CAZyme Information: TSTA_120560-t26_1-p1

Basic Information

• Species: Talaromyces stipitatus
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces stipitatus
• CAZyme ID: TSTA_120560-t26_1-p1
• CAZy Family: GT31
• CAZyme Description: laccase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
691	EQ962655|CGC15	77337.66	6.0146

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=EQ962655:2588829-2591203(-)

Full Sequence      

MQRRLSKRQQQQDATKSPDATAQPVEQQQKTEANDKRRGSKTTLHTPSILIALVCILPFL
ATVVLFVRYYYESNNDDSINRLSNSLHDHESISSTLKYDNRIHENGRLRPEDHIHRGAIT
QTLNWSVTAGQRRPDGVDKRIYLINDMFPGPSIEARSGDTLQILVHNNLEDEQISLHWHG
LNMRGANTMDGVIGVTQCGIQPGQSFWYNFTISETQSGTFWYHAHSAVQRADGLYGSLVV
HRPDSTLVSPNERSEMVSDSVKYGYDKEIVLMIGDWYHRTATDVASWYLWWGSMGYEPVP
DSLLVNGAGRFNCSRAVRARPLDCIGSADEMPPLILDGNSSYRVRVVNTGSLTGIILGFA
PGTSIQVITIDGGNPVEMEAVDGGRSSVGILFPGQRVDFVLRPLKGQTSWMTVKMDDSYV
SPYTLYKTAELSVSSDFTIGNPALVPQQSFPIFQTPLPSDSLPSSPTAQSNNTNDIEEDD
IININTLPSTRTLLSSLPPKSEQTHIVYTKVEKLSRLDNIPHGFFNRTTWKIQSDPPYPL
LGLPRNQWDKHQFAVSTGNKNGWVDLVVNNLDEGAHPFHLHGYNFYVVDIYESPEGSGRW
GSYNPWTSPSFNENIDPYDLTKAVLRDTVQIPRRGYAVLRFKADNPGVWLFHCHVMWHLA
GGMAMVIDSGSGDDSVAHEPWLAEEGMECRV

Enzyme Prediction     

No EC number prediction in TSTA_120560-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	137	664	8.5e-92	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	9.30e-68	123	670	4	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.
177843	PLN02191	1.98e-65	113	670	17	547	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	6.16e-61	507	669	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.
215324	PLN02604	1.15e-60	125	670	29	547	oxidoreductase
274556	laccase	1.16e-60	139	672	22	524	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA16928.1|AA1	0.0	1	691	1	690
QKX62088.1|AA1	1.37e-281	32	691	21	675
UPX44859.1|AA1	7.32e-189	108	688	80	646
QRD88142.1|AA1	2.89e-185	32	670	17	616
QMW25836.1|AA1	2.89e-185	32	670	17	616

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	3.48e-55	120	688	2	498	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]
3V9E_A	4.98e-49	119	665	66	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
1AOZ_A	1.11e-48	125	670	8	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]
3SQR_A	1.28e-48	119	665	66	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]
3KW7_A	7.86e-48	118	673	1	476	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RMG9|FET3_GIBZE	1.14e-66	118	663	22	490	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
sp|K7NCS2|FETC_EPIFE	2.04e-63	118	663	20	489	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|Q6CII3|FET3_KLULA	1.25e-56	118	667	25	503	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|W3X7K0|PFMAD_PESFW	5.16e-56	118	667	20	487	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1
sp|J9VY90|LAC1_CRYNH	1.04e-55	120	681	61	574	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999894	0.000125

TMHMM  Annotations     

Start	End
49	71