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Database: UniProt
Entry: E4ZPJ3_LEPMJ
LinkDB: E4ZPJ3_LEPMJ
Original site: E4ZPJ3_LEPMJ 
ID   E4ZPJ3_LEPMJ            Unreviewed;       237 AA.
AC   E4ZPJ3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   28-JUN-2023, entry version 56.
DE   RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN   ORFNames=LEMA_P041190.1 {ECO:0000313|EMBL:CBX93218.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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}.
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DR   EMBL; FP929105; CBX93218.1; -; Genomic_DNA.
DR   RefSeq; XP_003836583.1; XM_003836535.1.
DR   AlphaFoldDB; E4ZPJ3; -.
DR   STRING; 985895.E4ZPJ3; -.
DR   EnsemblFungi; CBX93218; CBX93218; LEMA_P041190.1.
DR   GeneID; 13287353; -.
DR   eggNOG; KOG3003; Eukaryota.
DR   HOGENOM; CLU_057217_0_0_1; -.
DR   InParanoid; E4ZPJ3; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; 151932at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IEA:EnsemblFungi.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
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:UP000002668}.
FT   REGION          45..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   237 AA;  26495 MW;  4C2BFD02F2D16C18 CRC64;
     MLQRTILRAS RQAARRTPAF APLRQQFVVS RVAATPAIRW YSDAAPAKEG EAAEKKEGET
     AEKKEDAPSA ANDEAAKLKE QIEKKDKEII ELKDKYLRSV ADFRNLQERT ARETKAAKDF
     AIQRFARDLV ESVDNLDRAL GTVPAEKLKS DNADLIALHD GIKMTDTILI NTLKKHGLER
     FDPSETGDKF DPNIHEAVFQ APQPDKEDGC CFHTQQKGFM LNGRVLRPAK VGVVKNA
//
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