ID   A0A0N5BXU4_STREA        Unreviewed;       123 AA.
AC   A0A0N5BXU4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=Prefoldin subunit 4 {ECO:0000256|PIRNR:PIRNR016477};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001061200.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001061200.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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|ARBA:ARBA00011695,
CC       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   AlphaFoldDB; A0A0N5BXU4; -.
DR   STRING; 174720.A0A0N5BXU4; -.
DR   WBParaSite; SPAL_0001061200.1; SPAL_0001061200.1; SPAL_0001061200.
DR   Proteomes; UP000046392; Unplaced.
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|ARBA:ARBA00023186, ECO:0000256|PIRNR:PIRNR016477}.
SQ   SEQUENCE   123 AA;  13892 MW;  12815F72BDE5E6E9 CRC64;
     MSASNLKVSK EDQAKINKFA TGHAKSVSLK REIEKLKTFL ENCKEAEEEI ILVDSETIPY
     KVGNAFFELT LDEINDQLAK DIELNNSKLT EKQLALEKVT SELNGLKKDL YAKFGKAINL
     EEE
//