ID   IMG1_YEAST              Reviewed;         169 AA.
AC   P25626; D6VR55;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Large ribosomal subunit protein bL19m {ECO:0000303|PubMed:24675956};
DE   AltName: Full=54S ribosomal protein IMG1, mitochondrial;
DE   AltName: Full=Integrity of mitochondrial genome protein 1;
DE   AltName: Full=PetCR46;
DE   Flags: Precursor;
GN   Name=IMG1; Synonyms=PETCR46; OrderedLocusNames=YCR046C;
GN   ORFNames=YCR46C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION.
RX   PubMed=8771712;
RX   DOI=10.1002/(sici)1097-0061(199605)12:6<577::aid-yea950>3.0.co;2-2;
RA   Coppee J.-Y., Rieger K.-J., Kaniak A., di Rago J.-P., Groudinsky O.,
RA   Slonimski P.P.;
RT   "PetCR46, a gene which is essential for respiration and integrity of the
RT   mitochondrial genome.";
RL   Yeast 12:577-582(1996).
RN   [5]
RP   IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL LARGE COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12392552; DOI=10.1046/j.1432-1033.2002.03226.x;
RA   Gan X., Kitakawa M., Yoshino K., Oshiro N., Yonezawa K., Isono K.;
RT   "Tag-mediated isolation of yeast mitochondrial ribosome and mass
RT   spectrometric identification of its new components.";
RL   Eur. J. Biochem. 269:5203-5214(2002).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25609543; DOI=10.1038/ncomms7019;
RA   Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.;
RT   "Organization of the mitochondrial translation machinery studied in situ by
RT   cryoelectron tomography.";
RL   Nat. Commun. 6:6019-6019(2015).
RN   [10]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), AND SUBUNIT.
RX   PubMed=24675956; DOI=10.1126/science.1249410;
RA   Amunts A., Brown A., Bai X.C., Llacer J.L., Hussain T., Emsley P., Long F.,
RA   Murshudov G., Scheres S.H., Ramakrishnan V.;
RT   "Structure of the yeast mitochondrial large ribosomal subunit.";
RL   Science 343:1485-1489(2014).
CC   -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a
CC       dedicated translation machinery responsible for the synthesis of
CC       mitochondrial genome-encoded proteins, including at least some of the
CC       essential transmembrane subunits of the mitochondrial respiratory
CC       chain. The mitoribosomes are attached to the mitochondrial inner
CC       membrane and translation products are cotranslationally integrated into
CC       the membrane (PubMed:25609543, PubMed:24675956). bL19m is essential for
CC       respiration (PubMed:8771712). {ECO:0000269|PubMed:8771712,
CC       ECO:0000305|PubMed:24675956, ECO:0000305|PubMed:25609543}.
CC   -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC       LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S)
CC       and a large (54S) subunit. The 37S small subunit contains a 15S
CC       ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large
CC       subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins.
CC       {ECO:0000269|PubMed:12392552, ECO:0000269|PubMed:24675956}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the
CC       mitochondrial inner membrane and spatially aligned with the membrane
CC       insertion machinery through two distinct membrane contact sites, formed
CC       by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein
CC       MBA1. {ECO:0000269|PubMed:25609543}.
CC   -!- MISCELLANEOUS: Present with 4150 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family.
CC       {ECO:0000305}.
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DR   EMBL; X59720; CAA42294.1; -; Genomic_DNA.
DR   EMBL; AY692869; AAT92888.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07524.1; -; Genomic_DNA.
DR   PIR; S19459; S19459.
DR   RefSeq; NP_009975.1; NM_001178760.1.
DR   PDB; 3J6B; EM; 3.20 A; M=1-169.
DR   PDB; 5MRC; EM; 3.25 A; M=16-166.
DR   PDB; 5MRE; EM; 3.75 A; M=16-166.
DR   PDB; 5MRF; EM; 4.97 A; M=16-166.
DR   PDBsum; 3J6B; -.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; P25626; -.
DR   EMDB; EMD-3551; -.
DR   EMDB; EMD-3552; -.
DR   EMDB; EMD-3553; -.
DR   SMR; P25626; -.
DR   BioGRID; 31028; 344.
DR   ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR   DIP; DIP-4995N; -.
DR   IntAct; P25626; 51.
DR   MINT; P25626; -.
DR   STRING; 4932.YCR046C; -.
DR   MaxQB; P25626; -.
DR   PaxDb; 4932-YCR046C; -.
DR   PeptideAtlas; P25626; -.
DR   EnsemblFungi; YCR046C_mRNA; YCR046C; YCR046C.
DR   GeneID; 850413; -.
DR   KEGG; sce:YCR046C; -.
DR   AGR; SGD:S000000642; -.
DR   SGD; S000000642; IMG1.
DR   VEuPathDB; FungiDB:YCR046C; -.
DR   eggNOG; KOG1698; Eukaryota.
DR   HOGENOM; CLU_076387_2_0_1; -.
DR   InParanoid; P25626; -.
DR   OMA; DNFVGYV; -.
DR   OrthoDB; 2047640at2759; -.
DR   BioCyc; YEAST:G3O-29357-MONOMER; -.
DR   BioGRID-ORCS; 850413; 9 hits in 10 CRISPR screens.
DR   PRO; PR:P25626; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25626; Protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; NAS:ComplexPortal.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal.
DR   Gene3D; 2.30.30.790; -; 1.
DR   InterPro; IPR001857; Ribosomal_bL19.
DR   InterPro; IPR038657; Ribosomal_bL19_sf.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR15680:SF9; 39S RIBOSOMAL PROTEIN L19, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR15680; RIBOSOMAL PROTEIN L19; 1.
DR   Pfam; PF01245; Ribosomal_L19; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Transit peptide.
FT   TRANSIT         1..16
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..169
FT                   /note="Large ribosomal subunit protein bL19m"
FT                   /id="PRO_0000030477"
SQ   SEQUENCE   169 AA;  19394 MW;  56C79944D654FA21 CRC64;
     MWSRNVRLLG SWTRSYMVPA TKRKTIPVYP PVQRIASSQI MKQVALSEIE SLDPGAVKRK
     LISKKNKDRL KAGDVVRIVY DSSKCSYDTF VGYILSIDRK QLVQDASLLL RNQIAKTAVE
     IRVPLFSPLI ERIDLLTPHV SSRQRNKHYY IRGTRLDVGD LEAGLRRKK
//