ID RLA2_LEIBR Reviewed; 105 AA.
AC O44010; A4HIV9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 08-NOV-2023, entry version 97.
DE RecName: Full=Large ribosomal subunit protein P2 {ECO:0000305};
DE AltName: Full=60S acidic ribosomal protein P2;
DE AltName: Full=Acidic ribosomal P2 beta protein;
DE Short=P2B-protein;
GN Name=LIP2; ORFNames=LbrM30_V2.3760, LbrM_30_3760;
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=MHOM/PE/85/LH166;
RA Padilla C., Carrillo C., Montoya Y.;
RT "Characterization of the ribosomal P2 beta protein from Leishmania (V.)
RT braziliensis.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904;
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [3]
RP STRUCTURE BY NMR OF 93-105.
RX PubMed=14988012; DOI=10.1016/s0014-5793(04)00088-2;
RA Soares M.R., Bisch P.M., Campos de Carvalho A.C., Valente A.P.,
RA Almeida F.C.;
RT "Correlation between conformation and antibody binding: NMR structure of
RT cross-reactive peptides from T. cruzi, human and L. braziliensis.";
RL FEBS Lett. 560:134-140(2004).
CC -!- FUNCTION: Plays an important role in the elongation step of protein
CC synthesis. {ECO:0000250}.
CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF045020; AAC02540.1; -; mRNA.
DR EMBL; FR799005; CAM40525.1; -; Genomic_DNA.
DR RefSeq; XP_001566999.1; XM_001566949.1.
DR PDB; 1S4H; NMR; -; A=93-105.
DR PDBsum; 1S4H; -.
DR AlphaFoldDB; O44010; -.
DR SMR; O44010; -.
DR STRING; 5660.O44010; -.
DR GeneID; 5417901; -.
DR KEGG; lbz:LBRM_30_3760; -.
DR VEuPathDB; TriTrypDB:LbrM.30.3760; -.
DR VEuPathDB; TriTrypDB:LBRM2903_300045000; -.
DR InParanoid; O44010; -.
DR OMA; MKVIASY; -.
DR EvolutionaryTrace; O44010; -.
DR Proteomes; UP000007258; Chromosome 30.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0002182; P:cytoplasmic translational elongation; IEA:InterPro.
DR CDD; cd05833; Ribosomal_P2; 1.
DR Gene3D; 1.10.10.1410; -; 1.
DR HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR InterPro; IPR038716; P1/P2_N_sf.
DR InterPro; IPR027534; Ribosomal_P1/P2.
DR InterPro; IPR001859; Ribosomal_P1/P2_euk.
DR InterPro; IPR044076; Ribosomal_P2.
DR PANTHER; PTHR21141; 60S ACIDIC RIBOSOMAL PROTEIN FAMILY MEMBER; 1.
DR PANTHER; PTHR21141:SF58; ACIDIC RIBOSOMAL PROTEIN P2, PUTATIVE-RELATED; 1.
DR Pfam; PF00428; Ribosomal_60s; 1.
DR PRINTS; PR00456; RIBOSOMALP2.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..105
FT /note="Large ribosomal subunit protein P2"
FT /id="PRO_0000157655"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1S4H"
SQ SEQUENCE 105 AA; 10601 MW; 16A72873D5AB3602 CRC64;
MQYLAAYALV ALSGKTPCKA DVQAVLKAAG VAIELSRVDA LFQELEGKSF DELMTEGRSK
LVGSGSAAPA AAASTAGAAV AAAADAKKEA SEEEADDDMG FGLFD
//
