ID A0A0M0C1D8_9ARCH Unreviewed; 104 AA.
AC A0A0M0C1D8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Large ribosomal subunit protein P1 {ECO:0000256|HAMAP-Rule:MF_01478};
GN Name=rpl12p {ECO:0000313|EMBL:KON34500.1};
GN Synonyms=rpl12 {ECO:0000256|HAMAP-Rule:MF_01478};
GN ORFNames=AC479_00055 {ECO:0000313|EMBL:KON34500.1};
OS miscellaneous Crenarchaeota group-6 archaeon AD8-1.
OC Archaea; Candidatus Bathyarchaeota; Candidatus Bathyarchaeia.
OX NCBI_TaxID=1685126 {ECO:0000313|EMBL:KON34500.1, ECO:0000313|Proteomes:UP000037259};
RN [1] {ECO:0000313|EMBL:KON34500.1, ECO:0000313|Proteomes:UP000037259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD8-1 {ECO:0000313|EMBL:KON34500.1};
RA Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA Teske A.P.;
RT "New insights into the roles of widespread benthic archaea in carbon and
RT nitrogen cycling.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KON34500.1}.
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DR EMBL; LFWW01000001; KON34500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0C1D8; -.
DR STRING; 1685126.AC479_00055; -.
DR PATRIC; fig|1685126.3.peg.736; -.
DR Proteomes; UP000037259; 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 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 59..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 104 AA; 11131 MW; C096E7305B746348 CRC64;
MEYVYAAMLL HKAGKEISEE NVSNILTAAG ITVDAVRVKA LVASLSEVDI DEAIKSAPTM
MTAPVSAPET PTKSEEKKPK EEKKPKDEKE QEDAALEGLG ALFG
//