CAZyme Information: PV10_08610-t45_1-p1

Basic Information

• Species: Exophiala mesophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
• CAZyme ID: PV10_08610-t45_1-p1
• CAZy Family: GT39
• CAZyme Description: hypothetical protein, variant 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
624		68536.57	5.6391

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=KN847525:2024462-2026494(-)

Full Sequence      

MRAALVSAILSTVFAHGALAHLGKWVGGGDCPWGDRKASNTHPADFPDTGVTRYYDFTVA
RGSFAPDGVQQSMIVINGQFPGPLIEANWGDWIEVNVHNEITGPEDLTMLHWHGLNQPGT
PYMDGVSSVSQCPIVPGGNLTYRFRADEHGSTWYHAHYSAQYVSGVYGPMVIHGPNDVPY
DEDLGPILVSDWYHDSYEHIVDLVMQPTNGPPFRPVSDSNLVGGKGQFPCENVTSGAPCT
VNPYASWEIEPGKTYRARFINTGATAFETISLDGHTFTVIANDMVPIQPYDTDFVTIGVG
QRVDVVFTASAGSGSFWLRAFNSPCGDTNGSDGRGIIYYKGTDPSTPPTSQGKQAPENPF
CQNDPLSQTVPQYVMPAAEPDMTITLTIGGAPDEKGIFRWTFNDITYEGDLDTPNLFEAI
AGIPLPPSRNVYLTDTHEVVRIIVINTLPAPHPMHIHGHDFQVLAEGTGTWDGVVVNPSN
PQRRDVQMSHAGADRGQGTTNYIVIQYEQDNPGVWPFHCHIAWHLSAGMSIMLMERPAEI
AKIEVPSSVKATCDAYKAWEAANPHIPVDEGLRKRDLAKRMVDFMKGHTSHSAKHQKRGY
HGFSHQDRHGAWKGVEEPRKRDEV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	45	351	2.4e-110	0.9551282051282052

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.97e-72	52	549	1	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	6.78e-65	41	543	16	554	L-ascorbate oxidase
225043	SufI	4.92e-64	75	538	56	451	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	1.14e-63	50	173	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	4.13e-63	52	529	3	513	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIW99529.1|AA1_3	5.50e-173	21	572	98	663
CDP23915.1|AA1_3	1.38e-169	32	571	58	593
CAP67656.1|AA1_3	1.38e-169	32	571	58	593
AEO65600.1|AA1_3	1.96e-169	32	571	58	593
VBB73055.1|AA1_3	3.92e-169	32	571	58	593

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	1.47e-108	32	565	3	534	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.51e-108	32	565	4	535	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	2.31e-108	32	565	31	562	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3V9E_A	4.95e-100	33	572	49	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.37e-99	33	572	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	1.74e-142	32	572	44	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	5.81e-116	33	572	54	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|P78722|LAC2_PODAS	3.38e-105	47	573	73	606	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	1.66e-102	33	572	47	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q96WM9|LAC2_BOTFU	9.42e-100	33	572	49	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000221	0.999748	CS pos: 20-21. Pr: 0.9756

TMHMM  Annotations     

There is no transmembrane helices in PV10_08610-t45_1-p1.