ID   PFDA_HALS3              Reviewed;         154 AA.
AC   B0R7X6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Prefoldin subunit alpha {ECO:0000255|HAMAP-Rule:MF_00308};
DE   AltName: Full=GimC subunit alpha {ECO:0000255|HAMAP-Rule:MF_00308};
GN   Name=pfdA {ECO:0000255|HAMAP-Rule:MF_00308}; OrderedLocusNames=OE_4456R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
CC   -!- FUNCTION: Molecular chaperone capable of stabilizing a range of
CC       proteins. Seems to fulfill an ATP-independent, HSP70-like function in
CC       archaeal de novo protein folding. {ECO:0000255|HAMAP-Rule:MF_00308}.
CC   -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00308}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00308}.
CC   -!- SIMILARITY: Belongs to the prefoldin alpha subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00308}.
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DR   EMBL; AM774415; CAP14845.1; -; Genomic_DNA.
DR   RefSeq; WP_010903841.1; NC_010364.1.
DR   AlphaFoldDB; B0R7X6; -.
DR   SMR; B0R7X6; -.
DR   EnsemblBacteria; CAP14845; CAP14845; OE_4456R.
DR   GeneID; 5953761; -.
DR   GeneID; 62887705; -.
DR   KEGG; hsl:OE_4456R; -.
DR   HOGENOM; CLU_091867_1_3_2; -.
DR   OMA; ELQNQFM; -.
DR   PhylomeDB; B0R7X6; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.370; -; 1.
DR   HAMAP; MF_00308; PfdA; 1.
DR   InterPro; IPR011599; PFD_alpha_archaea.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR004127; Prefoldin_subunit_alpha.
DR   PANTHER; PTHR12674; PTHR12674; 1.
DR   Pfam; PF02996; Prefoldin; 1.
DR   TIGRFAMs; TIGR00293; TIGR00293; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm.
FT   CHAIN           1..154
FT                   /note="Prefoldin subunit alpha"
FT                   /id="PRO_1000115626"
FT   REGION          123..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   154 AA;  16704 MW;  7F8E6F03AE0D7A07 CRC64;
     MSLGGGGQQQ LQQLSQEIQA IEEEVEELEA DVASLRQEQT EIEEAKEALD VLETGATVQV
     PLGGDAYVRA EVKDMDEVVV SLGGGYAAEQ DSDAAASVLD EKKATIDGRI DDVQAEIADL
     SEEAEQLEQQ AQQAQQQMMQ QQMQAQQQPQ DGEQ