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Database: UniProt
Entry: GEP3_VANPO
LinkDB: GEP3_VANPO
Original site: GEP3_VANPO 
ID   GEP3_VANPO              Reviewed;         551 AA.
AC   A7TQC5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 61.
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=Kpol_479p12;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480456; EDO15524.1; -; Genomic_DNA.
DR   RefSeq; XP_001643382.1; XM_001643332.1.
DR   AlphaFoldDB; A7TQC5; -.
DR   STRING; 436907.A7TQC5; -.
DR   GeneID; 5543597; -.
DR   KEGG; vpo:Kpol_479p12; -.
DR   eggNOG; ENOG502S0UP; Eukaryota.
DR   HOGENOM; CLU_025792_1_0_1; -.
DR   InParanoid; A7TQC5; -.
DR   OMA; IIPPFYG; -.
DR   OrthoDB; 1983973at2759; -.
DR   PhylomeDB; A7TQC5; -.
DR   Proteomes; UP000000267; 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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR46434; GENETIC INTERACTOR OF PROHIBITINS 3, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR46434:SF1; GENETIC INTERACTOR OF PROHIBITINS 3, MITOCHONDRIAL; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..551
FT                   /note="Genetic interactor of prohibitins 3, mitochondrial"
FT                   /id="PRO_0000409641"
FT   DOMAIN          118..299
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
SQ   SEQUENCE   551 AA;  63674 MW;  F21B90606EEB0AAB CRC64;
     MFVVRRSIVF QQSRRQFSGS IAWLQACSSC GIKLQSKNPA LIGYYTKPKP LEVGKVETLE
     DVKYMLFSQD IQKIKEIEDG TTLEDEKNRI PHSLICKRCS DAVHQNKYDV MDFKNCSLKE
     VIRSVPNDKP IVSIASLPEF PFHVNKNILE NEKESVLVFT KADQVLKTSS ATSTRLPIFF
     KDYFKYHLGL QVNKVLAVSS LKKWNLSGLL SNLRNNSYFL GNPNVGKSTL MNSLIQRYNG
     TKLDFNSNIS DDMVNDAQHK HLRKAQLAGV SHIPNLTREC QGYQVDKKRI YDLPGYSENV
     DELPLERIVK SNWLEWVRKT NLFDTKKVKK KPYITIKGTE NGRCYTIGGL FFLQPPPYSI
     NQIIKFIPGE PYIFKNVTRA LETFKSVYGN DTPHPLEKYC GINDEYCDIT KYQRHVIPPF
     QGSIEIVFKD IGYILLRSTG RYSFNGLYEI WVPKGISVCI REPLEKLIEE GYVQYTESKN
     KISSCPKGRP LVSSTYIMDP NEEDTFAKIR EMYLDRTENE ISVRRLVKED PLEVVSNKHD
     TPPNLYWHYK W
//
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