RT22_YEAST
ID RT22_YEAST Reviewed; 628 AA.
AC P36056; D6VX43;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial;
DE EC=2.1.1.-;
DE Flags: Precursor;
GN Name=RSM22; OrderedLocusNames=YKL155C; ORFNames=YKL610;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091859; DOI=10.1002/yea.320100005;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT of chromosome XI of Saccharomyces cerevisiae.";
RL Yeast 10:S35-S40(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL
RP COMPLEX, AND 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 [5]
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 [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], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [9]
RP PROBABLE FUNCTION.
RX PubMed=19351663; DOI=10.1074/mcp.m900025-mcp200;
RA Petrossian T.C., Clarke S.G.;
RT "Multiple motif scanning to identify methyltransferases from the yeast
RT proteome.";
RL Mol. Cell. Proteomics 8:1516-1526(2009).
RN [10]
RP FUNCTION.
RX PubMed=22689777; DOI=10.1093/bioinformatics/bts211;
RA Park Y., Bader J.S.;
RT "How networks change with time.";
RL Bioinformatics 28:I40-I48(2012).
RN [11]
RP PROBABLE SUBSTRATE SPECIFICITY.
RX PubMed=24651469; DOI=10.1371/journal.pcbi.1003514;
RA Szczepinska T., Kutner J., Kopczynski M., Pawlowski K., Dziembowski A.,
RA Kudlicki A., Ginalski K., Rowicka M.;
RT "Probabilistic approach to predicting substrate specificity of
RT methyltransferases.";
RL PLoS Comput. Biol. 10:E1003514-E1003514(2014).
RN [12]
RP SHOWS THAT RSM22 IS NOT A CONSTITUENT OF THE MITOCHONDRIAL RIBOSOMAL SMALL
RP COMPLEX.
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: Probable S-adenosyl-L-methionine-dependent RNA
CC methyltransferase (PubMed:19351663, PubMed:24651469). May provide the
CC activity for methylation of the rRNA of the small mitochondrial
CC subunit, which is required for the assembly and stability of the
CC mitochondrial ribosome (PubMed:22689777). Has no protein
CC methyltransferase activity (PubMed:24651469).
CC {ECO:0000269|PubMed:24651469, ECO:0000305|PubMed:19351663,
CC ECO:0000305|PubMed:22689777}.
CC -!- SUBUNIT: Associates with mitochondrial ribosomes.
CC {ECO:0000269|PubMed:11278769, ECO:0000269|PubMed:12392552}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11278769,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 1900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Although reported constituent of the mitochondrial small
CC ribosomal subunit (PubMed:11278769), it has not been identified in the
CC structure of the yeast mitoribosome (PubMed:28154081), indicating that
CC RSM22 only transiently interacts with the mitoribosome.
CC {ECO:0000305|PubMed:11278769, ECO:0000305|PubMed:28154081}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Rsm22 family.
CC {ECO:0000305}.
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DR EMBL; Z26877; CAA81498.1; -; Genomic_DNA.
DR EMBL; Z28155; CAA81996.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09009.1; -; Genomic_DNA.
DR PIR; S37795; S37795.
DR RefSeq; NP_012767.1; NM_001179721.1.
DR AlphaFoldDB; P36056; -.
DR SASBDB; P36056; -.
DR BioGRID; 33982; 108.
DR DIP; DIP-756N; -.
DR IntAct; P36056; 7.
DR MINT; P36056; -.
DR STRING; 4932.YKL155C; -.
DR iPTMnet; P36056; -.
DR MaxQB; P36056; -.
DR PaxDb; P36056; -.
DR PRIDE; P36056; -.
DR EnsemblFungi; YKL155C_mRNA; YKL155C; YKL155C.
DR GeneID; 853701; -.
DR KEGG; sce:YKL155C; -.
DR SGD; S000001638; RSM22.
DR VEuPathDB; FungiDB:YKL155C; -.
DR eggNOG; KOG2539; Eukaryota.
DR GeneTree; ENSGT00940000175583; -.
DR HOGENOM; CLU_024759_0_0_1; -.
DR InParanoid; P36056; -.
DR OMA; HRKCPLQ; -.
DR BioCyc; YEAST:G3O-31925-MON; -.
DR PRO; PR:P36056; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36056; protein.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR InterPro; IPR015324; Ribosomal_Rsm22-like.
DR InterPro; IPR016522; Ribosome_S22_mit_bud.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF09243; Rsm22; 2.
DR PIRSF; PIRSF007797; RSM22; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transferase; Transit peptide.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 16..628
FT /note="Probable S-adenosyl-L-methionine-dependent RNA
FT methyltransferase RSM22, mitochondrial"
FT /id="PRO_0000203144"
SQ SEQUENCE 628 AA; 72190 MW; 9612A09DA01CD969 CRC64;
MMKRCFSILP QNVRFSSKFT SLNLPKLDLA DFIDSNKRGI NVLPSYRDET ASTTQATNSK
ELRLLSKTLQ GQSYRDQLEL NPDVSKAINN NIMAVHIPNN LRRVATNYYK EIQEPNSLHR
PCRTKMEVDA HIASIFLQNY GSIFQSLKEL QKRVGPDNFK PQRILDVGYG PATGIVALND
ILGPNYRPDL KDAVILGNAE MQERAKIILS RQLNEVVDTV EENVSTEKEQ ETDRRNKNFQ
EDEHIGEVMT KKINIMTNLR SSIPASKEYD LIILTHQLLH DGNQFPIQVD ENIEHYLNIL
APGGHIVIIE RGNPMGFEII ARARQITLRP ENFPDEFGKI PRPWSRGVTV RGKKDAELGN
ISSNYFLKVI APCPHQRKCP LQVGNPNFYT HKEGKDLKFC NFQKSIKRPK FSIELKKGKL
LATSWDGSQG NASRLKGTGR RNGRDYEILN YSYLIFERSH KDENTLKEIK KLRNENVNGK
YDIGSLGDDT QNSWPRIIND PVKRKGHVMM DLCAPSGELE KWTVSRSFSK QIYHDARKSK
KGDLWASAAK TQIKGLGDLN VKKFHKLEKE RIKQLKKEER QKARKAMESY NELEDSLQFD
DHQFSNFEVM KKLSTFHGND FLQHVNRK
