ID A0A1I7UHU0_9PELO Unreviewed; 225 AA.
AC A0A1I7UHU0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g9477.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g9477.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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; A0A1I7UHU0; -.
DR STRING; 1561998.A0A1I7UHU0; -.
DR WBParaSite; Csp11.Scaffold629.g9477.t1; Csp11.Scaffold629.g9477.t1; Csp11.Scaffold629.g9477.
DR eggNOG; KOG3003; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Mitochondrion {ECO:0000256|RuleBase:RU000640}.
FT COILED 64..91
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 225 AA; 24967 MW; 2F6B14E86D51105E CRC64;
MMRKGASFIG QVVQQTIATA SQSSEEVNYE IKKNGKRLRG ADYEEVVLSS ISAEDKTMIP
KAAFDVLLKE YDEVQAEIAD FKDKYQRSLA ETENVRRRGI KQTDDAKVFA IQSFCKDLLE
VSDILDIAIK SVKPEELESG GKAMKDLFEG VSMTRTVLAK TFSKHGLVAV DPTNQKFDPN
LHEAVFQIPS ANAKQPVGHI EVCTKIGYSL KERPIRPAQV GVVSQ
//
