CAZyme Information: EPE04327.1

Basic Information

• Species: Ophiostoma piceae
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Ophiostoma; Ophiostoma piceae
• CAZyme ID: EPE04327.1
• CAZy Family: GH11
• CAZyme Description: Multicopper oxidase [Source:UniProtKB/TrEMBL;Acc:S3BV04]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
588	KE148161|CGC3	64365.91	4.2090

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_OpiceaeUAMH11346	8884	1262450	0	8884

• Gene Location: location=KE148161:185063-186878(+)

Full Sequence      

MHFRSLLASAALLGSASAFPHIWNSPSKAVEAKSVSPELEAHKSVHKRCTNSADDRSCWG
DYDISTNYYDESPDTGVTREFWWDITNTTASPDGIERIILAINGTVPGPTIYADWGDIIV
VHVTNSLANNGSSIHFHGIRQNYTNQNDGVPSVTQCPIAPGESYTYTWKATQYGSSWYHS
HYYVQAWDGVFGGIQINGPATANYDVDLGTMMLNDWMHETADAMLIRAETSGPPTLNGGL
LNGTNTYTDSTTGTTTGSRYETTFVAGQRYRLRLVNAAADTQFKFSIDNHTLEVIAADFV
PINPYAAESVSISMGQRYDVIVTANATTTSTTDFWMRAVMVQACSDNDSPNNLLGIVRYD
STSTTDPTSTAWTSAEDNGDSCADEPMASLVPYLSIDATDDPTNTTDFDVGLYINSGIDL
WEMGSTSFVSQWDYPSLLQVSEGNDTWGAAQNVYQYPSANKWAYMVIQTSNQVPHPMHMH
GHDFWVLGQGDGSFVATTATLTLTNAPRRDVVLLPADGYLVIAFYTDNPGVWLMHCHIAW
HTTEGLAIQLLERESEIPALLDTALNTTCAAWDTYANSVDVVQTDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	66	375	9.6e-132	0.9839743589743589

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	2.03e-69	401	551	5	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.
259923	CuRO_1_MaLCC_like	3.01e-69	76	197	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.
274555	ascorbase	1.26e-63	78	558	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	8.97e-59	75	565	20	559	L-ascorbate oxidase
215324	PLN02604	3.82e-57	78	559	24	556	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA14113.1|AA1_3	0.0	36	588	18	568
AVO20570.1|AA1_3	1.45e-288	32	588	14	561
AAY99671.1|AA1_3	9.84e-255	29	588	12	567
CAK44895.1|AA1_3	1.60e-239	44	588	26	559
BCR82613.1|AA1_3	1.35e-225	49	588	28	557

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	3.04e-182	59	576	32	557	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.36e-181	59	576	4	529	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.40e-181	59	576	5	530	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3SQR_A	3.36e-166	39	588	29	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	6.74e-166	39	588	29	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12570|LAC1_BOTFU	1.93e-178	3	588	5	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q96WM9|LAC2_BOTFU	5.34e-170	39	588	29	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	1.15e-168	46	588	41	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	3.13e-130	107	549	1	451	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q03966|LAC1_CRYPA	3.89e-123	51	588	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
0.001322	0.998669	CS pos: 18-19. Pr: 0.9669

TMHMM  Annotations     

There is no transmembrane helices in EPE04327.1.