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VEA_BOTFB
ID   VEA_BOTFB               Reviewed;         575 AA.
AC   L0PQS5;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Developmental and secondary metabolism regulator VEL1 {ECO:0000305};
DE   AltName: Full=Velvet complex subunit 1 {ECO:0000305};
GN   Name=VEL1 {ECO:0000303|PubMed:23118899};
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=B05.10;
RX   PubMed=23118899; DOI=10.1371/journal.pone.0047840;
RA   Schumacher J., Pradier J.M., Simon A., Traeger S., Moraga J., Collado I.G.,
RA   Viaud M., Tudzynski B.;
RT   "Natural variation in the VELVET gene bcvel1 affects virulence and light-
RT   dependent differentiation in Botrytis cinerea.";
RL   PLoS ONE 7:E47840-E47840(2012).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23147398; DOI=10.1016/j.fgb.2012.10.003;
RA   Yang Q., Chen Y., Ma Z.;
RT   "Involvement of BcVeA and BcVelB in regulating conidiation, pigmentation
RT   and virulence in Botrytis cinerea.";
RL   Fungal Genet. Biol. 50:63-71(2013).
RN   [3]
RP   IDENTIFICATION IN THE VELVET COMPLEX, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25625818; DOI=10.1094/mpmi-12-14-0411-r;
RA   Schumacher J., Simon A., Cohrs K.C., Traeger S., Porquier A., Dalmais B.,
RA   Viaud M., Tudzynski B.;
RT   "The VELVET complex in the gray mold fungus Botrytis cinerea: impact of
RT   BcLAE1 on differentiation, secondary metabolism, and virulence.";
RL   Mol. Plant Microbe Interact. 28:659-674(2015).
CC   -!- FUNCTION: Component of the velvet transcription factor complex that
CC       controls sexual/asexual developmental ratio in response to light,
CC       promoting sexual development in the darkness while stimulating asexual
CC       sporulation under illumination (PubMed:23118899). The velvet complex
CC       hat acts as a global regulator for secondary metabolite gene expression
CC       (By similarity). Controls the expression of the oxalic acid and melanin
CC       gene clusters (PubMed:23118899, PubMed:23147398). Controls also the
CC       expression of proteases and carbohydrate-active enzymes
CC       (PubMed:25625818). Involved in the resistance to oxidative stress
CC       (PubMed:23147398). Required for full virulence (PubMed:23118899,
CC       PubMed:23147398). {ECO:0000250|UniProtKB:C8VTV4,
CC       ECO:0000269|PubMed:23118899, ECO:0000269|PubMed:23147398,
CC       ECO:0000269|PubMed:25625818}.
CC   -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC       LAE1, VEL1 and VEL2; VEL1 acting as a bridging protein between LAE1 and
CC       VEL2 (PubMed:25625818). {ECO:0000269|PubMed:25625818}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23118899}. Cytoplasm
CC       {ECO:0000250|UniProtKB:C8VTV4}. Note=Enriched in the nucleus in the
CC       dark (By similarity). {ECO:0000250|UniProtKB:C8VTV4}.
CC   -!- DOMAIN: The C-terminal PEST domain is a region rich in proline,
CC       glutamic acid, serine and threonine residues that is required for the
CC       light-dependent regulation of development and secondary metabolism (By
CC       similarity). {ECO:0000250|UniProtKB:C8VTV4}.
CC   -!- DISRUPTION PHENOTYPE: Leads to light-independent conidiation, loss of
CC       sclerotial development and oxalic acid production, and reduced
CC       virulence on several host plants (PubMed:23118899, PubMed:25625818).
CC       Increases conidiation and melanin biosynthesis (PubMed:23147398).
CC       {ECO:0000269|PubMed:23118899, ECO:0000269|PubMed:23147398}.
CC   -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR   EMBL; HE977589; CCK35904.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0PQS5; -.
DR   SMR; L0PQS5; -.
DR   VEuPathDB; FungiDB:Bcin15g03390; -.
DR   OrthoDB; 1171722at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.3960; -; 1.
DR   InterPro; IPR021740; Velvet.
DR   InterPro; IPR037525; Velvet_dom.
DR   InterPro; IPR038491; Velvet_dom_sf.
DR   PANTHER; PTHR33572; PTHR33572; 1.
DR   Pfam; PF11754; Velvet; 2.
DR   PROSITE; PS51821; VELVET; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Sporulation; Transcription; Transcription regulation.
FT   CHAIN           1..575
FT                   /note="Developmental and secondary metabolism regulator
FT                   VEL1"
FT                   /id="PRO_0000435775"
FT   DOMAIN          21..225
FT                   /note="Velvet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT   REGION          36..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..509
FT                   /note="PEST"
FT                   /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT   REGION          513..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           35..40
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT   COMPBIAS        231..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..349
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  63594 MW;  EEEE33E3B33486C3 CRC64;
     MAASIGPKSI PETITRQTKG GRKLKYTLTV IQQPERARAC GSGAKSSADR RPVDPPPVVQ
     LRIYDETDPR QEKEITFHYN ANFFLFATLE VARNIAQGRV QTSAPQAPVL TGMPVSGMAY
     LDRPNEAGYF IFPDLSVRHE GQYKLSFNLY EETKEEKDTD IEPSNDSSMR QMSSAAAAAE
     SSFDWRMELK SDQFTVYSAK KFPGLSESTD LSRTVAEQGC RVRIRRDVRM RRRDTKPGGD
     FGEKEDEYQQ GRATSPPFDY NIQAARQRAL SASVHEDPQQ RRGSGEISPY HSPVVNTPFR
     TPSISPSTPN APLPPGNQLG WIPNGPGYAA APSIQPPHPP PPPPSSYPQS MPATHHNQGP
     STQFRQQPPQ GPPPAPIGYD ERRSSYSQFR PPTNPSQQQS YESDYRRMSF GYQIPASSQG
     PQPIAPAVQN PAYNQQSMEP TYSRNPPAYS TSFQDSVALA PLRAAEQPLA MSPLASVTSI
     SRGTQNSAPM PSHNYNKLER SGSYSQYAPI EAEAPKSTNK RSFNDVFSTP TESLSNGRRP
     SAIGIDIEEN TRKQEQMIYR RANGNIQNKP APGLN
 
 
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