ID W0I0V8_9EURY Unreviewed; 104 AA.
AC W0I0V8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Large ribosomal subunit protein P1 {ECO:0000256|HAMAP-Rule:MF_01478};
GN Name=rpl12 {ECO:0000256|HAMAP-Rule:MF_01478};
GN ORFNames=TES1_0286 {ECO:0000313|EMBL:AHF79681.1};
OS Thermococcus paralvinellae.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=582419 {ECO:0000313|EMBL:AHF79681.1, ECO:0000313|Proteomes:UP000019027};
RN [1] {ECO:0000313|EMBL:AHF79681.1, ECO:0000313|Proteomes:UP000019027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES1 {ECO:0000313|EMBL:AHF79681.1,
RC ECO:0000313|Proteomes:UP000019027};
RX PubMed=25082851; DOI=10.1099/ijs.0.066100-0;
RA Hensley S.A., Jung J.H., Park C.S., Holden J.F.;
RT "Thermococcus paralvinellae sp. nov. and Thermococcus cleftensis sp. nov.
RT of hyperthermophilic heterotrophs from deep-sea hydrothermal vents.";
RL Int. J. Syst. Evol. Microbiol. 64:3655-3659(2014).
CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central role in
CC the interaction of the ribosome with GTP-bound translation factors.
CC {ECO:0000256|HAMAP-Rule:MF_01478}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Homodimer, it forms part of
CC the ribosomal stalk which helps the ribosome interact with GTP-bound
CC translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex,
CC where L10 forms an elongated spine to which the L12 dimers bind in a
CC sequential fashion. {ECO:0000256|HAMAP-Rule:MF_01478}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000256|ARBA:ARBA00005436, ECO:0000256|HAMAP-Rule:MF_01478}.
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DR EMBL; CP006965; AHF79681.1; -; Genomic_DNA.
DR RefSeq; WP_042679577.1; NZ_CP006965.1.
DR AlphaFoldDB; W0I0V8; -.
DR STRING; 582419.TES1_0286; -.
DR GeneID; 24907508; -.
DR KEGG; ths:TES1_0286; -.
DR HOGENOM; CLU_114656_2_0_2; -.
DR OrthoDB; 3337at2157; -.
DR Proteomes; UP000019027; Chromosome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR CDD; cd05832; Ribosomal_L12p; 1.
DR Gene3D; 1.10.10.1410; -; 1.
DR HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR InterPro; IPR038716; P1/P2_N_sf.
DR InterPro; IPR027534; Ribosomal_P1/P2.
DR InterPro; IPR022295; Ribosomal_P1_arc.
DR NCBIfam; TIGR03685; ribo_P1_arch; 1.
DR PANTHER; PTHR45696; 60S ACIDIC RIBOSOMAL PROTEIN P1; 1.
DR PANTHER; PTHR45696:SF10; 60S ACIDIC RIBOSOMAL PROTEIN P1-RELATED; 1.
DR Pfam; PF00428; Ribosomal_60s; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01478};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01478}.
FT REGION 70..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 104 AA; 10700 MW; 4B59594513247B48 CRC64;
MEYVYAALLL HAAGKEITEE NLKAVLEAAG VTPDEARIKA LVAALEGVNI DEVIEKAAMP
VAVAAAPAAA PAAAEEAPAQ EEEEEEEEEV SEEEALAGLG ALFG
//
