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Database: UniProt
Entry: Q46Y53_CUPPJ
LinkDB: Q46Y53_CUPPJ
Original site: Q46Y53_CUPPJ 
ID   Q46Y53_CUPPJ            Unreviewed;       592 AA.
AC   Q46Y53;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   OrderedLocusNames=Reut_A2569 {ECO:0000313|EMBL:AAZ61930.1};
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ61930.1};
RN   [1] {ECO:0000313|EMBL:AAZ61930.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JMP134 {ECO:0000313|EMBL:AAZ61930.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome1 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) 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; CP000090; AAZ61930.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46Y53; -.
DR   STRING; 264198.Reut_A2569; -.
DR   KEGG; reu:Reut_A2569; -.
DR   eggNOG; COG0539; Bacteria.
DR   HOGENOM; CLU_015805_2_1_4; -.
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; cd05689; S1_RPS1_repeat_ec4; 1.
DR   CDD; cd05691; S1_RPS1_repeat_ec6; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 6.
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:AAZ61930.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          54..120
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          138..204
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          225..293
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          310..380
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          397..467
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          484..553
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   592 AA;  64996 MW;  546D11717208BC42 CRC64;
     MFNLTPLHMA DCARSSRRPV YRGLLLTFMS DLQTNESFAA LFEESIARSN MKAGEVISAE
     VVRIDHNFVV VNAGLKSEAF VPVEEFLNDQ GELEVQAGDY VSVAIDALEN GYGDTILSRD
     KAKRLASWLN LEKALEDGEI ISGTVTGKVK GGLTVMVNGI RAFLPGSLVD VRPIKDTTPY
     EGKTLEFKVI KLDRKRNNVV LSRRAVVEAT LGEERQKLME TLKEGAIVNG IVKNITDYGA
     FVDLGGIDGL LHITDLAWRR VRHPSEVLSV GQEITAKILK FDQEKNRVSL GVKQLGEDPW
     VGISRRYPQG TRLFGKVTNL TDYGAFVEIE AGIEGLVHVS EMDWTNKNVA PSKVVQLGDE
     VEVMVLDIDE DKRRISLGMK QCKANPWDDF SRNHKKGDKL SGQIKSITDF GVFIGLPGGI
     DGLVHLSDLS WQETGEEAVR KYKKGDEVEA VVLGIDVDKE RISLGIKQLS GDPFNNFISA
     NDKGSLVTGT IKAVDPKGAV VQLADDVEGY LRASEISADR VEDARNVLKE GEQITALVVN
     VDRKSRNINL SIKAKDNVEQ QEAMQKFQAD TSTAGTTNLG ALLKAKLGQD NQ
//
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