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Database: UniProt
Entry: D3S1Z2_FERPA
LinkDB: D3S1Z2_FERPA
Original site: D3S1Z2_FERPA 
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}.
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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
//
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