ID   MGR1_CANGA              Reviewed;         483 AA.
AC   Q6FX96;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Mitochondrial inner membrane i-AAA protease complex subunit MGR1;
GN   Name=MGR1; OrderedLocusNames=CAGL0B00682g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Component of the mitochondrial inner membrane i-AAA protease
CC       complex required for mitochondrial inner membrane protein turnover.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the mitochondrial inner membrane i-AAA protease
CC       complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MGR1 family. {ECO:0000305}.
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DR   EMBL; CR380948; CAG57900.1; -; Genomic_DNA.
DR   RefSeq; XP_445000.1; XM_445000.1.
DR   AlphaFoldDB; Q6FX96; -.
DR   STRING; 5478.XP_445000.1; -.
DR   EnsemblFungi; CAG57900; CAG57900; CAGL0B00682g.
DR   GeneID; 2886622; -.
DR   KEGG; cgr:CAGL0B00682g; -.
DR   CGD; CAL0127118; CAGL0B00682g.
DR   VEuPathDB; FungiDB:CAGL0B00682g; -.
DR   eggNOG; ENOG502QR67; Eukaryota.
DR   HOGENOM; CLU_039216_0_0_1; -.
DR   InParanoid; Q6FX96; -.
DR   OMA; FYHEGID; -.
DR   Proteomes; UP000002428; Chromosome B.
DR   GO; GO:0031942; C:i-AAA complex; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:EnsemblFungi.
DR   InterPro; IPR013911; i-AAA_Mgr1.
DR   Pfam; PF08602; Mgr1; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..483
FT                   /note="Mitochondrial inner membrane i-AAA protease complex
FT                   subunit MGR1"
FT                   /id="PRO_0000324411"
FT   TOPO_DOM        1..59
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        60..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..205
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        206..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..483
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  54049 MW;  8DE712D412E4A4B3 CRC64;
     MGIFTPPGKS DKRDANEEKP TLLGSNSKDE TDVEKFWVRP SLGLKLWGPL VPASDNKTGL
     WTLVAVQSMV GLLCFYRFKS LRIIDRNGAL NSVGKSGIRP TSVLVNEPKL YNSAFTQQEA
     VSGKPLVKKD IADFPTLNRF STTHGDMFVN TTNVNRNTPS LSAAPVVASP VLSSAGHQSE
     IMAKSEAKNN WKSFFKSDNW LIFKKVFYLL AGSIILSQSM LEACRLTILR YDPWCEEAKT
     VREKKFFNNI VKFYHEGIDP TKVKVKDAVS GNIMPTNVPE VRQSVALVRA QTEAENPIIS
     WFGPIEYKPM TFSEFLDRLE YHLDMFEYFQ GKRAANETAL GFLTGIKTET SNLRDQNAQN
     RSRILKELKS EDQLSNDLSI KTGNAKIPKG TQRHGFSAAA NRSIILEEDV AVPEDIDLNE
     IWTLYDPWLN LALETSLSIK FIPTVLINQD GITENSMMDT EATIGDKAGV IPENSNKPEE
     PRQ