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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//