ID   VELB_PENRW              Reviewed;         361 AA.
AC   B6HU70;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Velvet complex subunit B {ECO:0000305};
GN   Name=velB {ECO:0000303|PubMed:20543063}; ORFNames=PCH_Pc22g22320;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
RN   [2]
RP   INTERACTION WITH VELA, AND SUBCELLULAR LOCATION.
RX   PubMed=20543063; DOI=10.1128/ec.00077-10;
RA   Hoff B., Kamerewerd J., Sigl C., Mitterbauer R., Zadra I., Kuernsteiner H.,
RA   Kueck U.;
RT   "Two components of a velvet-like complex control hyphal morphogenesis,
RT   conidiophore development, and penicillin biosynthesis in Penicillium
RT   chrysogenum.";
RL   Eukaryot. Cell 9:1236-1250(2010).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH VOSA, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=23264641; DOI=10.1128/ec.00272-12;
RA   Kopke K., Hoff B., Bloemendal S., Katschorowski A., Kamerewerd J.,
RA   Kueck U.;
RT   "Members of the Penicillium chrysogenum velvet complex play functionally
RT   opposing roles in the regulation of penicillin biosynthesis and
RT   conidiation.";
RL   Eukaryot. Cell 12:299-310(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). Component of the velB-VosA heterodimeric complex that
CC       plays a dual role in activating genes associated with spore maturation
CC       and repressing certain development-associated genes (By similarity).
CC       The velB-VosA complex binds DNA through the DNA-binding domain of vosA
CC       that 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). Controls conidiophore formation
CC       (PubMed:23264641). {ECO:0000250|UniProtKB:C8VTS4,
CC       ECO:0000269|PubMed:23264641}.
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). Interacts with velA (PubMed:20543063). Forms a
CC       heterodimeric complex with vosA; the formation of the velB-vosA complex
CC       is light-dependent (By similarity). Interacts with velA
CC       (PubMed:20543063). Interacts with vosA (PubMed:23264641).
CC       {ECO:0000250|UniProtKB:C8VTS4, ECO:0000269|PubMed:20543063}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20543063,
CC       ECO:0000269|PubMed:23264641}. Cytoplasm {ECO:0000250|UniProtKB:C8VTS4}.
CC       Note=Nuclear localization is mediated by velA (By similarity).
CC       {ECO:0000250|UniProtKB:C8VTS4}.
CC   -!- DISRUPTION PHENOTYPE: Shows reduced conidiospore formation but does not
CC       affect penicillin production (PubMed:23264641).
CC       {ECO:0000269|PubMed:23264641}.
CC   -!- SIMILARITY: Belongs to the velvet family. VelB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AM920437; CAP99520.1; -; Genomic_DNA.
DR   RefSeq; XP_002566127.1; XM_002566081.1.
DR   AlphaFoldDB; B6HU70; -.
DR   SMR; B6HU70; -.
DR   STRING; 1108849.XP_002566127.1; -.
DR   EnsemblFungi; CAP99520; CAP99520; PCH_Pc22g22320.
DR   GeneID; 8308394; -.
DR   KEGG; pcs:Pc22g22320; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g22320; -.
DR   eggNOG; ENOG502S1B4; Eukaryota.
DR   HOGENOM; CLU_022491_0_0_1; -.
DR   OMA; KIGVWFI; -.
DR   OrthoDB; 1407766at2759; -.
DR   BioCyc; PCHR:PC22G22320-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
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; -; 2.
DR   InterPro; IPR021740; Velvet.
DR   InterPro; IPR037525; Velvet_dom.
DR   InterPro; IPR038491; Velvet_dom_sf.
DR   PANTHER; PTHR33572; PTHR33572; 2.
DR   Pfam; PF11754; Velvet; 1.
DR   PROSITE; PS51821; VELVET; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Reference proteome; Sporulation; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..361
FT                   /note="Velvet complex subunit B"
FT                   /id="PRO_0000435910"
FT   DOMAIN          47..353
FT                   /note="Velvet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   361 AA;  39437 MW;  49B6FA6E02737203 CRC64;
     MYAVEDRHHP VPPPLSMDRI SAPSVQYPSG TTSLRQSDHL APVSNYQDGR SWSLQVVQQP
     IRARMCGFGD KVGDFSAVIL LPLPNTSQDR RPITPPPCIR LIVRDAQTDK EIDIKCVQPA
     TLIPLSFLTV SSSSEIDTSF YVLTVDLWNA DGTSEVNLVK HSATSPSIST AMSSSYPPPP
     QSVSPTYPGY NQNQYPVGYP PQMNNYYGGQ QVAYQNQYGQ PVTYPQYYSG GQMPASMSPA
     AQPVTGGPGG MFTRNLIGSL SASAFRLTDP DNKIGVWFIL QDLSVRTEGT FRLKMSFVDV
     GTSTETSNGA PVIEPHQSWP RFSLNPSRSS PPKSSPVLLR APSSASALRY RVSRSPFART
     E