ID E1Z993_CHLVA Unreviewed; 153 AA.
AC E1Z993;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
DE Flags: Fragment;
GN ORFNames=CHLNCDRAFT_11196 {ECO:0000313|EMBL:EFN57477.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN [1] {ECO:0000313|EMBL:EFN57477.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN57477.1,
RC ECO:0000313|Proteomes:UP000008141};
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
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; GL433839; EFN57477.1; -; Genomic_DNA.
DR RefSeq; XP_005849579.1; XM_005849517.1.
DR AlphaFoldDB; E1Z993; -.
DR STRING; 554065.E1Z993; -.
DR GeneID; 17356934; -.
DR KEGG; cvr:CHLNCDRAFT_11196; -.
DR eggNOG; KOG3003; Eukaryota.
DR InParanoid; E1Z993; -.
DR OMA; QHELICH; -.
DR OrthoDB; 151932at2759; -.
DR Proteomes; UP000008141; 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:UP000008141}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFN57477.1"
FT NON_TER 153
FT /evidence="ECO:0000313|EMBL:EFN57477.1"
SQ SEQUENCE 153 AA; 16939 MW; D4FD58478F8841FD CRC64;
EDLKDKLLRT LADMENLRER TARTSAETKQ FAVQGLVKNL LEVADNLERA AGSVPPEDVH
QDSEIDRDRA LKLLRSLREG VLMTDTVLMK ASRAGWGGVT RYDPLGDKFD PNLHNALFEV
PDATKDPGTV AVVVKRGYEL NERVVRAAEV GVS
//
