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Database: UniProt
Entry: A0A0D2GDB0_9EURO
LinkDB: A0A0D2GDB0_9EURO
Original site: A0A0D2GDB0_9EURO 
ID   A0A0D2GDB0_9EURO        Unreviewed;       135 AA.
AC   A0A0D2GDB0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Prefoldin subunit 4 {ECO:0000256|PIRNR:PIRNR016477};
GN   ORFNames=PV04_02390 {ECO:0000313|EMBL:KIW70084.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW70084.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW70084.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW70084.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC       transfers target proteins to it. Binds to nascent polypeptide chain and
CC       promotes folding in an environment in which there are many competing
CC       pathways for nonnative proteins. {ECO:0000256|PIRNR:PIRNR016477}.
CC   -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC       subunits. {ECO:0000256|PIRNR:PIRNR016477}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC       {ECO:0000256|ARBA:ARBA00008045, ECO:0000256|PIRNR:PIRNR016477}.
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DR   EMBL; KN846957; KIW70084.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2GDB0; -.
DR   STRING; 5601.A0A0D2GDB0; -.
DR   HOGENOM; CLU_130032_0_0_1; -.
DR   OrthoDB; 5476468at2759; -.
DR   Proteomes; UP000054266; Unassembled WGS sequence.
DR   GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.370; -; 1.
DR   InterPro; IPR002777; PFD_beta-like.
DR   InterPro; IPR016661; PFDN4.
DR   InterPro; IPR009053; Prefoldin.
DR   PANTHER; PTHR21100; PREFOLDIN SUBUNIT 4; 1.
DR   PANTHER; PTHR21100:SF9; PREFOLDIN SUBUNIT 4; 1.
DR   Pfam; PF01920; Prefoldin_2; 1.
DR   PIRSF; PIRSF016477; Prefoldin_subunit_4; 1.
DR   SUPFAM; SSF46579; Prefoldin; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|PIRNR:PIRNR016477};
KW   Coiled coil {ECO:0000256|SAM:Coils}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          31..122
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   135 AA;  15370 MW;  4B5015768E18AFDD CRC64;
     MLSRRVLSRE EESESTDAEV TKEDQDKINA FSRLHNRSKA LEEELSTKQK DKEDLDELST
     ELELADEDDL IRYKIGDSFM HLPLSEAQDL LAEQTSEIES EVSALEEELG GIKEEISTLK
     AHLYARFGRG INLEA
//
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