RF1M_YEAST
ID RF1M_YEAST Reviewed; 413 AA.
AC P30775; D6VU06;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Peptide chain release factor 1, mitochondrial;
DE Short=MRF-1;
DE Short=MtRF-1;
DE Flags: Precursor;
GN Name=MRF1; OrderedLocusNames=YGL143C;
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=1475194; DOI=10.1093/nar/20.23.6339;
RA Pel H.J., Maat M.J., Rep M., Grivell L.A.;
RT "The yeast nuclear gene MRF1 encodes a mitochondrial peptide chain release
RT factor and cures several mitochondrial RNA splicing defects.";
RL Nucleic Acids Res. 20:6339-6346(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046099;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<177::aid-yea62>3.0.co;2-2;
RA Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.;
RT "The sequence of a nearly unclonable 22.8 kb segment on the left arm
RT chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A, TIP1,
RT MRF1 genes and six new open reading frames.";
RL Yeast 13:177-182(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
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 [6]
RP METHYLATION AT GLN-287, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16321977; DOI=10.1074/jbc.m507651200;
RA Polevoda B., Span L., Sherman F.;
RT "The yeast translation release factors Mrf1p and Sup45p (eRF1) are
RT methylated, respectively, by the methyltransferases Mtq1p and Mtq2p.";
RL J. Biol. Chem. 281:2562-2571(2006).
CC -!- FUNCTION: Mitochondrial peptide chain release factor that directs the
CC termination of translation in response to the peptide chain termination
CC codons UAA and UAG.
CC -!- INTERACTION:
CC P30775; P53944: MTQ1; NbExp=2; IntAct=EBI-14964, EBI-28737;
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- PTM: Methylation of glutamine in the GGQ triplet is conserved from
CC bacteria to mammals (By similarity). N5-methylated on Gln-287 by MTQ1.
CC {ECO:0000250, ECO:0000269|PubMed:16321977}.
CC -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC 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; X60381; CAA42932.1; -; Genomic_DNA.
DR EMBL; X99960; CAA68219.1; -; Genomic_DNA.
DR EMBL; Z72665; CAA96855.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07967.1; -; Genomic_DNA.
DR PIR; S28602; S28602.
DR RefSeq; NP_011372.3; NM_001181008.3.
DR AlphaFoldDB; P30775; -.
DR SMR; P30775; -.
DR BioGRID; 33109; 97.
DR DIP; DIP-2626N; -.
DR IntAct; P30775; 2.
DR MINT; P30775; -.
DR STRING; 4932.YGL143C; -.
DR iPTMnet; P30775; -.
DR MaxQB; P30775; -.
DR PaxDb; P30775; -.
DR PRIDE; P30775; -.
DR EnsemblFungi; YGL143C_mRNA; YGL143C; YGL143C.
DR GeneID; 852734; -.
DR KEGG; sce:YGL143C; -.
DR SGD; S000003111; MRF1.
DR VEuPathDB; FungiDB:YGL143C; -.
DR eggNOG; KOG2726; Eukaryota.
DR GeneTree; ENSGT00940000172260; -.
DR HOGENOM; CLU_036856_0_8_1; -.
DR InParanoid; P30775; -.
DR OMA; HEANIFT; -.
DR BioCyc; YEAST:G3O-30637-MON; -.
DR PRO; PR:P30775; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P30775; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0003747; F:translation release factor activity; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR GO; GO:0070126; P:mitochondrial translational termination; IMP:SGD.
DR GO; GO:0006415; P:translational termination; IMP:SGD.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 1: Evidence at protein level;
KW Methylation; Mitochondrion; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..413
FT /note="Peptide chain release factor 1, mitochondrial"
FT /id="PRO_0000030337"
FT REGION 335..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 287
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:16321977"
SQ SEQUENCE 413 AA; 46770 MW; AAAD4829748C7604 CRC64;
MWLSKFQFPS RSIFKGVFLG HKLPLLVRLT STTTNSKSNG SIPTQYTELS PLLVKQAEKY
EAELKDLDKD LSCGIHFDVN KQKHYAKLSA LTDTFIEYKE KLNELKSLQE MIVSDPSLRA
EAEQEYAELV PQYETTSSRL VNKLLPPHPF ADKPSLLELR PGVGGIEAMI FTQNLLDMYI
GYANYRKWKY RIISKNENES GSGIIDAILS IEEAGSYDRL RFEAGVHRVQ RIPSTETKGR
THTSTAAVVV LPQIGDESAK SIDAYERTFK PGEIRVDIMR ASGKGGQHVN TTDSAVRLTH
IPSGIVVSMQ DERSQHKNKA KAFTILRARL AEKERLEKEE KERKARKSQV SSTNRSDKIR
TYNFPQNRIT DHRCGFTLLD LPGVLSGERL DEVIEAMSKY DSTERAKELL ESN
