CAZyme Information: TSTA_082450-t26_1-p1

Basic Information

• Species: Talaromyces stipitatus
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces stipitatus
• CAZyme ID: TSTA_082450-t26_1-p1
• CAZy Family: GH36
• CAZyme Description: multicopper oxidase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
360		40180.13	4.6243

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TstipitatusATCC10500	12629	441959	146	12483

• Gene Location: location=EQ962653:534775-536181(-)

Full Sequence      

MTISSPRLWYTLLANLPLAIAIRQPHYILRIASENITVACRTRLSAVVNGTVPGPAIYLK
ENQTTWVRVYNDLLHDNTTMFVAPYSDGTPQASQWLIKAQNFFDYELRPEIGAAGSSFYH
FHVGFQAVTASGPLIVEEADGEVPYDYDEDRMISFSELFNNTDKAVEDALTAPLKRLQVN
GNGFPALLGNETDAFGKLPDNAPPSSSNDTCHPEIIQVEPNKTYRFRAIGGVALSPLVFT
LEDHRNLTIVAADSYYTQPASTDIIQMGGGQRYDFLLRTKTEDELKVLGKTDFWVQIESR
YREENSTFYALLSYTSNQSASAAPSSPPGQHPVSIPYSLQDWMEYTLEPLNQMGFQALIK

Enzyme Prediction     

No EC number prediction in TSTA_082450-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	41	325	7.9e-57	0.7597765363128491

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	5.13e-123	24	352	8	334	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	1.39e-68	149	314	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.
259916	CuRO_1_AAO_like_2	4.53e-40	25	138	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.
274555	ascorbase	1.27e-31	40	317	17	300	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	1.25e-26	40	307	39	312	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA14799.1|AA1	1.72e-168	1	357	1	379
QKX59572.1|AA1	6.02e-138	24	357	31	380
QIW98575.1|AA1	1.65e-111	25	357	29	379
QBZ60051.1|AA1	1.48e-86	24	351	29	354
QDS68174.1|AA1	1.81e-83	24	351	34	357

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6KLG_A	1.66e-16	23	347	2	346	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]
3V9E_A	1.89e-12	27	277	70	315	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.89e-12	27	277	70	315	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]
3X1B_A	4.17e-12	42	350	42	330	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	1.71e-11	42	277	22	247	Chain A, LACCASE 1 [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q0D1P3|TERE_ASPTN	2.13e-86	83	360	11	286	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|I1RF64|AURL2_GIBZE	5.02e-79	24	360	27	360	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|G2QFD0|LMCO1_MYCTT	8.35e-71	25	351	31	392	Laccase-like multicopper oxidase 1 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=LMCO1 PE=1 SV=1
sp|Q40588|ASO_TOBAC	4.51e-22	48	338	54	349	L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1
sp|M4DUF2|ASO_BRARP	3.59e-21	40	332	36	333	L-ascorbate oxidase OS=Brassica rapa subsp. pekinensis OX=51351 GN=AO PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.563870	0.436123

TMHMM  Annotations     

There is no transmembrane helices in TSTA_082450-t26_1-p1.