ID   PRF1_ELSFA              Reviewed;         197 AA.
AC   B0ZT47;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Prefoldin subunit 3 {ECO:0000303|PubMed:18957608};
DE   AltName: Full=Elsinochromes biosynthesis cluster protein PRF1 {ECO:0000303|PubMed:18957608};
GN   Name=PRF1 {ECO:0000303|PubMed:18957608};
OS   Elsinoe fawcettii (Citrus scab fungus) (Sphaceloma fawcettii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX   NCBI_TaxID=40997;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND INDUCTION.
RX   PubMed=18957608; DOI=10.1099/mic.0.2008/019414-0;
RA   Chung K.R., Liao H.L.;
RT   "Determination of a transcriptional regulator-like gene involved in
RT   biosynthesis of elsinochrome phytotoxin by the citrus scab fungus, Elsinoe
RT   fawcettii.";
RL   Microbiology 154:3556-3566(2008).
RN   [2]
RP   REVIEW.
RX   PubMed=21199563; DOI=10.1111/j.1364-3703.2010.00663.x;
RA   Chung K.R.;
RT   "Elsinoe fawcettii and Elsinoe australis: the fungal pathogens causing
RT   citrus scab.";
RL   Mol. Plant Pathol. 12:123-135(2011).
CC   -!- FUNCTION: Prefoldin subunit; part of the gene cluster that mediates the
CC       biosynthesis of elsinochromes, pigments consisting of at least four
CC       interconvertible tautomers (A, B, C and D) that have a core phenolic
CC       quinone to which various side chains are attached and which play an
CC       important role in fungal pathogenesis (PubMed:18957608). The non-
CC       reducing polyketide synthase PKS1 was proposed to iteratively catalyze
CC       decarboxylation between acetyl-CoA and malonyl-CoA subunits for
CC       polyketide chain elongation. The released polyketide undergoes
CC       cyclization to form an aromatic ring, and proceeds via serial
CC       modification steps to produce the heptaketide back- bone of
CC       elsinochrome. As elsinochrome has a symmetrical structure, two
CC       identical heptaketides are fused to form a core 1,2-dihydrobenzo-
CC       perylene ring structure, which can then be successively modified to
CC       produce the various derivatives of elsinochrome. Some of these
CC       reactions may be cooperatively carried out, at least in part, by the
CC       products of RDT1, OXR1 and PKS1. PRF1, embedded within the elsinochrome
CC       cluster possibly functions to stabilize some of the biosynthetic
CC       enzymes required for elsinochrome production. As prefoldin is a hexamer
CC       containing 2 a and 4 b subunits, additional prefoldin subunits, whose
CC       coding genes may not immediately link to the elsinochrome biosynthetic
CC       gene cluster, are required to fulfill the chaperone function. In
CC       addition, no methyltransferase-coding gene exists within the
CC       biosynthetic gene cluster, even though elsinochrome has four methyl
CC       groups at positions C3, C7, C8 and C12. Apparently, the identified gene
CC       cluster does not contain the entire entourage of genes responsible for
CC       elsinochrome biosynthesis. Once elsinochrome is synthesized, it must be
CC       exported outside the fungal cells, which is probably accomplished by
CC       the ECT1 transporter, to avoid toxicity (PubMed:21199563).
CC       {ECO:0000269|PubMed:18957608, ECO:0000303|PubMed:21199563}.
CC   -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC       subunits. {ECO:0000250|UniProtKB:P48363}.
CC   -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC       transcription factor TSF1 (PubMed:18957608). Expression is induced by
CC       the presence of the cluster-specific polyketide synthase PKS1
CC       (PubMed:18957608). Expression is up-regulated in the presence of large
CC       amounts of glucose, during nitrogen starvation or at alkaline pH,
CC       conditions highly conducive to elsinochrome accumulation
CC       (PubMed:18957608). {ECO:0000269|PubMed:18957608}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC       {ECO:0000305}.
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DR   EMBL; EU401707; ABZ01833.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0ZT47; -.
DR   SMR; B0ZT47; -.
DR   GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.10.287.370; -; 1.
DR   InterPro; IPR016655; PFD3.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR004127; Prefoldin_subunit_alpha.
DR   PANTHER; PTHR12409; PTHR12409; 1.
DR   Pfam; PF02996; Prefoldin; 1.
DR   PIRSF; PIRSF016396; Prefoldin_subunit_3; 1.
PE   2: Evidence at transcript level;
KW   Chaperone.
FT   CHAIN           1..197
FT                   /note="Prefoldin subunit 3"
FT                   /id="PRO_0000445819"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   197 AA;  22121 MW;  DC26601E6F5A0823 CRC64;
     MASLALRGSS ENPAPTKDTT TNPRGIPYAP FVDRVEDYVT STTDVESTLK SFSEMISKYQ
     FMESNTQRRS AGLKDKIPEI QKTLAMVRFL AGREEDDEPL ETHFELNDTL YAKALVPTTK
     EVYLWLGANV MLAYPVDEAE ELLVGKLGAA KTSLENCDED LDFLREQITT LEVATARVYN
     WDVGQRRKER EGKGGKS