ID   MG101_CANPC             Reviewed;         266 AA.
AC   G8B839;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Mitochondrial genome maintenance protein MGM101 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=MGM101 {ECO:0000303|PubMed:26743001}; OrderedLocusNames=CPAR2_106590;
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646;
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA   Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT   response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(2011).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND STRUCTURE BY ELECTRON
RP   MICROSCOPY OF THE MGM101-DNA COMPLEX.
RX   PubMed=26743001; DOI=10.1093/nar/gkv1529;
RA   Pevala V., Truban D., Bauer J.A., Kostan J., Kunova N., Bellova J.,
RA   Brandstetter M., Marini V., Krejci L., Tomaska L., Nosek J., Kutejova E.;
RT   "The structure and DNA-binding properties of Mgm101 from a yeast with a
RT   linear mitochondrial genome.";
RL   Nucleic Acids Res. 44:2227-2239(2016).
CC   -!- FUNCTION: Plays a role in the replication of the mitochondrial genome
CC       and the maintenance of its telomeres (PubMed:26743001). Able to
CC       catalyze strand annealing and D-loop formation (PubMed:26743001). Binds
CC       a wide variety of DNA substrates (PubMed:26743001). Exhibited the
CC       highest affinity for DNA molecules carrying 3' ssDNA overhangs (Y-form,
CC       3' FLAP, 3' overhang) and for substrates with complex structures (X-O
CC       and Fork) (PubMed:26743001). Forms homogeneous ring-shaped structures
CC       at the ssDNA native telomeres ends (PubMed:26743001). Oligomers seem to
CC       bind to the ssDNA as a filament until they reach the double-stranded
CC       region and induce the formation of bends and loops within the double-
CC       stranded part of the molecules (PubMed:26743001).
CC       {ECO:0000269|PubMed:26743001}.
CC   -!- SUBUNIT: Forms homooligomers in vitro (PubMed:26743001).
CC       {ECO:0000269|PubMed:26743001}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC       {ECO:0000269|PubMed:26743001}.
CC   -!- SIMILARITY: Belongs to the MGM101 family. {ECO:0000305}.
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DR   EMBL; HE605203; CCE40624.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8B839; -.
DR   STRING; 578454.G8B839; -.
DR   EnsemblFungi; CCE40624; CCE40624; CPAR2_106590.
DR   CGD; CAL0000156327; MGM101.
DR   VEuPathDB; FungiDB:CPAR2_106590; -.
DR   eggNOG; ENOG502RXU4; Eukaryota.
DR   Proteomes; UP000005221; Chromosome 1.
DR   GO; GO:0000262; C:mitochondrial chromosome; IEA:InterPro.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:CGD.
DR   GO; GO:0005634; C:nucleus; IDA:CGD.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:CGD.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:CGD.
DR   GO; GO:0036297; P:interstrand cross-link repair; IEA:EnsemblFungi.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IDA:CGD.
DR   GO; GO:0000725; P:recombinational repair; IEA:EnsemblFungi.
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..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..266
FT                   /note="Mitochondrial genome maintenance protein MGM101"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000436005"
FT   REGION          37..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   266 AA;  29989 MW;  A69E5F64E28551CF CRC64;
     MLHSTKLVFR ATPQALCFPV RSYSRYVRTV PKTASAKTTS KLAPSITTED EVAEQDPSLQ
     EPQSATSTAS FAFHDAPPET RSVLNSSTNN NIDWSDSYHG LGSQPFSREI ADILLAPIKD
     QDIEIKPDGL LYLPEIKYRR ILNKAFGPGG WGLVPRTESL ITKSQISREY GLICHGRLIS
     IARGEQDYFG GEEKVTTALE GCKSNALMRC CKDLGIASEL WDPGFIRKWK AKYCEEVFVE
     HVVNKKKKKL WKLKSNKKIE YPYKQL