ID H1KZ08_9EURY Unreviewed; 102 AA.
AC H1KZ08;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Large ribosomal subunit protein P1 {ECO:0000256|HAMAP-Rule:MF_01478};
GN Name=rpl12 {ECO:0000256|HAMAP-Rule:MF_01478};
GN ORFNames=MetfoDRAFT_1028 {ECO:0000313|EMBL:EHP86588.1};
OS Methanotorris formicicus Mc-S-70.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanotorris.
OX NCBI_TaxID=647171 {ECO:0000313|EMBL:EHP86588.1, ECO:0000313|Proteomes:UP000003706};
RN [1] {ECO:0000313|EMBL:EHP86588.1, ECO:0000313|Proteomes:UP000003706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mc-S-70 {ECO:0000313|EMBL:EHP86588.1,
RC ECO:0000313|Proteomes:UP000003706};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sieprawska-Lupa M., Takai K., Miyazaki J.,
RA Whitman W., Woyke T.J.;
RT "The draft genome of Methanotorris formicicus Mc-S-70.";
RL Submitted (SEP-2011) 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:EHP86588.1}.
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DR EMBL; AGJL01000022; EHP86588.1; -; Genomic_DNA.
DR RefSeq; WP_007044460.1; NZ_AGJL01000022.1.
DR AlphaFoldDB; H1KZ08; -.
DR STRING; 647171.MetfoDRAFT_1028; -.
DR PATRIC; fig|647171.4.peg.1005; -.
DR OrthoDB; 3337at2157; -.
DR Proteomes; UP000003706; 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 65..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 102 AA; 10378 MW; B9C14FC12AC224DD CRC64;
MEYVYAALLL HAAGKEITED AVKSVLSAAG VDVDDARVKA LVAALEGVNI DEAIENAAMP
VAAAAPAAAP TPAAEEKKEE EKKEEKKEDT TAAAAGLAAL FG
//
