CAZyme Information: NEUDI_25956T0-p1

Basic Information

• Species: Neurospora discreta
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora discreta
• CAZyme ID: NEUDI_25956T0-p1
• CAZy Family: GH47
• CAZyme Description: Multicopper oxidases

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
697		77867.97	4.7008

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_NdiscretaFGSC8579	10345	510953	397	9948

• Gene Location: location=NdisFGSC8579_SC008:733939-736334(+)

Full Sequence      

MACRLNLFQSLFCVLALCERILAADFAQAYKSGLLSPRLYTEYDLISDKTSNHVSFHPEG
STEGFYCHYPELSSQEWEACNDEADTRWCWLRQLQAQEGESLLKGYTVTTDYDNFAPIGI
QRHYHLDISKQTITPDGFPREARLMNGTYPGPLIEACWGDTVIVHVTNNLDDEGSVIHWH
GLRQYYNNDHDGVALTQCPIARGSTWTYNFTMLQYGTTWYHSHYILQYADGVLGPLVVHG
PASAPYDVSHPQPYFMSDWVHRKAEEEFDNEKDPEVRGSKADNILVNGIGRSKEAVSAYN
GEDIRSLYDITEILPGQRVRLRLINGAAGTSFIFSVDGHALEVIANDLVPVKPTVVDSLL
VAIGQRYDIIIHGLESPSPSGNYWIRTHPADGCNVFRNGLFNSTDSTNEDPLDPRTGILH
YGHPDATYLSLPDSTLNTIPDYSCARIAEQTSLRPVVPWSISSTPLNNLTLSTFYPSHQT
EVDEPYGNYTHWLLRLDPLVEKQGGITFHNPLFANFSTPSLLDFTNIGQGENDNVIRLPY
SPDSTEYIHMVIDGSLLPATNQTDLDPDVIPLLAHPMHWHGSDVVLLAQSEQPFDPATSR
DTWNYENPPRRDTIMAPAGGYVAVAFKPDNPGVWLVHCHIAWHASAGLALQMVVDDGKGM
VQNMLAGERLERLSGGCEKWKADLGQVVDFQKEESGV

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	110	397	6.3e-109	0.8942307692307693

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	8.14e-65	119	239	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.
177843	PLN02191	4.68e-62	122	653	24	545	L-ascorbate oxidase
274555	ascorbase	6.84e-62	122	648	2	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.
274556	laccase	1.64e-58	122	666	4	531	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.
259947	CuRO_2_MaLCC_like	1.59e-57	253	441	3	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAA29734.1|AA1_3	0.0	1	697	1	700
VBB81165.1|AA1_3	3.32e-223	54	697	68	714
CDP29383.1|AA1_3	2.18e-215	54	660	115	718
CAP64870.1|AA1_3	9.04e-207	54	655	115	702
AUS45849.1|AA1_3	2.32e-168	54	697	56	671

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	2.99e-101	79	697	38	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	5.88e-101	79	697	38	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	6.36e-86	104	680	5	525	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	6.53e-86	104	680	6	526	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	9.31e-86	104	680	33	553	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|D4APX3|LAC1_ARTBC	8.89e-105	67	682	51	612	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	4.68e-99	79	697	38	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	8.49e-87	71	697	35	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	1.11e-86	75	697	32	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|A0A067XMP0|PTAE_PESFW	4.28e-83	79	690	25	599	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
0.000217	0.999735	CS pos: 23-24. Pr: 0.9761

TMHMM  Annotations     

There is no transmembrane helices in NEUDI_25956T0-p1.