CAZyme Information: KLU86987.1

Basic Information

• Species: Magnaporthiopsis poae
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
• CAZyme ID: KLU86987.1
• CAZy Family: GH18
• CAZyme Description: laccase-2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
574	GL876970|CGC1	63852.89	9.3839

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=GL876970:379005-380863(+)

Full Sequence      

MKFLAVSLFALVCGSAALATPANDSVSTSSLQYHPKPPNPPSPHKPSKPSRPSKPTHPPK
PTHPHKPPQSGCKNGPNSRNCWGKHSIDTNYYETAPDTGVTREYWLSVEEGICNNDGYKR
YCQTFNGSFPGPLIWANWGDNLVIHVTNNMKTNGTSIHWHGLHQRGSVEYDGVPGVTQCP
IAPGKSLTYKFRVTQYGTTWYHSHFSLQYAEGLVGPMIFYGPTTANYDEDLGTLFLQDWD
HDTVWNGWEKVASKGPGPLPANGLINGTNTFDCKNTTDSKCVGGGKKFSANFKKGKKHLI
RLINNSADAHFQFSIDGHELTVVANDLVPIKPYKTKSVKISIGQRFDVIVEANAKPGDYW
LRSGMSCVPNDQGELRKRVTGIIRYDSKSKADPKTTSDVVVDETCADESPEKLVPHLALD
VTHTSEPLRTDLGTRPNGTASEGQNWFQWTLNNSSLVLDWHDPTLERIFAKQVIFPSRYN
VHRAEPVKNGPSKQWFTLVIQSNDIPLAHPIHLHGHDFWLLSQSSSKWDGTTRGFKTKNP
TRRDTAMLPAGRPPRHRVPARQPGRLDGVLPHRL

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	89	405	1.4e-129	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	2.20e-71	99	220	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.
259947	CuRO_2_MaLCC_like	7.30e-61	231	398	1	162	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.
177843	PLN02191	1.16e-54	98	551	20	512	L-ascorbate oxidase
274555	ascorbase	4.64e-54	101	548	1	485	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.
400195	Cu-oxidase_3	2.11e-52	108	222	2	117	Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ63059.1|AA1_3	3.29e-225	68	551	38	524
AGZ62514.1|AA1_3	5.05e-189	69	549	34	501
EAA30359.3|AA1_3	6.12e-188	68	549	37	511
CAP64719.1|AA1_3	2.69e-186	68	549	36	522
CDP30116.1|AA1_3	2.69e-186	68	549	36	522

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.45e-182	72	549	39	505	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.45e-182	72	549	39	505	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]
5LWX_A	7.28e-126	82	553	32	492	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	3.50e-125	82	553	4	464	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.61e-125	82	553	5	465	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96WM9|LAC2_BOTFU	9.58e-183	72	549	39	506	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	3.17e-159	72	549	44	514	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	2.79e-147	72	551	37	486	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|A0A067XMP0|PTAE_PESFW	5.85e-106	72	545	26	524	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|Q4WQY8|TPCJ_ASPFU	3.75e-103	72	551	28	529	Oxidoreductase tpcJ OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=tpcJ PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000254	0.999723	CS pos: 19-20. Pr: 0.9768

TMHMM  Annotations     

There is no transmembrane helices in KLU86987.1.