ID A0A2H9HZV6_9ARCH Unreviewed; 101 AA.
AC A0A2H9HZV6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Large ribosomal subunit protein P1 {ECO:0000256|HAMAP-Rule:MF_01478};
GN Name=rpl12p {ECO:0000313|EMBL:PDM26126.1};
GN Synonyms=rpl12 {ECO:0000256|HAMAP-Rule:MF_01478};
GN ORFNames=CP083_05500 {ECO:0000313|EMBL:PDM26126.1};
OS Candidatus Bathyarchaeota archaeon B24-2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=2041147 {ECO:0000313|EMBL:PDM26126.1, ECO:0000313|Proteomes:UP000228824};
RN [1] {ECO:0000313|EMBL:PDM26126.1, ECO:0000313|Proteomes:UP000228824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B24-2 {ECO:0000313|EMBL:PDM26126.1};
RA Feng X., Perumal V., Wang F.;
RT "Metabolic analysis of an uncultured genome Bathyarchaeota B242 based on
RT metagenomic technology.";
RL Submitted (SEP-2017) 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:PDM26126.1}.
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DR EMBL; PCNA01000052; PDM26126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9HZV6; -.
DR Proteomes; UP000228824; 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; 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 62..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 101 AA; 10827 MW; AF223FA9580E8F8C CRC64;
MEYVYAAMLL HKAGKEITEE NLTEVLKAAG VNVEPAKVKA LVASLSEIDI DEAIKSAPMF
AAAPAPAAPA EEKKEEVKEE KKEEEEKEEE AALEGLGALF G
//