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VOSA_AJECA
ID   VOSA_AJECA              Reviewed;         404 AA.
AC   B2CQK0;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Spore development regulator RYP2 {ECO:0000305};
GN   Name=RYP2 {ECO:0000303|PubMed:18791067};
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 RYP2-RYP3 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). Required for viable spore production
CC       and regulation of sporulation in response to temperature and for the
CC       switch to yeast-form in the presence of host cells (PubMed:18791067).
CC       {ECO:0000250|UniProtKB:Q5BBX1, ECO:0000269|PubMed:18791067}.
CC   -!- SUBUNIT: Forms a heterodimeric complex with RYP3; the formation of the
CC       RYP2-RYP3 complex is light-dependent (By similarity).
CC       {ECO:0000250|UniProtKB:Q5BBX1}.
CC   -!- INTERACTION:
CC       B2CQK0; B2CQK1: RYP3; NbExp=4; IntAct=EBI-16068756, EBI-16068767;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5BBX1}.
CC   -!- INDUCTION: Expression is increased at higher temperature (37 degrees
CC       Celsius) and regulated by the transcription factor RYP1
CC       (PubMed:18791067). {ECO:0000269|PubMed:18791067}.
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   -!- DISRUPTION PHENOTYPE: Leads to predominant production of large
CC       tuberculate spores with spores severe viability defects
CC       (PubMed:18791067). {ECO:0000269|PubMed:18791067}.
CC   -!- SIMILARITY: Belongs to the velvet family. VosA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; EU543495; ACB59236.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2CQK0; -.
DR   SMR; B2CQK0; -.
DR   DIP; DIP-60479N; -.
DR   IntAct; B2CQK0; 2.
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   Nucleus; Sporulation; Transcription; Transcription regulation.
FT   CHAIN           1..404
FT                   /note="Spore development regulator RYP2"
FT                   /id="PRO_0000435790"
FT   DOMAIN          17..194
FT                   /note="Velvet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01165"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  44157 MW;  B12A00F206096F84 CRC64;
     MSAPTFAEDP VTQRPALQSA DFRLTVRQNP ERARVAGGKE KERKAVDPPP IIQLKIDESK
     DPGQNYLQSP FYFMCCTLYN ATEDTPATTA QSTALAGTLV SSLHRLKDTD NMEGGFFVFG
     DLSVKIEGEF RLKFNLFEMR EVKRCGGSRD EVVYIKSILS KPFTVLPPKN FPGMTESTWL
     SRSFADQGVK LRIRKEARTL LKRPLNRAEP DYPAPPTQPR TPERSGASSQ QMVAAYQTNR
     DYPFYNGPDA KRPRSSVDMS GRGLYEGDAR YSYPPHAANP YQGQTYQQGM MQGYPTAGAG
     VSDYAIRQAQ QGSTPTPFGS ADESIGSIRS PGAGGYIGQP RYQSYSGAQM PYNLASSTQM
     SQMGESTPGR TGQAANMGGI VSGQSFSQSA GHMQSPSQVP PAWG
 
 
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