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RL11_THETH
ID   RL11_THETH              Reviewed;         147 AA.
AC   P36238;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Synonyms=rpl11 {ECO:0000255|HAMAP-Rule:MF_00736};
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VK1;
RA   Ossina N., Eliseikina I., Garber M.B., Jonsson B.-H.;
RT   "Cloning and overexpression of the ribosomal protein L1 gene from Thermus
RT   thermophilus VK1. Crystallization of the recombinant protein L1.";
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC       interact with GTP-bound translation factors. {ECO:0000255|HAMAP-
CC       Rule:MF_00736}.
CC   -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit.
CC       Interacts with L10 and the large rRNA to form the base of the stalk.
CC       L10 forms an elongated spine to which L12 dimers bind in a sequential
CC       fashion forming a multimeric L10(L12)X complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00736}.
CC   -!- INTERACTION:
CC       P36238; Q84BQ9: prmA; Xeno; NbExp=2; IntAct=EBI-15714407, EBI-7202232;
CC   -!- PTM: One or more lysine residues are methylated. {ECO:0000255|HAMAP-
CC       Rule:MF_00736}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR   EMBL; X81375; CAA57138.1; -; Genomic_DNA.
DR   RefSeq; WP_011174097.1; NZ_VHHQ01000027.1.
DR   PDB; 2E34; NMR; -; A=1-147.
DR   PDB; 2E35; NMR; -; A=1-147.
DR   PDB; 2E36; NMR; -; A=1-147.
DR   PDB; 2H8W; NMR; -; A=1-147.
DR   PDB; 2KLM; Other; -; A=2-147.
DR   PDB; 2NXN; X-ray; 2.40 A; B=1-147.
DR   PDB; 3CJQ; X-ray; 2.70 A; B/E/H=2-147.
DR   PDB; 3CJR; X-ray; 2.05 A; B=1-147.
DR   PDB; 3CJS; X-ray; 1.37 A; B/C=1-72.
DR   PDB; 3CJT; X-ray; 2.30 A; B/D/F/H/J/L/N/P=1-147.
DR   PDB; 4V67; X-ray; 3.00 A; BK/DK=1-147.
DR   PDBsum; 2E34; -.
DR   PDBsum; 2E35; -.
DR   PDBsum; 2E36; -.
DR   PDBsum; 2H8W; -.
DR   PDBsum; 2KLM; -.
DR   PDBsum; 2NXN; -.
DR   PDBsum; 3CJQ; -.
DR   PDBsum; 3CJR; -.
DR   PDBsum; 3CJS; -.
DR   PDBsum; 3CJT; -.
DR   PDBsum; 4V67; -.
DR   AlphaFoldDB; P36238; -.
DR   BMRB; P36238; -.
DR   SMR; P36238; -.
DR   DIP; DIP-46023N; -.
DR   IntAct; P36238; 2.
DR   GeneID; 3168343; -.
DR   EvolutionaryTrace; P36238; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0070180; F:large ribosomal subunit 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; cd00349; Ribosomal_L11; 1.
DR   Gene3D; 1.10.10.250; -; 1.
DR   Gene3D; 3.30.1550.10; -; 1.
DR   HAMAP; MF_00736; Ribosomal_L11; 1.
DR   InterPro; IPR000911; Ribosomal_L11/L12.
DR   InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR   InterPro; IPR006519; Ribosomal_L11_bac-typ.
DR   InterPro; IPR020783; Ribosomal_L11_C.
DR   InterPro; IPR036769; Ribosomal_L11_C_sf.
DR   InterPro; IPR020785; Ribosomal_L11_CS.
DR   InterPro; IPR020784; Ribosomal_L11_N.
DR   PANTHER; PTHR11661; PTHR11661; 1.
DR   Pfam; PF00298; Ribosomal_L11; 1.
DR   Pfam; PF03946; Ribosomal_L11_N; 1.
DR   SMART; SM00649; RL11; 1.
DR   SUPFAM; SSF46906; SSF46906; 1.
DR   SUPFAM; SSF54747; SSF54747; 1.
DR   TIGRFAMs; TIGR01632; L11_bact; 1.
DR   PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Methylation; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..147
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_0000104400"
FT   STRAND          4..13
FT                   /evidence="ECO:0007829|PDB:3CJS"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:2NXN"
FT   HELIX           23..28
FT                   /evidence="ECO:0007829|PDB:3CJS"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:3CJS"
FT   HELIX           34..45
FT                   /evidence="ECO:0007829|PDB:3CJS"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:3CJS"
FT   STRAND          52..60
FT                   /evidence="ECO:0007829|PDB:3CJS"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:2E34"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:3CJS"
FT   HELIX           74..78
FT                   /evidence="ECO:0007829|PDB:3CJR"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:2H8W"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:2E34"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:3CJR"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:3CJR"
FT   TURN            112..114
FT                   /evidence="ECO:0007829|PDB:3CJR"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:2NXN"
FT   HELIX           124..132
FT                   /evidence="ECO:0007829|PDB:3CJR"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:3CJR"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:2E34"
SQ   SEQUENCE   147 AA;  15505 MW;  3D8DECEBE85B5FE9 CRC64;
     MKKVVAVVKL QLPAGKATPA PPVGPALGQH GANIMEFVKA FNAATANMGD AIVPVEITIY
     ADRSFTFVTK TPPASYLIRK AAGLEKGAHK PGREKVGRIT WEQVLEIAKQ KMPDLNTTDL
     EAAARMIAGS ARSMGVEVVG APEVKDA
 
 
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