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Database: UniProt
Entry: F0LPH8_VIBFN
LinkDB: F0LPH8_VIBFN
Original site: F0LPH8_VIBFN 
ID   F0LPH8_VIBFN            Unreviewed;       556 AA.
AC   F0LPH8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   10-APR-2019, entry version 35.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   OrderedLocusNames=vfu_A02423 {ECO:0000313|EMBL:ADT87550.1};
OS   Vibrio furnissii (strain DSM 14383 / NCTC 11218 / VL 6966).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=903510 {ECO:0000313|EMBL:ADT87550.1, ECO:0000313|Proteomes:UP000007456};
RN   [1] {ECO:0000313|EMBL:ADT87550.1, ECO:0000313|Proteomes:UP000007456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14383 / NCTC 11218 {ECO:0000313|Proteomes:UP000007456};
RX   PubMed=21217006; DOI=10.1128/JB.01512-10;
RA   Lux T.M., Lee R., Love J.;
RT   "Complete genome sequence of a free-living Vibrio furnissii sp. nov.
RT   strain (NCTC 11218).";
RL   J. Bacteriol. 193:1487-1488(2011).
CC   -!- FUNCTION: Binds mRNA; thus facilitating recognition of the
CC       initiation point. It is needed to translate mRNA with a short
CC       Shine-Dalgarno (SD) purine-rich sequence.
CC       {ECO:0000256|PIRNR:PIRNR002111}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000256|PIRNR:PIRNR002111}.
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DR   EMBL; CP002377; ADT87550.1; -; Genomic_DNA.
DR   RefSeq; WP_014205409.1; NC_016602.1.
DR   EnsemblBacteria; ADT87550; ADT87550; vfu_A02423.
DR   KEGG; vfu:vfu_A02423; -.
DR   PATRIC; fig|903510.3.peg.2340; -.
DR   eggNOG; ENOG4105CAV; Bacteria.
DR   eggNOG; COG0539; LUCA.
DR   KO; K02945; -.
DR   OMA; SLNEFRY; -.
DR   OrthoDB; 1235756at2; -.
DR   BioCyc; VFUR903510:G1GQK-2385-MONOMER; -.
DR   Proteomes; UP000007456; Chromosome 1.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000110; Ribosomal_S1.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF00575; S1; 6.
DR   PIRSF; PIRSF002111; RpsA; 1.
DR   SMART; SM00316; S1; 6.
DR   SUPFAM; SSF50249; SSF50249; 6.
DR   TIGRFAMs; TIGR00717; rpsA; 1.
DR   PROSITE; PS50126; S1; 6.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007456};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:ADT87550.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN       21     87       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      105    171       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      192    260       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      277    347       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      364    434       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      451    520       S1 motif. {ECO:0000259|PROSITE:PS50126}.
SQ   SEQUENCE   556 AA;  61044 MW;  8223DEB0B5CDE0D1 CRC64;
     MTESFAQLFE EFLNETEFQQ GTIVKGTVVA IENGYVLVDA GLKSESAIPA EQFKNAAGEL
     EVEVGSEVDV ALDAVEDGFG ETQLSREKAK RHEAWIVLEK AYEEAETVVG IINGKVKGGF
     TVELNGIRAF LPGSLVDVRP IRDTAHLENK ELEFKVIKLD QKRNNVVVSR RAVIESESSV
     ERDELLETLQ EGTEVKGIVK NLTDYGAFVD LGGVDGLLHI TDMAWKRVKH PSEIVNVGDE
     ILVKVLKFDR DRTRVSLGLK QLGEDPWVAI AKRYPEGHKL TGRVTNLTDY GCFVEIEEGV
     EGLVHVSEMD WTNKNIHPSK VVNVGDEVEV MVLDIDEERR RISLGLKQCK ANPWQSFAEA
     QAKGDKVTGK IKSITDFGIF IGLEGGIDGL VHLSDISWNV PGEEAVREYK KGDEISAVVL
     AVDAERERIS LGVKQMENDP FNAYVADNKK GVLVNGTVTA VDAKGATIEL EDGVEGYIRA
     SEVSRDRVED ASLILSIGDK VEAKFTGVDR KNRVINLSIK AKDEAEEQEA MASINKQDDA
     AFGNAMADAF KAAKGE
//
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