RMRP_YEAST
ID RMRP_YEAST Reviewed; 198 AA.
AC P40993; D6VTA1; Q6B1P4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ribonuclease MRP protein subunit SNM1;
DE AltName: Full=RNA-processing protein SNM1;
DE AltName: Full=RNase MRP 22.5 kDa subunit;
GN Name=SNM1; OrderedLocusNames=YDR478W; ORFNames=D8035.21;
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], FUNCTION, AND RNA-BINDING.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7958920; DOI=10.1101/gad.8.21.2617;
RA Schmitt M.E., Clayton D.A.;
RT "Characterization of a unique protein component of yeast RNase MRP: an RNA-
RT binding protein with a zinc-cluster domain.";
RL Genes Dev. 8:2617-2628(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
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 IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY.
RX PubMed=15637077; DOI=10.1074/jbc.m409568200;
RA Salinas K., Wierzbicki S., Zhou L., Schmitt M.E.;
RT "Characterization and purification of Saccharomyces cerevisiae RNase MRP
RT reveals a new unique protein component.";
RL J. Biol. Chem. 280:11352-11360(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Essential component of the MRP ribonucleoprotein
CC endoribonuclease that cleaves mitochondrial primer RNA sequences.
CC {ECO:0000269|PubMed:7958920}.
CC -!- SUBUNIT: Component of RNase MRP complex which consists of an RNA moiety
CC and at least 10 protein subunits including POP1, POP3, POP4, POP5,
CC POP6, POP7, POP8, RMP1, RPP1 and SNM1, many of which are shared with
CC the RNase P complex. {ECO:0000269|PubMed:15637077}.
CC -!- INTERACTION:
CC P40993; P41812: POP1; NbExp=4; IntAct=EBI-15622, EBI-13621;
CC P40993; P38336: POP4; NbExp=4; IntAct=EBI-15622, EBI-13646;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z37982; CAA86054.1; -; Genomic_DNA.
DR EMBL; U33050; AAB64905.1; -; Genomic_DNA.
DR EMBL; AY693036; AAT93055.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12311.1; -; Genomic_DNA.
DR PIR; S48236; S48236.
DR RefSeq; NP_010766.3; NM_001180786.3.
DR PDB; 6W6V; EM; 3.00 A; K=1-198.
DR PDB; 7C79; EM; 2.50 A; K=1-198.
DR PDB; 7C7A; EM; 2.80 A; K=1-198.
DR PDBsum; 6W6V; -.
DR PDBsum; 7C79; -.
DR PDBsum; 7C7A; -.
DR AlphaFoldDB; P40993; -.
DR SMR; P40993; -.
DR BioGRID; 32530; 469.
DR ComplexPortal; CPX-3284; Nucleolar ribonuclease MRP complex.
DR DIP; DIP-5233N; -.
DR IntAct; P40993; 13.
DR MINT; P40993; -.
DR STRING; 4932.YDR478W; -.
DR iPTMnet; P40993; -.
DR MaxQB; P40993; -.
DR PaxDb; P40993; -.
DR PRIDE; P40993; -.
DR EnsemblFungi; YDR478W_mRNA; YDR478W; YDR478W.
DR GeneID; 852089; -.
DR KEGG; sce:YDR478W; -.
DR SGD; S000002886; SNM1.
DR VEuPathDB; FungiDB:YDR478W; -.
DR eggNOG; ENOG502S5IC; Eukaryota.
DR HOGENOM; CLU_122019_0_0_1; -.
DR InParanoid; P40993; -.
DR OMA; SPMINST; -.
DR BioCyc; YEAST:G3O-30004-MON; -.
DR PRO; PR:P40993; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P40993; protein.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IBA:GO_Central.
DR GO; GO:0000172; C:ribonuclease MRP complex; IPI:SGD.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IDA:ComplexPortal.
DR GO; GO:0006397; P:mRNA processing; IMP:SGD.
DR GO; GO:0030541; P:plasmid partitioning; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR Pfam; PF04032; Rpr2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Nuclease; Nucleus; Reference proteome;
KW RNA-binding; rRNA processing.
FT CHAIN 1..198
FT /note="Ribonuclease MRP protein subunit SNM1"
FT /id="PRO_0000097366"
FT REGION 141..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:7C7A"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 30..47
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6W6V"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:7C7A"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:7C79"
SQ SEQUENCE 198 AA; 22541 MW; 67C262585D3BEA3A CRC64;
MNKDQAEKYQ ERSLRQKYNL LHVLPTLNSR ALSGLYYKNF HNSVKRYQIM LPEQLKSGKF
CSHCGCVYVP NFNASLQLTT NTEQGDSDEL GGESMEGPKK CIQVNCLNCE KSKLFEWKSE
FVVPTFGQDV SPMINSTSSG KVSYAVKKPQ KSKTSTGKER SKKRKLNSLT NLLSKRNQEK
KMEKKKSSSL SLESFMKS
