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Database: UniProt
Entry: M7UB18_BOTF1
LinkDB: M7UB18_BOTF1
Original site: M7UB18_BOTF1 
ID   M7UB18_BOTF1            Unreviewed;       136 AA.
AC   M7UB18;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=Prefoldin subunit 4 {ECO:0000256|PIRNR:PIRNR016477};
GN   ORFNames=BcDW1_554 {ECO:0000313|EMBL:EMR90850.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR90850.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
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; KB707685; EMR90850.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7UB18; -.
DR   STRING; 1290391.M7UB18; -.
DR   HOGENOM; CLU_130032_0_0_1; -.
DR   Proteomes; UP000012045; 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}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   136 AA;  15892 MW;  B631B6049D3ADC71 CRC64;
     MQRRMLSKED EAAVGADEVE VRREDQDKIN RFSRLHQREI GLEDELKSKH KEKEDLDDVS
     GELELADEDD MIPYKIGDSF ISLPLPEVQE LLTKSTENIE EEVILVEEKL STIREEMTRL
     KVELYARFGR SINLET
//
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