1
• CAZy Family: GH32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
609		67703.17	5.5112

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FpedrosoiCBS271-37	12573	1442368	46	12527

• Gene Location: location=KN846972:3237627-3239679(-)

Full Sequence      

MFKEILVYLGLLRPDWSVWPLPSHSNLVLKVTNPFPPLRETQCNSPSQRGRWCDGFSIDT
VPDEDGPTTGNVCEYLFIITNTTKDFDGVERLALAVNGQVPGPAIECQWGDILRVNVTNK
MQNNQTAMHWHGISQRGGTTNDQDGVPGVTECAIPPGHSRIYEFKLKQFGTAWWHSHALS
QFGDGIHGPIIIHGPATADYDIDMGAIMIDNLFDNSSNPISTPAYASRVLHVNGTGFWNY
VLNGANTSPDLTRGRHAFWSVKPGKRYRFRIINSAVQSAWAVHFDHHKMTVIAADLVPIK
PYTAEWLNIGNGQRYDVIVEMDQPADAYFLRAVAQLGCPDETQNNGLGLANGIFLYQGAS
LSLPSSTAGNKTAADFLYCADEPLSSLTPWIEKSAGSRAAFEAKAKTLPSGDRYRLTFSD
DGTVWRWPLNGTITVNYTQPTLELLAHGISPYDRPIEQQIVLPEKDQWVYFIIQNLFYAA
HPMHLHGHDMAILGQGKEEWNASLISTLNFENPPRRDTALVVGNIEKDPNVGGYLVLGFK
TDNPGVWLLHCHIIWHSESGMGLQFIERPDEIPAKAYTSKESFVQECAAELEYEEEDPSH
KKSESVSGV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	64	370	2.6e-100	0.9647435897435898

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	1.18e-62	87	569	48	450	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].
259923	CuRO_1_MaLCC_like	1.78e-61	70	193	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.
259968	CuRO_3_MaLCC_like	9.53e-59	417	566	16	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.
274555	ascorbase	1.09e-58	87	576	16	535	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.
177843	PLN02191	9.47e-55	87	576	38	558	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAK03309.1|AA1_3	6.20e-172	44	593	224	780
QIX00022.1|AA1_3|CBM20	5.66e-133	41	589	83	611
QSS61236.1|AA1_3	9.42e-130	4	588	12	570
QSS72037.1|AA1_3	1.82e-129	4	605	12	586
QSS57203.1|AA1_3	1.02e-128	4	593	12	574

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	2.60e-120	14	608	2	571	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	9.87e-119	55	608	6	543	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.02e-118	55	608	7	544	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3V9E_A	2.86e-113	44	588	41	562	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	7.98e-113	44	588	41	562	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J5JH35|OPS5_BEAB2	6.52e-124	44	586	46	586	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.13e-112	31	588	25	563	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|P06811|LAC1_NEUCR	5.78e-109	43	589	55	588	Laccase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=lacc PE=1 SV=3
sp|Q0CCX6|GEDJ_ASPTN	3.05e-108	44	572	30	565	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q70KY3|LAC1_MELAO	1.65e-105	39	572	50	574	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000047	0.000003

TMHMM  Annotations     

There is no transmembrane helices in Z517_06970-t43_1-p1.