ID A0A0J8TVE6_COCIT Unreviewed; 252 AA.
AC A0A0J8TVE6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 03-MAY-2023, entry version 24.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN ORFNames=CISG_01598 {ECO:0000313|EMBL:KMU77842.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU77842.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(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; DS268121; KMU77842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8TVE6; -.
DR STRING; 454286.A0A0J8TVE6; -.
DR Proteomes; UP000054559; 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:UP000054559}.
FT REGION 51..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 252 AA; 28362 MW; D4A9883173242EAB CRC64;
MFRRALIRQS QAARSAFTTR SISSSPLSRK QPLLQTFTQF GKPLPSRVCQ RFNSTESQQK
NAENASADGK NGEQKPSESQ LSEAEATLRK EVEKQEREII DLKDKYLRSV ADFRNLQERT
KRDVDAARSF AIQRFGADLI ESIDNFERAL EAVPSEKLNN GENKDLADLY DGLKMTEKVI
MNTLKKHGLE RFDPSELVEG KPQKFDPKLH EATFMAPAPG KEDGDILHVQ TKGFILNGRV
LRAAKVGVVK NA
//
