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Database: UniProt
Entry: A0A1S9E0X5_ASPOZ
LinkDB: A0A1S9E0X5_ASPOZ
Original site: A0A1S9E0X5_ASPOZ 
ID   A0A1S9E0X5_ASPOZ        Unreviewed;       247 AA.
AC   A0A1S9E0X5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN   ORFNames=OAory_01035830 {ECO:0000313|EMBL:OOO14988.1};
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO14988.1, ECO:0000313|Proteomes:UP000190312};
RN   [1] {ECO:0000313|EMBL:OOO14988.1, ECO:0000313|Proteomes:UP000190312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC7051 {ECO:0000313|EMBL:OOO14988.1,
RC   ECO:0000313|Proteomes:UP000190312};
RA   Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA   Jeennor S., Laoteng K.;
RT   "Genome sequencing of Aspergillus oryzae BCC7051.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OOO14988.1}.
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DR   EMBL; MKZY01000001; OOO14988.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9E0X5; -.
DR   VEuPathDB; FungiDB:AO090026000264; -.
DR   eggNOG; KOG3003; Eukaryota.
DR   OMA; YAYEKIA; -.
DR   Proteomes; UP000190312; 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:UP000190312}.
FT   REGION          28..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   247 AA;  28091 MW;  9D7C82FCA81DF660 CRC64;
     MFQRTILRQA QAARSLLSVR STSSAPLALR RTSQFQPQSL RPLAPLPGLR NYSTENKAEE
     DKQEKNENAE SESQNTEDAV RKELEKKEKE VVDLKDKYVR SVADFLNLQE RTKRDMDNAR
     NFAIQRFAVD LLESIDNFDR ALLAVPEAKL NSNEPEHKDI RDLVSGLKMT QNVLMNALKK
     HGLERFDPSE PAEDGKTQKF DPNMHEATFM AKAEGKENGD IMYTQSKGFR LNGRVLRAAK
     VGVVKND
//
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