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Database: UniProt
Entry: A0A2T1A0A0_9ACTN
LinkDB: A0A2T1A0A0_9ACTN
Original site: A0A2T1A0A0_9ACTN 
ID   A0A2T1A0A0_9ACTN        Unreviewed;       304 AA.
AC   A0A2T1A0A0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Small ribosomal subunit protein uS3 {ECO:0000256|ARBA:ARBA00035257, ECO:0000256|HAMAP-Rule:MF_01309};
GN   Name=rpsC {ECO:0000256|HAMAP-Rule:MF_01309};
GN   ORFNames=CLV47_107157 {ECO:0000313|EMBL:PRZ42029.1};
OS   Antricoccus suffuscus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Antricoccaceae; Antricoccus.
OX   NCBI_TaxID=1629062 {ECO:0000313|EMBL:PRZ42029.1, ECO:0000313|Proteomes:UP000237752};
RN   [1] {ECO:0000313|EMBL:PRZ42029.1, ECO:0000313|Proteomes:UP000237752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100065 {ECO:0000313|EMBL:PRZ42029.1,
RC   ECO:0000313|Proteomes:UP000237752};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in
CC       the 70S ribosome, positioning it for translation.
CC       {ECO:0000256|ARBA:ARBA00024998, ECO:0000256|HAMAP-Rule:MF_01309}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex with
CC       proteins S10 and S14. {ECO:0000256|HAMAP-Rule:MF_01309}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC       {ECO:0000256|ARBA:ARBA00010761, ECO:0000256|HAMAP-Rule:MF_01309,
CC       ECO:0000256|RuleBase:RU003624}.
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:PRZ42029.1}.
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DR   EMBL; PVUE01000007; PRZ42029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T1A0A0; -.
DR   OrthoDB; 9806396at2; -.
DR   Proteomes; UP000237752; 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: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   CDD; cd02412; KH-II_30S_S3; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.30.1140.32; Ribosomal protein S3, C-terminal domain; 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; IPR036419; Ribosomal_S3_C_sf.
DR   InterPro; IPR005704; Ribosomal_uS3_bac-typ.
DR   InterPro; IPR001351; Ribosomal_uS3_C.
DR   InterPro; IPR018280; Ribosomal_uS3_CS.
DR   NCBIfam; TIGR01009; rpsC_bact; 1.
DR   PANTHER; PTHR11760:SF19; 30S RIBOSOMAL PROTEIN S3, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11760; 30S/40S RIBOSOMAL PROTEIN S3; 1.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF00189; Ribosomal_S3_C; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR   SUPFAM; SSF54821; Ribosomal protein S3 C-terminal domain; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
DR   PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000237752};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01309};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01309};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01309};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01309}.
FT   DOMAIN          38..106
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50823"
FT   REGION          212..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   304 AA;  33336 MW;  61C4237A05895DDE CRC64;
     MGQKVNPHGF RLGITTEWKS RWFADKQYAD YVKEDVAIRR LMTTGMERAG ISSVEIERTR
     DRVRVDIHTA RPGIVIGRRG AEAERLRGEL EKLTSKQVQL NILEVKNPEA DAQLVAQGIA
     EQLSSRVAFR RAMKKAQQSA MRAQGVKGIR IQCGGRLGGA EMSRSEFYRE GRVPLHTLRA
     NIDYGTYEAR TTFGRIGVKV WIYKGDVTQS KAEREAAETA LREHRRQRPE RRPRRSGSSG
     TTGTSTEAGR AAAQASVAPA PEEADTTSTE AIATEVAEAI VEAPAAAPAE TTEAGSGTES
     EKDA
//
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