ID   GRPE_DEBHA              Reviewed;         243 AA.
AC   Q6BTP9;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=GrpE protein homolog, mitochondrial;
DE   Flags: Precursor;
GN   Name=mge1; OrderedLocusNames=DEHA2C16830g;
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: Essential component of the PAM complex, a complex required
CC       for the translocation of transit peptide-containing proteins from the
CC       inner membrane into the mitochondrial matrix in an ATP-dependent
CC       manner. Seems to control the nucleotide-dependent binding of SSC1 to
CC       substrate proteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the PAM complex, at least composed of mtHsp70,
CC       MGE1, TIM44, PAM16, PAM17 and PAM18. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
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DR   EMBL; CR382135; CAG86502.1; -; Genomic_DNA.
DR   RefSeq; XP_458420.1; XM_458420.1.
DR   AlphaFoldDB; Q6BTP9; -.
DR   SMR; Q6BTP9; -.
DR   STRING; 4959.XP_458420.1; -.
DR   EnsemblFungi; CAG86502; CAG86502; DEHA2C16830g.
DR   GeneID; 2900035; -.
DR   KEGG; dha:DEHA2C16830g; -.
DR   VEuPathDB; FungiDB:DEHA2C16830g; -.
DR   eggNOG; KOG3003; Eukaryota.
DR   HOGENOM; CLU_057217_0_0_1; -.
DR   InParanoid; Q6BTP9; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; 1525208at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00446; GrpE; 1.
DR   Gene3D; 2.30.22.10; -; 1.
DR   Gene3D; 3.90.20.20; -; 1.
DR   HAMAP; MF_01151; GrpE; 1.
DR   InterPro; IPR000740; GrpE.
DR   InterPro; IPR013805; GrpE_coiled_coil.
DR   InterPro; IPR009012; GrpE_head.
DR   PANTHER; PTHR21237; PTHR21237; 1.
DR   Pfam; PF01025; GrpE; 1.
DR   PRINTS; PR00773; GRPEPROTEIN.
DR   SUPFAM; SSF51064; SSF51064; 1.
DR   SUPFAM; SSF58014; SSF58014; 1.
DR   PROSITE; PS01071; GRPE; 1.
PE   3: Inferred from homology;
KW   Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..243
FT                   /note="GrpE protein homolog, mitochondrial"
FT                   /id="PRO_0000013042"
FT   REGION          42..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   243 AA;  27231 MW;  16D49823C4D8F1E8 CRC64;
     MQRALLSSLR RSAGIRSGVN SMRVVRPTVL APRMSMIRFA STEASKKEGK EDKAEAQGSQ
     EPETAAETNK EAEGAKVEVS EIDELKAKLT KKDRELADMK NHYARAIADF RNLQESTKLE
     KQKARDFALQ KFAKDLLESV DNFDLALNAV KEDTLKNNSE VKNLYDGVDM TRNVFEKTLA
     RHGIEKVDPI GEQFDPNQHE ATFEIAQPDK EPGTVFHVQQ NGYTLNSRVL RPAKVGVVKD
     AEN