RL3_PYRAB
ID RL3_PYRAB Reviewed; 361 AA.
AC Q9V1T5; G8ZHX6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=PYRAB03420;
GN ORFNames=PAB2120;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49264.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69719.1; -; Genomic_DNA.
DR PIR; A75148; A75148.
DR RefSeq; WP_010867464.1; NC_000868.1.
DR AlphaFoldDB; Q9V1T5; -.
DR SMR; Q9V1T5; -.
DR STRING; 272844.PAB2120; -.
DR EnsemblBacteria; CAB49264; CAB49264; PAB2120.
DR GeneID; 1495232; -.
DR KEGG; pab:PAB2120; -.
DR PATRIC; fig|272844.11.peg.363; -.
DR eggNOG; arCOG04070; Archaea.
DR HOGENOM; CLU_033361_2_0_2; -.
DR OMA; HQRTEYN; -.
DR OrthoDB; 31722at2157; -.
DR PhylomeDB; Q9V1T5; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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..361
FT /note="50S ribosomal protein L3"
FT /id="PRO_0000077216"
FT REGION 339..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 40853 MW; B9B69823FB784A0A CRC64;
MGKVHRPRRG SLAFSPRKRA KSIVPRIRSW PKETEVRMLG FAGYKAGMTH ILMIDDEPGL
TNGKEIFMPV TIIETPPLRV FGIRAYRQGY LGLETATEVI VPDFELDNYV SKKAKGRKFT
FYQLLKRRIA TLPKNYTKDD FEQKLGNLED MIKEGEIVEV RALVATQPWV IKLKKKPEVM
EYAIGGTSVE EKFNYIKEKL GKELRVGEVL KEGELLDVIA VTKGKGTQGP VKRWGIKLRA
HKDSKGRRKV GSIGPWHPAR VMWTVPMAGQ MGFHHRTELN KRLIAIGENG KLVIDGNEIE
ITPKGGFPHY GIVRSDFMMI AGSVPGAIKR IIRVRPAIRP PKKKPPVQRP QITYVSVESK
Q