ID I7CZH9_NATSJ Unreviewed; 115 AA.
AC I7CZH9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Large ribosomal subunit protein P1 {ECO:0000256|HAMAP-Rule:MF_01478};
GN Name=rpl12 {ECO:0000256|HAMAP-Rule:MF_01478};
GN OrderedLocusNames=NJ7G_3055 {ECO:0000313|EMBL:AFO58276.1};
OS Natrinema sp. (strain J7-2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=406552 {ECO:0000313|EMBL:AFO58276.1, ECO:0000313|Proteomes:UP000006507};
RN [1] {ECO:0000313|EMBL:AFO58276.1, ECO:0000313|Proteomes:UP000006507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J7-2 {ECO:0000313|EMBL:AFO58276.1,
RC ECO:0000313|Proteomes:UP000006507};
RX PubMed=22911826; DOI=10.1371/journal.pone.0041621;
RA Feng J., Liu B., Zhang Z., Ren Y., Li Y., Gan F., Huang Y., Chen X.,
RA Shen P., Wang L., Tang B., Tang X.F.;
RT "The complete genome sequence of Natrinema sp. J7-2, a haloarchaeon capable
RT of growth on synthetic media without amino acid supplements.";
RL PLoS ONE 7:E41621-E41621(2012).
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; CP003412; AFO58276.1; -; Genomic_DNA.
DR RefSeq; WP_014864901.1; NC_018224.1.
DR AlphaFoldDB; I7CZH9; -.
DR STRING; 406552.NJ7G_3055; -.
DR GeneID; 13349674; -.
DR KEGG; nat:NJ7G_3055; -.
DR PATRIC; fig|406552.5.peg.2679; -.
DR eggNOG; arCOG04287; Archaea.
DR HOGENOM; CLU_114656_2_0_2; -.
DR OrthoDB; 3337at2157; -.
DR Proteomes; UP000006507; 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 63..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 115 AA; 11635 MW; 030E1EA51252AFBF CRC64;
MEYVYAALIL NESDEEINED NLTNVLDAAG VDVEESRVKA LVAALEDVDI DEAVSEAAAV
PAGGAAAGGA AGGEAAADEG GEEEEAEETS DVPDTTDDDD DDDEADGEGL GELFG
//
