ID M0EHL8_9EURY Unreviewed; 114 AA.
AC M0EHL8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Large ribosomal subunit protein P1 {ECO:0000256|HAMAP-Rule:MF_01478};
GN Name=rpl12p {ECO:0000313|EMBL:ELZ47250.1};
GN Synonyms=rpl12 {ECO:0000256|HAMAP-Rule:MF_01478};
GN ORFNames=C463_02998 {ECO:0000313|EMBL:ELZ47250.1};
OS Halorubrum californiense DSM 19288.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227465 {ECO:0000313|EMBL:ELZ47250.1, ECO:0000313|Proteomes:UP000011586};
RN [1] {ECO:0000313|EMBL:ELZ47250.1, ECO:0000313|Proteomes:UP000011586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19288 {ECO:0000313|EMBL:ELZ47250.1,
RC ECO:0000313|Proteomes:UP000011586};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ47250.1}.
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DR EMBL; AOJK01000015; ELZ47250.1; -; Genomic_DNA.
DR RefSeq; WP_008440928.1; NZ_AOJK01000015.1.
DR AlphaFoldDB; M0EHL8; -.
DR STRING; 1227465.C463_02998; -.
DR PATRIC; fig|1227465.4.peg.587; -.
DR OrthoDB; 3337at2157; -.
DR Proteomes; UP000011586; Unassembled WGS sequence.
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 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 59..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 114 AA; 11511 MW; 576239279FE8AD6A CRC64;
MEYVYAALIL NETGEEINED NVTGVLEAAG VDVEESRVKA LVAALEDVDI EEAIETAAAA
PAAGAASGGS ADADASADEA DDDDEADEAD ADDEADDDDE EEGDGGEGLG ELFG
//
