VEA_ASPNA
ID VEA_ASPNA Reviewed; 555 AA.
AC G3YHA8;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 33.
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:25367340}; ORFNames=ASPNIDRAFT_55789;
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC 328 / USDA 3528.7;
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=25367340; DOI=10.1007/s10482-014-0316-z;
RA Wang F., Dijksterhuis J., Wyatt T., Woesten H.A., Bleichrodt R.J.;
RT "VeA of Aspergillus niger increases spore dispersing capacity by impacting
RT conidiophore architecture.";
RL Antonie Van Leeuwenhoek 107:187-199(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 (By similarity). The velvet complex hat
CC acts as a global regulator for secondary metabolite gene expression (By
CC similarity). Increases spore dispersing capacity by impacting
CC conidiophore architecture (PubMed:25367340).
CC {ECO:0000250|UniProtKB:C8VTV4, ECO:0000269|PubMed:25367340}.
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:25367340}. Cytoplasm
CC {ECO:0000269|PubMed:25367340}. Note=Enriched in the nucleus in the dark
CC (PubMed:25367340). {ECO:0000269|PubMed:25367340}.
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 nearly twofold the length and width of
CC the conidiophore stalk and vesicle (PubMed:25367340).
CC {ECO:0000269|PubMed:25367340}.
CC -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR EMBL; ACJE01000021; EHA18105.1; -; Genomic_DNA.
DR AlphaFoldDB; G3YHA8; -.
DR SMR; G3YHA8; -.
DR STRING; 380704.G3YHA8; -.
DR PRIDE; G3YHA8; -.
DR EnsemblFungi; EHA18105; EHA18105; ASPNIDRAFT_55789.
DR HOGENOM; CLU_022491_2_0_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..555
FT /note="Developmental and secondary metabolism regulator
FT veA"
FT /id="PRO_0000435774"
FT DOMAIN 25..228
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..479
FT /note="PEST"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT MOTIF 39..44
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT COMPBIAS 235..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 61318 MW; FA08FA877DB94102 CRC64;
MATRPPLSPP VNETEHSVSR ITREGKRITY KLNVMQQPER ARACGAGAKS SADRRPVDPP
PVVELRIFES DPNDDVHKTD ITFAYNANFF LFATLETARP MAQGRLAPTP TFPVLTGVPV
AGVAYLDRPS QAGYFIFPDL SVRHEGIYRL SFHLYEETKD SKDADESAPI RSPMMKGKPS
IPKSFLNFRL EVVSVPFTVF SAKKFPGLTT STSLSRIIAE QGCRVRIRRD VRMRRRGDKR
SDDYDFDEER SHRGRIPDRY STPDAYANPV ERPRSTSIGS VDPAFSYGPE ASRRPSATEY
GFSNPQAYPR AIPPAPAPAP PSSSTPTPVA PIAPSRSSSY TSHLSFGATR TQYPAPQLPG
TPQSATTPTQ VYSPHPTYTH ARNPSTSTEY EPMPSGYPPS RLPAERSTYS KPLPPIRVLH
HSDPTTYRAM ANPVPPRAQT PSNAAPSLPP IASISAEYSN NLPQPPSNLA PSPNREPRGF
LWDTRAAASS KRPHEDAFSH SERPLYNGMR PDNDSYPSAD RRPSDVHRAT LLSDRDEMAY
KRANGRMATK ISPAI