RS3_ACAM1
ID RS3_ACAM1 Reviewed; 241 AA.
AC B0C1D9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309};
GN Synonyms=rps3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN OrderedLocusNames=AM1_4702;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC -!- FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in
CC the 70S ribosome, positioning it for translation. {ECO:0000255|HAMAP-
CC Rule:MF_01309}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex with
CC proteins S10 and S14. {ECO:0000255|HAMAP-Rule:MF_01309}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01309}.
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DR EMBL; CP000828; ABW29674.1; -; Genomic_DNA.
DR RefSeq; WP_010469315.1; NC_009925.1.
DR AlphaFoldDB; B0C1D9; -.
DR SMR; B0C1D9; -.
DR STRING; 329726.AM1_4702; -.
DR PRIDE; B0C1D9; -.
DR EnsemblBacteria; ABW29674; ABW29674; AM1_4702.
DR KEGG; amr:AM1_4702; -.
DR eggNOG; COG0092; Bacteria.
DR HOGENOM; CLU_058591_0_2_3; -.
DR OMA; KTNPIGN; -.
DR OrthoDB; 1132353at2; -.
DR Proteomes; UP000000268; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1140.32; -; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR HAMAP; MF_01309_B; Ribosomal_S3_B; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR005704; Ribosomal_S3_bac-typ.
DR InterPro; IPR001351; Ribosomal_S3_C.
DR InterPro; IPR036419; Ribosomal_S3_C_sf.
DR InterPro; IPR018280; Ribosomal_S3_CS.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR SUPFAM; SSF54821; SSF54821; 1.
DR TIGRFAMs; TIGR01009; rpsC_bact; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..241
FT /note="30S ribosomal protein S3"
FT /id="PRO_1000086080"
FT DOMAIN 39..109
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
FT REGION 213..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 27579 MW; 7EDB25CF62259A45 CRC64;
MGQKIHPTGF RLGITQDHWS RWFADTDRYP ELLQEDFKVR NYVNKNLSNA GIAGVRIERK
ADQIDLEVRT ARPGVVVGRG GSGIESLRVG LQKELGDDRP IRINVVEVAR VDAEATLIAE
YIVQQLVRRV SFRRVVRQAI QRAQRAGVEG IKIQVGGRLN GAEIARSEWT REGRVPLHTL
RANIDYSYRT ASTTYGILGV KVWVFKGEVI PGADEQPTNR EPQQRRRQQQ RRRQQFEDRS
E