CAZyme Information: KID69371.1

Basic Information

• Species: Metarhizium anisopliae
• Lineage: Ascomycota; Sordariomycetes; ; Clavicipitaceae; Metarhizium; Metarhizium anisopliae
• CAZyme ID: KID69371.1
• CAZy Family: GT1
• CAZyme Description: Multicopper oxidase family protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
611	AZNF01000002|CGC10	67266.87	6.2881

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=AZNF01000002:996200-998163(-)

Full Sequence      

MSDRGDEEDRRLLDEALAADPPSYEYDAGAKSRSGRSAWTWLGLVLVTVLLAMPLLAYVR
RGGEASPASGPDGQQLAIALHPEEHVWRGAKTLHFHWNVTLGTMSPDGVEKQVYLVNGAF
PGPTIEARSGDSIIVHVHNGLADEGLSIHWHGLRMKGFNAMDGAVGFTQCPIAAGRDFEY
NFTIGDDEHGTFWWHSHAEVQRGDGLYGGFVVHRPGVGPKHQEALVLVGDWFHRRQTDVF
DWFFNWASVGNEPVPDSVLVNGRGRYNCSMAVPARPVVCTQRSREDLPPLLYRRPKDAPV
KLRVVNAGTVAGVTLRADGATMQPAAVDGGCAVDDRPGRSVGVLYPGERVDLLVNGDGVG
EQNYQLHVELDDEHFGGFPNPALDPIHTFDFFPSRLRSRQEDGPPILPPDDGQHRDLATL
TAATPTDVLAPKAQETMVLYFKMQMLSRLQNRPMGFVNNTSWKPQNPPLLATDRSLWDAD
QFIPFINSSKTRDVDIVINNLDDGTHPVHLHGYSFHVLSSFRAEGRSGWGSYNPFESGPL
VPPNLVDPVRKDTVGVPRRGHVVIRVRADNPGVWMMHCHMLVHMGTGMVTGLHVEGDEKI
VGVERAARLCA

Enzyme Prediction     

No EC number prediction in KID69371.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	109	588	6.6e-85	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.32e-74	94	610	3	538	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	3.74e-67	90	610	21	561	L-ascorbate oxidase
215324	PLN02604	1.99e-66	90	600	22	551	oxidoreductase
274556	laccase	2.01e-57	90	595	1	520	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.
259926	CuRO_1_Diphenol_Ox	1.07e-53	94	213	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI71515.1|AA1	0.0	1	611	1	611
UNI22443.1|AA1	1.15e-250	1	594	1	606
QKD61545.1|AA1	1.37e-221	6	610	5	616
AVI02163.1|AA1	6.34e-220	6	610	5	616
UKZ83242.1|AA1	1.06e-217	4	610	2	630

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.63e-52	94	610	5	538	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]
3V9E_A	4.82e-47	92	588	67	536	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.24e-46	92	588	67	536	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]
1ZPU_A	7.08e-45	91	589	1	476	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
5Z1X_A	7.37e-42	104	587	15	458	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	3.06e-61	92	598	61	572	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	2.11e-59	92	595	61	561	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|I1RMG9|FET3_GIBZE	7.47e-59	90	589	22	491	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
sp|E9R598|FETC_ASPFU	4.23e-58	90	588	20	486	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|K7NCS2|FETC_EPIFE	7.24e-58	90	589	20	490	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999977	0.000062

TMHMM  Annotations     

Start	End
37	59