ID   MGR1_DEBHA              Reviewed;         342 AA.
AC   Q6BNL9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Mitochondrial inner membrane i-AAA protease complex subunit MGR1;
GN   Name=MGR1; OrderedLocusNames=DEHA2E20680g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAG88474.2; -; Genomic_DNA.
DR   RefSeq; XP_460201.2; XM_460201.1.
DR   AlphaFoldDB; Q6BNL9; -.
DR   STRING; 4959.XP_460201.2; -.
DR   EnsemblFungi; CAG88474; CAG88474; DEHA2E20680g.
DR   GeneID; 2902711; -.
DR   KEGG; dha:DEHA2E20680g; -.
DR   VEuPathDB; FungiDB:DEHA2E20680g; -.
DR   eggNOG; ENOG502QR67; Eukaryota.
DR   HOGENOM; CLU_871878_0_0_1; -.
DR   InParanoid; Q6BNL9; -.
DR   OMA; EFEMVWL; -.
DR   OrthoDB; 931061at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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..342
FT                   /note="Mitochondrial inner membrane i-AAA protease complex
FT                   subunit MGR1"
FT                   /id="PRO_0000324412"
FT   TOPO_DOM        1..56
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        57..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..99
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        100..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..342
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   342 AA;  39393 MW;  8BEE2F4434ABDCBA CRC64;
     MGVYIPPGSG GNDNGKSGGS GDNTLTIPNP ASFIPQNPSL GLRLWGPLVP ASDNLPALYF
     LTSLQIGIGL LSFNKVRYLR RSNLARFGIE NTWQRRSTKW LCAIGGSYLV YQSGIEMSRL
     AMPYDPWYDE AKFYRKLAIK NGDNPSWWFG ATGYYKPMNY KEWYTKIDKW FNNQINIIDA
     EHENVDTASS QVSTRGKHPQ SPLLSSLSRK GKYSEIYQSL HESNIKRYKK LLDQSLKDVN
     ELNKAERLDL IMEGKSSIKY NEEYLKPHIQ LGNHRIDTDE EFEMVWLNFE PWDELKMETD
     YDIRLVPRWR WSEDEDVEAS STESVPTEPT TNLVNEVDES HI