CAZyme Information: PV10_08492-t45_1-p1

Basic Information

• Species: Exophiala mesophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
• CAZyme ID: PV10_08492-t45_1-p1
• CAZy Family: GT39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
460	KN847525|CGC7	51328.94	6.2196

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EmesophilaCBS40295	9237	N/A	56	9181

• Gene Location: location=KN847525:1690513-1691946(-)

Full Sequence      

MEHRVCCTRFLIACSYYLSQVGFTQCPIAPQKSFTYRFRAELFGTTWYHAHYSSQYADGV
VGPIVIYGPSEEDYDIDLGPILLSDYYHRNSREIVKEIVSARPGLPPPKPVSDNNLINGK
MNFDCSTATTTTAKCFDHAGFARFKFQAGKRHRLRLINSGADAVQRFSIDGHKMMVIEND
FVAVEPYETEVVTLGVGQRTDVIVEGVGSPTAAYWIRSNATCAESRQPSALAIVQYEQTE
PMVLPRSTPWSVPDSCDNDPLEKTIPLYKMSPGAPEATYTLGMTVGQDESGVWLWHMNSS
SFRADVSYPSLLQAQTGNLTFLRERNVINTGSAKSYLFVLNNKSPVPHPMHLHGHNMYIL
AVGHGVWDGSIVRPENPQRRDVQNVPANGYMVWQADADNPGSWAFHCHIAWHAAVGLTVD
ILEHPEQIVNLAVPDDVYRVCHDWRDAFATGKIELLDSGV

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	22	417	4.1e-85	0.8184357541899442

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	6.06e-65	271	422	2	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.
259947	CuRO_2_MaLCC_like	5.29e-55	78	255	1	167	The second 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. 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.
274555	ascorbase	4.01e-46	22	431	75	531	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.
215324	PLN02604	2.12e-45	22	431	98	554	oxidoreductase
225043	SufI	3.01e-45	22	417	104	442	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
ATZ46043.1|AA1_3	8.11e-159	24	460	153	593
QFF92556.1|AA1_3	4.61e-158	24	460	153	593
QFF92555.1|AA1_3	9.25e-158	24	460	153	593
AEO65600.1|AA1_3	1.35e-157	22	459	155	593
QSZ30962.1|AA1_3	7.28e-155	24	460	153	595

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.96e-82	22	460	141	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	3.86e-82	22	460	141	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3PPS_A	4.79e-77	22	460	151	604	Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_B Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_C Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_D Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius]
6F5K_A	9.04e-72	22	460	110	559	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
2Q9O_A	2.49e-71	22	460	110	559	Near-atomic resolution structure of a Melanocarpus albomyces laccase [Melanocarpus albomyces],2Q9O_B Near-atomic resolution structure of a Melanocarpus albomyces laccase [Melanocarpus albomyces],3FU7_A Melanocarpus albomyces laccase crystal soaked (4 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU8_A Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU8_B Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	2.78e-121	22	460	137	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	9.43e-86	22	460	147	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.46e-83	22	460	142	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|P78722|LAC2_PODAS	1.20e-71	22	460	155	605	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|Q96UM2|LAC3_BOTFU	1.41e-71	22	419	46	450	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.861864	0.138127

TMHMM  Annotations     

There is no transmembrane helices in PV10_08492-t45_1-p1.