ID A0A285IF23_9RHOB Unreviewed; 560 AA.
AC A0A285IF23;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN ORFNames=SAMN06297129_0950 {ECO:0000313|EMBL:SNY46387.1};
OS Pseudooceanicola antarcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1247613 {ECO:0000313|EMBL:SNY46387.1, ECO:0000313|Proteomes:UP000231655};
RN [1] {ECO:0000313|EMBL:SNY46387.1, ECO:0000313|Proteomes:UP000231655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12662 {ECO:0000313|EMBL:SNY46387.1,
RC ECO:0000313|Proteomes:UP000231655};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-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; OBEA01000002; SNY46387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285IF23; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000231655; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:SNY46387.1}; 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; 61422 MW; A5FFD3A5C0C18425 CRC64;
MAQNTSMEEF EALLNESFEM DTPEEGSVVK GKVIAVEAGQ AIIDVGYKME GRVDLKEFAN
PGEAPEITVG DEVEVFLRSA ENARGEAVIS REMARREEAW DRLEKAYADD ARVEGAIFGR
VKGGFTVDLG GAVAFLPGSQ VDVRPVRDAG PLMGLKQPFQ ILKMDRRRGN IVVSRRAILE
ESRAEQRAEV IANLSEGQAV DGVVKNITEY GAFVDLGGVD GLLHVTDMAW RRVNHPSEIL
SIGETVKVQV IKINKETHRI SLGMKQLQED PWDLVAAKYP LSSVHTGRVT NITDYGAFVE
LEPGVEGLVH VSEMSWTKKN VHPGKIVSTS QEVEVMVLEI DAAKRRVSLG LKQTMRNPWE
VFSETHPEGT VVEGEVKNIT EFGLFVGLPG DIDGMVHLSD LSWDERGEDA IQNYRKGDMV
QAVVSEVDID KERISLSIKN VGGDKFAEAV GGVKRGSIVT VEVTAIEDGG VEVEYEGMKS
FIRRSDLSRD RAEQRPERFS VGDKIDVRVT NVDSKTRRLG LSIKAREIAE EKEAVEQYGS
SDSGASLGDI LGAALKGDNE
//
