MG101_YEAST
ID MG101_YEAST Reviewed; 269 AA.
AC P32787; D6VWW3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Mitochondrial genome maintenance protein MGM101;
DE Flags: Precursor;
GN Name=MGM101; Synonyms=MGM9; OrderedLocusNames=YJR144W; ORFNames=J2181;
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=8346025; DOI=10.1093/nar/21.15.3473;
RA Chen X.-J., Guan M.-X., Clark-Walker G.D.;
RT "MGM101, a nuclear gene involved in maintenance of the mitochondrial genome
RT in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 21:3473-3477(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10209025; DOI=10.1083/jcb.145.2.291;
RA Meeusen S., Tieu Q., Wong E., Weiss E., Schieltz D., Yates J.R. III,
RA Nunnari J.;
RT "Mgm101p is a novel component of the mitochondrial nucleoid that binds DNA
RT and is required for the repair of oxidatively damaged mitochondrial DNA.";
RL J. Cell Biol. 145:291-304(1999).
RN [5]
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).
RN [6]
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: Performs an essential function in the repair of oxidatively
CC damaged mtDNA that is required for the maintenance of the mitochondrial
CC genome. Binds to DNA. {ECO:0000269|PubMed:10209025}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000269|PubMed:10209025, ECO:0000269|PubMed:14576278}.
CC -!- SIMILARITY: Belongs to the MGM101 family. {ECO:0000305}.
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DR EMBL; X68482; CAA48502.1; -; Genomic_DNA.
DR EMBL; Z49644; CAA89677.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08929.1; -; Genomic_DNA.
DR PIR; S34849; S34849.
DR RefSeq; NP_012678.1; NM_001181802.1.
DR AlphaFoldDB; P32787; -.
DR BioGRID; 33900; 284.
DR DIP; DIP-5044N; -.
DR IntAct; P32787; 18.
DR MINT; P32787; -.
DR STRING; 4932.YJR144W; -.
DR iPTMnet; P32787; -.
DR UCD-2DPAGE; P32787; -.
DR MaxQB; P32787; -.
DR PaxDb; P32787; -.
DR PRIDE; P32787; -.
DR EnsemblFungi; YJR144W_mRNA; YJR144W; YJR144W.
DR GeneID; 853609; -.
DR KEGG; sce:YJR144W; -.
DR SGD; S000003905; MGM101.
DR VEuPathDB; FungiDB:YJR144W; -.
DR eggNOG; ENOG502RXU4; Eukaryota.
DR HOGENOM; CLU_028692_1_0_1; -.
DR InParanoid; P32787; -.
DR OMA; TKIWTRK; -.
DR BioCyc; YEAST:G3O-31758-MON; -.
DR PRO; PR:P32787; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P32787; protein.
DR GO; GO:0000262; C:mitochondrial chromosome; IEA:InterPro.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0036297; P:interstrand cross-link repair; IGI:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0000725; P:recombinational repair; IMP:SGD.
DR InterPro; IPR009446; Mgm101.
DR PANTHER; PTHR31404; PTHR31404; 1.
DR Pfam; PF06420; Mgm101p; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA-binding; Mitochondrion; Mitochondrion nucleoid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..269
FT /note="Mitochondrial genome maintenance protein MGM101"
FT /id="PRO_0000021719"
SQ SEQUENCE 269 AA; 30091 MW; E14C17F2E837D6F0 CRC64;
MKSIFKVRGC VSHAAQFCQK RTVVSTGTSN TATAGAVRKS FNSTETKPVF ATKSEAGNGS
HMKEYSSGIN SKLGGTPLET RSTADDSLNN SYKQVKGDID WYTSWYGLGM KPFEAKVQKD
LIEPLDPKDI EIKPDGLIYL PEIKYRRILN KAFGAGGWGL VPRSQTIVTS KLVTREYGLI
CHGQLISVAR GEQDYFNEAG IPTATEGCKS NALMRCCKDL GVGSELWDPV FIKKFKVDHC
TEKFVEHVTT KRKKKIWLRK DRQVEYPYK