ID A0A098VVW2_9MICR Unreviewed; 206 AA.
AC A0A098VVW2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 03-MAY-2023, entry version 28.
DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE EC=1.16.3.1 {ECO:0000256|RuleBase:RU361145};
GN ORFNames=DI09_110p20 {ECO:0000313|EMBL:KGG53092.1};
OS Mitosporidium daphniae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG53092.1, ECO:0000313|Proteomes:UP000029725};
RN [1] {ECO:0000313|EMBL:KGG53092.1, ECO:0000313|Proteomes:UP000029725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGP3 {ECO:0000313|EMBL:KGG53092.1,
RC ECO:0000313|Proteomes:UP000029725};
RC TISSUE=Spores {ECO:0000313|EMBL:KGG53092.1};
RA Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA Ebert D.;
RT "A new species of microsporidia sheds light on the evolution of extreme
RT parasitism.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGG53092.1}.
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DR EMBL; JMKJ01000012; KGG53092.1; -; Genomic_DNA.
DR RefSeq; XP_013239528.1; XM_013384074.1.
DR AlphaFoldDB; A0A098VVW2; -.
DR GeneID; 25258016; -.
DR VEuPathDB; MicrosporidiaDB:DI09_110p20; -.
DR HOGENOM; CLU_065681_4_0_1; -.
DR OrthoDB; 4611704at2759; -.
DR Proteomes; UP000029725; 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 CDD; cd01056; Euk_Ferritin; 1.
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; IPR014034; Ferritin_CS.
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; PS00204; FERRITIN_2; 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:UP000029725}.
FT DOMAIN 39..189
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
SQ SEQUENCE 206 AA; 23007 MW; 11765C5502C6A10F CRC64;
MAGDETQRRR KSTRQAIDRK SDKNAYLICH SLPMYSSKQN FSEACETALN KQVNMELGAS
YSYMSMSVFC SKDGVALPGL AAYCAKMSLE ERDHALMLQD YIIKRGGQVT YDTIAPHPKA
SAWKSALEIV EAMLELEKSV NVSLLDLNKL ASLKEDAHLS DFIEGTFLSE QVDSIKELVD
MLVQLQRAGV DGLGLYIWDQ NLLSKN
//