ID   PFDA_THEPD              Reviewed;         129 AA.
AC   A1RXA9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Tpen_0430;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5;
RX   PubMed=18263724; DOI=10.1128/jb.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000505; ABL77839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1RXA9; -.
DR   SMR; A1RXA9; -.
DR   STRING; 368408.Tpen_0430; -.
DR   EnsemblBacteria; ABL77839; ABL77839; Tpen_0430.
DR   KEGG; tpe:Tpen_0430; -.
DR   eggNOG; arCOG01341; Archaea.
DR   HOGENOM; CLU_091867_1_1_2; -.
DR   OMA; ELQNQFM; -.
DR   Proteomes; UP000000641; 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; Reference proteome.
FT   CHAIN           1..129
FT                   /note="Prefoldin subunit alpha"
FT                   /id="PRO_0000322256"
SQ   SEQUENCE   129 AA;  14579 MW;  A7BCF98734FCC063 CRC64;
     MAQSRERLAE EYSVLAQVAE ELQREIQLAQ TLIAEVDSAI LALKNISSLE DGKEILVPVS
     AGVYVRASIK RQEKFLVAIG SNILVEKSLD EAVEFLNKRK EELSQLVERR MNDLNKVVAR
     IREIESSIR