ID D7MV12_ARALL Unreviewed; 302 AA.
AC D7MV12;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN ORFNames=ARALYDRAFT_495605 {ECO:0000313|EMBL:EFH40642.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(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; GL348720; EFH40642.1; -; Genomic_DNA.
DR RefSeq; XP_002864383.1; XM_002864337.1.
DR AlphaFoldDB; D7MV12; -.
DR STRING; 81972.D7MV12; -.
DR EnsemblPlants; fgenesh2_kg.8__1421__AT5G55200.1; fgenesh2_kg.8__1421__AT5G55200.1; fgenesh2_kg.8__1421__AT5G55200.1.
DR Gramene; fgenesh2_kg.8__1421__AT5G55200.1; fgenesh2_kg.8__1421__AT5G55200.1; fgenesh2_kg.8__1421__AT5G55200.1.
DR eggNOG; KOG3003; Eukaryota.
DR HOGENOM; CLU_057217_1_0_1; -.
DR OrthoDB; 151932at2759; -.
DR Proteomes; UP000008694; 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 GO; GO:0009411; P:response to UV; IEA:EnsemblPlants.
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:SF43; GRPE PROTEIN HOMOLOG 1, 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:UP000008694}.
FT REGION 77..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 33261 MW; D0CFBDD9E0933795 CRC64;
MLVSRVLSRV SRSAGLRSSL SSVVTPKRNQ IPIVSSRFHS LVHGNPNKLV AVPVSLLNHG
TLDLNVLQRF GFFSSSSAEP KGNESYTEVP KTGEASEDVE VGRDTDAEID FDDMSRDDLV
KLVGEKEDLL KVQQEDIKEM KDKFLRTYAE QQNLMDRTKR NAENAKKFAV QNFATSLLDV
ADNLERASSV VKESFSKIDT SKDSAGAAPL LKNLLEGVEM TEKQLAEVFK KSGLVKEDPL
NEPFDPNKHN AVFQVPDASK PKGTIAHVLK PGYSLYDRVI RPAEVGVTCA VENEEGEKES
AA
//
