ID   RK5_EUGLO               Reviewed;         179 AA.
AC   P14757;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=50S ribosomal protein L5, plastid;
GN   Name=rpl5;
OS   Euglena longa (Euglenophycean alga) (Astasia longa).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCAP 1204-17a;
RX   PubMed=2078869; DOI=10.1007/bf00309917;
RA   Siemeister G., Buchholz C., Hachtel W.;
RT   "Genes for ribosomal proteins are retained on the 73 kb DNA from Astasia
RT   longa that resembles Euglena chloroplast DNA.";
RL   Curr. Genet. 18:457-464(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCAP 1204-17a;
RX   PubMed=7972503; DOI=10.1104/pp.105.4.1443;
RA   Gockel G., Baier S., Hachtel W.;
RT   "Plastid ribosomal protein genes from the nonphotosynthetic flagellate
RT   Astasia longa.";
RL   Plant Physiol. 105:1443-1444(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1204-17a;
RX   PubMed=11212895; DOI=10.1078/s1434-4610(04)70033-4;
RA   Gockel G., Hachtel W.;
RT   "Complete gene map of the plastid genome of the nonphotosynthetic euglenoid
RT   flagellate Astasia longa.";
RL   Protist 151:347-351(2000).
CC   -!- FUNCTION: Binds 5S rRNA, forms part of the central protuberance of the
CC       50S subunit. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit; contacts the 5S rRNA.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ294725; CAC24576.1; -; Genomic_DNA.
DR   PIR; S14150; R5IT5.
DR   RefSeq; NP_074965.1; NC_002652.1.
DR   AlphaFoldDB; P14757; -.
DR   SMR; P14757; -.
DR   GeneID; 802522; -.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.30.1440.10; -; 1.
DR   HAMAP; MF_01333_B; Ribosomal_L5_B; 1.
DR   InterPro; IPR002132; Ribosomal_L5.
DR   InterPro; IPR020930; Ribosomal_L5_bac-type.
DR   InterPro; IPR031309; Ribosomal_L5_C.
DR   InterPro; IPR020929; Ribosomal_L5_CS.
DR   InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR   InterPro; IPR031310; Ribosomal_L5_N.
DR   PANTHER; PTHR11994; PTHR11994; 1.
DR   Pfam; PF00281; Ribosomal_L5; 1.
DR   Pfam; PF00673; Ribosomal_L5_C; 1.
DR   PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR   SUPFAM; SSF55282; SSF55282; 1.
DR   PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE   3: Inferred from homology;
KW   Plastid; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..179
FT                   /note="50S ribosomal protein L5, plastid"
FT                   /id="PRO_0000125035"
SQ   SEQUENCE   179 AA;  20161 MW;  3B0B4746077A8248 CRC64;
     MQKLKSIYIT KVCPILVNEF LYTNFFEIPK INKVVISRGF GESCNSSKIL ESLLVELKNI
     SGQKPILCKS KNSISNFKVK KGMPIGMFVT LHGDKMYSFL DRLINLSFPR MRDFNGLNIK
     GFDGFGNYNV GLSEQSIFPE IEYSSILKNK GMNITIVTTA KTDLESFSLL KGLGFPFCV