VEA_AJECA
ID VEA_AJECA Reviewed; 591 AA.
AC B2CQJ9;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Developmental and secondary metabolism regulator VEA1 {ECO:0000305};
DE AltName: Full=Velvet complex subunit 1 {ECO:0000305};
GN Name=VEA1 {ECO:0000303|PubMed:18791067};
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26032 / G217B;
RX PubMed=18791067; DOI=10.1073/pnas.0806221105;
RA Webster R.H., Sil A.;
RT "Conserved factors Ryp2 and Ryp3 control cell morphology and infectious
RT spore formation in the fungal pathogen Histoplasma capsulatum.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:14573-14578(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22841690; DOI=10.1016/j.fgb.2012.07.001;
RA Laskowski-Peak M.C., Calvo A.M., Rohrssen J., Smulian A.G.;
RT "VEA1 is required for cleistothecial formation and virulence in Histoplasma
RT capsulatum.";
RL Fungal Genet. Biol. 49:838-846(2012).
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). Regulates cleistothecial formation and hyphal growth
CC (PubMed:22841690). Acts as a positive regulator of virulence
CC (PubMed:22841690). {ECO:0000250|UniProtKB:C8VTV4,
CC ECO:0000269|PubMed:22841690}.
CC -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC LAE1, VEA1 and VEL2; VEA1 acting as a bridging protein between LAE1 and
CC VEL2 (By similarity). {ECO:0000250|UniProtKB:C8VQG9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VTV4}. 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: Abolishes cleistothecial formation, switches to
CC mycelial phase faster, and shows impaired switching to the yeast phase
CC once in mycelial phase (PubMed:22841690). Attenuates virulence in mice
CC and macrophages (PubMed:22841690). {ECO:0000269|PubMed:22841690}.
CC -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR EMBL; EU543494; ACB59235.1; -; Genomic_DNA.
DR AlphaFoldDB; B2CQJ9; -.
DR SMR; B2CQJ9; -.
DR PHI-base; PHI:2588; -.
DR PHI-base; PHI:2609; -.
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..591
FT /note="Developmental and secondary metabolism regulator
FT VEA1"
FT /id="PRO_0000435773"
FT DOMAIN 26..235
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..493
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 241..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 65803 MW; 7388975ED4394F89 CRC64;
MATKASSILH PPNETEHTMS RITQEGKKLT YNLKVIQQPE RARACGAGAK SSADRRPVDP
PPVVELRVFE SDLNDQHKTD ITFSYNANFF LFATLEWARP IAHGRVQTQT PSCPVLTGVP
VAGIAYLDRP TQAGYFIFPD LSVRHEGLYR LNFNLYEEMK EPKHADKGGL VPHSQNHMAP
LTPSKPRSPH QFLHFRLVVK SVPFTVYSAK KFPGLAESTS LSRIVAEQGC RVRIRRDVRM
RRREPKPNKD YGAYDDRRIT PDPYPGTPVE RPRSASNASM DDPYRYPTGP PQVQPSPDYG
YHHPSHQQPS PNLAATPQSH LSFGAAPPQY HAPPPPPTAH PAPPPAYTSP HLGYTHTRQL
SAGPEYDPHR QKYTQYPPPS PHSDIYDQSK SSLPMNPSVD HPSYPPMPYE QRMSDPKLYA
PPSQLHPTQQ YQQPTPPPPP PAAIAPHPPH QRTPTKPSPS TFFPPTPSRL SVEVDSSNEA
DDAILNAIRT RRGYILDEKS GATKRSRDSS DHDLKPLRNG QRPVVSGDEA AKGEIGETSG
GSDDEIMTYR RADGRLVAKQ RVSVHSKGKE VNIPRDVDLL PRRPEVCAVA E
