ID   RL3_PYRNV               Reviewed;         338 AA.
AC   B1YD88;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=Tneu_0813;
OS   Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS   V24Sta) (Thermoproteus neutrophilus).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=444157;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L14 and L24e. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR   EMBL; CP001014; ACB39751.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1YD88; -.
DR   SMR; B1YD88; -.
DR   STRING; 444157.Tneu_0813; -.
DR   EnsemblBacteria; ACB39751; ACB39751; Tneu_0813.
DR   KEGG; tne:Tneu_0813; -.
DR   eggNOG; arCOG04070; Archaea.
DR   HOGENOM; CLU_033361_2_0_2; -.
DR   OMA; HQRTEYN; -.
DR   Proteomes; UP000001694; Chromosome.
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   Gene3D; 4.10.960.10; -; 1.
DR   HAMAP; MF_01325_A; Ribosomal_L3_A; 1.
DR   InterPro; IPR045077; L3_arc_euk.
DR   InterPro; IPR000597; Ribosomal_L3.
DR   InterPro; IPR019928; Ribosomal_L3_arc.
DR   InterPro; IPR019926; Ribosomal_L3_CS.
DR   InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR11363; PTHR11363; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR03626; L3_arch; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..338
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000353628"
FT   REGION          230..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   338 AA;  37426 MW;  CB5CCBE213A437E6 CRC64;
     MGLKINRPRR GSMGVYPRKR AADIVPRVRT WPEVNLGKPA LLGFAAYKAG MLHAVVVEDR
     PTSPLYGKEV VRPVTVLDAP PLFIWGFRLY TLDPTNGYRR SIAEVWAPEL PAYIRRVLTL
     PEKADVDKQM KKVEEFKDVA VDVRALVATQ PHLSGIGKKT PELLEIPIGG VPSVDERIKF
     AVSLLGKTVS PKEVFTAGQL VDVIAVTKGK GYQGVIKRFG VTILPRWHKH RKGHRRTGTI
     GPQAPALMFT QPRPGQMGFH QRTEYNKRVV KIGDNGAEIT PKSGFLHYGV IRGPYILIQG
     TVPGAKKRLV VLRHPARPPK KAPPAAEPQV VWLSSQSI