ID K9GGG3_PEND2 Unreviewed; 136 AA.
AC K9GGG3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE RecName: Full=Prefoldin subunit 4 {ECO:0000256|PIRNR:PIRNR016477};
GN ORFNames=PDIG_35820 {ECO:0000313|EMBL:EKV13838.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV13838.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV13838.1}.
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DR EMBL; AKCT01000150; EKV13838.1; -; Genomic_DNA.
DR AlphaFoldDB; K9GGG3; -.
DR STRING; 1170229.K9GGG3; -.
DR eggNOG; KOG1760; Eukaryota.
DR HOGENOM; CLU_130032_0_0_1; -.
DR InParanoid; K9GGG3; -.
DR OMA; KFGRAIN; -.
DR OrthoDB; 5476468at2759; -.
DR Proteomes; UP000009882; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009882}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 39..69
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 96..123
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 136 AA; 15722 MW; 764CD16A87C64347 CRC64;
MVQPRMLTKA DETSVNDENE VRREDQEKIN RFSRLHQRET VLEEQLKGKQ KDKEDLEEVS
MELELADEDE LVPYKIGDSF FQLPLSDAQG MLSASTEKID ADVSKLEDSL GDLREEMQQL
KVALYARFGR SINLET
//
