MRS1_YEAST
ID MRS1_YEAST Reviewed; 363 AA.
AC P07266; D6VVV1;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Mitochondrial RNA-splicing protein MRS1;
GN Name=MRS1; Synonyms=PET157; OrderedLocusNames=YIR021W;
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].
RX PubMed=2443348; DOI=10.1002/j.1460-2075.1987.tb02479.x;
RA Kreike J., Schulze M., Ahne F., Lang B.F.;
RT "A yeast nuclear gene, MRS1, involved in mitochondrial RNA splicing:
RT nucleotide sequence and mutational analysis of two overlapping open reading
RT frames on opposite strands.";
RL EMBO J. 6:2123-2129(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 CHARACTERIZATION.
RX PubMed=1699677; DOI=10.1007/bf00312599;
RA Bousquet I., Dujardin G., Poyton R.O., Slonimski P.P.;
RT "Two group I mitochondrial introns in the cob-box and coxI genes require
RT the same MRS1/PET157 nuclear gene product for splicing.";
RL Curr. Genet. 18:117-124(1990).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11773622; DOI=10.1073/pnas.012579299;
RA Bassi G.S., de Oliveira D.M., White M.F., Weeks K.M.;
RT "Recruitment of intron-encoded and co-opted proteins in splicing of the bI3
RT group I intron RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:128-133(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).
CC -!- FUNCTION: Function in mitochondrial RNA splicing in the excision of
CC mitochondrial group I introns aI5 beta from COX1 and bI3 from COB
CC transcripts and thus would be involved in obtaining the correct
CC structure of the intron, to allow the RNA catalyzed reactions to occur.
CC {ECO:0000269|PubMed:11773622}.
CC -!- SUBUNIT: Homodimer. Forms a ribonucleoprotein complex composed of
CC maturase bI3 and 2 dimers of MRS1 that assemble around the bI3 RNA.
CC {ECO:0000269|PubMed:11773622}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
CC -!- MISCELLANEOUS: Present with 5240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X05509; CAA29053.1; -; Genomic_DNA.
DR EMBL; Z38061; CAA86181.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08567.1; -; Genomic_DNA.
DR PIR; S48483; S48483.
DR RefSeq; NP_012287.3; NM_001179543.3.
DR AlphaFoldDB; P07266; -.
DR SMR; P07266; -.
DR BioGRID; 35012; 93.
DR ComplexPortal; CPX-1331; bI3 intron splicing factor complex.
DR DIP; DIP-5607N; -.
DR IntAct; P07266; 2.
DR MINT; P07266; -.
DR STRING; 4932.YIR021W; -.
DR MaxQB; P07266; -.
DR PaxDb; P07266; -.
DR PRIDE; P07266; -.
DR EnsemblFungi; YIR021W_mRNA; YIR021W; YIR021W.
DR GeneID; 854839; -.
DR KEGG; sce:YIR021W; -.
DR SGD; S000001460; MRS1.
DR VEuPathDB; FungiDB:YIR021W; -.
DR eggNOG; ENOG502S46R; Eukaryota.
DR GeneTree; ENSGT00940000176739; -.
DR HOGENOM; CLU_055501_0_0_1; -.
DR InParanoid; P07266; -.
DR OMA; DIDPLMC; -.
DR BioCyc; YEAST:G3O-31441-MON; -.
DR PRO; PR:P07266; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P07266; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:SGD.
DR GO; GO:0000402; F:crossed form four-way junction DNA binding; IBA:GO_Central.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0070336; F:flap-structured DNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0000403; F:Y-form DNA binding; IBA:GO_Central.
DR GO; GO:0000372; P:Group I intron splicing; IDA:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IBA:GO_Central.
DR GO; GO:0000963; P:mitochondrial RNA processing; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IDA:ComplexPortal.
DR InterPro; IPR039197; Mrs1/Cce1.
DR InterPro; IPR015242; Ydc2_cat.
DR PANTHER; PTHR28072; PTHR28072; 1.
DR Pfam; PF09159; Ydc2-catalyt; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; mRNA processing; Reference proteome.
FT CHAIN 1..363
FT /note="Mitochondrial RNA-splicing protein MRS1"
FT /id="PRO_0000096580"
FT CONFLICT 182
FT /note="S -> P (in Ref. 1; CAA29053)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="V -> A (in Ref. 1; CAA29053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 41290 MW; 6270FCD7EBF8267E CRC64;
MSPKNITRSV IPAIDLYCRK ANFKTLKSLS MILGSKKEWY DTKKAPLRTF LVSRCGIFEQ
LRGRLVEDGK VNLFSVFLTN DSFSFCKMTV DDKFNTSLVD WQKIPFDSTF ATDRRQNISL
LPVDTLFATE KIISILGVSP NMTNLVSIER ERSDLVDFNC KLQSNILEHL LYAKCQGVYV
TSTNEKARLL AAVCNPEFID TFWCELTPIR VSLKENPSIS VPREYQMYDP VVRATIKEVV
TKRLLRSAFD NDIDPLMCLH LDKGWKLKFP ILSSTTGLNF SLKDCLSLDT GKDASDMTEV
FLATMESSKV LRTYSNLVDI VMKDNGRLDS GVLKQFNDYV KQEKLNLQHF QAGSSKFLKG
AKI
