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Database: UniProt
Entry: A0A0D6KQG9_9CYAN
LinkDB: A0A0D6KQG9_9CYAN
Original site: A0A0D6KQG9_9CYAN 
ID   A0A0D6KQG9_9CYAN        Unreviewed;       161 AA.
AC   A0A0D6KQG9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Ferritin-like domain protein {ECO:0000313|EMBL:EKF01711.1};
GN   ORFNames=FDUTEX481_07582 {ECO:0000313|EMBL:EKF01711.1};
OS   Tolypothrix sp. PCC 7601.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF01711.1, ECO:0000313|Proteomes:UP000032761};
RN   [1] {ECO:0000313|EMBL:EKF01711.1, ECO:0000313|Proteomes:UP000032761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX   PubMed=25953173;
RA   Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA   Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA   Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA   Kehoe D.M., Weinstock G.M.;
RT   "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT   Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT   PCC 7601.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- SIMILARITY: Belongs to the Dps family. {ECO:0000256|ARBA:ARBA00009497,
CC       ECO:0000256|RuleBase:RU003875}.
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:EKF01711.1}.
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DR   EMBL; AGCR01000037; EKF01711.1; -; Genomic_DNA.
DR   RefSeq; WP_045870784.1; NZ_JH930361.1.
DR   AlphaFoldDB; A0A0D6KQG9; -.
DR   STRING; 1188.FDUTEX481_07582; -.
DR   PATRIC; fig|1188.3.peg.4598; -.
DR   HOGENOM; CLU_098183_2_1_3; -.
DR   OrthoDB; 9797023at2; -.
DR   Proteomes; UP000032761; Unassembled WGS sequence.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0016722; F:oxidoreductase activity, acting on metal ions; IEA:InterPro.
DR   CDD; cd01043; DPS; 1.
DR   Gene3D; 1.20.1260.10; -; 1.
DR   InterPro; IPR002177; DPS_DNA-bd.
DR   InterPro; IPR023188; DPS_DNA-bd_CS.
DR   InterPro; IPR012347; Ferritin-like.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
DR   PANTHER; PTHR42932:SF3; DNA PROTECTION DURING STARVATION PROTEIN; 1.
DR   PANTHER; PTHR42932; GENERAL STRESS PROTEIN 20U; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   PIRSF; PIRSF005900; Dps; 1.
DR   PRINTS; PR01346; HELNAPAPROT.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00818; DPS_1; 1.
DR   PROSITE; PS00819; DPS_2; 1.
PE   3: Inferred from homology;
FT   DOMAIN          22..160
FT                   /note="Ferritin/DPS protein"
FT                   /evidence="ECO:0000259|Pfam:PF00210"
SQ   SEQUENCE   161 AA;  18074 MW;  723554196FCE6CC9 CRC64;
     MPSKPETLNI GIDDASRAKI AEGLSRLLAD TYTLYLKTHN FHWNVTGPMF QTLHLMFETQ
     YTELALAVDL IAERIRALGY PAPGTYSEYV KLSSIPETPG VPKATEMIRL LVAGQEAVVR
     TARSVFPVVD EVNDEPTADL LTQRMQVHEK TAWMLRSLLE E
//
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