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Database: UniProt
Entry: K9YN42_CYASC
LinkDB: K9YN42_CYASC
Original site: K9YN42_CYASC 
ID   K9YN42_CYASC            Unreviewed;       121 AA.
AC   K9YN42;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Ferredoxin (2Fe-2S) {ECO:0000313|EMBL:AFZ47877.1};
GN   OrderedLocusNames=Cyast_1924 {ECO:0000313|EMBL:AFZ47877.1};
OS   Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Cyanobacterium.
OX   NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ47877.1, ECO:0000313|Proteomes:UP000010483};
RN   [1] {ECO:0000313|Proteomes:UP000010483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC       {ECO:0000256|ARBA:ARBA00007874}.
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DR   EMBL; CP003940; AFZ47877.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9YN42; -.
DR   STRING; 292563.Cyast_1924; -.
DR   KEGG; csn:Cyast_1924; -.
DR   PATRIC; fig|292563.3.peg.2014; -.
DR   eggNOG; COG0633; Bacteria.
DR   HOGENOM; CLU_082632_7_3_3; -.
DR   BioCyc; CSTA292563:G1353-1931-MONOMER; -.
DR   Proteomes; UP000010483; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR010241; Fd_pln.
DR   NCBIfam; TIGR02008; fdx_plant; 1.
DR   PANTHER; PTHR43112; FERREDOXIN; 1.
DR   PANTHER; PTHR43112:SF10; FERREDOXIN C 2, CHLOROPLASTIC; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022714};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010483};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          4..96
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   121 AA;  13805 MW;  1B60704D215B9FE3 CRC64;
     MRNYKVTIHN RQKNTTQTVV VPEDQYILRT AENQDADAPF SCRNGACTTC AVRVLEGDIY
     QPEAMGLSPD LQKQGYALLC VSYPRSDLVV ETQDEDEVYE LQFGRYFGRG KVRFGFPIED
     D
//
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