ID A0A2Z6QZ16_9GLOM Unreviewed; 222 AA.
AC A0A2Z6QZ16;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 03-MAY-2023, entry version 13.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN ORFNames=RCL2_001723700 {ECO:0000313|EMBL:GES90388.1}, RclHR1_02240014
GN {ECO:0000313|EMBL:GBB93842.1};
OS Rhizophagus clarus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=94130 {ECO:0000313|EMBL:GBB93842.1, ECO:0000313|Proteomes:UP000247702};
RN [1] {ECO:0000313|EMBL:GBB93842.1, ECO:0000313|Proteomes:UP000247702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|EMBL:GBB93842.1,
RC ECO:0000313|Proteomes:UP000247702};
RA Kobayashi Y.;
RT "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT auxotrophy among arbuscular mycorrhizal fungi.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GES90388.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HR1 {ECO:0000313|EMBL:GES90388.1};
RA Maeda T., Kobayashi Y., Nakagawa T., Ezawa T., Yamaguchi K., Bino T.,
RA Nishimoto Y., Shigenobu S., Kawaguchi M.;
RT "Conservation and host-specific expression of non-tandemly repeated
RT heterogenous ribosome RNA gene in arbuscular mycorrhizal fungi.";
RL Submitted (OCT-2019) 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:GBB93842.1}.
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DR EMBL; BEXD01001380; GBB93842.1; -; Genomic_DNA.
DR EMBL; BLAL01000194; GES90388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6QZ16; -.
DR STRING; 94130.A0A2Z6QZ16; -.
DR Proteomes; UP000247702; Unassembled WGS sequence.
DR Proteomes; UP000615446; 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:UP000247702}.
FT REGION 41..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 222 AA; 24858 MW; DEBC5596CF722227 CRC64;
MSLSLSLLRR GVFNKVRGSF LPSSSIRITR PPHRILLSTA AQETNTTNNS DNAEKAEKIE
KTENVEETAA KDKQIAELKD SYLRCLADME NLRERTRREV ESTAQFAIQK FAKDLLNTVD
ILSLALSSVP TEIRNDTQNN PHLVNLYTGV SLTESELLNI LKRHGVEKID PLGEKFDPNL
HEAVYQVNDP NKESGIVCDV QKVGYSLFGR VIRPAQVGVN NN
//