ID D3S1Z2_FERPA Unreviewed; 106 AA.
AC D3S1Z2;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=Ferp_0268 {ECO:0000313|EMBL:ADC64449.1};
OS Ferroglobus placidus (strain DSM 10642 / AEDII12DO).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Ferroglobus.
OX NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC64449.1, ECO:0000313|Proteomes:UP000002613};
RN [1] {ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D.,
RA Lovley D., Kyrpides N., Anderson I.J., Woyke T.;
RT "Complete sequence of Ferroglobus placidus DSM 10642.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADC64449.1, ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RX PubMed=22180810; DOI=10.4056/sigs.2225018;
RA Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A.,
RA Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T.,
RA Lovley D., Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Ferroglobus placidus AEDII12DO.";
RL Stand. Genomic Sci. 5:50-60(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001899; ADC64449.1; -; Genomic_DNA.
DR AlphaFoldDB; D3S1Z2; -.
DR STRING; 589924.Ferp_0268; -.
DR PaxDb; 589924-Ferp_0268; -.
DR KEGG; fpl:Ferp_0268; -.
DR eggNOG; arCOG04287; Archaea.
DR HOGENOM; CLU_114656_2_0_2; -.
DR Proteomes; UP000002613; 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 Reference proteome {ECO:0000313|Proteomes:UP000002613};
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 68..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 106 AA; 11282 MW; 0BC8B29D1E96E859 CRC64;
MGMEYVYAAL LLHSAGKEIN EENVKAVLEA AGIEVNEARV KALVTALEGI NIDEAISKAA
FVAAPAAAPA APAEEAKEEE KKEEKKEEEE EVKEEEVLEG LGALFG
//