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VEA_ACRCH
ID   VEA_ACRCH               Reviewed;         514 AA.
AC   A0A086T5L8; A5AC80;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 2.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Developmental and secondary metabolism regulator veA {ECO:0000305};
DE   AltName: Full=Velvet complex subunit A {ECO:0000305};
GN   Name=veA {ECO:0000303|PubMed:17400783}; ORFNames=ACRE_045050;
OS   Acremonium chrysogenum (Cephalosporium acremonium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX   NCBI_TaxID=5044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   TISSUE=Mycelium;
RX   PubMed=17400783; DOI=10.1128/aem.00129-07;
RA   Dreyer J., Eichhorn H., Friedlin E., Kaernsteiner H., Kueck U.;
RT   "A homologue of the Aspergillus velvet gene regulates both cephalosporin C
RT   biosynthesis and hyphal fragmentation in Acremonium chrysogenum.";
RL   Appl. Environ. Microbiol. 73:3412-3422(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11550 / CBS 779.69 / DSM 880 / IMI 49137;
RA   Terfehr D., Dahlmann T.A., Specht T., Zadra I., Kurnsteiner H., Kuck U.;
RT   "Draft genome sequence of Acremonium chrysogenum, the producer of the beta-
RT   lactam antibiotic cephalosporin C.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). The velvet complex hat
CC       acts as a global regulator for secondary metabolite gene expression
CC       (PubMed:17400783). Controls the expression of the cephalosporin C gene
CC       cluster (PubMed:17400783). Regulates hyphal fragmentation
CC       (PubMed:17400783). {ECO:0000250|UniProtKB:C8VTV4,
CC       ECO:0000269|PubMed:17400783}.
CC   -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC       laeA, veA and velB; VeA acting as a bridging protein between laeA and
CC       velB (By similarity). {ECO:0000250|UniProtKB:C8VTV4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17400783}. 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: Reduces by 80% cephalosporin C production and
CC       leads to an altered hyphal morphology (PubMed:17400783).
CC       {ECO:0000269|PubMed:17400783}.
CC   -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=KFH44650.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AM410093; CAL68582.1; -; Genomic_DNA.
DR   EMBL; JPKY01000044; KFH44650.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A0A086T5L8; -.
DR   SMR; A0A086T5L8; -.
DR   EnsemblFungi; KFH44650; KFH44650; ACRE_045050.
DR   HOGENOM; CLU_022491_2_0_1; -.
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   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Sporulation; Transcription; Transcription regulation.
FT   CHAIN           1..514
FT                   /note="Developmental and secondary metabolism regulator
FT                   veA"
FT                   /id="PRO_0000435765"
FT   DOMAIN          26..218
FT                   /note="Velvet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT   REGION          219..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..448
FT                   /note="PEST"
FT                   /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT   MOTIF           40..45
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT   COMPBIAS        224..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  57247 MW;  5FC6A95D9CD6C8B2 CRC64;
     MATPSLIPTD ADRDHPVRIH RVTRTNRHLW YQLTVLQQPE RARACGAGTK DSDRRPVDPP
     PVVELRIKEG NSFEEGKEIT FDYNANFFLY ASLEQSRRIA PGRMQGQPNP PILTGSPVSG
     MAYLDRPAAA GYFIFPDLSV RHEGHYRLSF SLFETTKDEK DLDIERASDD RLDTGADWRM
     EIKTSPFDVF SAKKFPGLME STPLSKEVAD QGCHVRIRRD VRMRKRDAKS NNGRDRREDD
     MARRRTVTPA SEDPHSAAAR ARSMSNSSEH RVPGPPEPPG HPSAVDPAGR GHLSFGGPQY
     ASPHQYGLQS RLPPPSPGGP YNPATQYIKP EHQSYRYPPS RDMSQTGPSP APRQDGHDRR
     QSGPYVPPSP SVYSNDGRSR PESHPSYPST PVSSHPANLP SDPSLVLPRI KSPSNSVSPS
     NSSLKITDLL VQPLPSSEPK LEVGSAPCPP PKTPIGSKRK HDQTFVQNDR ALRNHQRQLD
     PHYNPVARPC SPVGEQYKRA DGTYMYAKFS VFTM
 
 
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