CAZyme Information: KLU86825.1

Basic Information

• Species: Magnaporthiopsis poae
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
• CAZyme ID: KLU86825.1
• CAZy Family: GH18
• CAZyme Description: laccase-2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
494		54098.38	8.0621

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MpoaeATCC64411	12363	644358	200	12163

• Gene Location: location=GL876969:3349305-3351805(-)

Full Sequence      

MRLLHLLAGFLSVFAVQADPLPLLKPDPVLPAGALQPRQTIIPGGPPCGQNNATNRGCWK
NYWNVSTDYELTIPTGTTRVIDLTITNITSFSADGVAKPVMLINGGFPGPVIHCDWGDWL
ELRVHNNLKDNGTGIHWHGLRQHNSNNQDGAGGITECPIAPGSSRSYTFRAVQYGTSWYH
SHFSVQYGNGVVGAVVVNGPASANYDIDLGPFVITDWYWQTADILQLRAEQATGGPPPAD
NILFNGTNINPRGSGGRYQRVKLTPGKKHRLRIINTSVDNGFTVSLVGHSFTVIATDLVP
TRPVVKNQLFLGVGQRYDVIIDANQPVANYWFNVTVGGGGVCGVCKNPFPASIFSYDGAP
ANANPTNRGTRITADCKDTVGPFVPVVSRFNPAADVGRLNFDNPVRRDVAMLPPGWMVIA
FETNNPGAWLMHCHIAWHVSQGLSVQFLEIQDEIPLVMKLDQLQPTCDAWRAYWPRAYYP
KIDSGLRRRRELGD

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	67	376	1.4e-122	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	5.29e-63	76	187	1	111	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.
259947	CuRO_2_MaLCC_like	1.81e-55	209	372	1	165	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.
225043	SufI	4.73e-43	71	447	25	446	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].
400195	Cu-oxidase_3	1.48e-39	84	187	1	104	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.
259869	CuRO_1_LCC_like	3.10e-38	79	187	1	109	Cupredoxin domain 1 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 1 of 3-domain MCOs contains 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 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ56961.1|AA1_3	2.85e-272	16	488	20	595
AUS45837.1|AA1_3	9.69e-247	25	486	22	585
BAB32575.1|AA1_3	1.52e-195	48	486	37	589
VBB86211.1|AA1_3	2.48e-189	26	489	24	594
AFK76451.1|AA1_3	5.11e-189	48	486	34	590

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1GW0_A	3.01e-147	51	486	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]
3PPS_A	3.08e-147	6	486	10	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]
2Q9O_A	4.26e-147	51	486	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	1.71e-146	51	485	5	558	L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces],3DKH_B L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces]
6F5K_A	1.00e-142	51	486	5	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|P06811|LAC1_NEUCR	6.34e-158	6	487	9	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|P78722|LAC2_PODAS	5.60e-154	12	494	4	613	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|Q03966|LAC1_CRYPA	1.45e-149	35	486	28	591	Laccase OS=Cryphonectria parasitica OX=5116 GN=LAC-1 PE=3 SV=1
sp|Q70KY3|LAC1_MELAO	1.57e-148	4	490	8	613	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	1.65e-116	108	447	1	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000278	0.999680	CS pos: 18-19. Pr: 0.9764

TMHMM  Annotations     

There is no transmembrane helices in KLU86825.1.