CAZyme Information: KLU86700.1

Basic Information

• Species: Magnaporthiopsis poae
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
• CAZyme ID: KLU86700.1
• CAZy Family: GH17
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
635	GL876969|CGC10	69988.16	6.1484

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=GL876969:2922363-2924392(-)

Full Sequence      

MVTRGLAPRTTAIIGLVVAINIIVLSLGLKSGLKFRAAPLFGFVGPPNHTRPAPPRLPGL
PLQPGTPEEWRLNTDREYLLDMAWDLNAAPTTRRYDFVITQGKAWPDGVVRDMLLVNGQF
PGPLIEANRGDRILVNVTNKLASEPTAIHWHGIHQRGTPWFDGTAGVTQCGIPPGQSLLY
NFTLDGQFGTFWWHAHYSAQAIDGVLGPLVIHAPEEAALRETYQQDRVLLLQDWYHDTSK
VDLAKYLAPNVENNEPIPSSGLINGRNYFDCSRYGPDSGKSCYGNASHSVLSLEPHSRTR
LRLINGGAFTSFEFSVDKHPLNVIEADSILTRPHSTNRLPIHVGQRYSAVLDTNQEAGTN
YWVRAAMVTFRFKGDENPVLDSTTKAVLSYVGKTDATLTPDPAQSTDWQAEANAVVCKDP
EDATLVPLVSKPPPPATRFVAVDFHFAIGANQMSYAKVNETVTWKPQLNSTTLLDAVEGL
RSPVAASWSMPAPEGRVEVFQQDQYVVGVSNDTAEVVDLLVYSLDDGSHPFHLHGHDFWI
MERGGGAFDWTHYHSEVAVPGPSVLDRPRRDTVTIEPYSWVLVRFVADNPGLWAFHCHMA
WHMEAGLLMQFMSGASMLAKTEIPEHIASLCASAG

Enzyme Prediction     

No EC number prediction in KLU86700.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	109	607	4.7e-118	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	6.84e-96	92	627	1	535	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.
177843	PLN02191	1.85e-88	87	625	18	556	L-ascorbate oxidase
215324	PLN02604	1.75e-81	92	614	24	547	oxidoreductase
259926	CuRO_1_Diphenol_Ox	5.35e-76	93	212	1	119	The first 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
274556	laccase	2.02e-66	92	612	3	518	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ62742.1|AA1	6.61e-305	6	631	92	722
AUS45844.1|AA1	3.98e-253	65	631	96	655
AEO70365.1|AA1	4.16e-246	57	635	76	662
QKX53525.1|AA1	8.65e-148	66	592	80	589
ATY60613.1|AA1	4.12e-143	71	635	102	667

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.01e-82	77	619	51	548	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	1.98e-82	77	619	51	548	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
1HFU_A	1.10e-75	99	631	11	487	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.13e-75	99	631	11	487	Chain A, Laccase [Coprinopsis cinerea]
1AOZ_A	3.68e-75	116	620	27	530	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	3.25e-92	78	632	47	579	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|Q55P57|LAC1_CRYNB	9.49e-91	78	632	47	579	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	1.37e-82	78	632	47	579	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|Q96WM9|LAC2_BOTFU	3.81e-82	77	619	51	549	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|A0A067XMP0|PTAE_PESFW	5.72e-81	95	618	60	570	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 OTHER

Other	SP_Sec_SPI	CS Position
1.000005	0.000002

TMHMM  Annotations     

Start	End
12	29