CAZyme Information: SOCG_02962-t26_1-p1

Basic Information

• Species: Schizosaccharomyces octosporus
• Lineage: Ascomycota; Schizosaccharomycetes; ; Schizosaccharomycetaceae; Schizosaccharomyces; Schizosaccharomyces octosporus
• CAZyme ID: SOCG_02962-t26_1-p1
• CAZy Family: GT20
• CAZyme Description: iron transport multicopper oxidase Fio1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
607		68835.71	4.4033

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SoctosporusyFS286	5355	483514	361	4994

• Gene Location: location=KE503206:764871-766694(+)

Full Sequence      

MFLPSFGLVLCTLVGSALAKTRLFEWNVTDIDNLDVDKSGHPRWVMGVNNQWPIEPLVVD
YGDQVIIKMSNHLRDNRTCSLHSHGIFQRHNGYMDGVPQMTQCSIPPGSTYYYNFTADQT
GTYWVHSHDMSQYPDGLRTSFVINNPNEPYDYDEDYIISLTDWYYEPFYKLVPEQFVSWH
NPTGAEPVPDTGLINDSINSTFKMEPGKTYRLRFVNLGAFNNYDIMLEDHNMTIIEVDGI
YTKPQEVSSIHITTAQRYSVLVTAKNSTDRNYAMTAYMDESLFDQVPPNYNPNITAWLSY
NSNSPNNYALPVDEINSYDDAELQPLYDVNWGEADHNVSLWFDFFTLENGANYAEINGKS
FKYPKVPGLMIANSTNYDDYNMKPITYGPYTNAFIFDYNQTVDVVIDNHDTGKHPFHLHG
HVFQVLERGDENAGEYNDQTEHKVYDHPIRRDTIEIHPGSFVRLRFLADNPGAWLLHCHI
EWHMESGLVATFLEAPDRVPYITAPEFVRRQCIMQNIEVSGNGAGNTYNISNLTGAPAPP
GEMPSGWTSKAIASVAMCVLAACIGMGSIVFYGIQVQPLTTEEPDDEEDIKAAVKENAAD
IMSPSEM

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	43	376	2.8e-130	0.9881305637982196

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	1.12e-87	45	496	54	450	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].
259966	CuRO_3_Fet3p	1.80e-75	335	496	3	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	6.44e-71	154	302	1	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.
274555	ascorbase	1.19e-67	45	499	22	528	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	2.00e-65	2	499	5	551	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
NP_594494.1|AA1_2	0.0	4	599	8	602
BAE61606.1|AA1_2	2.21e-171	16	588	27	595
UDD60384.1|AA1_2	9.06e-171	16	588	17	585
QMW43510.1|AA1_2	1.73e-169	16	572	17	571
QMW31452.1|AA1_2	1.73e-169	16	572	17	571

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.78e-130	20	546	1	534	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]
1V10_A	4.59e-67	3	504	1	499	Chain A, Laccase [Rigidoporus microporus]
3KW7_A	1.68e-62	28	497	5	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]
2QT6_A	2.97e-62	31	512	10	487	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
1KYA_A	4.23e-62	31	497	10	473	Chain A, Laccase [Trametes versicolor],1KYA_B Chain B, Laccase [Trametes versicolor],1KYA_C Chain C, Laccase [Trametes versicolor],1KYA_D Chain D, Laccase [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q09920|FIO1_SCHPO	0.0	4	599	8	602	Iron transport multicopper oxidase fio1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=fio1 PE=3 SV=1
sp|E9R598|FETC_ASPFU	2.77e-164	19	574	20	573	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	9.65e-156	9	579	10	580	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	1.77e-147	17	605	20	616	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|Q6CII3|FET3_KLULA	1.63e-138	2	583	8	597	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000376	0.999600	CS pos: 19-20. Pr: 0.9793

TMHMM  Annotations     

Start	End
552	574