ID A0A1I5B515_9FLAO Unreviewed; 246 AA.
AC A0A1I5B515;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05421741_10963 {ECO:0000313|EMBL:SFN69792.1};
OS Paenimyroides ummariense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Paenimyroides.
OX NCBI_TaxID=913024 {ECO:0000313|EMBL:SFN69792.1, ECO:0000313|Proteomes:UP000199036};
RN [1] {ECO:0000313|Proteomes:UP000199036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-12 {ECO:0000313|Proteomes:UP000199036};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOVI01000009; SFN69792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5B515; -.
DR STRING; 913024.SAMN05421741_10963; -.
DR OrthoDB; 9806396at2; -.
DR Proteomes; UP000199036; 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 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..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 246 AA; 27460 MW; 15C8634266D7BEA0 CRC64;
MGQKTNPIGN RLGIIRGWDS NWYGGNDYGD KLAEDAKIRK YIHARLAKAS VSKIIIERTL
KLVTVTITTA RPGIIIGKGG QEVDKLKEEL KKITNKEVQI NIFEIKRPEL DAYLAATSIA
RQIESRISYR RAIKMAIAAA MRMNAEGMKV QISGRLNGAE MARSENFKDG RIPLSTFRAD
IDYALAEAHT TYGRMGIKVW IMKGEVYGKR DLSPLAGMDK QQKSSKPAGS GKPNGRPNQQ
RNNKRK
//
