VEA_GIBF5
ID VEA_GIBF5 Reviewed; 530 AA.
AC S0DHV6; E0WDF7;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 25-MAY-2022, entry version 25.
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:20572938}; ORFNames=FFUJ_01649;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH LAEA, AND DISRUPTION PHENOTYPE.
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=20572938; DOI=10.1111/j.1365-2958.2010.07263.x;
RA Wiemann P., Brown D.W., Kleigrewe K., Bok J.W., Keller N.P., Humpf H.U.,
RA Tudzynski B.;
RT "FfVel1 and FfLae1, components of a velvet-like complex in Fusarium
RT fujikuroi, affect differentiation, secondary metabolism and virulence.";
RL Mol. Microbiol. 77:972-994(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24389666; DOI=10.1007/s00253-013-5453-1;
RA Niehaus E.M., von Bargen K.W., Espino J.J., Pfannmueller A., Humpf H.U.,
RA Tudzynski B.;
RT "Characterization of the fusaric acid gene cluster in Fusarium fujikuroi.";
RL Appl. Microbiol. Biotechnol. 98:1749-1762(2014).
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:20572938). The velvet complex
CC hat acts as a global regulator for secondary metabolite gene expression
CC (PubMed:20572938). Controls positively the expression of the
CC gibberellins, fumonisins and fusarin C gene clusters (PubMed:20572938).
CC Controls the expression of the fusaric acid gene cluster
CC (PubMed:24389666). Controls negatively the expression of the bikaverin
CC gene cluster (PubMed:20572938). Regulates the expression of laeA
CC (PubMed:20572938). Plays a crucial role in virulence (PubMed:20572938).
CC {ECO:0000250|UniProtKB:C8VTV4, ECO:0000269|PubMed:20572938,
CC ECO:0000269|PubMed:24389666}.
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 (By similarity). Interacts with LAE1 (PubMed:20572938).
CC {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:20572938}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20572938}. Cytoplasm
CC {ECO:0000250|UniProtKB:C8VTV4}. Note=Enriched in the nucleus in the
CC dark (By similarity). {ECO:0000250|UniProtKB:C8VTV4}.
CC -!- INDUCTION: Expression is repressed in media containing high amounts of
CC nitrogen (PubMed:20572938). {ECO:0000269|PubMed:20572938}.
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: Impairs the production of gibberellins,
CC fumonisins and fusarin C (PubMed:20572938). Reduces both the fusaric
CC acid gene cluster expression and production of fusaric acid
CC (PubMed:24389666). Affects conidiation associated with stunted aerial
CC hyphae (PubMed:20572938). {ECO:0000269|PubMed:20572938,
CC ECO:0000269|PubMed:24389666}.
CC -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR EMBL; FN548142; CBE54373.1; -; Genomic_DNA.
DR EMBL; HF679023; CCT61859.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DHV6; -.
DR SMR; S0DHV6; -.
DR EnsemblFungi; CCT61859; CCT61859; FFUJ_01649.
DR VEuPathDB; FungiDB:FFUJ_01649; -.
DR Proteomes; UP000016800; Chromosome 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 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..530
FT /note="Developmental and secondary metabolism regulator
FT VEL1"
FT /id="PRO_0000435767"
FT DOMAIN 26..220
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 206..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..460
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 215..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 58837 MW; E70157D51B038E8D CRC64;
MATPSSIPAE PKRDVVNRIH RVTRGNRSLW YQMTVLQQPE RARACGSGSK ANSDRRPVDP
PPVVELRIIE GPSVEEGKDI TFDYNANFFL YASLEHARPL ARGRVNTPAA GNPPILTGVP
ASGMAYLDRP TEAGYFIFPD LSVRHEGLYI LTFSLFETTK EERDFDLEPA DGDLPPGVDY
RMEIKTDPFS VYSAKKFPGL MESTQLSKTV ADQGCQVRIR RDVRMRKRES KPGAGNSNSG
GNGFERREED FGRRRTITPA SEDPHSIRNR SHSNSSEQRT PYTDASRRPS MVDSYPPPPP
PPSYEPAPSA SRHLDFGDSS AAQYPTPRQY AHQPGLQITP GPPSGSYAPT AQSPYSKTDA
PYGYVNRNIP PSCPSPAPSV KHDLYDRRQS TSSYVPPSPS VYSTEGHHRR DSRPSYPPTP
VAAPRPRPMH SQTSLPALKI DQLVSPVSPL PPIEPQTGPA PELPPINVGG KRKHESVFAQ
STRPLHNGQR QVDPHYGRSH RGYSPDHDQG WYSRADGQIS SVQFNRYYDE
