CAZyme Information: PV06_07758-t43_1-p1

Basic Information

• Species: Exophiala oligosperma
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala oligosperma
• CAZyme ID: PV06_07758-t43_1-p1
• CAZy Family: GH72
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
715		77384.09	5.1380

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EoligospermaCBS72588	11938	N/A	45	11893

• Gene Location: location=KN847338.1:1291856-1294102(+)

Full Sequence      

MQGHSFSLLELFVFLLITNFAAGASSGTTSSLPTTSSTSWHRPSPTTSWYNGTTTSIRSS
STTTTTSEALTTVLPQSISDIIFPTAFPFQKPIHPWNIPSGRWRLSQSQTNGKGLLGTIP
LGGQGGAPRFPAFVGAPGPKGVYTGGSSGSGPSSSGSSGGGSNPPKTFPWGSRTANNTNP
YTNPPKTGVVRSYNFVLERGVLAPDGVQRDVILINGQFPGPTIEANWGDTIEVTVTNLIS
EPKEGTSLHWHGLLQQGTPWEDGVPGITQCPIAPGATFTYSYLADLYGTSWYHAHYSAQY
AAGLFGAIIIHGPSNANYDVDLGPVLLTDYYHREYYDIVEEVMGTDLSKVAPYSDNNLIN
GKGTFDCNLLANDTTCTPNAGYAKFQFTKGQKYRLRLINAGAEGLQKFSIDNHQLTVMAY
DFVPIQPYTTEIVTLGVGQRADVIVEATGGVNDAVWMRSVISNCSLANQPYGYAMVYYQN
ANTDFKPNSTAWTDTTDACANDDLSKTVPYYQITPPGTPAKEVTVDVNFGVNATGSLVWT
MNNSTFRTCYNDPALFRAQELITSPNSTFEYPDEWNVYDMGEASSIRVIVNNLTPVSHPM
HLHGHNMHVLAEGTGTWDGTVVNPSNPARRDTQLLRPVDASGNPGYLVMQFDADNPGMWP
FHCHIAWHVSGGLYINILERPNDIPTNTPGGFNDMCTTWGQYTSLGPIDQIDSGL

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	178	499	2.1e-121	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.52e-74	190	673	1	517	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	7.88e-71	190	690	24	560	oxidoreductase
259923	CuRO_1_MaLCC_like	1.48e-68	188	311	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	1.46e-67	514	678	1	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.
177843	PLN02191	2.91e-65	187	690	20	560	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA07098.1|AA1_3	1.20e-236	105	715	21	596
ATZ46043.1|AA1_3	6.11e-231	105	715	21	593
QFF92556.1|AA1_3	7.47e-227	105	715	21	593
QFF92555.1|AA1_3	1.06e-226	105	715	21	593
ATZ52184.1|AA1_3	7.44e-226	165	715	40	589

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	8.02e-112	170	715	49	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	1.58e-111	170	715	49	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	2.53e-111	177	707	10	533	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.60e-111	177	707	11	534	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	2.87e-111	177	707	38	561	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|A0A067XMP2|PTAK_PESFW	4.58e-184	165	715	40	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q96WM9|LAC2_BOTFU	3.30e-114	170	715	49	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	6.54e-113	170	715	54	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	3.96e-109	170	715	47	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|A0A067XMP0|PTAE_PESFW	3.19e-103	188	715	55	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
0.000714	0.999293	CS pos: 23-24. Pr: 0.9782

TMHMM  Annotations     

There is no transmembrane helices in PV06_07758-t43_1-p1.