CAZyme Information: MELLADRAFT_90334-t26_1-p1

Basic Information

• Species: Melampsora larici-populina
• Lineage: Basidiomycota; Pucciniomycetes; ; Melampsoraceae; Melampsora; Melampsora larici-populina
• CAZyme ID: MELLADRAFT_90334-t26_1-p1
• CAZy Family: GT39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
514	GL883125|CGC1	58050.56	7.8649

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Mlarici-populina98AG31	16380	747676	8	16372

• Gene Location: location=GL883125:882282-884397(-)

Full Sequence      

MKTLTRTLSFIKTFAFVLLILSWTCGVAKAHWHPNAILRISKGFLAGDCTVRPSVIINGT
SPGPELRFKEGQRVWIRVYNDLPDQNTTLHFHGLSQFGSPFADGTPATSQFQLESGSAGT
YMYHTHVDFQLVTAHGAFIVEDEGPPPYSYDEELTLLFATPFQWPGEPSSLTVNGNALAH
CDPSRGYRCSGECHQHVMNLKPSRTYRVRFIGITALTFLYIGLEDHHEFEIIEADAAYLK
PTRTDHLELHSGQRYSFLLRTKSRAELRALNKTTFWGRIESRWRPIRDKGSFVITYDRGY
EQELATFPPRNLARRVFLPDERVSWVNRAFAPLRQHDVSPTEQEVTRRIMIRAQQLTTAG
GGSQYFVNGQAAYLNPSSLQPDYGQAEVNHGYDSSTSSFPLRLGETVEIVIFNFASSLGE
AEAHPWHFHGQHPFMVAQGYGKYSPEAARRIEAQNFVKYGGLPHRRDTQVILPGQGATYE
DEKIAEGTLSSWIVLRMRVSVSGAFLVHCHIQRV

Enzyme Prediction     

No EC number prediction in MELLADRAFT_90334-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	52	512	8.1e-58	0.952513966480447

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	4.46e-142	34	511	9	517	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.
259941	CuRO_2_AAO_like_2	5.21e-89	134	296	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.
274555	ascorbase	8.90e-53	44	512	12	510	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.
259962	CuRO_3_AAO_like_2	6.03e-51	344	512	1	174	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.
259916	CuRO_1_AAO_like_2	3.54e-50	34	142	1	117	The first 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 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
QDS68174.1|AA1	7.82e-101	18	511	14	540
QBZ60051.1|AA1	2.15e-95	18	511	9	549
UPL03177.1|AA1	6.55e-93	27	513	21	545
QPC76805.1|AA1	6.90e-93	29	513	20	545
QPC67932.1|AA1	1.36e-92	34	513	28	545

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.58e-42	44	512	14	510	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	2.08e-29	52	512	22	466	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	9.17e-26	34	512	4	452	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]
3X1B_A	6.49e-25	28	512	19	478	Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus],3X1B_B Crystal structure of laccase from Lentinus sp. at 1.8 A resolution [Lentinus]
1HFU_A	1.48e-23	38	512	9	455	Chain A, LACCASE 1 [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	1.36e-94	34	511	31	579	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	3.69e-92	29	513	20	545	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	1.32e-57	89	510	1	473	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P14133|ASO_CUCSA	4.23e-44	44	512	49	546	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|Q40588|ASO_TOBAC	6.58e-43	27	512	37	537	L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.002998	0.996972	CS pos: 30-31. Pr: 0.9180

TMHMM  Annotations     

Start	End
13	35