ID   VELB_AJECA              Reviewed;         373 AA.
AC   B2CQK1;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Velvet complex subunit RYP3 {ECO:0000305};
GN   Name=RYP3;
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], INDUCTION, FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
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).
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 RYP2-RYP3 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 complex binds DNA through the DNA-binding domain of RYP2 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). Required for viable spore production
CC       and regulation of sporulation in response to temperature, as well as
CC       for the switch to yeast-form in the presence of host cells
CC       (PubMed:18791067). {ECO:0000250|UniProtKB:C8VTS4,
CC       ECO:0000269|PubMed:18791067}.
CC   -!- SUBUNIT: Component of the heterotrimeric velvet complex composed of
CC       LAE1, VEL1 and VEL2; VEL1A acting as a bridging protein between LAE1
CC       and VEL2 (By similarity). Forms a heterodimeric complex with VOS1; the
CC       formation of the VEL2-VOS1 complex is light-dependent (By similarity).
CC       {ECO:0000250|UniProtKB:C8VTS4}.
CC   -!- INTERACTION:
CC       B2CQK1; B2CQK0: RYP2; NbExp=4; IntAct=EBI-16068767, EBI-16068756;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VTS4}. Cytoplasm
CC       {ECO:0000250|UniProtKB:C8VTS4}. Note=Nuclear localization is mediated
CC       by VEL1 (By similarity). {ECO:0000250|UniProtKB:C8VTS4}.
CC   -!- INDUCTION: Expression is increased at higher temperature (37 degrees
CC       Celsius) (PubMed:18791067). {ECO:0000269|PubMed:18791067}.
CC   -!- DISRUPTION PHENOTYPE: Leads to predominant production of large
CC       tuberculate spores with severe viability defects (PubMed:18791067).
CC       {ECO:0000269|PubMed:18791067}.
CC   -!- SIMILARITY: Belongs to the velvet family. VelB subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU543496; ACB59237.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2CQK1; -.
DR   SMR; B2CQK1; -.
DR   DIP; DIP-60480N; -.
DR   IntAct; B2CQK1; 2.
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; 1.
DR   Pfam; PF11754; Velvet; 1.
DR   PROSITE; PS51821; VELVET; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Sporulation; Transcription; Transcription regulation.
FT   CHAIN           1..373
FT                   /note="Velvet complex subunit RYP3"
FT                   /id="PRO_0000435786"
FT   DOMAIN          48..344
FT                   /note="Velvet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   373 AA;  40230 MW;  73A667F217B00430 CRC64;
     MYTLKQDRPH PVPPPPPLTM DHLQHGYSTN TPVTLPGIPE AARSVSTVYE GRIYSLDVVQ
     QPIRARMCGF GDKDRRPLTP PPCIRLIVRD ATTQKEIDIN EIDTSFYVLT VDLWNAEGTS
     EVNLVRHSAT SPSISTATSS AYPPPANIMP FPQYAQTHGY PQTAYPPYYG GQPGYNPHAG
     YQYPQGGPDP YYPGLPAAST YYPPGTPTQA LGPQSALGPH ISSASTGMFT RNLIGSLSAS
     AFRLTDPDDK IGVWFVLQDL SVRTEGSFRL KMNFVNVGTQ SQAQDQSPGG TPSSPVINVG
     SAPVLASAFS EVFQVYSAKK FPGVIESTPL SKCFAFQGIK IPIRKDGVKG PRGGQSHGSK
     GQDGEGEDWE NEG