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Database: UniProt
Entry: A0A0E0QHM1_ORYRU
LinkDB: A0A0E0QHM1_ORYRU
Original site: A0A0E0QHM1_ORYRU 
ID   A0A0E0QHM1_ORYRU        Unreviewed;       335 AA.
AC   A0A0E0QHM1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI08G12600.1, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI08G12600.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0QHM1; -.
DR   STRING; 4529.A0A0E0QHM1; -.
DR   EnsemblPlants; ORUFI08G12600.1; ORUFI08G12600.1; ORUFI08G12600.
DR   Gramene; ORUFI08G12600.1; ORUFI08G12600.1; ORUFI08G12600.
DR   eggNOG; KOG3003; Eukaryota.
DR   HOGENOM; CLU_057217_1_0_1; -.
DR   OMA; NARMRHQ; -.
DR   Proteomes; UP000008022; 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:SF28; GRPE PROTEIN HOMOLOG; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008022}.
FT   REGION          69..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          146..191
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        86..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  36395 MW;  F64236701BE52BF9 CRC64;
     MAAAARLLAR ISRQGVASAA AARRQAEAAA LLGASAGRHL APPCSSIKAL PLLNQPRLYS
     TSTFQRFGFS SSAPQQDDKA ANKQTEDGVN KSTQSEASNE TNSSPGTENA SQAGSQDSVP
     QSNRRRRGTK RTAFSDSDTE DLDLSKEDLT KLVLEKEELL KSKDEEVKDM KDKVLRSYAE
     MENVIARTKR ESDNAKKYAV QGFSKSLLDV ADNLSRASSV VKESFSKIDT SNESAEAVKL
     LNTLLEGVEM TEKQLGEVFK KFGVEKFDPL NEKFDPNKHA ALFQIPDPSK PSGTVAAVVK
     VGYMLHDRVL RPAEVGVTEG GPIEEEPEEK SDKSD
//
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