ID A0A1C0UTC3_9CYAN Unreviewed; 202 AA.
AC A0A1C0UTC3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Small ribosomal subunit protein uS4 {ECO:0000256|ARBA:ARBA00035254, ECO:0000256|HAMAP-Rule:MF_01306};
GN Name=rpsD {ECO:0000256|HAMAP-Rule:MF_01306};
GN Synonyms=rps4 {ECO:0000256|HAMAP-Rule:MF_01306};
GN ORFNames=BCR12_15530 {ECO:0000313|EMBL:OCQ88782.1};
OS Limnothrix sp. P13C2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Limnothrix.
OX NCBI_TaxID=1880902 {ECO:0000313|EMBL:OCQ88782.1, ECO:0000313|Proteomes:UP000093334};
RN [1] {ECO:0000313|EMBL:OCQ88782.1, ECO:0000313|Proteomes:UP000093334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P13C2 {ECO:0000313|EMBL:OCQ88782.1};
RA Tan B., Te S.H., Gin K., Thompson J.;
RT "Draft genome of Limnothrix sp. P13C2.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01306}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC interaction surface between S4 and S5 is involved in control of
CC translational fidelity. {ECO:0000256|HAMAP-Rule:MF_01306}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000256|ARBA:ARBA00007465, ECO:0000256|HAMAP-Rule:MF_01306,
CC ECO:0000256|RuleBase:RU003699}.
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:OCQ88782.1}.
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DR EMBL; MBRF01000033; OCQ88782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C0UTC3; -.
DR STRING; 1880902.BCR12_15530; -.
DR Proteomes; UP000093334; Unassembled WGS sequence.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
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; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR InterPro; IPR022801; Ribosomal_uS4.
DR InterPro; IPR005709; Ribosomal_uS4_bac-type.
DR InterPro; IPR018079; Ribosomal_uS4_CS.
DR InterPro; IPR001912; Ribosomal_uS4_N.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR NCBIfam; TIGR01017; rpsD_bact; 1.
DR PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1.
DR PANTHER; PTHR11831:SF4; 37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000093334};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01306};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01306};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01306};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01306}.
FT DOMAIN 3..89
FT /note="Small ribosomal subunit protein uS4 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01390"
FT DOMAIN 90..154
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 202 AA; 23294 MW; 7B336250DF8B1F84 CRC64;
MSRYRGPRLR IVRRLGELPG LTRKSAKRAY PPGQHGQNRK KRSEYAVRLE EKQKLRFNYG
VSERQMLRYV RKARRAAGST GTVLLQLLEM RLDNTVFRLG MAPTIPAARQ LVNHGHIMVN
GRRVDVASYQ CRPGDVVTVR PKDQSRKIVE NNLQFPGLAN MPSHLEFDKE KLTGKVNSVI
DREWVALQIN ELLVVEYYSR QA
//
