PFDA_AERPE
ID PFDA_AERPE Reviewed; 151 AA.
AC Q9YD28;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Prefoldin subunit alpha;
DE AltName: Full=GimC subunit alpha;
GN Name=pfdA; OrderedLocusNames=APE_1084.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; BA000002; BAA80069.2; -; Genomic_DNA.
DR PIR; E72708; E72708.
DR AlphaFoldDB; Q9YD28; -.
DR SMR; Q9YD28; -.
DR STRING; 272557.APE_1084.1; -.
DR EnsemblBacteria; BAA80069; BAA80069; APE_1084.1.
DR KEGG; ape:APE_1084.1; -.
DR eggNOG; arCOG01341; Archaea.
DR Proteomes; UP000002518; 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 Pfam; PF02996; Prefoldin; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..151
FT /note="Prefoldin subunit alpha"
FT /id="PRO_0000153669"
SQ SEQUENCE 151 AA; 16536 MW; C38467A04518F12D CRC64;
MAQQMPSPEE IAAQLQMIRD QIAELQGVLA QLELRLRSVQ AAKETVEKAA GQDGETLFPG
DPELNTILKA RLLEPGKAIV HLGLNVYAKL DTAKATEILA KKEDALKRSL ETLKQELDKL
SRTHDQYLQL LQALTAGQAA QQAGQQQKQG S