CAZyme Information: TSTA_060530-t26_1-p1

Basic Information

• Species: Talaromyces stipitatus
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces stipitatus
• CAZyme ID: TSTA_060530-t26_1-p1
• CAZy Family: GH20
• CAZyme Description: multicopper oxidase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
455	EQ962652|CGC12	50616.69	4.6184

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=EQ962652:224759-226613(+)

Full Sequence      

MSQEHIGTIVSIVPSPIWIIVNMIICHSPSQYVDGIRGPILVNDPLSPYAGQIDGELVVT
LSDWYHEQGASLQVYYLSLPGNPNALEPIPMSALMNDQLWPTFSVLPNKTYFVRVLNIAG
YAQFYFHIDGHNMTIIQADGVYTDPQQVQDLYLATGQRYGVLLHTLPTANQNYAILGAMD
IAGFPRSAPPPANPNVTGVLVYDPFLSIPSTPVVQQFSTFDDFCLNPFDKIPLLYPPNKE
IVLNLSTFSQTVPLNEQNRGGFNNITYITQRVPSLYTALSGGLYALNPIVYGNHSNPFVL
SLGDFVETTIYNYDTGLHPIHTHGHTVQLVARTGSECNYRSIPMRRDTWMEPRWNSSDPN
HPSTVVRFIADNPGIWFFHCHMEWHLVAGMDIILVEDPLQIQTGQPDIPLSMKLICLEQG
IPLMGNAAGNWINFLDLTGEVNVAPMECGSDYPPC

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	26	281	9.5e-68	0.7359050445103857

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259966	CuRO_3_Fet3p	4.48e-72	236	398	1	160	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains 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 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.
259945	CuRO_2_Fet3p_like	6.92e-57	56	204	2	148	The second Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains 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.
225043	SufI	6.73e-39	27	390	133	442	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
274555	ascorbase	5.29e-37	27	396	104	523	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.
395317	Cu-oxidase	7.46e-35	55	204	1	145	Multicopper oxidase. Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX61482.1|AA1_2	5.92e-122	27	454	130	629
QOX58957.1|AA1_2	1.13e-110	27	447	127	544
QYT01328.1|AA1_2	3.09e-110	27	454	126	550
QIW96265.1|AA1_2	2.18e-109	27	449	127	545
QKD56481.1|AA1_2	6.32e-108	27	449	127	547

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	7.55e-87	27	440	107	524	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]
3KW7_A	1.13e-40	27	416	111	491	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]
1GYC_A	6.62e-38	27	416	111	488	Chain A, LACCASE 2 [Trametes versicolor]
3X1B_A	1.21e-37	27	416	132	510	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]
1V10_A	1.21e-37	27	411	132	497	Chain A, Laccase [Rigidoporus microporus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RMG9|FET3_GIBZE	4.44e-102	27	440	128	539	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|E9R598|FETC_ASPFU	1.23e-100	27	449	126	545	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|K7NCS2|FETC_EPIFE	2.53e-97	27	440	126	538	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|Q96WT3|FET3_CANGA	3.74e-88	27	440	124	545	Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1
sp|P78591|FET3_CANAX	5.68e-88	27	449	128	551	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.996561	0.003461

TMHMM  Annotations     

There is no transmembrane helices in TSTA_060530-t26_1-p1.