CAZyme Information: KID64078.1

Basic Information

• Species: Metarhizium anisopliae
• Lineage: Ascomycota; Sordariomycetes; ; Clavicipitaceae; Metarhizium; Metarhizium anisopliae
• CAZyme ID: KID64078.1
• CAZy Family: GH15
• CAZyme Description: Cupredoxin

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
667		73538.92	6.5022

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ManisopliaeARSEF549	10891	1276135	0	10891

• Gene Location: location=AZNF01000009:1616535-1619017(+)

Full Sequence      

MSLKIEMNYSRFAFLSVVLLLYQSSMSFAALRSYNFTIHSETRAPDGVSREVYLINGQQP
GPLIDVDEGDSLEIFVQNNLPVDTTIHWHGILQRASPQMDGVPGVTQYPIPAGGNFTYRF
NLRDEYGFFWYHSHLRAYYNDAIRGPLLVRPLPSRRRPFEQLASTEGERKLLMNAERDAP
SILLNDWTHDPSDVIWSRYFTTGAFPNCVDSILANGNGRVQCLPEFQNGMMPKADPTSLS
TSSTAMMMSGMNKRMKMDGSSMDMGTTTMAMEGPTRTTVPDTATTASTTMMMASLGPRGC
AMPMMFNPGYNASSLPPETCTNTTSNLLNISANGTTGWLALNLVNSGAVSALRVSLDGHS
MFVYAADGSFVQLQEVKVLHMALGQRYSVMIRLNQMPGNYYLRFATYPVGDMQQVMEGQA
IISYNTTSNISTDAMDDPSIVWMLKNGSAKSEASLLNPWKLAPFESNSPPSKAADRTQLF
AINQTGVTAWVMNKAPFTEPRVPILYGAQSEGWLANTTIRMPSNSVIDIVMNVANESLDT
MGHPMHLHGHKFWVLGTGTGTFPYATAQEAPKSLINLQNPPYRDTVELPSSGWAVIRYIT
DNPGAWLMHCHLQWHIVSGMAVVLIEGEDKLPGLLGSKAPPTISTAVSFRSGYQHIAWAT
VAIFLLF

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	44	233	1.2e-50	0.44972067039106145
AA1	340	621	2.5e-42	0.49162011173184356

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.07e-66	32	643	2	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	1.41e-65	15	631	9	551	L-ascorbate oxidase
259919	CuRO_1_Abr2_like	7.57e-65	36	150	1	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), 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 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	9.01e-57	11	643	4	558	oxidoreductase
274556	laccase	1.51e-55	29	632	1	525	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
QLI72976.1|AA1	0.0	1	667	1	687
QPG98040.1|AA1	9.15e-273	29	662	23	672
QOD95012.1|AA1	4.86e-257	15	666	10	677
ATY66532.1|AA1	2.42e-248	29	663	17	660
UNI13709.1|AA1	5.04e-247	29	667	23	679

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.54e-50	32	631	68	547	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	3.99e-50	32	631	68	547	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]
1AOZ_A	5.95e-49	31	648	3	544	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]
3X1B_A	1.56e-47	35	641	28	503	Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus],3X1B_B Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus]
5EHF_A	2.61e-47	45	626	17	467	Laccase from Antrodiella faginea [Antrodiella faginea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	9.00e-102	18	631	10	567	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	1.27e-82	29	641	17	586	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	4.74e-79	50	634	59	610	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|E9E686|MLAC1_METAQ	1.53e-74	15	632	8	603	Laccase 1 OS=Metarhizium acridum (strain CQMa 102) OX=655827 GN=Mlac1 PE=3 SV=2
sp|A0A0B4HQH6|MLAC1_METMF	5.98e-73	10	632	2	604	Laccase 1 OS=Metarhizium majus (strain ARSEF 297) OX=1276143 GN=Mlac1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000257	0.999725	CS pos: 29-30. Pr: 0.9769

TMHMM  Annotations     

Start	End
12	31