ID RT23_SCHPO Reviewed; 476 AA.
AC O59677;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Small ribosomal subunit protein mS29 {ECO:0000305};
DE AltName: Full=37S ribosomal protein S23, mitochondrial;
DE Flags: Precursor;
GN Name=rsm23; ORFNames=SPBC29A3.15c;
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 [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 [2]
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 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. mS29 binds GTP and is probably an active GTPase. GTP
CC hydrolysis may be linked to subunit association. mS29 also has an
CC extraribosomal function, being required for maintenance of
CC mitochondrial DNA. {ECO:0000250|UniProtKB:Q01163}.
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 at least 32 different proteins. The 54S
CC large subunit contains a 21S rRNA (21S mt-rRNA) and at least 45
CC different proteins. {ECO:0000250|UniProtKB:Q01163}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS29 family. {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; CU329671; CAA18392.1; -; Genomic_DNA.
DR PIR; T40086; T40086.
DR RefSeq; NP_595843.1; NM_001021747.2.
DR AlphaFoldDB; O59677; -.
DR SMR; O59677; -.
DR BioGRID; 277035; 1.
DR STRING; 284812.O59677; -.
DR MaxQB; O59677; -.
DR PaxDb; 4896-SPBC29A3-15c-1; -.
DR EnsemblFungi; SPBC29A3.15c.1; SPBC29A3.15c.1:pep; SPBC29A3.15c.
DR GeneID; 2540507; -.
DR KEGG; spo:SPBC29A3.15c; -.
DR PomBase; SPBC29A3.15c; rsm23.
DR VEuPathDB; FungiDB:SPBC29A3.15c; -.
DR eggNOG; KOG3928; Eukaryota.
DR HOGENOM; CLU_044511_0_0_1; -.
DR InParanoid; O59677; -.
DR OMA; GLAHWMT; -.
DR PhylomeDB; O59677; -.
DR PRO; PR:O59677; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; ISS:PomBase.
DR InterPro; IPR019368; Ribosomal_mS29.
DR InterPro; IPR017082; Ribosomal_mS29_fun.
DR PANTHER; PTHR12810:SF0; 28S RIBOSOMAL PROTEIN S29, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12810; MITOCHONDRIAL 28S RIBOSOMAL PROTEIN S29; 1.
DR Pfam; PF10236; DAP3; 1.
DR PIRSF; PIRSF036996; RSM23; 1.
PE 3: Inferred from homology;
KW ATP-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..54
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 55..476
FT /note="Small ribosomal subunit protein mS29"
FT /id="PRO_0000372636"
FT REGION 58..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 476 AA; 53230 MW; 6341C49358599689 CRC64;
MLPKFRSRSS IIKNTERISN ILSGGKLTVC GSKLGGLYTF EKCTFNKYYS SSQYQHTGRP
VGGNIHSSSN QQRQKNSEAP RINEIPPSTS SVEKSTTIPN SSVVLDHLLN EGENTLEEVK
PSEIHPHMSW SSKSEGKMFK IPEELLNKLN GFGALEKQKK SFSFFTSASL LHRKITTELV
NVLQRSKDQG TKDGRFLLDG APGSGRSIAL IQAELFALSQ PNFIVLPVHN CEGWVNSTSS
YGYDEQLKLW VQPDLIKGFL TSVMKTNSDK LKKLKTFESH ELLQNECIPA GTDLLSFLHK
LIASSNAPKS LEIFLQELNN NTKSNSNMKV LLVIDNISIL SVVTKYKDKK NNFLPPKDFY
FINLLFKYIS GSLTFNRGTV LAATSSQPRV STPSLDIALG VAHRNPYKSS DETILDSLQS
VHILNMEPYT LDESRRMMEY LVSSNVCLEK VDNYLQNHVL SGGNPRKFFD ACTRLA
//
