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Database: UniProt
Entry: A0A401L3K4_ASPAW
LinkDB: A0A401L3K4_ASPAW
Original site: A0A401L3K4_ASPAW 
ID   A0A401L3K4_ASPAW        Unreviewed;       137 AA.
AC   A0A401L3K4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Prefoldin subunit 4 {ECO:0000256|PIRNR:PIRNR016477};
GN   ORFNames=AAWM_08973 {ECO:0000313|EMBL:GCB26088.1};
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB26088.1, ECO:0000313|Proteomes:UP000286921};
RN   [1] {ECO:0000313|EMBL:GCB26088.1, ECO:0000313|Proteomes:UP000286921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB26088.1,
RC   ECO:0000313|Proteomes:UP000286921};
RA   Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT   "Aspergillus awamori IFM 58123T.";
RL   Submitted (SEP-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCB26088.1}.
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DR   EMBL; BDHI01000028; GCB26088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401L3K4; -.
DR   STRING; 105351.A0A401L3K4; -.
DR   Proteomes; UP000286921; 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   Reference proteome {ECO:0000313|Proteomes:UP000286921}.
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   137 AA;  15946 MW;  3C211B10B11A02EA CRC64;
     MMQTRMLTKE DEALTGSEDN EVRREDQEKI NRFSRLHQRE TLLEEQLKLK MKDKEDLEEI
     STELELADED ELVPYKIGDA FFQLPLEEAQ SLLSKATEQV DADVGKLEEG LSDLREELQQ
     LKVALYARFG RSINLET
//
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