ID   MGR1_ASHGO              Reviewed;         395 AA.
AC   Q751V6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Mitochondrial inner membrane i-AAA protease complex subunit MGR1;
GN   Name=MGR1; OrderedLocusNames=AFR719W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS54091.1; -; Genomic_DNA.
DR   RefSeq; NP_986267.1; NM_212403.1.
DR   AlphaFoldDB; Q751V6; -.
DR   STRING; 33169.AAS54091; -.
DR   EnsemblFungi; AAS54091; AAS54091; AGOS_AFR719W.
DR   GeneID; 4622556; -.
DR   KEGG; ago:AGOS_AFR719W; -.
DR   eggNOG; ENOG502QR67; Eukaryota.
DR   HOGENOM; CLU_039216_0_0_1; -.
DR   InParanoid; Q751V6; -.
DR   OMA; FYHEGID; -.
DR   Proteomes; UP000000591; Chromosome VI.
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..395
FT                   /note="Mitochondrial inner membrane i-AAA protease complex
FT                   subunit MGR1"
FT                   /id="PRO_0000324409"
FT   TOPO_DOM        1..52
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        53..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..139
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        140..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..395
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   395 AA;  44313 MW;  85901F24947FFE22 CRC64;
     MALFTPPSED KDGRDRSGGG DKASGVVRTP FHLRPSLGLA LWGPLVPASD NRAGLWTLVG
     LQTLMGAFFV SRFRALRPKL LKRDIADFPS LNRFSKTSGD MHVGPVHVFA DFGGTHSFHR
     RAGESPGFFQ SRRFVSLKRA LYLSTGVVLL VQSALESARL TLLVYDPWEE QARGVRDKQF
     YNDVVRYYHE GVDPARFIVK DPASGNTLPV NVPEVKQGVA LARAHTNARN IITRWLGPLD
     CKPLSSSEFL DKLEHYLDTC DFIQDMNNKR LFGNPAEVKA RQKALDALIQ ANKENRRRIR
     HILDITPPRG LPLSPKAVDQ GLRSIILDPD HESTEDLDLH ELWSIYNPWV DLALDTSLSI
     KFLPTVRTPE ELLGDSEDTA VEQKNPPVQI KRERG