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RS19_THETH
ID   RS19_THETH              Reviewed;          93 AA.
AC   P80381;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=30S ribosomal protein S19;
GN   Name=rpsS; Synonyms=rps19;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND STRUCTURE BY NMR.
RC   STRAIN=VK1;
RX   PubMed=9350986; DOI=10.1016/s0014-5793(97)01112-5;
RA   Davydova N.L., Rak A.V., Gryaznova O.I., Liljas A., Jonsson B.-H.,
RA   Berglund H., Haerd T., Garber M.B.;
RT   "Preliminary NMR studies of Thermus thermophilus ribosomal protein S19
RT   overproduced in Escherichia coli.";
RL   FEBS Lett. 415:155-159(1997).
RN   [2]
RP   STRUCTURE BY NMR.
RC   STRAIN=VK1;
RX   PubMed=10512703; DOI=10.1006/jmbi.1999.3122;
RA   Helgstrand M., Rak A.V., Allard P., Davydova N., Garber M.B., Haerd T.;
RT   "Solution structure of the ribosomal protein S19 from Thermus
RT   thermophilus.";
RL   J. Mol. Biol. 292:1071-1081(1999).
CC   -!- FUNCTION: Protein S19 forms a complex with S13 that binds strongly to
CC       the 16S ribosomal RNA. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS19 family.
CC       {ECO:0000305}.
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DR   EMBL; X84059; CAA58878.1; -; Genomic_DNA.
DR   RefSeq; WP_011173711.1; NZ_VHHQ01000024.1.
DR   PDB; 1QKF; NMR; -; A=2-93.
DR   PDB; 1QKH; NMR; -; A=2-93.
DR   PDB; 4V4G; X-ray; 11.50 A; S=2-81.
DR   PDB; 4V8X; X-ray; 3.35 A; AS/CS=1-93.
DR   PDBsum; 1QKF; -.
DR   PDBsum; 1QKH; -.
DR   PDBsum; 4V4G; -.
DR   PDBsum; 4V8X; -.
DR   AlphaFoldDB; P80381; -.
DR   BMRB; P80381; -.
DR   SMR; P80381; -.
DR   GeneID; 66942385; -.
DR   OMA; FPEMVGH; -.
DR   EvolutionaryTrace; P80381; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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   Gene3D; 3.30.860.10; -; 1.
DR   HAMAP; MF_00531; Ribosomal_S19; 1.
DR   InterPro; IPR020934; Ribosomal_S15/S19_CS.
DR   InterPro; IPR002222; Ribosomal_S19.
DR   InterPro; IPR005732; Ribosomal_S19_bac-type.
DR   InterPro; IPR023575; Ribosomal_S19_S15_SF.
DR   PANTHER; PTHR11880; PTHR11880; 1.
DR   Pfam; PF00203; Ribosomal_S19; 1.
DR   PIRSF; PIRSF002144; Ribosomal_S19; 1.
DR   PRINTS; PR00975; RIBOSOMALS19.
DR   SUPFAM; SSF54570; SSF54570; 1.
DR   TIGRFAMs; TIGR01050; rpsS_bact; 1.
DR   PROSITE; PS00323; RIBOSOMAL_S19; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..93
FT                   /note="30S ribosomal protein S19"
FT                   /id="PRO_0000129928"
FT   HELIX           13..25
FT                   /evidence="ECO:0007829|PDB:1QKF"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:1QKF"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1QKF"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1QKF"
FT   STRAND          47..52
FT                   /evidence="ECO:0007829|PDB:1QKF"
FT   STRAND          57..62
FT                   /evidence="ECO:0007829|PDB:1QKF"
FT   TURN            64..68
FT                   /evidence="ECO:0007829|PDB:1QKF"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:1QKF"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:1QKF"
SQ   SEQUENCE   93 AA;  10581 MW;  D77C0FC2D4D2DE04 CRC64;
     MPRSLKKGVF VDDHLLEKVL ELNAKGEKRL IKTWSRRSTI VPEMVGHTIA VYNGKQHVPV
     YITENMVGHK LGEFAPTRTY RGHGKEAKAT KKK
 
 
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