ID   T1IR02_STRMM            Unreviewed;       304 AA.
AC   T1IR02;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Large ribosomal subunit protein uL18 {ECO:0000256|ARBA:ARBA00035197};
DE   AltName: Full=60S ribosomal protein L5 {ECO:0000256|ARBA:ARBA00035352};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR003483-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR003483-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
CC   -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell. The small
CC       ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC       encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC       molecules. The large subunit (LSU) contains the ribosomal catalytic
CC       site termed the peptidyl transferase center (PTC), which catalyzes the
CC       formation of peptide bonds, thereby polymerizing the amino acids
CC       delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC       leave the ribosome through a tunnel in the LSU and interact with
CC       protein factors that function in enzymatic processing, targeting, and
CC       the membrane insertion of nascent chains at the exit of the ribosomal
CC       tunnel. {ECO:0000256|ARBA:ARBA00004021}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000256|ARBA:ARBA00007116}.
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DR   EMBL; JH431327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1IR02; -.
DR   STRING; 126957.T1IR02; -.
DR   EnsemblMetazoa; SMAR003483-RA; SMAR003483-PA; SMAR003483.
DR   eggNOG; KOG0875; Eukaryota.
DR   HOGENOM; CLU_056222_1_0_1; -.
DR   OMA; CQIASAH; -.
DR   OrthoDB; 1105861at2759; -.
DR   PhylomeDB; T1IR02; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
DR   GO; GO:0022626; C:cytosolic ribosome; IEA:UniProt.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0008097; F:5S rRNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd00432; Ribosomal_L18_L5e; 1.
DR   Gene3D; 3.30.420.100; -; 1.
DR   HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR   InterPro; IPR005485; Rbsml_uL18_euk/arc.
DR   InterPro; IPR025607; Ribosomal_uL18_C_euk.
DR   PANTHER; PTHR23410:SF12; 60S RIBOSOMAL PROTEIN L5; 1.
DR   PANTHER; PTHR23410; RIBOSOMAL PROTEIN L5-RELATED; 1.
DR   Pfam; PF14204; Ribosomal_L18_c; 1.
DR   Pfam; PF17144; Ribosomal_L5e; 1.
DR   PRINTS; PR00058; RIBOSOMALL5.
DR   SUPFAM; SSF53137; Translational machinery components; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT   DOMAIN          239..293
FT                   /note="Large ribosomal subunit protein uL18 C-terminal
FT                   eukaryotes"
FT                   /evidence="ECO:0000259|Pfam:PF14204"
SQ   SEQUENCE   304 AA;  35049 MW;  955CE05CB99EDEC7 CRC64;
     MVKKGFVKVI KNKAYFKRFQ VKFKRRREGK TDYFARKRLV VQDKNKYNTP KYRMIVRTTN
     TDIICQVAYA RIEGDVVVCA AYAHELPRYG VKVGLTNYAA AYCTGLLLAR RLLKKLKLDK
     IYVGCEEATG EEYNVEDIDG KPGAFRAYLD VGLARTTTGA RVFGAMKGAV DGGIDIPHSN
     KRFPGYNSES KDFHADVHRK HIFGQHVADY MKHLMEEDDG AYKRQFSRYI KVGIQADQIE
     KIYKNAHKAI RAQPDHKPVV KDRSKMIKKR WNRAKMSLAE RKNRINLKKA SYLKKLEAEA
     KKTE
//