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Database: UniProt
Entry: A0A2C5XJ78_9PEZI
LinkDB: A0A2C5XJ78_9PEZI
Original site: A0A2C5XJ78_9PEZI 
ID   A0A2C5XJ78_9PEZI        Unreviewed;       249 AA.
AC   A0A2C5XJ78;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   03-MAY-2023, entry version 15.
DE   RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN   Name=grpe {ECO:0000313|EMBL:PHH55704.1};
GN   ORFNames=CFIMG_000272RA {ECO:0000313|EMBL:PHH55704.1};
OS   Ceratocystis fimbriata CBS 114723.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX   NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH55704.1, ECO:0000313|Proteomes:UP000222788};
RN   [1] {ECO:0000313|EMBL:PHH55704.1, ECO:0000313|Proteomes:UP000222788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH55704.1,
RC   ECO:0000313|Proteomes:UP000222788};
RX   PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA   Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT   "Analysis of microsatellite markers in the genome of the plant pathogen
RT   Ceratocystis fimbriata.";
RL   Fungal Biol. 117:545-555(2013).
RN   [2] {ECO:0000313|EMBL:PHH55704.1, ECO:0000313|Proteomes:UP000222788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH55704.1,
RC   ECO:0000313|Proteomes:UP000222788};
RX   PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA   Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT   "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT   the plant pathogen, Ceratocystis fimbriata.";
RL   IMA Fungus 4:357-358(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. {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:PHH55704.1}.
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DR   EMBL; APWK03000008; PHH55704.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5XJ78; -.
DR   STRING; 1035309.A0A2C5XJ78; -.
DR   OrthoDB; 151932at2759; -.
DR   Proteomes; UP000222788; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222788}.
FT   REGION          48..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  27493 MW;  B2C186E00F52AD97 CRC64;
     MLKQSIIRSS RVALRSQSII RVPFVSSIPA ARSPATAVPQ SAFRWYSSEA PPKEGEAAPK
     EGEAAPKEAD DELSILKKKL ETKEKEALEF KDRYLRSVAD FRNLQDRMTR DMKSARDFAI
     QKFAKDLTDS VDNLDRALVM VPEAKRTAPA DDAAATLTAA DAALYAQDLA NLYEGLKMTE
     NILVSTLAKH GLERFDPEGS KFNPNEHDAT FMAPQADKED GTVFHVQQKG FKLNGRVLRA
     AKVGVVKNA
//
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