ID   GEP3_YEAS7              Reviewed;         556 AA.
AC   A6ZP48;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Genetic interactor of prohibitins 3, mitochondrial;
DE   AltName: Full=Altered inheritance of mitochondria protein 40;
DE   AltName: Full=Found in mitochondrial proteome protein 38;
DE   Flags: Precursor;
GN   Name=GEP3; Synonyms=AIM40, FMP48; ORFNames=SCY_5263;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Interacts genetically with prohibitins and thus may be
CC       involved in the mitochondrial lipid metabolism. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. GEP3
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR   EMBL; AAFW02000032; EDN63538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZP48; -.
DR   SMR; A6ZP48; -.
DR   PRIDE; A6ZP48; -.
DR   EnsemblFungi; EDN63538; EDN63538; SCY_5263.
DR   HOGENOM; CLU_025792_1_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   Mitochondrion; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..556
FT                   /note="Genetic interactor of prohibitins 3, mitochondrial"
FT                   /id="PRO_0000409645"
FT   DOMAIN          113..305
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
SQ   SEQUENCE   556 AA;  63866 MW;  021BC19D2DECE69D CRC64;
     MLNLCHALRG VRQFSCSVIV KVKCASCSIK LQDQDPSKPG YYTKPKSLPD SKLNPDLQDL
     KYLLFSQDIQ LSKQAIQNDP DLKTKRDLLL RVICKRCSNA LHHNNYNPEE FPESTLNDIL
     NYVPRGSNVM HIVPFVEFPL HLDPNVLKRN DLDTTLVLTK SDQVFKDKNA VSKKVPIFMK
     QFLKNTLRID SNKTFAISAL KNWNISMFYN YFKNYTYLLG NPNVGKSTLI NTLLQKYLGY
     KVKIDSTGKI NSPSEEVMQE AFTNPKNFFK IQAAGVSHIP NLTRSVQAYQ VGGKILFDLP
     GYSTSTSRLR LEELIDERWL QRLRKTDLFN RKHIKQKTYE SMKGTSQGGC YTVGGIFYLV
     PPKGSINQIV KYIPGPSKTF KNIEKGIDVF NSCNSSSGTH PLSRYCGIKS VICEKSQYKR
     YAIPPFIGSI EIVLKDIGYI LLRTTGRYEF KGLHEIWIPR GIQVGIREPL ENLIESGYQR
     YIETNGKESS CPRDRPIISS LYEMAPDEAD TLNAVKKSYL EKTEKDLSAR RFVDDDPYDL
     VQHLEKKKNP YWYYQW