ID A0A1Y5RKA8_9RHOB Unreviewed; 559 AA.
AC A0A1Y5RKA8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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:SLN19305.1};
GN ORFNames=PEL8287_00782 {ECO:0000313|EMBL:SLN19305.1};
OS Roseovarius litorisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN19305.1, ECO:0000313|Proteomes:UP000193827};
RN [1] {ECO:0000313|EMBL:SLN19305.1, ECO:0000313|Proteomes:UP000193827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN19305.1,
RC ECO:0000313|Proteomes:UP000193827};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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}.
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DR EMBL; FWFL01000002; SLN19305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5RKA8; -.
DR Proteomes; UP000193827; 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; 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:UP000193827};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:SLN19305.1}; 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 559 AA; 61411 MW; 6F73AC7443462C53 CRC64;
MAQNTSMEEF EALLNESFEM DTPEEGTVVK GKVIAIEAGQ AIIDVGYKME GRVDLKEFAN
PGEAPEIAVG DEVEVFLRSA ENSRGEAVVS REMARREEAW DRLEKAYADE ERVEGAIFGR
VKGGFTVDLG GAVAFLPGSQ VDVRPVRDAG PLMGLKQPFQ ILKMDRRRGN IVVSRRAILE
ESRAEQRAEV IGNLTEGQNV EGVVKNITEY GAFVDLGGVD GLLHVTDMAW RRVNHPSEIL
SIGETVNVQV IKINKETHRI SLGMKQLQDD PWDLVAGKYP LGSVHTGRVT NITDYGAFVE
LEPGVEGLVH VSEMSWTKKN VHPGKIVSTS QEVEVMVLEI DGAKRRVSLG LKQTQRNPWE
VFAETHPEGT EVEGEVKNIT EFGLFIGLEG EIDGMVHLSD ISWDERGEDV IQNYRKGDMV
SAVVSEVDTE KERISLSIKA LGGDKFAEAV GGVKRGSIIT VEVTAIEDGG IEVEYEGMKS
FIRRSDLSRD RSEQRPERFS VGNKVDVRVT NVDSKTRRLG LSIKAREIAE EKEAVEQYGS
SDSGASLGDI LGAALKGDE
//