ID A0A2H9I1M3_9ARCH Unreviewed; 183 AA.
AC A0A2H9I1M3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Small ribosomal subunit protein uS4 {ECO:0000256|HAMAP-Rule:MF_01306};
GN Name=rps4 {ECO:0000256|HAMAP-Rule:MF_01306};
GN ORFNames=CP083_02610 {ECO:0000313|EMBL:PDM26662.1};
OS Candidatus Bathyarchaeota archaeon B24-2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=2041147 {ECO:0000313|EMBL:PDM26662.1, ECO:0000313|Proteomes:UP000228824};
RN [1] {ECO:0000313|EMBL:PDM26662.1, ECO:0000313|Proteomes:UP000228824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B24-2 {ECO:0000313|EMBL:PDM26662.1};
RA Feng X., Perumal V., Wang F.;
RT "Metabolic analysis of an uncultured genome Bathyarchaeota B242 based on
RT metagenomic technology.";
RL Submitted (SEP-2017) 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 -!- 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:PDM26662.1}.
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DR EMBL; PCNA01000017; PDM26662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9I1M3; -.
DR Proteomes; UP000228824; 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_A; Ribosomal_S4_A; 1.
DR InterPro; IPR022801; Ribosomal_uS4.
DR InterPro; IPR022802; Ribosomal_uS4_arc.
DR InterPro; IPR018079; Ribosomal_uS4_CS.
DR InterPro; IPR005710; Ribosomal_uS4_euk/arc.
DR InterPro; IPR001912; Ribosomal_uS4_N.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR NCBIfam; TIGR01018; uS4_arch; 1.
DR PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1.
DR PANTHER; PTHR11831:SF5; 40S RIBOSOMAL PROTEIN S9; 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 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 5..102
FT /note="Small ribosomal subunit protein uS4 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01390"
FT DOMAIN 103..165
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 160..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 183 AA; 21161 MW; 0809C9A95B45586C CRC64;
MGDPKKQRKK YTTPKFPWQA ETLQAELKLI GEYGLRNKRE LWRYTTMLSK FRSNARSLLS
KPPEERGLLE NQLLSRLKRM GVLMEDAVLD DVLDLSVEDL LERRLQTIVY RKGLAKTPYQ
ARQLITHGHI AIGDRRVFSP GYLVMKDEEE AVTYYYKSPL ADPSHPLRQS IGKTEKPEIK
SGG
//
