CAZyme Information: RL4_JR_04067-RA-p1

Basic Information

• Species: Raffaelea lauricola
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Raffaelea; Raffaelea lauricola
• CAZyme ID: RL4_JR_04067-RA-p1
• CAZy Family: GH16
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
558		61100.54	5.9679

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RlauricolaRL4	10461	N/A	146	10315

• Gene Location: location=JACBXF010000067:184983-186763(-)

Full Sequence      

MSSDGVPPQQLGILLHPQDHIWRSAQTIELNWNITAGMRSPDGVEKRVYLINGDFPGPTI
EARSGDELVVHVHNGLEKEGVSLHWHGLHLLGQNLMDGAVGLTQCPIPAGGDFIYRVRIG
DDEHGTFWWHSHEKGQRADGLFGGLVVHRPEGEDEVSSAPYSDEILLMIGDWFHLSADET
QEWYLSSVHYGNEPVPDSLLINGKGKFDCSRATPARPLNCTTVPVARGSLLSDRLPATSR
WRIINTGSIAGFSLMIPSAQFNVTHVDGGSQVAPVDGNGFGILYPGERVDVIVTAPSDTN
ASRLFLSIDDENLAYTNPSLQENQSFPVSPHSFLKEDSQPPFPEFPGNHFVDLATLVSRK
NNLAPGWPVEAHQTLAVYSKVQILVKYASRTRGYMNHSCWAPQTPPLASLSRQLWNSNQL
VPFVASGGSADSPQWVDLVINNLDDGSHPFHFHGHSFYILSTHMSQPGGWGSYNPFESDM
PPSGLNMVNPLRKDTVRVPRRGHVVIRFQADNPGIWMLHCHMAVHLGGGLSMAIHVGAPE
DEGHVAELSSSAAELCKA

Enzyme Prediction     

No EC number prediction in RL4_JR_04067-RA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	44	530	5.8e-86	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.69e-74	29	530	3	517	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	8.07e-68	25	551	22	557	oxidoreductase
177843	PLN02191	1.12e-66	24	532	20	542	L-ascorbate oxidase
274556	laccase	1.43e-58	46	549	22	528	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.
259977	CuRO_3_MCO_like_4	6.06e-58	377	536	3	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
UPK99837.1|AA1	5.41e-199	10	556	81	620
UNI22443.1|AA1	7.09e-198	1	556	75	626
ATY65896.1|AA1	7.16e-195	10	558	91	637
QKD61545.1|AA1	5.76e-194	1	557	67	617
QYT05468.1|AA1	7.07e-193	10	558	93	638

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	7.91e-56	40	532	80	538	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	1.52e-55	40	532	80	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
1AOZ_A	4.66e-55	25	537	1	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	2.36e-54	26	557	1	501	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]
5LM8_A	2.88e-51	33	534	32	502	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	2.61e-65	27	556	61	578	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	1.89e-64	27	556	61	578	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	5.49e-64	27	540	61	563	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|K7NCS2|FETC_EPIFE	1.83e-63	24	558	19	516	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	3.73e-61	33	532	82	547	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000057	0.000004

TMHMM  Annotations     

There is no transmembrane helices in RL4_JR_04067-RA-p1.