VOSA_MAGO7
ID VOSA_MAGO7 Reviewed; 501 AA.
AC G4NB64;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Spore development regulator VOSA {ECO:0000305};
GN Name=VOSA {ECO:0000303|PubMed:24632440}; ORFNames=MGG_00617;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION.
RX PubMed=24632440; DOI=10.1016/j.fgb.2014.02.011;
RA Kim H.J., Han J.H., Kim K.S., Lee Y.H.;
RT "Comparative functional analysis of the velvet gene family reveals unique
RT roles in fungal development and pathogenicity in Magnaporthe oryzae.";
RL Fungal Genet. Biol. 66:33-43(2014).
CC -!- FUNCTION: Component of the VELB-VOSA heterodimeric complex that plays a
CC dual role in activating genes associated with spore maturation and
CC repressing certain development-associated genes (By similarity). The
CC complex binds DNA through the DNA-binding domain of VOSA that
CC recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3'
CC consisting of two motifs in the promoters of key developmental
CC regulatory genes (By similarity). Appears dispensable for the
CC development and pathogenicity (PubMed:24632440).
CC {ECO:0000250|UniProtKB:Q5BBX1, ECO:0000269|PubMed:24632440}.
CC -!- SUBUNIT: Forms a heterodimeric complex with VELB; the formation of the
CC VELB-VOSA complex is light-dependent (By similarity).
CC {ECO:0000250|UniProtKB:Q5BBX1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5BBX1}.
CC -!- DOMAIN: The N-terminal velvet domain contains a NF-kappa-B-like fold
CC and is involved in DNA-binding (By similarity).
CC {ECO:0000250|UniProtKB:Q5BBX1}.
CC -!- SIMILARITY: Belongs to the velvet family. VosA subfamily.
CC {ECO:0000305}.
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DR EMBL; CM001235; EHA48826.1; -; Genomic_DNA.
DR RefSeq; XP_003718410.1; XM_003718362.1.
DR AlphaFoldDB; G4NB64; -.
DR SMR; G4NB64; -.
DR STRING; 318829.MGG_00617T0; -.
DR EnsemblFungi; MGG_00617T0; MGG_00617T0; MGG_00617.
DR GeneID; 2674880; -.
DR KEGG; mgr:MGG_00617; -.
DR VEuPathDB; FungiDB:MGG_00617; -.
DR eggNOG; ENOG502RYQD; Eukaryota.
DR HOGENOM; CLU_544081_0_0_1; -.
DR InParanoid; G4NB64; -.
DR OMA; HRINTQV; -.
DR OrthoDB; 1407766at2759; -.
DR PHI-base; PHI:4110; -.
DR Proteomes; UP000009058; Chromosome 5.
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 Nucleus; Reference proteome; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..501
FT /note="Spore development regulator VOSA"
FT /id="PRO_0000435916"
FT DOMAIN 52..223
FT /note="Velvet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT REGION 26..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 364..371
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:M2TGT8"
FT COMPBIAS 26..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 54285 MW; 551465FA0F71C2E8 CRC64;
MSLPSIGSVG SDRMAAYMHG QQVYTGQFGD PNLTPPQAET QMSAQASAQA VGQEPEPDYK
LVIRQEPQRA RVAQGKEKGT DRKPIDPPPI VQLIRTARSD PAQIYLQSPY YFMACTLIKG
SDDDPDPNPN SMLGTLVSSL HKLRDLNNED GGFFIFGDLS IKIEGVFRLQ FTLFQMKDST
CVFLDSATSQ PFTVYPQKNF EGMAESTFLT RSFSDQGVRL RVRKDSRAMT TRKRNHQHAE
VAKKHSEWDR KQTSAVSRHS SINENDSTPT DTRGLASFAG AGSSGYYDQH RSHYGETYGH
DTYYGGARSV KRARHEVSPG QYALPDLPQQ AYATRQPSFS DSVASMTMPP VTTAAPSLAG
INPMSSHHGY TGSAHPGFAP HRINTQVGGS HLAPQPHSAI GSVNQGYQSP STHHQPHPHT
AHPAGGQAYP SPSPRQSPGT APNYHYGSHH SQQTPVSLGL ETYTSAGVVG MPGPGQLVGT
SAPSPHLGQG YRHGMINEPG A