ID A0A423WCT3_9PEZI Unreviewed; 517 AA.
AC A0A423WCT3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Transcriptional adapter 2 {ECO:0000256|PIRNR:PIRNR025024};
GN ORFNames=VSDG_02866 {ECO:0000313|EMBL:ROW01073.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW01073.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW01073.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW01073.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is
CC involved in RNA polymerase II-dependent transcriptional regulation.
CC {ECO:0000256|PIRNR:PIRNR025024}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR025024}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROW01073.1}.
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DR EMBL; LJZO01000007; ROW01073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WCT3; -.
DR STRING; 252740.A0A423WCT3; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0035065; P:regulation of histone acetylation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02335; ZZ_ADA2; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR041983; ADA2-like_ZZ.
DR InterPro; IPR016827; Ada2/TADA2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR PANTHER; PTHR12374:SF20; TRANSCRIPTIONAL ADAPTER 2-ALPHA; 1.
DR PANTHER; PTHR12374; TRANSCRIPTIONAL ADAPTOR 2 ADA2 -RELATED; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
DR PROSITE; PS51293; SANT; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|PIRNR:PIRNR025024};
KW Reference proteome {ECO:0000313|Proteomes:UP000284375};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR025024};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR025024}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 66..119
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 71..115
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 126..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 58404 MW; 4AEBDAB0BA297520 CRC64;
MNPRRTIETD MGVPFLCSPQ VRIRCAHSAC NDYDLCVQCF SKGASSNNHQ PSTHSYRVIE
QNSFPIFDEG WGADEELLLL EGCEIYGIGS WADIADHIGG YRNKDEVRDH YEKVYIESSK
FPLPERCSPK DTSLANATTR EDFQARKKQR IEERKEAIKN APAPPPKTKP TASVPSCHEI
QGYMPGRLEF ETEHANEAEE AVQLMQFEPG DGINPNTGQL EPEMELKLTV MEIYNSRLTQ
RVERKKVVFE HNLLDYRENT KQDKKRSKEE RDILNKAKPF ARMMNHKDFE DFNQGLIDEL
NLRQAITQLQ DWRNMGIGDL RSGEQYEQAK VVRAQNRIPM GSMDRERLAA AQRNKQPVQP
EPQSGAALLV APELPIRTMA KNGSPNSDVA TNGDSKLANG NHANGSVFVA NGVDPAKKPT
HVPQPISGVT PLQLSRDMPD YHLLTPEEVR LCEVIRMQPK PYVMVKSEII REAVKGNGSL
KKKQVKEICS RNPSSWDSRK AGTVFECMVA WGYISKA
//
