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Database: UniProt
Entry: A0A1L9NVD9_9RHOB
LinkDB: A0A1L9NVD9_9RHOB
Original site: A0A1L9NVD9_9RHOB 
ID   A0A1L9NVD9_9RHOB        Unreviewed;       557 AA.
AC   A0A1L9NVD9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   Name=rpsA {ECO:0000313|EMBL:OJI93247.1};
GN   ORFNames=PFRI_25060 {ECO:0000313|EMBL:OJI93247.1};
OS   Planktotalea frisia.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Planktotalea.
OX   NCBI_TaxID=696762 {ECO:0000313|EMBL:OJI93247.1, ECO:0000313|Proteomes:UP000184514};
RN   [1] {ECO:0000313|EMBL:OJI93247.1, ECO:0000313|Proteomes:UP000184514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH6-1 {ECO:0000313|EMBL:OJI93247.1,
RC   ECO:0000313|Proteomes:UP000184514};
RA   Poehlein A., Bakenhus I., Voget S., Brinkhoff T., Simon M.;
RT   "Genome sequence of Planktotalea frisia SH6-1.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds mRNA; thus facilitating recognition of the initiation
CC       point. It is needed to translate mRNA with a short Shine-Dalgarno (SD)
CC       purine-rich sequence. {ECO:0000256|ARBA:ARBA00025604,
CC       ECO:0000256|PIRNR:PIRNR002111}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000256|ARBA:ARBA00006767, ECO:0000256|PIRNR:PIRNR002111}.
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:OJI93247.1}.
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DR   EMBL; MLCB01000150; OJI93247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9NVD9; -.
DR   STRING; 696762.PFRI_25060; -.
DR   Proteomes; UP000184514; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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   CDD; cd05687; S1_RPS1_repeat_ec1_hs1; 1.
DR   CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR   CDD; cd05688; S1_RPS1_repeat_ec3; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 5.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000110; Ribosomal_bS1.
DR   InterPro; IPR035104; Ribosomal_protein_S1-like.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR00717; rpsA; 1.
DR   PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR   PANTHER; PTHR10724:SF7; 30S RIBOSOMAL PROTEIN S1, CHLOROPLASTIC; 1.
DR   Pfam; PF00575; S1; 6.
DR   PIRSF; PIRSF002111; RpsA; 1.
DR   PRINTS; PR00681; RIBOSOMALS1.
DR   SMART; SM00316; S1; 6.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 6.
DR   PROSITE; PS50126; S1; 6.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000184514};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:OJI93247.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          24..90
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          108..174
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          195..263
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          280..350
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          367..437
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          454..522
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   557 AA;  61244 MW;  2E6E3F5C00F0512A CRC64;
     MANLMDEFEA LLTESFEMDT PDEGTVVKGK VIAIEAGQAI IDVGYKMEGR VDIKEFANPG
     EAPEIAVGDE VEVFLRSAEN SRGEAVISRE MARREEAWDR LEKAYADEER VEGAIFGRVK
     GGFTVDLGGA VAFLPGSQVD VRPVRDAGPL MGMKQPFQIL KMDRRRGNIV VSRRAILEES
     RAEQRAEVIG NLTEGQAVDG VVKNITEYGA FVDLGGVDGL LHVTDMAWRR VNHPSEILTI
     GETVKVQVIK INKETHRISL GMKQLQEDPW DLVAGKYPLE STHTGRVTNI TDYGAFVELE
     PGVEGLVHVS EMSWTKKNVH PGKIVSTSQE VEVMVLEIDG TKRRVSLGLK QTQRNPWEVF
     AEQFPEGTEV EGEVKNITEF GLFIGLEGDI DGMVHLSDLS WDERGEEAIQ SYHKNDIVQA
     VVSEVDVEKE RISLSVKALG GDKFAEAVGG VKRGSIVTVT VTAIEEGGVE VEYEGMKSFI
     RRSDLSRDRA EQRPERFSVG DKVDVRITNV DAKTRRLGVS VKAREIAEEK EAVEQYGSSD
     SGASLGDILG AALKSDD
//
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