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VEA_COCH5
ID   VEA_COCH5               Reviewed;         593 AA.
AC   M2SQ20; G4XKY8;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 28.
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:22383877}; ORFNames=COCHEDRAFT_1113718;
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C5 / ATCC 48332 / race O; TISSUE=Mycelium;
RX   PubMed=22383877; DOI=10.1371/journal.ppat.1002542;
RA   Wu D., Oide S., Zhang N., Choi M.Y., Turgeon B.G.;
RT   "ChLae1 and ChVel1 regulate T-toxin production, virulence, oxidative stress
RT   response, and development of the maize pathogen Cochliobolus
RT   heterostrophus.";
RL   PLoS Pathog. 8:E1002542-E1002542(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O;
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [3] {ECO:0000312|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000312|Proteomes:UP000016936};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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 acts
CC       as a global regulator for secondary metabolite gene expression (By
CC       similarity). Controls the expression of the T-toxin gene cluster
CC       (PubMed:22383877). Promotes oxidative stress tolerance and acts as a
CC       virulence factors during infection (PubMed:22383877). Negatively
CC       regulate mycelial pigmentation and controls sexual development, as well
CC       as asexual development during vegetative growth (PubMed:22383877).
CC       {ECO:0000250|UniProtKB:C8VTV4, ECO:0000269|PubMed:22383877}.
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). {ECO:0000250|UniProtKB:C8VTV4}.
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: Leads to hypersensitivity to oxidative stress,
CC       compromised reproductive development, repression of asexual
CC       sporulation, and reduction of virulence during maize infection
CC       (PubMed:22383877). {ECO:0000269|PubMed:22383877}.
CC   -!- SIMILARITY: Belongs to the velvet family. VeA subfamily. {ECO:0000305}.
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DR   EMBL; JF826791; AEP40317.1; -; Genomic_DNA.
DR   EMBL; KB445582; EMD87380.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2SQ20; -.
DR   SMR; M2SQ20; -.
DR   STRING; 701091.M2SQ20; -.
DR   EnsemblFungi; EMD87380; EMD87380; COCHEDRAFT_1113718.
DR   eggNOG; ENOG502S0HV; Eukaryota.
DR   HOGENOM; CLU_022491_2_0_1; -.
DR   OMA; NHFVTHR; -.
DR   PHI-base; PHI:2316; -.
DR   Proteomes; UP000016936; Unassembled WGS sequence.
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; Reference proteome; Sporulation; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..593
FT                   /note="Developmental and secondary metabolism regulator
FT                   VEL1"
FT                   /id="PRO_0000435776"
FT   DOMAIN          21..212
FT                   /note="Velvet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..487
FT                   /note="PEST"
FT                   /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT   MOTIF           35..40
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:C8VTV4"
FT   COMPBIAS        218..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  65813 MW;  0ADDE08CCFF68B45 CRC64;
     MSNIVVSNET KSQSVRTTKD GRQIRYNLQV IQQPERARAC GSGAKSSADR RPVDPPPIVE
     LRVFENDQEI TFAYNANFFL HASLENARTI APGRAPSTAG PSFPVLTGTP VAGMAYLDRP
     TPAGYFIFPD LSVRHEGKYR LSFALFENLA EVKDLDPEDP DVIYDGNHFV THRCEVKSAP
     FTVFSAKKFP GLSESTALSR MVAEQGCRVR IRRDVRMRRR ENKSSKEWDE YDEEGGGYDR
     ARGTATPDNY GQAPNAPLGD RPRSLSSASN PALAPPRRPS IEEMGHGYSA SNGYQQQMPP
     PQTPAYAQMP SYGSNQPQYS QQYQTPQPAP MMQPPQPPQH STPYSQHSQH SSYSSQHQAQ
     PPVPMNQQYG YSNYQQQPQQ PQSQSQPQYD HAAPPRQEQM SSDYAHPSDY RRSSITQSPA
     QQYTASSHPV QPYHPMDQYG RSQQMSQPLH SSPQSYASSA PSHQSLPSLR PIVADKLEPV
     SPSYQSPPTS MSAAISVNSD GSNQHYALPK FNPQTQGLPP MSATSNKRSF SSTFDSRHLN
     ERMVAGSRPQ PSGAGYSYDP GSPDMEEPMD RAAMSYRRAD GTQRQRHVPE VGS
 
 
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