ID   GEP3_DEBHA              Reviewed;         593 AA.
AC   Q6BMA8;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Genetic interactor of prohibitins 3, mitochondrial;
DE   AltName: Full=Found in mitochondrial proteome protein 38;
DE   Flags: Precursor;
GN   Name=GEP3; Synonyms=FMP48; OrderedLocusNames=DEHA2F07018g;
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: May be involved in the mitochondrial lipid metabolism.
CC       {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; CR382138; CAG88995.2; -; Genomic_DNA.
DR   RefSeq; XP_460663.2; XM_460663.1.
DR   AlphaFoldDB; Q6BMA8; -.
DR   SMR; Q6BMA8; -.
DR   STRING; 4959.XP_460663.2; -.
DR   EnsemblFungi; CAG88995; CAG88995; DEHA2F07018g.
DR   GeneID; 2904137; -.
DR   KEGG; dha:DEHA2F07018g; -.
DR   VEuPathDB; FungiDB:DEHA2F07018g; -.
DR   eggNOG; ENOG502S067; Eukaryota.
DR   HOGENOM; CLU_025792_0_0_1; -.
DR   InParanoid; Q6BMA8; -.
DR   OMA; QIVKYIP; -.
DR   OrthoDB; 612803at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
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; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..61
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           62..593
FT                   /note="Genetic interactor of prohibitins 3, mitochondrial"
FT                   /id="PRO_0000409634"
FT   DOMAIN          142..349
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
SQ   SEQUENCE   593 AA;  67131 MW;  8DE2A133DE22762E CRC64;
     MLGRIRPFVR YSVFRAGTYR TLFTSPYRMQ ISLIYNLFAT CNSCGIKLQN ENPSKPGFYR
     PPSARPKLVK PEDESFNRLM DGLSVEDRKL LLNSSDATLP QPVTASTAAA TTTNTKKEGD
     IQCIRCREAM YKSNFSWDEL PVESIDKIMS TIPPDGNVVY IVNAVDFPLS LNRSIFKYRN
     PSQITFLVTK CDLLFPSAQL SNRYGATFFK DYLSRTHGAD PEKVFVTSGM IDWNMKDIIK
     ALPDNSYMVG GVNSGKSTVI KSLLYTMEKS KPNYLSSKQQ TKLEKQQDRM INSNAVNRHQ
     HTKSQRKVEQ KFKMTYGPGT SYMPGFTRGH IVHDIDGKTI VDVPGFSANE SHGIYGYLDP
     STIKTLSKGV KVHKRGMYDS LYESVRNGQV LTIGGLFYLA TPQNAVYQIK NCINHKFHVF
     NSMDKAISIL QTIEKNKALE NVFLVNKQSL DKLQKFIIPP FYGSIDLVIK NLGHLNITPT
     GKKIDNEPLV IYLPEGVEAI IRQPLTRYIT RSLAGRDKNG NPLRKELWKS KSVTHLQRFN
     GTTPFASLLI PSTGSDNLQC ISEYNSKLND TPITYDNNTH LDESNKYKYW VNI