ID NAM9_YEAST Reviewed; 486 AA. AC P27929; D6W145; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 27-MAR-2024, entry version 184. DE RecName: Full=Small ribosomal subunit protein uS4m {ECO:0000303|PubMed:28154081}; DE AltName: Full=37S ribosomal protein NAM9, mitochondrial; DE AltName: Full=Nuclear accommodation of mitochondria protein 9; GN Name=NAM9; Synonyms=MNA6; OrderedLocusNames=YNL137C; GN ORFNames=N1211, N1840; 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. RX PubMed=1729612; DOI=10.1128/mcb.12.1.402-412.1992; RA Boguta M., Dmochowska A., Borsuk P., Wrobel K., Gargouri A., Lazowska J., RA Slonimski P.P., Szczesniak B., Kruszewska A.; RT "NAM9 nuclear suppressor of mitochondrial ochre mutations in Saccharomyces RT cerevisiae codes for a protein homologous to S4 ribosomal proteins from RT chloroplasts, bacteria, and eucaryotes."; RL Mol. Cell. Biol. 12:402-412(1992). RN [2] RP SEQUENCE REVISION. RA Boguta M.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8619318; DOI=10.1002/yea.320111210; RA Mallet L., Bussereau F., Jacquet M.; RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2, RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine RT deaminase gene and 14 new open reading frames."; RL Yeast 11:1195-1209(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(1997). RN [5] 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 [6] RP FUNCTION, AND MUTAGENESIS OF SER-82. RX PubMed=7557422; DOI=10.1016/0378-1119(95)00311-s; RA Dmochowska A., Konopinska A., Krzymowska M., Szczesniak B., Boguta M.; RT "The NAM9-1 suppressor mutation in a nuclear gene encoding ribosomal RT mitochondrial protein of Saccharomyces cerevisiae."; RL Gene 162:81-85(1995). RN [7] RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-109; ARG-111; PRO-424 RP AND PRO-438. RX PubMed=10529174; DOI=10.1021/bi990058u; RA Biswas T.K., Getz G.S.; RT "The single amino acid changes in the yeast mitochondrial S4 ribosomal RT protein cause temperature-sensitive defect in the accumulation of RT mitochondrial 15S rRNA."; RL Biochemistry 38:13042-13054(1999). RN [8] RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL COMPLEX, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=11278769; DOI=10.1074/jbc.m010864200; RA Saveanu C., Fromont-Racine M., Harington A., Ricard F., Namane A., RA Jacquier A.; RT "Identification of 12 new yeast mitochondrial ribosomal proteins including RT 6 that have no prokaryotic homologues."; RL J. Biol. Chem. 276:15861-15867(2001). RN [9] RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL 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 [10] 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 [11] 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 [12] 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 [13] 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 [14] RP STRUCTURE BY ELECTRON MICROSCOPY (3.25 ANGSTROMS), AND SUBUNIT. RX PubMed=28154081; DOI=10.1126/science.aal2415; RA Desai N., Brown A., Amunts A., Ramakrishnan V.; RT "The structure of the yeast mitochondrial ribosome."; RL Science 355:528-531(2017). 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. {ECO:0000305|PubMed:25609543, CC ECO:0000305|PubMed:28154081}. CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt- CC SSU). 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 uS3m, uS4m and uS5m form the narrow entry site of the mRNA channel. CC {ECO:0000269|PubMed:10529174, ECO:0000269|PubMed:11278769, CC ECO:0000269|PubMed:12392552, ECO:0000269|PubMed:28154081}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10529174, CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. CC Note=Mitoribosomes are tethered to the mitochondrial inner membrane and CC spatially aligned with the membrane insertion machinery through two CC distinct membrane contact sites, formed by the 21S rRNA expansion CC segment 96-ES1 and the inner membrane protein MBA1. CC {ECO:0000269|PubMed:25609543}. CC -!- MISCELLANEOUS: Present with 3270 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 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; M60730; AAA19439.1; -; Unassigned_DNA. DR EMBL; Z46843; CAA86888.1; -; Genomic_DNA. DR EMBL; Z71413; CAA96019.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10411.1; -; Genomic_DNA. DR PIR; S55146; S55146. DR RefSeq; NP_014262.3; NM_001182975.3. DR PDB; 5MRC; EM; 3.25 A; DD=1-486. DR PDB; 5MRE; EM; 3.75 A; DD=1-486. DR PDB; 5MRF; EM; 4.97 A; DD=1-486. DR PDB; 8D8J; EM; 3.80 A; D=1-486. DR PDB; 8D8K; EM; 3.13 A; D=1-486. DR PDB; 8D8L; EM; 2.60 A; D=1-486. DR PDBsum; 5MRC; -. DR PDBsum; 5MRE; -. DR PDBsum; 5MRF; -. DR PDBsum; 8D8J; -. DR PDBsum; 8D8K; -. DR PDBsum; 8D8L; -. DR AlphaFoldDB; P27929; -. DR EMDB; EMD-3551; -. DR EMDB; EMD-3552; -. DR EMDB; EMD-3553; -. DR SMR; P27929; -. DR BioGRID; 35689; 94. DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit. DR DIP; DIP-6702N; -. DR IntAct; P27929; 34. DR MINT; P27929; -. DR STRING; 4932.YNL137C; -. DR iPTMnet; P27929; -. DR MaxQB; P27929; -. DR PaxDb; 4932-YNL137C; -. DR PeptideAtlas; P27929; -. DR EnsemblFungi; YNL137C_mRNA; YNL137C; YNL137C. DR GeneID; 855585; -. DR KEGG; sce:YNL137C; -. DR AGR; SGD:S000005081; -. DR SGD; S000005081; NAM9. DR VEuPathDB; FungiDB:YNL137C; -. DR eggNOG; ENOG502QTS9; Eukaryota. DR HOGENOM; CLU_026386_0_0_1; -. DR InParanoid; P27929; -. DR OMA; GDMFQVE; -. DR OrthoDB; 1347927at2759; -. DR BioCyc; YEAST:G3O-33156-MONOMER; -. DR BioGRID-ORCS; 855585; 1 hit in 10 CRISPR screens. DR PRO; PR:P27929; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P27929; Protein. DR GO; GO:0005743; C:mitochondrial inner membrane; NAS:ComplexPortal. DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IBA:GO_Central. DR CDD; cd00165; S4; 1. DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1. DR InterPro; IPR022801; Ribosomal_uS4. DR InterPro; IPR018079; Ribosomal_uS4_CS. DR InterPro; IPR002942; S4_RNA-bd. DR InterPro; IPR036986; S4_RNA-bd_sf. DR PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1. DR PANTHER; PTHR11831:SF4; 37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1. DR PROSITE; PS00632; RIBOSOMAL_S4; 1. DR PROSITE; PS50889; S4; 1. PE 1: Evidence at protein level; KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1..486 FT /note="Small ribosomal subunit protein uS4m" FT /id="PRO_0000030639" FT DOMAIN 103..172 FT /note="S4 RNA-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182" FT MUTAGEN 82 FT /note="S->L: In NAM9-1; suppressor for ocher mutations in FT mitochondrial DNA, possibly through decreasing the fidelity FT of translation." FT /evidence="ECO:0000269|PubMed:7557422" FT MUTAGEN 109 FT /note="L->F: In MNA6-3; causes temperature-dependent loss FT of the 15S rRNA." FT /evidence="ECO:0000269|PubMed:10529174" FT MUTAGEN 111 FT /note="R->K: In MNA6-1; causes temperature-dependent loss FT of the 15S rRNA." FT /evidence="ECO:0000269|PubMed:10529174" FT MUTAGEN 424 FT /note="P->L: In MNA6-4; causes temperature-dependent loss FT of the 15S rRNA." FT /evidence="ECO:0000269|PubMed:10529174" FT MUTAGEN 438 FT /note="P->L: In MNA6-2; causes temperature-dependent loss FT of the 15S rRNA." FT /evidence="ECO:0000269|PubMed:10529174" FT TURN 11..13 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 22..31 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 41..55 FT /evidence="ECO:0007829|PDB:8D8L" FT TURN 56..59 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 62..68 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 93..103 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 105..111 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 118..126 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 149..152 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 154..161 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 168..191 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 193..206 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 212..218 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 375..379 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 388..391 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 395..401 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 405..410 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 414..416 FT /evidence="ECO:0007829|PDB:8D8K" FT STRAND 419..421 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 439..444 FT /evidence="ECO:0007829|PDB:8D8L" FT TURN 445..448 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 449..452 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 462..465 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 471..482 FT /evidence="ECO:0007829|PDB:8D8L" FT TURN 483..485 FT /evidence="ECO:0007829|PDB:8D8L" SQ SEQUENCE 486 AA; 56356 MW; 4A5CB85B354955D1 CRC64; MPRKANLLKS LARGRVRTSF NKYNLFNLYK KGGVDLKSKS LYQQKWTAKQ ETRAYHGEHL TEKRWQTVFK PKLDSVAQLD ASLRGGEIKE TPFLLQTFAV LEKRLDFALF RAMFASSVRQ ARQFILHGNV RVNGVKIKHP SYTLKPGDMF SVKPDKVLEA LGAKKPSFQE ALKIDKTQIV LWNKYVKEAK TEPKEVWEKK LENFEKMSDS NPKKLQFQEF LRQYNKNLES QQYNALKGCT QEGILRKLLN VEKEIGKSNN EPLSIDELKQ GLPEIQDSQL LESLNNAYQE FFKSGEIRRE IISKCQPDEL ISLATEMMNP NETTKKELSD GAKSALRSGK RIIAESVKLW TKNITDHFKT RMSDISDGSL TFDPKWAKNL KYHDPIKLSE LEGDEPKARK LINLPWQKNY VYGRQDPKKP FFTPWKPRPF LSPFAILPHH LEISFKTCHA VYLRDPVARP GQSEVISPFD VPVHERAYMY YLRNGK //