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Database: UniProt
Entry: A0A1X1QN41_9GAMM
LinkDB: A0A1X1QN41_9GAMM
Original site: A0A1X1QN41_9GAMM 
ID   A0A1X1QN41_9GAMM        Unreviewed;       555 AA.
AC   A0A1X1QN41;
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:ORU92625.1};
GN   ORFNames=A6F72_05125 {ECO:0000313|EMBL:ORU92625.1};
OS   Cycloclasticus sp. symbiont of Poecilosclerida sp. N.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=1840472 {ECO:0000313|EMBL:ORU92625.1, ECO:0000313|Proteomes:UP000193416};
RN   [1] {ECO:0000313|EMBL:ORU92625.1, ECO:0000313|Proteomes:UP000193416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Specimen N {ECO:0000313|EMBL:ORU92625.1};
RA   Rubin Blum M., Dubilier N.;
RT   "Short-chain alkanes fuel the metabolism of mussel and sponge
RT   Cycloclasticus symbionts from deep-sea gas and oil seeps.";
RL   Submitted (APR-2016) 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|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:ORU92625.1}.
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DR   EMBL; LWTM01000072; ORU92625.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1QN41; -.
DR   STRING; 1840472.A6F72_05125; -.
DR   Proteomes; UP000193416; 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; 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; 5.
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:UP000193416};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:ORU92625.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          21..87
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          105..171
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          192..260
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          277..347
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          364..434
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          451..520
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   555 AA;  61394 MW;  B294CA4F8687EAD3 CRC64;
     MSENFAELFE ESIKSAELTP GTLITGLVVD ITNDSVIVNA NLKSEGNVPR WQFVDAKGEL
     EVAIGDEVAV VLEMVEDGLG STLLSRDKAK KAAAWKFLEK AAEEKETVIG VITGKVRGGF
     TVEVGGLSGF LPGSLVDVRP LRDTTFLEGK DLEFKVIKLD EKRNNVVVSR RAVLETEYSA
     EREELLKNLK EGAVLKGMVK NLTDYGAFID LGGVDGLLHI TDMAWKRVKH PSEVIKIGQD
     IEVIVLRYDE EKQRVSLGMK QLGEDPWVNI LSRYPVQSKI NGRVTNLTDY GCFIEIEDGI
     EGLVHVSEMD WTNKNVNPAK VVALGDEVEV MVLEIDDSRR RISLGMKQCK GNPWEDFSAI
     HKKGDKITGL IKSITDFGVF IGLDGDIDGL IHLSDISWDE NSEEDLLTYK KGMEIETVIL
     AIDSDRERIS LGIKQLEQDP FQDFLDKNGK NSIVKGIVKE ADVKGAVITL ADGIEGYLRA
     SELNRDRVDD ARNVLTEGDE IEAKFIGIDR KNKIINLSIK AKDNDEEKAV ISDYATQSSS
     APTLGDIFKS SMDDK
//
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