CAZyme Information: NEUDI_129406T0-p1

Basic Information

• Species: Neurospora discreta
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora discreta
• CAZyme ID: NEUDI_129406T0-p1
• CAZy Family: CE8
• CAZyme Description: Multicopper oxidases

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
401	NdisFGSC8579_SC018|CGC1	45034.94	8.9882

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_SC018:50592-51852(+)

Full Sequence      

MIQDYYRRTADRLHYVAELVQNSPPPDSSTITFHGKSINPTRPGVAYDRLVLTPGTKHLL
RLINASVDNSFTISLVGHNFTVLATDLVPVTPVVCSKLFMAFGQRYDAHVILEANQAVGG
QLLAQPIIQYSGASSTTILTIKGTPVIAGCVGKSGFAPIVKRTISSSLFVAPSTLPISLN
TPTKPQDQVLEWRIRNSPIVVEWNHPVLEYILEGNTSFPAAINLVEVPSSAKSWTFWVLQ
TDFTLPHPIHLHGHDFLTLDIGTHTFSTSTMMNQLYFNNPVRRDLVQIPGGGWLEMAYKT
DNLGVWLMHCHIGWRVAIGLGIQFLERKDKIKQLMKLDQMEPNCQEWRTYQPTSPYLPKV
DSRLKLKRGVEDEEGVKLMRDGFNFREAGLEVREPAVRRLR

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	1	320	5e-40	0.6396648044692738

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	1.16e-55	169	325	6	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.
259947	CuRO_2_MaLCC_like	5.82e-34	1	148	5	166	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.
400194	Cu-oxidase_2	4.40e-30	201	329	2	137	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259870	CuRO_3_LCC_like	2.63e-23	237	324	47	131	Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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. Also included in this family are cupredoxin domains 2, 4, and 6 of the 6-domain MCO ceruloplasmin and similar proteins.
259971	CuRO_3_Diphenol_Ox	8.92e-22	203	319	33	151	The third cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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. 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
VBB86211.1|AA1_3	1.76e-166	1	400	210	609
CDP31732.1|AA1_3	1.79e-165	1	400	228	627
CAP68261.1|AA1_3	1.79e-165	1	400	228	627
UQC84870.1|AA1_3	7.37e-109	1	362	705	1075
BAB32575.1|AA1_3	3.57e-108	2	364	204	589

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1GW0_A	2.62e-87	2	364	172	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	2.62e-87	2	364	172	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	5.20e-87	2	362	172	557	L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces],3DKH_B L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces]
3PPS_A	1.71e-85	2	364	213	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]
6F5K_A	2.66e-83	2	364	172	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|Q70KY3|LAC1_MELAO	1.81e-89	2	374	222	619	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1
sp|P78722|LAC2_PODAS	2.00e-83	2	370	217	611	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|P06811|LAC1_NEUCR	6.14e-81	2	365	223	607	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|Q03966|LAC1_CRYPA	4.35e-77	1	362	204	589	Laccase OS=Cryphonectria parasitica OX=5116 GN=LAC-1 PE=3 SV=1
sp|Q96UM2|LAC3_BOTFU	7.66e-71	25	324	129	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000068	0.000000

TMHMM  Annotations     

There is no transmembrane helices in NEUDI_129406T0-p1.