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Database: UniProt
Entry: A0A1L9SY59_9EURO
LinkDB: A0A1L9SY59_9EURO
Original site: A0A1L9SY59_9EURO 
ID   A0A1L9SY59_9EURO        Unreviewed;       231 AA.
AC   A0A1L9SY59;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   03-MAY-2023, entry version 15.
DE   RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE            EC=1.16.3.1 {ECO:0000256|RuleBase:RU361145};
GN   ORFNames=ASPSYDRAFT_73949 {ECO:0000313|EMBL:OJJ52162.1};
OS   Aspergillus sydowii CBS 593.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ52162.1, ECO:0000313|Proteomes:UP000184356};
RN   [1] {ECO:0000313|Proteomes:UP000184356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC       Important for iron homeostasis. Iron is taken up in the ferrous form
CC       and deposited as ferric hydroxides after oxidation.
CC       {ECO:0000256|RuleBase:RU361145}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC         Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC         Evidence={ECO:0000256|RuleBase:RU361145};
CC   -!- SIMILARITY: Belongs to the ferritin family.
CC       {ECO:0000256|ARBA:ARBA00007513, ECO:0000256|RuleBase:RU361145}.
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DR   EMBL; KV878604; OJJ52162.1; -; Genomic_DNA.
DR   STRING; 1036612.A0A1L9SY59; -.
DR   VEuPathDB; FungiDB:ASPSYDRAFT_73949; -.
DR   OrthoDB; 2344109at2759; -.
DR   Proteomes; UP000184356; Unassembled WGS sequence.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   Gene3D; 1.20.1260.10; -; 1.
DR   InterPro; IPR001519; Ferritin.
DR   InterPro; IPR012347; Ferritin-like.
DR   InterPro; IPR009040; Ferritin-like_diiron.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
DR   PANTHER; PTHR11431; FERRITIN; 1.
DR   PANTHER; PTHR11431:SF75; FERRITIN; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361145};
KW   Iron storage {ECO:0000256|ARBA:ARBA00022434,
KW   ECO:0000256|RuleBase:RU361145};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361145};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361145};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184356}.
FT   DOMAIN          25..177
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000259|PROSITE:PS50905"
SQ   SEQUENCE   231 AA;  26178 MW;  8510A7B718780834 CRC64;
     MATEEAKKII ADISSQDIDQ WLQVKSMTPE LQESVRGHIH QELTSWLFFR KLAADCSRSN
     IALHGFAQLW ERSAAECLID FHWLEKYFVS RGGRSKPSAI EPTQVDWPDN PVEPVGPCKE
     XFLVEKRLLE DLERLAALAN KCGDSSLQDA IETRFLRKEV KHVKDLGDLL QQVVRVSKQP
     GLGIYLLDKE LRAHGGSIPW ANMNNPDKHD NVVRDNVVRG ITASVRDGLE F
//
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