CAZyme Information: PV06_03979-t43_1-p1

Basic Information

• Species: Exophiala oligosperma
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala oligosperma
• CAZyme ID: PV06_03979-t43_1-p1
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
610	KN847334.1|CGC13	67693.81	6.7717

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=KN847334.1:3472668-3474500(-)

Full Sequence      

MAPTKSLAMFLFLSLSSFLFCHSLAAFIPTAELVQLSPRDLGPRQASTSSSSSATTTKKA
DAQCTNGPFTRQCWGNGFSIATNYDSTWPNTRHTEYYDLEITNTTMSPDGVPRIVYAINN
QYPGPTIRAKWGDTLQIRVKNSLTTNGTSIHWHGVRQWYSNQMDGTNGVTECPLAPGQTR
TYTFLCTQFGTTWFHSHYSDQYSDGVVGTIIIDGPTTSNYDVDLGAFPITDWYYRPAFEI
APLVQHAVIRGPPPGDNILINGTNVKVNGTVGKYSRTTLTKGKKYKLRLINTSTNDNFKV
GLDGHSFTVVTADFVPIKPFVTNWLFLAIGQRYDVIIEANQPVDSYWFHVVPQAGCSNNL
NKNALAIFSYAGATSTTPPNATRSNAPPGAPDCNDPNKSLVPYVKLDVPDNYTIPQSSHL
DVGFAIVQDAAQQTQVQWNLNFNAINVPWGDPTLQYVLDNNTNFPASMNLISLPNANTWS
YWVIQALQTQAPPQPHPIHLHGHDFYVLGADSGVYNNSQTLNYKNPPRRDVAMLPANGYL
VLAFITDNPGAWLMHCHIAFHVSLGFGAQFLEQPDYIRSKLPIGQDWHNECTSWNKYYAT
AQYQQEDSGL

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	82	382	5.6e-126	0.9711538461538461

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.01e-78	91	582	1	532	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	6.33e-75	97	582	26	555	L-ascorbate oxidase
215324	PLN02604	4.77e-70	94	582	24	555	oxidoreductase
259923	CuRO_1_MaLCC_like	3.43e-68	93	213	2	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	6.73e-66	417	571	9	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALR81978.1|AA1_3	1.56e-218	60	610	116	671
QSZ31194.1|AA1_3	4.57e-213	37	610	42	621
ATZ47489.1|AA1_3	9.48e-213	60	610	107	663
CCD50266.1|AA1_3	1.34e-212	60	610	107	663
QSS57203.1|AA1_3	5.50e-211	60	610	47	588

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3PPS_A	1.75e-164	66	610	46	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]
1GW0_A	4.60e-164	66	610	5	559	Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form [Melanocarpus albomyces],1GW0_B Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form [Melanocarpus albomyces],2IH8_A A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase [Melanocarpus albomyces],2IH8_B A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase [Melanocarpus albomyces],2IH9_A A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase [Melanocarpus albomyces],2IH9_B A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase [Melanocarpus albomyces],3FU7_B Melanocarpus albomyces laccase crystal soaked (4 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU9_A Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU9_B Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3QPK_A Probing oxygen channels in Melanocarpus albomyces laccase [Melanocarpus albomyces],3QPK_B Probing oxygen channels in Melanocarpus albomyces laccase [Melanocarpus albomyces]
2Q9O_A	6.51e-164	66	610	5	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]
3DKH_A	2.61e-163	66	609	5	558	L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces],3DKH_B L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces]
6F5K_A	1.28e-152	63	610	2	559	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96UM2|LAC3_BOTFU	4.51e-176	123	570	1	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q70KY3|LAC1_MELAO	1.88e-162	66	610	55	609	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1
sp|P06811|LAC1_NEUCR	5.28e-161	66	610	56	606	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|P78722|LAC2_PODAS	9.16e-157	71	610	55	605	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|Q03966|LAC1_CRYPA	1.80e-154	66	610	37	591	Laccase OS=Cryphonectria parasitica OX=5116 GN=LAC-1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.017173	0.982785	CS pos: 25-26. Pr: 0.9406

TMHMM  Annotations     

Start	End
7	29