RR4_ANEMR
ID RR4_ANEMR Reviewed; 202 AA.
AC A2T833; A2T834; B0YPN5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Plastid 30S ribosomal protein S4;
GN Name=rps4;
OS Aneura mirabilis (Parasitic liverwort) (Cryptothallus mirabilis).
OG Plastid; Non-photosynthetic plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Jungermanniopsida; Metzgeriidae; Metzgeriales; Aneuraceae; Aneura.
OX NCBI_TaxID=280810;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18056074; DOI=10.1093/molbev/msm267;
RA Wickett N.J., Zhang Y., Hansen S.K., Roper J.M., Kuehl J.V., Plock S.A.,
RA Wolf P.G., dePamphilis C.W., Boore J.L., Goffinet B.;
RT "Functional gene losses occur with minimal size reduction in the plastid
RT genome of the parasitic liverwort Aneura mirabilis.";
RL Mol. Biol. Evol. 25:393-401(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-202.
RC STRAIN=49, and 51;
RA Wickett N.J., Goffinet B.;
RT "Origin and relationships of the myco-heterotrophic liverwort Cryptothallus
RT mirabilis Malmb. (Metzgeriales, Marchantiophyta).";
RL Submitted (SEP-2006) 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:0000250}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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DR EMBL; EU043314; ABS54482.1; -; Genomic_DNA.
DR EMBL; DQ983846; ABM88814.1; -; Genomic_DNA.
DR EMBL; DQ983847; ABM88815.1; -; Genomic_DNA.
DR RefSeq; YP_001687221.1; NC_010359.1.
DR AlphaFoldDB; A2T833; -.
DR SMR; A2T833; -.
DR GeneID; 5952238; -.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR005709; Ribosomal_S4_bac-type.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Plastid; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..202
FT /note="Plastid 30S ribosomal protein S4"
FT /id="PRO_0000293424"
FT DOMAIN 90..153
FT /note="S4 RNA-binding"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 15..16
FT /note="PG -> QA (in strain: 51)"
SQ SEQUENCE 202 AA; 23412 MW; B70D0D86307BB4BF CRC64;
MSRYRGPRMK MIRRPGTLPG LTSKTPGTKV GSSDRSTSSK KISQYRIRLE EKQKLRLHYG
LTERQLLKYV FTARGAKGST GQLLLQLLEM RLDNTIFRLG IVPTIPAARQ LVNHRHVSIN
EHIIDIPSYN CKPGDVITIN NREKCRLVDR RDMNSLQKPE IPNHLTFDSK EFLGSVQQII
DRDWIDLKIN ELLVVEYYSR RV