ID   GEP3_PICST              Reviewed;         676 AA.
AC   A3GEW8;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-MAY-2022, entry version 58.
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; ORFNames=PICST_28031;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; AAVQ01000001; EAZ63239.2; -; Genomic_DNA.
DR   RefSeq; XP_001387262.2; XM_001387225.1.
DR   AlphaFoldDB; A3GEW8; -.
DR   STRING; 4924.XP_001387262.2; -.
DR   PRIDE; A3GEW8; -.
DR   EnsemblFungi; EAZ63239; EAZ63239; PICST_28031.
DR   GeneID; 4850817; -.
DR   KEGG; pic:PICST_28031; -.
DR   eggNOG; ENOG502S0UP; Eukaryota.
DR   HOGENOM; CLU_025792_0_0_1; -.
DR   InParanoid; A3GEW8; -.
DR   OMA; QIVKYIP; -.
DR   OrthoDB; 612803at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
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..48
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..676
FT                   /note="Genetic interactor of prohibitins 3, mitochondrial"
FT                   /id="PRO_0000409640"
FT   DOMAIN          180..395
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          98..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  77595 MW;  8EF4D2A4324C7949 CRC64;
     MIRYSGFSVV RSCLSRTFSR NNSALSTAIT SSLLTNLFPT CKSCGVRLQS SDPKGPGYYI
     LEESKPAKRF VKSEDQVFAK YVNDLSLEDK KLLINEDSKK VSDSESRSES QDLSNEADID
     SSLVNSLGNK DYYASEIKKV SQKDKFKLEE KYNDSVECVR CRDATYRSNF KNFSQQEYPL
     ELLDNIMSRI PPHEQIVYIV NAQDFPMSIN PKIFQYRSSN ELKFIVNKAD LLFKSINLSK
     NYGQTFFSDY LFHKYRVPKE NVMVVSGTNY WDFDKVLDFV DDNSYLIGNV NCGKSTIIKG
     MLYTIDKSNK RKKFMSSRER TKMEKEQDML INRASRMKAM TAGEKKKEKK RYEMLFRSKV
     GPGVSHIPGF TRGFIQIDLE DMDKTIYDVP GFVNSENQLI HHHDIYNKIS SPKILKQIHK
     GVKVYDKGTY TSKYITAKGG QSLTIGGLFF LNFPQKSMYQ LRNCINHDFH LFSNFSRAVY
     ISSNLSKYPG MGSKFFIEHD DSSLKELRRF IIPPFHGSID LVIQNLGHIN IKPTGRKETN
     QPLILYLPPG VEAIIRLPIT NYIAKTFTGR DAKGNPLRKE NILTKGVLAL QRYTAKYPFY
     STLISANKGA EVSSELALIL KSEATCEPVT DAEQERLVKQ DFARIGEWAT IARGVECNYN
     ERTVVDERNK FDYWME