ID   PIG19_CLAP2             Reviewed;         296 AA.
AC   M1VWN2;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=SHSP domain-containing protein CPUR_05420 {ECO:0000305};
DE   AltName: Full=Ergochrome biosynthesis cluster protein CPUR_05420 {ECO:0000303|PubMed:30996871};
GN   ORFNames=CPUR_05420;
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1;
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
RN   [2]
RP   FUNCTION.
RX   PubMed=28955461; DOI=10.1186/s40694-016-0020-z;
RA   Neubauer L., Dopstadt J., Humpf H.U., Tudzynski P.;
RT   "Identification and characterization of the ergochrome gene cluster in the
RT   plant pathogenic fungus Claviceps purpurea.";
RL   Fungal Biol. Biotechnol. 3:2-2(2016).
RN   [3]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=30996871; DOI=10.1039/c8sc05126g;
RA   Greco C., de Mattos-Shipley K., Bailey A.M., Mulholland N.P., Vincent J.L.,
RA   Willis C.L., Cox R.J., Simpson T.J.;
RT   "Structure revision of cryptosporioptides and determination of the genetic
RT   basis for dimeric xanthone biosynthesis in fungi.";
RL   Chem. Sci. 10:2930-2939(2019).
RN   [4]
RP   FUNCTION.
RX   PubMed=32105084; DOI=10.1021/acs.orglett.0c00285;
RA   Wei X., Matsuda Y.;
RT   "Unraveling the fungal strategy for tetrahydroxanthone biosynthesis and
RT   diversification.";
RL   Org. Lett. 22:1919-1923(2020).
CC   -!- FUNCTION: Monooxygenase; part of the ergochrome gene cluster
CC       responsible for the typical purple-black color of the ergot sclerotia
CC       (Probable). The ergochrome gene cluster produces several ergot pigments
CC       including the yellow ergochrome secalonic acid and its derivatives, as
CC       well as the red anthraquinones endocrocin and clavorubin
CC       (PubMed:28955461). The pathway begins with the synthesis of
CC       atrochrysone thioester by the polyketide synthase (PKS) CPUR_05437 (By
CC       similarity). The atrochrysone carboxyl ACP thioesterase CPUR_05436 then
CC       breaks the thioester bond and releases the atrochrysone carboxylic acid
CC       from CPUR_05437 (By similarity). The atrochrysone carboxylic acid is
CC       then converted to atrochrysone which is further transformed into emodin
CC       anthrone (By similarity). The next step is performed by the anthrone
CC       oxygenase CPUR_05434 that catalyzes the oxidation of emodinanthrone to
CC       emodin (By similarity). Emodin is further modified to yield
CC       monodictyphenone via several steps involving CPUR_05427, CPUR_05428,
CC       CPUR_05429 and CPUR_05430 (By similarity). The short chain
CC       dehydrogenase/reductase CPUR_05418 then catalyzes the C-5 ketoreduction
CC       to give the xanthone skeleton of the monomeric units (PubMed:32105084).
CC       Ergochromes formation requires further dimerization steps of different
CC       xanthone units, probably catalyzed by the cytochrome P450 monooxygenase
CC       CPUR_05419 (PubMed:28955461). CPUR_05425, CPUR_05426 and CPUR_05431 are
CC       unique to Claviceps, thus it is likely that they are involved in
CC       further modification of xanthone units or in their dimerization
CC       (PubMed:28955461). The yellow ergochromes and the red anthraquinone
CC       pigments endocrocin and clavorubin are products from the same PKS
CC       derived precursors and the latter are likely shunt products in the
CC       pathway of xanthone biosynthesis (PubMed:28955461). It is proposed that
CC       atrochrysone carboxylic acid released from the PKS CPUR_05437 can also
CC       be converted to endocrocin anthrone which is further oxidized into
CC       endocrocin by CPUR_05435 (By similarity). Endocrocin could be then
CC       modified to clavorubin, possibly by CPUR_05423 and CPUR_05431
CC       (PubMed:28955461). Clavorubin is the principal anthraquinone metabolite
CC       produced by the cluster with a much higher yield compared to endocrocin
CC       (PubMed:28955461). {ECO:0000250|UniProtKB:Q4W944,
CC       ECO:0000250|UniProtKB:Q5BH30, ECO:0000269|PubMed:28955461,
CC       ECO:0000269|PubMed:32105084, ECO:0000305|PubMed:30996871}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000305}.
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DR   EMBL; CAGA01000032; CCE31567.1; -; Genomic_DNA.
DR   SMR; M1VWN2; -.
DR   STRING; 1111077.M1VWN2; -.
DR   EnsemblFungi; CCE31567; CCE31567; CPUR_05420.
DR   VEuPathDB; FungiDB:CPUR_05420; -.
DR   eggNOG; KOG0710; Eukaryota.
DR   HOGENOM; CLU_940093_0_0_1; -.
DR   OrthoDB; 1413403at2759; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   Pfam; PF00011; HSP20; 1.
DR   SUPFAM; SSF49764; SSF49764; 1.
DR   PROSITE; PS01031; SHSP; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Stress response.
FT   CHAIN           1..296
FT                   /note="SHSP domain-containing protein CPUR_05420"
FT                   /id="PRO_0000453512"
FT   DOMAIN          169..296
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   REGION          50..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   296 AA;  31899 MW;  44CBE362070D698D CRC64;
     MATMAHANTS HPLYVAGMAG NTNHMSPWGE DAHKRWLAAL GPSSLRGPFA WQTCPQQRHP
     HQPDVSGPPG SGFGEQPSQD TPNPMFGATG PHQQHNFPSH PYAAHNSKEA HEAWLKVYQS
     VWGNTKHAGA WSGPWSPAAG GRQHHMSGGG GGGGPRWMGG PMPWTQCDET KKSFTPDIDV
     VETPESYSVQ ASLPGAKKED VKVSWDPSTY ELRIEGVVSR SVGNDEEGEK KTEQSGRFSL
     RERQTGKFCR TVYLGSQVDG DKIEEGGLSA GMDDGVLRIA VPRQGSGKGV KEITIV