RL1_METTL
ID RL1_METTL Reviewed; 213 AA.
AC O52704;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
DE AltName: Full=ML6;
DE AltName: Full=MvaL1;
GN Name=rpl1 {ECO:0000255|HAMAP-Rule:MF_01318};
OS Methanothermococcus thermolithotrophicus (Methanococcus
OS thermolithotrophicus).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanothermococcus.
OX NCBI_TaxID=2186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Linhart A., Piendl W.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP BINDING TO ENDOGENOUS 23S RRNA, AND TO METHANOCOCCUS VANNIELII L1 MRNA.
RX PubMed=9746351; DOI=10.1046/j.1432-1327.1998.2560097.x;
RA Koehrer C., Mayer C., Neumair O., Groebner P., Piendl W.;
RT "Interaction of ribosomal L1 proteins from mesophilic and thermophilic
RT Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA.";
RL Eur. J. Biochem. 256:97-105(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=12037305; DOI=10.1107/s0907444902006157;
RA Nevskaya N., Tishchenko S., Paveliev M., Smolinskaya Y., Fedorov R.,
RA Piendl W., Nakamura Y., Toyoda T., Garber M.B., Nikonov S.;
RT "Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus.
RT Functionally important structural invariants on the L1 surface.";
RL Acta Crystallogr. D 58:1023-1029(2002).
CC -!- FUNCTION: Probably involved in E site tRNA release (By similarity).
CC Binds directly to 23S rRNA. {ECO:0000250}.
CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC controls the translation of its operon by binding to its mRNA.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
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DR EMBL; AF044919; AAC64510.1; -; Genomic_DNA.
DR PDB; 1DWU; X-ray; 2.80 A; A/B=1-213.
DR PDBsum; 1DWU; -.
DR AlphaFoldDB; O52704; -.
DR SMR; O52704; -.
DR EvolutionaryTrace; O52704; -.
DR GO; GO:0015934; C:large 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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR HAMAP; MF_01318_A; Ribosomal_L1_A; 1.
DR InterPro; IPR002143; Ribosomal_L1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR InterPro; IPR023669; Ribosomal_L1_arc.
DR InterPro; IPR023673; Ribosomal_L1_CS.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
DR PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Translation regulation; tRNA-binding.
FT CHAIN 1..213
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125802"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:1DWU"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:1DWU"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1DWU"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1DWU"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1DWU"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1DWU"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1DWU"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:1DWU"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:1DWU"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:1DWU"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1DWU"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:1DWU"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1DWU"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1DWU"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:1DWU"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:1DWU"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:1DWU"
FT HELIX 171..188
FT /evidence="ECO:0007829|PDB:1DWU"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1DWU"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:1DWU"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:1DWU"
SQ SEQUENCE 213 AA; 23794 MW; C435C5064300E5A8 CRC64;
MDRENILKAV KEARSLAKPR NFTQSLDLII NLKELDLSRP ENRLKEQVVL PNGRGKEPKI
AVIAKGDLAA QAEEMGLTVI RQDELEELGK NKKMAKKIAN EHDFFIAQAD MMPLVGKTLG
PVLGPRGKMP QPVPANANLT PLVERLKKTV LINTRDKPLF HVLVGNEKMS DEELAENIEA
ILNTVSRKYE KGLYHVKSAY TKLTMGPPAQ IEK
