ID A0A1X6ZVL8_9RHOB Unreviewed; 560 AA.
AC A0A1X6ZVL8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN Name=rpsA {ECO:0000313|EMBL:SLN62980.1};
GN ORFNames=PSM7751_03218 {ECO:0000313|EMBL:SLN62980.1};
OS Pseudooceanicola marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=396013 {ECO:0000313|EMBL:SLN62980.1, ECO:0000313|Proteomes:UP000193963};
RN [1] {ECO:0000313|EMBL:SLN62980.1, ECO:0000313|Proteomes:UP000193963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7751 {ECO:0000313|EMBL:SLN62980.1,
RC ECO:0000313|Proteomes:UP000193963};
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; FWFN01000006; SLN62980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6ZVL8; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000193963; 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:UP000193963};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:SLN62980.1}; 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; 61601 MW; 4C2FEBF6B56C3552 CRC64;
MAQNTSMEEF EALLNESFEM DTPNEGSVVK GKVIAIEAGQ AIIDVGYKME GRVELKEFAN
PGEAPEISVG DEVEVYLRAA ENARGEAVIS REMARREEAW DRLEKAYADD QRVEGAIFGR
VKGGFTVDLG GAVAFLPGSQ VDVRPVRDAG PLMGLKQPFQ ILKMDRRRGN IVVSRRAILE
ESRAEQRAEV ISNLQEGQAV EGVVKNITEY GAFVDLGGVD GLLHVTDMAW RRVNHPSEIL
SIGETVKVQV IKINKETHRI SLGMKQLQED PWDLVAAKYP LSSVHTGRVT NITDYGAFVE
LEPGVEGLVH VSEMSWTKKN VHPGKIVSTS QEVEVMVLEI DQAKRRVSLG LKQTMRNPWE
VFSETHPEGT VVEGEVKNIT EFGLFVGLPG DIDGMVHLSD LSWDERGEDA IQNYRKGDMV
QAVVSEVDID KERISLSIKN VGGDKFAEAV GGVKRGSIIT VNVTAIEDGG IEVEYEGMKS
FIRRSDLSRD RAEQRPERFS VGDHVDVRVT NVDSKSRRLG LSIKAREIAE EKEAVEQYGS
SDSGASLGDI LGAALKGDDE
//
