ID A0A2J2H7P4_9CREN Unreviewed; 168 AA.
AC A0A2J2H7P4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Large ribosomal subunit protein uL11 {ECO:0000256|HAMAP-Rule:MF_00736};
GN Name=rpl11 {ECO:0000256|HAMAP-Rule:MF_00736};
GN ORFNames=B7L68_06205 {ECO:0000313|EMBL:PLC63542.1};
OS Thermoproteus sp. CP80.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=1650659 {ECO:0000313|EMBL:PLC63542.1, ECO:0000313|Proteomes:UP000234457};
RN [1] {ECO:0000313|EMBL:PLC63542.1, ECO:0000313|Proteomes:UP000234457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP80 {ECO:0000313|EMBL:PLC63542.1,
RC ECO:0000313|Proteomes:UP000234457};
RX PubMed=27037359;
RA Urschel M.R., Hamilton T.L., Roden E.E., Boyd E.S.;
RT "Substrate preference, uptake kinetics and bioenergetics in a facultatively
RT autotrophic, thermoacidophilic crenarchaeote.";
RL FEMS Microbiol. Ecol. 92:FIW069-FIW069(2016).
CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors. {ECO:0000256|HAMAP-
CC Rule:MF_00736}.
CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit.
CC Interacts with L10 and the large rRNA to form the base of the stalk.
CC L10 forms an elongated spine to which L12 dimers bind in a sequential
CC fashion forming a multimeric L10(L12)X complex. {ECO:0000256|HAMAP-
CC Rule:MF_00736}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000256|ARBA:ARBA00010537, ECO:0000256|HAMAP-Rule:MF_00736}.
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:PLC63542.1}.
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DR EMBL; LCWM02000026; PLC63542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J2H7P4; -.
DR OrthoDB; 8842at2157; -.
DR Proteomes; UP000234457; 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:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.250; Ribosomal protein L11, C-terminal domain; 1.
DR Gene3D; 3.30.1550.10; Ribosomal protein L11/L12, N-terminal domain; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_uL11.
DR InterPro; IPR020783; Ribosomal_uL11_C.
DR InterPro; IPR036769; Ribosomal_uL11_C_sf.
DR InterPro; IPR036796; Ribosomal_uL11_N_sf.
DR PANTHER; PTHR11661:SF1; 39S RIBOSOMAL PROTEIN L11, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11661; 60S RIBOSOMAL PROTEIN L12; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF54747; Ribosomal L11/L12e N-terminal domain; 1.
DR SUPFAM; SSF46906; Ribosomal protein L11, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00736};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00736}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00736};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00736}.
FT DOMAIN 71..138
FT /note="Large ribosomal subunit protein uL11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00298"
SQ SEQUENCE 168 AA; 18191 MW; 719F18307B02EDC4 CRC64;
MAKRIINVPL QGGRFAPNPQ FQDALKSAGL DPNAVSQRIQ EAVKRYSGFP ISKIELEVDE
STRNFDVLVR LPPMGDLLLK VLGKDAGPHD AAKETIGDLS MEKIVQMAVA KYPELKSRSL
KSAVKQVLST CKAMGITVGG KPAAEVMREV DGGAYDDMIK KAEEQLAP
//
