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Database: UniProt
Entry: U2NAF5_9CLOT
LinkDB: U2NAF5_9CLOT
Original site: U2NAF5_9CLOT 
ID   U2NAF5_9CLOT            Unreviewed;       104 AA.
AC   U2NAF5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Large ribosomal subunit protein uL24 {ECO:0000256|ARBA:ARBA00035206, ECO:0000256|HAMAP-Rule:MF_01326};
GN   Name=rplX {ECO:0000256|HAMAP-Rule:MF_01326};
GN   ORFNames=CINTURNW_0063 {ECO:0000313|EMBL:ERK32497.1};
OS   Clostridium intestinale URNW.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK32497.1, ECO:0000313|Proteomes:UP000016721};
RN   [1] {ECO:0000313|EMBL:ERK32497.1, ECO:0000313|Proteomes:UP000016721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URNW {ECO:0000313|EMBL:ERK32497.1,
RC   ECO:0000313|Proteomes:UP000016721};
RX   PubMed=24136853;
RA   Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT   "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT   Clostridium intestinale Strain URNW.";
RL   Genome Announc. 1:e00871-13(2013).
CC   -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC       tunnel on the outside of the subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01326}.
CC   -!- FUNCTION: One of two assembly initiator proteins, it binds directly to
CC       the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000256|HAMAP-Rule:MF_01326}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01326}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC       {ECO:0000256|ARBA:ARBA00010618, ECO:0000256|HAMAP-Rule:MF_01326}.
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:ERK32497.1}.
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DR   EMBL; APJA01000001; ERK32497.1; -; Genomic_DNA.
DR   RefSeq; WP_021800165.1; NZ_KI273145.1.
DR   AlphaFoldDB; U2NAF5; -.
DR   STRING; 1294142.CINTURNW_0063; -.
DR   PATRIC; fig|1294142.3.peg.61; -.
DR   eggNOG; COG0198; Bacteria.
DR   HOGENOM; CLU_093315_2_3_9; -.
DR   OrthoDB; 9807419at2; -.
DR   Proteomes; UP000016721; 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:0019843; F: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; cd06089; KOW_RPL26; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR003256; Ribosomal_uL24.
DR   InterPro; IPR041988; Ribosomal_uL24_KOW.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   NCBIfam; TIGR01079; rplX_bact; 1.
DR   PANTHER; PTHR12903:SF0; 39S RIBOSOMAL PROTEIN L24, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12903; MITOCHONDRIAL RIBOSOMAL PROTEIN L24; 1.
DR   Pfam; PF00467; KOW; 1.
DR   Pfam; PF17136; ribosomal_L24; 1.
DR   SMART; SM00739; KOW; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016721};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01326};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01326,
KW   ECO:0000313|EMBL:ERK32497.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01326};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01326}.
FT   DOMAIN          4..31
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
SQ   SEQUENCE   104 AA;  11403 MW;  A22A8C8DB4CE99FE CRC64;
     MKVHVRKNDT VIVISGQDSG KTGEVLKVIP KSGKVIVKGV NIVSKHQKPN KENMQGGIIK
     KEAAIYSSKV MLYCTKCKNA TRIANKILED GSKVRVCKKC GETF
//
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