CAZyme Information: ATY65374.1

Basic Information

• Species: Cordyceps militaris
• Lineage: Ascomycota; Sordariomycetes; ; Cordycipitaceae; Cordyceps; Cordyceps militaris
• CAZyme ID: ATY65374.1
• CAZy Family: GT1
• CAZyme Description: Multicopper oxidase family

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
638	CP023326|CGC2	70735.06	6.8337

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CmilitarisATCC34164	9362	N/A	75	9287

• Gene Location: location=CP023326:335509-337727(-)

Full Sequence      

MYAPVKTTRLRQARSPRLSSLCGGLVVLAAATLLCYVVVALRYAHTLPLPFSRLAVPPGA
VDASNASNVAVADHDRFTLHPELHVARPRRTLVLDWSITREKRRPDGVLRDVYLINGQFP
GPTIEARSGDELQITVTNNILNDTDAGISMHWHGLFMKDANEMDGATGVTQCAVAEGQSF
TYTFRIDPAQHGTYWYHAHSAVKRADGLYGGLVIHKPADEGTGHTDQSRHEYDAERLLLI
GDWYHRDADTVLGEYKNRRNFAYEPVPDSLLINGVGSYKCSDARPARPIDCVETEVPALA
MVADKAVRLRVVNTGAAAGLSFQLQNGTVQLLTVDGGGYVADDTPQTATIGVLYPGERMD
VLLLPADTPADDEHVLDTQMKIVLDAELMPMKNWALTRIQDFPLTWRRRSTAASLARRDV
RPAVAVFNMKDAHGAEVPPDAALHRDAAETALLYTSLSINNFKKDEPWGEVNHTSWVWKD
PRAKPLLALDADAWANGTEQANTLRTFRAPWYRDGHDRWMDLVVNNVDDKGHPFHLHGYA
FHVIGARQLDLGRSYNPYEPGATQAQAQFFNTKTPRRKDTVYIESHGYVVLRFPLDNVGV
WLMHCHVLWHQAVGMGVVLQVGNVTAATKQRAAESCIA

Enzyme Prediction     

No EC number prediction in ATY65374.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	108	615	3.5e-89	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.89e-67	94	622	4	524	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.
215324	PLN02604	3.23e-60	86	622	22	547	oxidoreductase
177843	PLN02191	2.57e-59	96	622	28	547	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	1.89e-56	451	621	1	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. 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	7.20e-54	106	622	48	449	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
ATY65374.1|AA1	0.0	1	638	1	638
QLI63445.1|AA1	3.70e-263	65	636	58	625
QUC19070.1|AA1	4.50e-250	64	636	23	593
UNI19384.1|AA1	3.20e-244	74	636	168	725
QKX63685.1|AA1	3.47e-195	65	637	48	625

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	2.21e-48	97	615	73	536	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	5.72e-48	97	615	73	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]
1AOZ_A	4.21e-46	115	622	27	524	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]
1ZPU_A	2.10e-45	91	619	2	477	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]
6F5K_A	3.80e-44	75	618	15	516	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	3.12e-56	70	624	40	565	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|E9R598|FETC_ASPFU	8.59e-55	91	615	22	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|J9VQZ4|LAC2_CRYNH	2.33e-54	56	621	26	560	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|Q55P57|LAC1_CRYNB	1.38e-53	57	621	27	560	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|I1RMG9|FET3_GIBZE	4.81e-53	77	615	13	490	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000032	0.000009

TMHMM  Annotations     

Start	End
21	43