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Database: UniProt
Entry: A0A369TMA6_9RHOB
LinkDB: A0A369TMA6_9RHOB
Original site: A0A369TMA6_9RHOB 
ID   A0A369TMA6_9RHOB        Unreviewed;       560 AA.
AC   A0A369TMA6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=DU478_12855 {ECO:0000313|EMBL:RDD65804.1};
OS   Thalassococcus profundi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassococcus.
OX   NCBI_TaxID=2282382 {ECO:0000313|EMBL:RDD65804.1, ECO:0000313|Proteomes:UP000253977};
RN   [1] {ECO:0000313|EMBL:RDD65804.1, ECO:0000313|Proteomes:UP000253977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WRAS1 {ECO:0000313|EMBL:RDD65804.1,
RC   ECO:0000313|Proteomes:UP000253977};
RA   Yu M.;
RT   "Thalassococcus profundi sp. nov., a marine bacterium isolated from deep
RT   seawater of Okinawa Trough.";
RL   Submitted (JUL-2018) 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:RDD65804.1}.
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DR   EMBL; QPMK01000009; RDD65804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369TMA6; -.
DR   OrthoDB; 9804077at2; -.
DR   Proteomes; UP000253977; 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   CDD; cd05691; S1_RPS1_repeat_ec6; 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:UP000253977};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:RDD65804.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          26..92
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          110..176
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          197..265
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          282..352
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          369..439
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          456..524
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   560 AA;  61635 MW;  A817DE3D60F4A036 CRC64;
     MCAKASMEEF EALLNESFEM DTPDEGSVVK GKVIAIEAGQ AIIDVGYKME GRVELKEFAN
     PGEQPDISVG DEVEVFLRQV ENARGEAVIS REMARREEAW DRLEKAYADD ARVEGAIFGR
     VKGGFTVDLG GAVAFLPGSQ VDVRPVRDAG PLMGLKQPFQ ILKMDRRRGN IVVSRRAILE
     ESRAEQRAEV ISNLTEGQAV DGVVKNITEY GAFVDLGGVD GLLHVTDMAW RRVNHPSEIL
     SIGETVKVQV IKINKETHRI SLGMKQLQED PWDLVAAKYP LESVHAGRVT NITDYGAFVE
     LEPGVEGLVH VSEMSWTKKN VHPGKIVSTS QEVEVMVLEI DQAKRRVSLG LKQTMRNPWE
     VFAETHPEGT QVEGEVKNIT EFGLFIGLDG EIDGMVHLSD LSWDERGEDA IQNYRKGDVV
     QAVVSEVDTE KERISLSIKA LGGDKFAEAV GGVKRGSIIT VTVTAIEDGG IEVEYEGMKS
     FIRRSDLSRD RAEQRPERFS VGDKVDVRVT NVDSKTRRLG VSIKAREIAE EKEAVEQFGS
     SDSGASLGDI LGAALKRDDD
//
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