CAZyme Information: CCE27768.1

Basic Information

• Species: Claviceps purpurea
• Lineage: Ascomycota; Sordariomycetes; ; Clavicipitaceae; Claviceps; Claviceps purpurea
• CAZyme ID: CCE27768.1
• CAZy Family: CBM48
• CAZyme Description: Related to multicopper oxidase [Source:UniProtKB/TrEMBL;Acc:M1W6A9]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
608	CAGA01000005|CGC1	67976.83	7.2250

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Cpurpurea20.1	8979	1111077	156	8823

• Gene Location: location=CAGA01000005:756128-758246(-)

Full Sequence      

MATVWKSICVTGLAFWAIYYLIISTDSGYALTQSWSWQSPSSPERSDPFALRPEQHIFRR
PHTISLHWNITREARRPDGVLKETYLINGQFPGPTVEARSGDELHITVYNGITGSNDGVA
IHWHGITMKGFNEMDGAVGITQCAVGPGRTFIYKFQIDQQQHGTFWYHAHSAVQRADGMY
GGLVVHKPVGKQRKSDLSVHGYDSEKLLLIGDWYHRSADRVLAEYKDFRSFANEPVPDSL
LINGAGSYNCSNARPGKPVDCMNTETPVVHAHRGRVRLRIVNTGASAGYSLQLAGAAMKL
VTVDGGGFVSKRTPWTSTIGVLYPGERMDVVLLPSGEQTARVLKIALDPELMQLMNPALT
RMQEFPLKWTQPDSRSSRARGDRRELVDVVNLRDAQGVSTALDKVATDTALLYTSLAINS
FKNNEPWGELNHTSWMWKDPYAKPLLAINATAWQNGTEQANPFRAFKVPQFEAGEERWMD
LVVNNVDDRGHPFHLHGYEFYVLASRQDELGRAYNPFDNHGAEIPVNVRNPLRKDTVYIK
PRGYIVLRLRLDAPGLWLMHCHVLWHQAAGMGTVLQVGDISEATARKAEDSCQGYEIISG
HEGDNEAV

Enzyme Prediction     

No EC number prediction in CCE27768.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	80	571	1e-85	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.84e-67	66	578	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.
177843	PLN02191	3.85e-64	67	578	27	547	L-ascorbate oxidase
215324	PLN02604	1.03e-60	68	578	29	547	oxidoreductase
225043	SufI	1.01e-56	78	580	48	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].
259977	CuRO_3_MCO_like_4	4.01e-52	410	577	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI63445.1|AA1	5.08e-282	47	593	68	626
QUC19070.1|AA1	1.70e-266	40	593	27	594
UNI19384.1|AA1	2.81e-247	46	593	168	726
ATY65374.1|AA1	2.49e-246	47	592	75	636
QKX63685.1|AA1	1.58e-193	36	592	45	624

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.48e-51	87	578	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]
3V9E_A	2.38e-51	67	591	70	554	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	6.21e-51	67	591	70	554	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	1.26e-48	63	575	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	4.97e-48	60	595	34	543	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	4.14e-64	21	577	17	560	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|J9VQZ4|LAC2_CRYNH	5.98e-60	15	577	11	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|E9R598|FETC_ASPFU	1.11e-59	63	593	22	509	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|Q55P57|LAC1_CRYNB	2.58e-57	40	577	36	560	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|K7NCS2|FETC_EPIFE	1.74e-56	63	571	22	489	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
0.840172	0.159833

TMHMM  Annotations     

Start	End
7	24