PFDA_PYRHO
ID PFDA_PYRHO Reviewed; 148 AA.
AC O58263;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Prefoldin subunit alpha;
DE AltName: Full=GimC subunit alpha;
GN Name=pfdA; OrderedLocusNames=PH0527;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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 -!- INTERACTION:
CC O58263; O58268: pfdB; NbExp=2; IntAct=EBI-9014072, EBI-9014082;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA29615.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA29615.1; ALT_INIT; Genomic_DNA.
DR PIR; B71166; B71166.
DR RefSeq; WP_048053149.1; NC_000961.1.
DR PDB; 2ZDI; X-ray; 3.00 A; C=1-148.
DR PDBsum; 2ZDI; -.
DR AlphaFoldDB; O58263; -.
DR SMR; O58263; -.
DR DIP; DIP-29170N; -.
DR IntAct; O58263; 2.
DR STRING; 70601.3256932; -.
DR EnsemblBacteria; BAA29615; BAA29615; BAA29615.
DR GeneID; 1444414; -.
DR KEGG; pho:PH0527; -.
DR eggNOG; arCOG01341; Archaea.
DR OMA; ELQNQFM; -.
DR OrthoDB; 112405at2157; -.
DR EvolutionaryTrace; O58263; -.
DR Proteomes; UP000000752; 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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm.
FT CHAIN 1..148
FT /note="Prefoldin subunit alpha"
FT /id="PRO_0000153684"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:2ZDI"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:2ZDI"
FT HELIX 23..49
FT /evidence="ECO:0007829|PDB:2ZDI"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2ZDI"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2ZDI"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2ZDI"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:2ZDI"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2ZDI"
FT HELIX 93..126
FT /evidence="ECO:0007829|PDB:2ZDI"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:2ZDI"
FT TURN 138..143
FT /evidence="ECO:0007829|PDB:2ZDI"
SQ SEQUENCE 148 AA; 16603 MW; 46AB8EA20A4AC8BD CRC64;
MAQNNKELEK LAYEYQVLQA QAQILAQNLE LLNLAKAEVQ TVRETLENLK KIEEEKPEIL
VPIGAGSFLK GVIVDKNNAI VSVGSGYAVE RSIDEAISFL EKRLKEYDEA IKKTQGALAE
LEKRIGEVAR KAQEVQQKQS MTSFKVKK
