CAZyme Information: KLU82987.1

Basic Information

• Species: Magnaporthiopsis poae
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
• CAZyme ID: KLU82987.1
• CAZy Family: AA9
• CAZyme Description: laccase-1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
597	GL876967|CGC20	65162.89	7.1465

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=GL876967:541486-543488(+)

Full Sequence      

MPGTFLDKFKSGATAGAKSVYHTVCKLSQEKTNGKSRLGTLLAPLLPMFLSNNPLPHGFP
WGDKTINGTNPYHGCPTTGVIRSYDFTLSRATIAPDGYEVPALLVNGAFPGPTIEANWGD
TIQVTVHNNITGPEEGTAIHWHGILQRGTPWEDGVPGVTQCPIPPGKSYTYQFRADMFGT
SWYHAHFSAQYSAGIFGPMVVYGPETVPYDLDLGPVMLTDWYHNGYLKIIAEMLKPGGDP
RVFSDNNLINGKMNFDCTKVAPGDNTKCTSNAGISKFKFQSGKTHRLRLINSGADGVQRF
SIDQHTMTVIANDFVPIKPYEAKVVTLGVGQRVDVIVKADQGAPKSAFWMRSTLTKCTLA
RQPNAVAAIYYDEDTGAVPTSQPHDVPDPVTCANDDLALTQPLFPIPASEPSYAHTFNIE
LFRNASNVTLWKFDGVSARVNMNAPPLLLANLGNTSFPPEWNVHNVGSNSSIRMIVVNKT
PAAHPMHLHGANFQVLAEGVGPWDGKIVNPQNPMRRDVQQIRGAGGYLVLQFEADNAGAW
PFHCHIAWHASGGFFSTFLVQPEEIKKFQIPLSVGQTCRDWASYTQTNVPLQIDSGL

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	70	387	2.3e-124	0.9807692307692307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.23e-77	81	549	1	512	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.
259923	CuRO_1_MaLCC_like	7.39e-74	79	202	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.
215324	PLN02604	5.13e-69	81	549	24	535	oxidoreductase
259968	CuRO_3_MaLCC_like	1.06e-68	407	559	2	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.
225043	SufI	1.53e-67	91	563	45	451	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ65858.1|AA1_3	1.64e-305	13	597	8	595
AEO54598.1|AA1_3	5.90e-294	19	596	18	594
AEO65600.1|AA1_3	3.27e-293	21	596	19	593
AGT80114.1|AA1_3	1.63e-276	26	597	14	583
VBB73055.1|AA1_3	4.90e-276	10	596	8	593

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.34e-110	61	597	49	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.34e-110	61	597	49	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]
5LWX_A	2.77e-101	60	588	31	560	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
6F5K_A	4.70e-101	61	597	13	559	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
5LM8_A	1.39e-100	60	588	3	532	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	1.61e-193	54	597	38	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	1.78e-123	61	597	54	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q0CCX6|GEDJ_ASPTN	3.77e-113	61	597	45	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.96e-112	61	597	49	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q4WQY8|TPCJ_ASPFU	6.73e-104	40	590	19	599	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 OTHER

Other	SP_Sec_SPI	CS Position
0.999238	0.000764

TMHMM  Annotations     

There is no transmembrane helices in KLU82987.1.