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Database: UniProt
Entry: F0NRD6_SULIH
LinkDB: F0NRD6_SULIH
Original site: F0NRD6_SULIH 
ID   F0NRD6_SULIH            Unreviewed;       106 AA.
AC   F0NRD6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=SiH_1739 {ECO:0000313|EMBL:ADX83087.1};
OS   Sulfolobus islandicus (strain HVE10/4).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=930943 {ECO:0000313|EMBL:ADX83087.1, ECO:0000313|Proteomes:UP000006395};
RN   [1] {ECO:0000313|EMBL:ADX83087.1, ECO:0000313|Proteomes:UP000006395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HVE10/4 {ECO:0000313|EMBL:ADX83087.1,
RC   ECO:0000313|Proteomes:UP000006395};
RX   PubMed=21278296; DOI=10.1128/JB.01487-10;
RA   Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S.,
RA   Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q.,
RA   Huang L., Garrett R.A.;
RT   "Genome analyses of icelandic strains of Sulfolobus islandicus, model
RT   organisms for genetic and virus-host interaction studies.";
RL   J. Bacteriol. 193:1672-1680(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; CP002426; ADX83087.1; -; Genomic_DNA.
DR   RefSeq; WP_012711739.1; NC_017275.1.
DR   AlphaFoldDB; F0NRD6; -.
DR   GeneID; 84062115; -.
DR   KEGG; sih:SiH_1739; -.
DR   HOGENOM; CLU_114656_2_0_2; -.
DR   Proteomes; UP000006395; 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          68..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   106 AA;  11332 MW;  C519E9847D200D32 CRC64;
     MEYIYASLLL HSAKKEINED TLKNILTAAG ISVDEVRLKA VVAALKEVNI DEVLKNAAAM
     PVAVAAQPQA AQAQPAAEEK KEEKKEEEKK GPSEEEIASG LASLFG
//
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