MGR1_LODEL
ID MGR1_LODEL Reviewed; 406 AA.
AC A5DV96;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Mitochondrial inner membrane i-AAA protease complex subunit MGR1;
GN Name=MGR1; ORFNames=LELG_01282;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
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).
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; CH981524; EDK43104.1; -; Genomic_DNA.
DR RefSeq; XP_001528762.1; XM_001528712.1.
DR AlphaFoldDB; A5DV96; -.
DR STRING; 379508.A5DV96; -.
DR EnsemblFungi; EDK43104; EDK43104; LELG_01282.
DR GeneID; 5235696; -.
DR KEGG; lel:LELG_01282; -.
DR VEuPathDB; FungiDB:LELG_01282; -.
DR eggNOG; ENOG502QR67; Eukaryota.
DR HOGENOM; CLU_039216_0_0_1; -.
DR InParanoid; A5DV96; -.
DR OMA; EFEMVWL; -.
DR OrthoDB; 931061at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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; 2.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..406
FT /note="Mitochondrial inner membrane i-AAA protease complex
FT subunit MGR1"
FT /id="PRO_0000324414"
FT TOPO_DOM 1..68
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 69..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..137
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..406
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 45636 MW; 4E3A3A368D3885E7 CRC64;
MGYIPPPGDN DDNGKKSNKK TQNTSKPISS DSTPDGTTIT IINPMSLIPR NPSFGLIWGP
LTPASDNRPA MYTMVALQIA IGVRFFRYAR THLRRHPVPQ AQFHAPPGLG VNSMISTTAN
QTYSAPPQQF LRRSKGDVFK SILAITTGSL LIFGSGLEIA RMMLPYDPWY DEAQFYRKQA
VRNGDKPNFW FGAYQYYQPM TYKEWHSKVS KWIDSVEKEI KVDETTFVID KDGKARGGIG
PAGVGYVNGA GQQSGAASAA AAVAKPLFQI RNRAKYQQIH AKLYNANETR MRELLANELN
DTNVNELNKA ERLDKILEGK SDLVNPNFNK PSISLGNHPM ESDDEFEMVW LNFEPWDELK
METDYDIRLI PRYASVEELE QVDEGELFVV KKEELGETDN VVNESS