CAZyme Information: TREMEDRAFT_63702-t26_1-p1

Basic Information

• Species: Tremella mesenterica
• Lineage: Basidiomycota; Tremellomycetes; ; Tremellaceae; Tremella; Tremella mesenterica
• CAZyme ID: TREMEDRAFT_63702-t26_1-p1
• CAZy Family: GT24
• CAZyme Description: multi-copper oxidase laccase-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
643	JH711536|CGC6	71838.38	4.4499

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmesentericaDSM1558	8309	578456	1	8308

• Gene Location: location=JH711536:83613-86856(+)

Full Sequence      

MPHILLSLVILLLLLSLECDTCKLTELSEARLAIFHYRTTSTWLEFQCFSTVRFPLAYWA
LQLVSCDDCQPRQSVVINGTSPGPLLTFQEGQHYWVRVYNDLPDQNTTVHFHGFSQYASP
FSDGTPQASGWPIPPGDFYDYEFQLEYGFYGTYWYHSHVQNQVGTAQGPVIVEQVNKTDC
PVEYDEEIVMMISDYYHATDDVIIAGLLNTTVFGWLGEPQSLLVNGNAQGVCNASVLLPG
QTCGTGCGNNKQLVKPSTRYRVRIISSTSLSYVGLALEGHNMTVFEVDGTYVEPLPVTSL
EMGVGQRYSVLIETMDNPTQSDWYWRLRTMWRPTRVNGSAVWSYDSSATSDSFTRNSISQ
EPTPVGLNETVPLPDEVFGWVSGDFKQWNQSEYPPSDEEVTRIIILNAQQMVDMQGFRWS
INGQLNNSTLPNVPYLIQLYNETEDKRMPNYTTALQNGGYDIGSNTYPAKLGEVLDIVIQ
NRAGPTSGMVEAHPFHTHGAKYWDMGYGPGNFSYTALNTSRASMKGSPYLRDTSVVYSGP
GESYNSSVIDDDGPGGWRLFRIKVSDPGAWLIHCHITAHQIMGMQALFMYGAEDLPAIPD
SLLAEYLTYGGGSDSFDSHTYVPTSYFETMASLRIRDKGEVDG

Enzyme Prediction     

No EC number prediction in TREMEDRAFT_63702-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	72	585	1.2e-86	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	1.02e-160	69	595	24	537	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	8.48e-97	399	591	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	7.14e-89	68	604	16	537	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	1.54e-80	43	603	6	559	oxidoreductase
177843	PLN02191	3.91e-77	58	608	34	564	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS19632.1|AA1	4.02e-122	67	613	44	563
QMW38925.1|AA1	5.98e-121	69	627	53	586
QMW26845.1|AA1	5.98e-121	69	627	53	586
UDD54641.1|AA1	5.98e-121	69	627	53	586
QRD81157.1|AA1	6.16e-121	69	627	54	587

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	5.19e-68	58	604	14	537	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]
1V10_A	4.90e-36	67	599	38	495	Chain A, Laccase [Rigidoporus microporus]
5Z1X_A	2.94e-35	72	597	22	472	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]
3V9E_A	1.40e-34	68	589	82	541	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	3.44e-34	68	589	82	541	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	3.27e-117	69	628	46	632	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	3.77e-108	68	613	42	583	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	2.32e-80	109	623	1	521	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P24792|ASO_CUCMA	2.50e-67	58	604	44	567	L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2
sp|P37064|ASO_CUCPM	2.67e-67	58	604	14	537	L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000245	0.999746	CS pos: 21-22. Pr: 0.9347

TMHMM  Annotations     

There is no transmembrane helices in TREMEDRAFT_63702-t26_1-p1.