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Database: UniProt
Entry: A0A1Y3VCR5_9BACT
LinkDB: A0A1Y3VCR5_9BACT
Original site: A0A1Y3VCR5_9BACT 
ID   A0A1Y3VCR5_9BACT        Unreviewed;       165 AA.
AC   A0A1Y3VCR5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE            EC=1.16.3.2 {ECO:0000256|RuleBase:RU361145};
GN   ORFNames=B5G16_07060 {ECO:0000313|EMBL:OUN58881.1};
OS   Alistipes sp. An66.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1965650 {ECO:0000313|EMBL:OUN58881.1, ECO:0000313|Proteomes:UP000195674};
RN   [1] {ECO:0000313|Proteomes:UP000195674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An66 {ECO:0000313|Proteomes:UP000195674};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Iron-storage protein. {ECO:0000256|RuleBase:RU361145}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide;
CC         Xref=Rhea:RHEA:11972, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:78619; EC=1.16.3.2;
CC         Evidence={ECO:0000256|RuleBase:RU361145};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361145}.
CC   -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily.
CC       {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:OUN58881.1}.
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DR   EMBL; NFHT01000008; OUN58881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3VCR5; -.
DR   OrthoDB; 9801481at2; -.
DR   Proteomes; UP000195674; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   CDD; cd01055; Nonheme_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; IPR008331; Ferritin_DPS_dom.
DR   InterPro; IPR041719; Ferritin_prok.
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   Cytoplasm {ECO:0000256|RuleBase:RU361145};
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   Reference proteome {ECO:0000313|Proteomes:UP000195674}.
FT   DOMAIN          1..136
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000259|PROSITE:PS50905"
SQ   SEQUENCE   165 AA;  18699 MW;  4E64D67D693A5DD5 CRC64;
     MNAQINAELW SAYLYLSMSM DAEAKGLKGV ANWFYVQFQE EQDHARILMN YILSRDEKVT
     LLPIEEVRTE WASPLEMFQD TLTHEKKVTA MINNLAAIAA EDKDFASSNM LVWFVDEQVE
     EEESARGMIT ACEAVEGNKF GLYMLDKELA ARVYTQAAPL ASAND
//
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