CAZyme Information: SMAC_03279-t26_1-p1

Basic Information

• Species: Sordaria macrospora
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Sordaria; Sordaria macrospora
• CAZyme ID: SMAC_03279-t26_1-p1
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
600	NW_003546240|CGC1	66218.31	4.3933

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Smacrosporak-hell	11311	771870	484	10827

• Gene Location: location=NW_003546240:95771-97689(-)

Full Sequence      

MSDLNLTMHWHGLTQRMAPFADGTPQASQWPIPPGHFFDYEVATETGDAGTYFYHSHVAM
QATTCSGPLVVDDCSSCPFDYDDERILYFQDYLRESDQKMAQDVQGVPYRWPGGTNGIVL
NGRSIPIDSKVTPGPSGQNGVFGGGHASNPEGHPSPGVKQIANEEGCTLPVIDVEPGKTY
RFRIAGATGLSLLTMAIEDHAEFRVIQADGMQYLRPVDTRDLQLGPGQRFDVLFKAKTIE
ELAADGNKTTYYLQFETRSRPEQLRGYAVIRYDDNVAVPEEPAIPPVDLPANPNGWLEYT
FEPLTGVVAPAAEEVTRRITLEVVQLKDSDTGRQIWQLSGISWTEESNKVPLLVDIYQRG
RNAMPNYTVAKGNKGWDTKTGSFPIKLGEVVELVIQNTGTMSSDIGFVEAHPFHVHSQHV
FDIGSGPGVYDAEANNAKIERLGYKPTLRDTTMLYRYQDTVDPGQAAGWRAWRLKATAPG
VWMVHCHILAHMVMGMQAVFVVGNEWDIKEIAPNDVAGYLDYGGSVYGNSTFAPSPNEYF
SDVTDKCGVYAQSEEDDHEPSDYNSTSGYNSTSEYSNSTSDNDSTTEDEPETDDSVPSMH

Enzyme Prediction     

No EC number prediction in SMAC_03279-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	4	497	4.7e-69	0.88268156424581

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	0.0	1	509	57	538	L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized.
259962	CuRO_3_AAO_like_2	2.22e-84	314	503	1	188	The third cupredoxin domain of Ascorbate oxidase homologs. This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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 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.
274555	ascorbase	2.46e-68	5	503	54	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.
259941	CuRO_2_AAO_like_2	3.78e-63	83	272	1	161	The second cupredoxin domain of plant Ascorbate oxidase homologs. This family includes plant laccases similar to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couples oxidation of substrates with reduction of dioxygen to water. 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 2 of 3-domain MCOs has lost the ability to bind copper.
177843	PLN02191	4.01e-57	1	503	72	547	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VBB79804.1|AA1	2.31e-229	1	554	79	661
CDP28189.1|AA1	2.38e-222	1	547	79	647
QUC24037.1|AA1	5.74e-177	5	546	80	593
QRD04919.1|AA1	5.74e-161	1	542	219	722
SMR54647.1|AA1	4.90e-156	1	546	108	618

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	6.76e-52	6	505	57	526	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]
6KLG_A	9.04e-29	5	504	55	532	Crystal Structure of the Zea Mays laccase 3 [Zea mays],6KLI_A Crystal Structure of the Zea Mays laccase 3 complexed with sinapyl [Zea mays],6KLJ_A Crystal Structure of the Zea Mays laccase 3 complexed with coniferyl [Zea mays]
1ZPU_A	7.08e-23	1	501	52	478	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]
1HFU_A	5.96e-22	7	500	62	466	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	5.99e-22	7	500	62	466	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	1.17e-225	1	556	79	647	Laccase-like multicopper oxidase 1 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=LMCO1 PE=1 SV=1
sp|I1RF64|AURL2_GIBZE	2.93e-129	3	542	78	599	Multicopper oxidase aurL2 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=aurL2 PE=2 SV=1
sp|Q0D1P3|TERE_ASPTN	8.69e-126	8	540	1	527	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P14133|ASO_CUCSA	1.33e-52	6	503	92	560	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|P37064|ASO_CUCPM	3.48e-51	6	505	57	526	L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.998515	0.001507

TMHMM  Annotations     

There is no transmembrane helices in SMAC_03279-t26_1-p1.