(data stored in SCRATCH zone)

SWISSPROT: A4F6G2_SACEN

ID   A4F6G2_SACEN            Unreviewed;       163 AA.
AC   A4F6G2;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 69.
DE   SubName: Full=Starvation-inducible DNA-binding protein {ECO:0000313|EMBL:PFG93439.1};
DE   SubName: Full=Starvation-response DNA binding protein {ECO:0000313|EMBL:CAL99636.1};
GN   OrderedLocusNames=SACE_0287 {ECO:0000313|EMBL:CAL99636.1};
GN   ORFNames=A8924_0681 {ECO:0000313|EMBL:PFG93439.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99636.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99636.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99636.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93439.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93439.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Dps family. {ECO:0000256|RuleBase:RU003875,
CC       ECO:0000256|SAAS:SAAS00563186}.
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DR   EMBL; AM420293; CAL99636.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93439.1; -; Genomic_DNA.
DR   RefSeq; WP_009946964.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0287; -.
DR   EnsemblBacteria; CAL99636; CAL99636; SACE_0287.
DR   KEGG; sen:SACE_0287; -.
DR   eggNOG; ENOG4107Y5Q; Bacteria.
DR   eggNOG; COG0783; LUCA.
DR   HOGENOM; HOG000273542; -.
DR   KO; K04047; -.
DR   OMA; WFISAET; -.
DR   OrthoDB; 1742631at2; -.
DR   BioCyc; SERY405948:SACE_RS01405-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0016722; F:oxidoreductase activity, oxidizing metal ions; IEA:InterPro.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; 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; PTHR42932; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   PIRSF; PIRSF005900; Dps; 1.
DR   PRINTS; PR01346; HELNAPAPROT.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   PROSITE; PS00818; DPS_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F6G2.
DR   SWISS-2DPAGE; A4F6G2.
KW   DNA-binding {ECO:0000313|EMBL:PFG93439.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN          25..162
FT                   /note="Ferritin"
FT                   /evidence="ECO:0000259|Pfam:PF00210"
SQ   SEQUENCE   163 AA;  17892 MW;  F458A7055EB3D143 CRC64;
     MATKTAAKAP ITSALNDSDR DVTGKALQGT LLDLIDLHLV AKQAHWNVVG KFFRDVHLQL
     DELIDTARAF ADDVAERASA IGVSPDGRSS TVASGSGMPK FDAGWKNDRE VIEYIVSALS
     ELISRVRMRI DETDKTDLVT QDLLLSIASE LEKSHWMWQA QLA
//

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