ID   GRPE_ASHGO              Reviewed;         212 AA.
AC   Q75C01;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=GrpE protein homolog, mitochondrial;
DE   Flags: Precursor;
GN   Name=mge1; OrderedLocusNames=ACR118W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016816; AAS51344.1; -; Genomic_DNA.
DR   RefSeq; NP_983520.1; NM_208873.1.
DR   AlphaFoldDB; Q75C01; -.
DR   SMR; Q75C01; -.
DR   STRING; 33169.AAS51344; -.
DR   EnsemblFungi; AAS51344; AAS51344; AGOS_ACR118W.
DR   GeneID; 4619651; -.
DR   KEGG; ago:AGOS_ACR118W; -.
DR   eggNOG; KOG3003; Eukaryota.
DR   HOGENOM; CLU_057217_0_1_1; -.
DR   InParanoid; Q75C01; -.
DR   OMA; YAYEKIA; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
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           ?..212
FT                   /note="GrpE protein homolog, mitochondrial"
FT                   /id="PRO_0000013040"
SQ   SEQUENCE   212 AA;  23297 MW;  12694B99CC65E746 CRC64;
     MGPYLPAILR PIGRYATLYN VPRVAGQLRC YAADAKDAAD AQGESAADPR VAELEKQLAD
     KSKEAADLKD RLLRSVADFR NLQEVTRRDV QKARDFALQR FSKDLLESLD NFGHALGAVS
     PEALQRSPEI ADLHAGVRLT RDVFEKTLLK HGIAPIDALG QPFDPNLHEA TFELPQPDKT
     PGTVFHVQQP GYTLNGRVIR PAKVGVVKDP DA