ID   PFDA_NITMS              Reviewed;         145 AA.
AC   A9A592;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=Nmar_0395;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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; CP000866; ABX12291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A592; -.
DR   SMR; A9A592; -.
DR   STRING; 436308.Nmar_0395; -.
DR   EnsemblBacteria; ABX12291; ABX12291; Nmar_0395.
DR   KEGG; nmr:Nmar_0395; -.
DR   eggNOG; arCOG01341; Archaea.
DR   HOGENOM; CLU_091867_1_0_2; -.
DR   OMA; AYMNDIM; -.
DR   Proteomes; UP000000792; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016272; C:prefoldin complex; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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..145
FT                   /note="Prefoldin subunit alpha"
FT                   /id="PRO_1000115628"
SQ   SEQUENCE   145 AA;  15963 MW;  440DE0C2F3ED58E7 CRC64;
     MSQEQAEQLM QQMQMLETYF ADLSQRENTF LGVFREATAA IESIKSLSKN PESDTLVPIG
     LGTYVPTKIS SDSKIILNIG AGVAVEKDFP SAINYLEERI KEIEIAIQDT AAKKQDAAQR
     LEQGKAQVNQ LMQAMQQSGQ PPKSG