ID A0A0F2RRH7_9RHOB Unreviewed; 553 AA.
AC A0A0F2RRH7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN ORFNames=VR71_21835 {ECO:0000313|EMBL:KJS40636.1};
OS Roseovarius sp. BRH_c41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1629709 {ECO:0000313|EMBL:KJS40636.1, ECO:0000313|Proteomes:UP000033676};
RN [1] {ECO:0000313|EMBL:KJS40636.1, ECO:0000313|Proteomes:UP000033676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c41 {ECO:0000313|EMBL:KJS40636.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJS40636.1}.
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DR EMBL; LADY01000065; KJS40636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2RRH7; -.
DR PATRIC; fig|1629709.5.peg.4166; -.
DR Proteomes; UP000033676; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:KJS40636.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 20..86
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 104..170
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 191..259
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 276..346
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 363..433
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 450..518
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 553 AA; 60836 MW; 91CC116C0A220243 CRC64;
MEEFEALLNE SFEMDTPEEG SVVKGRVIAI EAGQAIIDVG YKMEGRVDLK EFANPGETPD
ISVGDEVEVF LRSAENSRGE AVISREMARR EEAWDRLEKA YADEERVDGA IFGRVKGGFT
VDLGGAVAFL PGSQVDVRPV RDAGPLMGLK QPFQILKMDR RRGNIVVSRR AILEESRAEQ
RAEVIGNLTE GQTVDGVVKN ITEYGAFVDL GGVDGLLHVT DMAWRRVNHP SEILTIGETV
KVQVIKINKD THRISLGMKQ LQEDPWDLVA AKYPLESTHT GRVTNITDYG AFVELEPGVE
GLVHVSEMSW TKKNVHPGKI VSTSQEVEVM VLEIDGAKRR VSLGLKQTMR NPWEVFAETH
PEGTEVEGEV KNITEFGLFI GLEGEIDGMV HLSDLSWDER GEDAIQSYKK GDMVHAVVSE
VDIEKERISL SIKALGGDKF SEAVGGVKRG SVITVAVTAI EDGGIEVEYE GMKSFIRRSD
LSRDRADQRP ERFSVGDKLD VRVTNVDAKT RRLGLSIKAR EIAEEKEAVE QYGSSDSGAS
LGDILGAALK GDR
//
