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Database: UniProt
Entry: Q95CA6
LinkDB: Q95CA6
Original site: Q95CA6 
ID   RR4_PSINU               Reviewed;         199 AA.
AC   Q95CA6; Q8WI16;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   10-OCT-2018, entry version 77.
DE   RecName: Full=30S ribosomal protein S4, chloroplastic;
GN   Name=rps4;
OS   Psilotum nudum (Whisk fern) (Lycopodium nudum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Ophioglossidae; Psilotales; Psilotaceae; Psilotum.
OX   NCBI_TaxID=3240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11214320; DOI=10.1038/35054555;
RA   Pryer K.M., Schneider H., Smith A.R., Cranfill R., Wolf P.G.,
RA   Hunt J.S., Sipes S.D.;
RT   "Horsetails and ferns are a monophyletic group and the closest living
RT   relatives to seed plants.";
RL   Nature 409:618-622(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kingyoku;
RX   PubMed=15240838; DOI=10.1093/molbev/msh203;
RA   Nishiyama T., Wolf P.G., Kugita M., Sinclair R.B., Sugita M.,
RA   Sugiura C., Wakasugi T., Yamada K., Yoshinaga K., Yamaguchi K.,
RA   Ueda K., Hasebe M.;
RT   "Chloroplast phylogeny indicates that bryophytes are monophyletic.";
RL   Mol. Biol. Evol. 21:1813-1819(2004).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC       directly to 16S rRNA where it nucleates assembly of the body of
CC       the 30S subunit. {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.
CC       The interaction surface between S4 and S5 is involved in control
CC       of translational fidelity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL26195.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AF313588; AAL26195.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP004638; BAB84218.1; -; Genomic_DNA.
DR   RefSeq; NP_569631.1; NC_003386.1.
DR   ProteinModelPortal; Q95CA6; -.
DR   SMR; Q95CA6; -.
DR   PRIDE; Q95CA6; -.
DR   GeneID; 2545177; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; -; 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   PANTHER; PTHR11831:SF4; PTHR11831:SF4; 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   Chloroplast; Plastid; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN         1    199       30S ribosomal protein S4, chloroplastic.
FT                                /FTId=PRO_0000132658.
FT   DOMAIN       84    146       S4 RNA-binding.
SQ   SEQUENCE   199 AA;  22911 MW;  8E99D1D93E16DF52 CRC64;
     MESDQSKVES DQSKMESDQS KVESDQSISQ STSKKRSQYS LRLEAKQRLR FNYGVTERQL
     LKYVCIAKKA RGSTGQVLLQ LLEMRLDNII FRLGLSPTIP GARQLVNHRH ILVNDQIVDI
     PSYRCKPNDI ITVRDHQKSQ ELIKRNIKLA KIDEIPSHLN ISYLEETKPK GFINKIVDRG
     SIGLEINELL VVEYYSRQA
//
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