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Database: UniProt
Entry: A0A0F7IGZ3_9EURY
LinkDB: A0A0F7IGZ3_9EURY
Original site: A0A0F7IGZ3_9EURY 
ID   A0A0F7IGZ3_9EURY        Unreviewed;       157 AA.
AC   A0A0F7IGZ3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 29.
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=GAH_00075 {ECO:0000313|EMBL:AKG92565.1};
OS   Geoglobus ahangari.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Geoglobus.
OX   NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG92565.1, ECO:0000313|Proteomes:UP000034723};
RN   [1] {ECO:0000313|EMBL:AKG92565.1, ECO:0000313|Proteomes:UP000034723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=234 {ECO:0000313|EMBL:AKG92565.1,
RC   ECO:0000313|Proteomes:UP000034723};
RA   Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA   Kashefi K.;
RT   "The complete genome sequence of the hyperthermophilic, obligate iron-
RT   reducing archaeon Geoglobus ahangari strain 234T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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       ECO:0000256|RuleBase:RU003978}.
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DR   EMBL; CP011267; AKG92565.1; -; Genomic_DNA.
DR   RefSeq; WP_048094177.1; NZ_CP011267.1.
DR   AlphaFoldDB; A0A0F7IGZ3; -.
DR   STRING; 113653.GAH_00075; -.
DR   GeneID; 24802665; -.
DR   KEGG; gah:GAH_00075; -.
DR   PATRIC; fig|113653.22.peg.74; -.
DR   HOGENOM; CLU_074237_4_0_2; -.
DR   InParanoid; A0A0F7IGZ3; -.
DR   OrthoDB; 8842at2157; -.
DR   Proteomes; UP000034723; Chromosome.
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   CDD; cd00349; Ribosomal_L11; 1.
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; IPR020784; Ribosomal_uL11_N.
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   Pfam; PF03946; Ribosomal_L11_N; 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   Reference proteome {ECO:0000313|Proteomes:UP000034723};
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          5..62
FT                   /note="Large ribosomal subunit protein uL11 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03946"
FT   DOMAIN          68..135
FT                   /note="Large ribosomal subunit protein uL11 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00298"
SQ   SEQUENCE   157 AA;  16838 MW;  BA9F6AD1E3171C26 CRC64;
     MPQVVEVLVP GGKATPGPPL GPAIGPLGLN VKQVVDRINE ATKDFDGLPV PVKIIAKEDR
     TFDIEVGVPP VSALIKKELG LEKGSKATGR EYVGDLTMEQ VIKIAKIKQK QMLAYDLKAA
     VLEVLGTAVS MGVKVEGKHP KEVQQEIKEG KIEIPEE
//
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