ID RL19A_SCHPO Reviewed; 193 AA.
AC P05734; O60194;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Large ribosomal subunit protein eL19A {ECO:0000305};
DE AltName: Full=60S ribosomal protein L19-A;
DE AltName: Full=SP-L15 {ECO:0000303|PubMed:6355773};
GN Name=rpl1901; Synonyms=rpl19, rpl19-1, rpl19a; ORFNames=SPBC56F2.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kawamukai M.;
RT "S.pombe ribosomal protein L19 homolog.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PROTEIN SEQUENCE OF 2-30.
RX PubMed=6355773; DOI=10.1007/bf00425772;
RA Otaka E., Higo K., Itoh T.;
RT "Yeast ribosomal proteins: VII. Cytoplasmic ribosomal proteins from
RT Schizosaccharomyces pombe.";
RL Mol. Gen. Genet. 191:519-524(1983).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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. eL19 may play a role in the last stages of translation
CC initiation, in particular subunit joining and shedding/releasing
CC factors. {ECO:0000250|UniProtKB:P0CX82}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and at
CC least 33 different proteins. The large 60S subunit contains 3 rRNA
CC molecules (25S, 5.8S and 5S rRNA) and at least 46 different proteins.
CC eL19 lies in close proximity to the binding site for eukaryotic
CC initiation factor eIF4G. {ECO:0000250|UniProtKB:P0CX82}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- MISCELLANEOUS: There are 2 genes for eL19 in S.pombe.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.
CC {ECO:0000305}.
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DR EMBL; AB015169; BAA28752.1; -; mRNA.
DR EMBL; CU329671; CAA18881.1; -; Genomic_DNA.
DR PIR; S10050; S10050.
DR PIR; T40542; T40542.
DR RefSeq; NP_596715.1; NM_001022640.2.
DR PDB; 8ESQ; EM; 2.80 A; R=1-193.
DR PDB; 8ESR; EM; 3.20 A; R=1-193.
DR PDB; 8ETC; EM; 3.10 A; R=1-193.
DR PDB; 8ETG; EM; 3.40 A; R=1-193.
DR PDB; 8ETJ; EM; 3.20 A; R=1-193.
DR PDB; 8EUG; EM; 2.80 A; R=1-193.
DR PDB; 8EUI; EM; 3.10 A; R=1-193.
DR PDBsum; 8ESQ; -.
DR PDBsum; 8ESR; -.
DR PDBsum; 8ETC; -.
DR PDBsum; 8ETG; -.
DR PDBsum; 8ETJ; -.
DR PDBsum; 8EUG; -.
DR PDBsum; 8EUI; -.
DR AlphaFoldDB; P05734; -.
DR SMR; P05734; -.
DR BioGRID; 277387; 7.
DR STRING; 284812.P05734; -.
DR iPTMnet; P05734; -.
DR MaxQB; P05734; -.
DR PaxDb; 4896-SPBC56F2-02-1; -.
DR EnsemblFungi; SPBC56F2.02.1; SPBC56F2.02.1:pep; SPBC56F2.02.
DR GeneID; 2540870; -.
DR KEGG; spo:SPBC56F2.02; -.
DR PomBase; SPBC56F2.02; rpl1901.
DR VEuPathDB; FungiDB:SPBC56F2.02; -.
DR eggNOG; KOG1696; Eukaryota.
DR HOGENOM; CLU_083919_0_1_1; -.
DR InParanoid; P05734; -.
DR OMA; WMLRIRA; -.
DR PhylomeDB; P05734; -.
DR PRO; PR:P05734; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:PomBase.
DR CDD; cd01417; Ribosomal_L19e_E; 1.
DR Gene3D; 1.10.1200.240; -; 1.
DR Gene3D; 1.10.1650.10; -; 1.
DR HAMAP; MF_01475; Ribosomal_eL19; 1.
DR InterPro; IPR035970; 60S_ribosomal_eL19_sf.
DR InterPro; IPR039547; Ribosomal_eL19.
DR InterPro; IPR000196; Ribosomal_eL19_dom.
DR InterPro; IPR015972; Ribosomal_eL19_dom1.
DR InterPro; IPR033935; Ribosomal_eL19_euk.
DR PANTHER; PTHR10722; 60S RIBOSOMAL PROTEIN L19; 1.
DR PANTHER; PTHR10722:SF0; 60S RIBOSOMAL PROTEIN L19; 1.
DR Pfam; PF01280; Ribosomal_L19e; 1.
DR SMART; SM01416; Ribosomal_L19e; 1.
DR SUPFAM; SSF48140; Ribosomal protein L19 (L19e); 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6355773"
FT CHAIN 2..193
FT /note="Large ribosomal subunit protein eL19A"
FT /id="PRO_0000131183"
FT REGION 156..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 24
FT /note="M -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="S -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:8ETC"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:8ETC"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:8ETC"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:8ETC"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:8ETC"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:8ETC"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:8ETC"
FT HELIX 91..111
FT /evidence="ECO:0007829|PDB:8ETC"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:8ETC"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:8ETC"
SQ SEQUENCE 193 AA; 22724 MW; 80B4ABACC075F81A CRC64;
MANLRTQKRL AASVLKCGKR KVWMDPNEIS EISNANSRQN VRKLIKDGLV IRKPNLMHSR
FRIRKTHAAK RLGRHTGYGK RKGTAEARMP SAVVWMRRQR VLRRLLRKYR ESGKIDKHLY
HTLYLEAKGN TFKHKRALIE HIQRAKAEAN RTKLIQEQQD ARRARAKAAR QRRAKAVEEK
REQLYTAAEK IEE
//
