ID C7GWF2_YEAS2 Unreviewed; 228 AA.
AC C7GWF2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 03-MAY-2023, entry version 45.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN Name=MGE1 {ECO:0000313|EMBL:EEU04882.1};
GN ORFNames=C1Q_04830 {ECO:0000313|EMBL:EEU04882.1};
OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=574961 {ECO:0000313|EMBL:EEU04882.1, ECO:0000313|Proteomes:UP000008073};
RN [1] {ECO:0000313|EMBL:EEU04882.1, ECO:0000313|Proteomes:UP000008073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAY291 {ECO:0000313|EMBL:EEU04882.1,
RC ECO:0000313|Proteomes:UP000008073};
RX PubMed=19812109; DOI=10.1101/gr.091777.109;
RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.,
RA Missawa S.K., Galzerani F., Costa G.G., Vidal R.O., Noronha M.F.,
RA Dominska M., Andrietta M.G., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA Tavares F.C., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA Pereira G.A.;
RT "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT bioethanol production.";
RL Genome Res. 19:2258-2270(2009).
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. {ECO:0000256|RuleBase:RU000640}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU000640}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|RuleBase:RU004478}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEU04882.1}.
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DR EMBL; ACFL01000381; EEU04882.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GWF2; -.
DR Proteomes; UP000008073; Unassembled WGS sequence.
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:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 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; GRPE PROTEIN; 1.
DR PANTHER; PTHR21237:SF23; GRPE PROTEIN HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF58014; Coiled-coil domain of nucleotide exchange factor GrpE; 1.
DR SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU000640};
KW Mitochondrion {ECO:0000256|RuleBase:RU000640}.
FT REGION 45..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 228 AA; 26039 MW; 18707CEE3D8BC4DB CRC64;
MRAFSAATVR ATTRKSFIPM APRTPFVTPS FTKSVGSMRR MRFYSDEAKS EESKENNEDL
TEEQSEIKKL ESQLSAKTKE ASELKDRLLR SVADFRNLQQ VTKKDIQKAK DFALQKFAKD
LLESVDNFGH ALNAFKEEDL QKSKEISDLY TGVRMTRDVF ENTLRKHGIE KLDPLGEPFD
PNKHEATFEL PQPDKEPGTV FHVQQLGFTL NDRVIRPAKV GIVKGEEN
//
