ID   PFDA_METMA              Reviewed;         142 AA.
AC   Q8PYQ1;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 111.
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=MM_0809;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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 subunit alpha family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM30505.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM30505.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048036279.1; NC_003901.1.
DR   AlphaFoldDB; Q8PYQ1; -.
DR   SMR; Q8PYQ1; -.
DR   STRING; 192952.MM_0809; -.
DR   EnsemblBacteria; AAM30505; AAM30505; MM_0809.
DR   GeneID; 44085951; -.
DR   GeneID; 66137792; -.
DR   KEGG; mma:MM_0809; -.
DR   PATRIC; fig|192952.21.peg.958; -.
DR   eggNOG; arCOG01341; Archaea.
DR   HOGENOM; CLU_091867_1_1_2; -.
DR   OMA; ELQNQFM; -.
DR   Proteomes; UP000000595; 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..142
FT                   /note="Prefoldin subunit alpha"
FT                   /id="PRO_0000153677"
SQ   SEQUENCE   142 AA;  15325 MW;  90BBB65E1ABEBDDC CRC64;
     MAEVSEEIRN LAARHQEFQR QAEALRQEMS MVQASIASCD QAIATINELK AASEAGRAAE
     TMVPVGFGSY VYAEVKNPDK VVVNLGAGFS AEETAEAAVE TLNRRKEQLT KILEQMNASL
     TKIAQGMQAL ETEAAKIQPG QA