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Database: UniProt
Entry: A0A420HBA2_9PEZI
LinkDB: A0A420HBA2_9PEZI
Original site: A0A420HBA2_9PEZI 
ID   A0A420HBA2_9PEZI        Unreviewed;       151 AA.
AC   A0A420HBA2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Transcription initiation factor TFIID subunit 13 {ECO:0000313|EMBL:RKF54712.1};
GN   ORFNames=OnM2_095033 {ECO:0000313|EMBL:RKF54712.1};
OS   Erysiphe neolycopersici.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF54712.1, ECO:0000313|Proteomes:UP000286134};
RN   [1] {ECO:0000313|EMBL:RKF54712.1, ECO:0000313|Proteomes:UP000286134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMSG2 {ECO:0000313|EMBL:RKF54712.1};
RX   PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA   Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA   Deng X., Wei C.I., Xiao S.;
RT   "Comparative genome analyses reveal sequence features reflecting distinct
RT   modes of host-adaptation between dicot and monocot powdery mildew.";
RL   BMC Genomics 19:705-705(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RKF54712.1}.
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DR   EMBL; MCFK01009555; RKF54712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420HBA2; -.
DR   STRING; 212602.A0A420HBA2; -.
DR   Proteomes; UP000286134; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd07978; TAF13; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR003195; TFIID_TAF13.
DR   PANTHER; PTHR11380; TRANSCRIPTION INITIATION FACTOR TFIID/SUPT3-RELATED; 1.
DR   PANTHER; PTHR11380:SF5; TRANSCRIPTION INITIATION PROTEIN SPT3 HOMOLOG; 1.
DR   Pfam; PF02269; TFIID-18kDa; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   4: Predicted;
KW   Initiation factor {ECO:0000313|EMBL:RKF54712.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:RKF54712.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286134}.
FT   REGION          126..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   151 AA;  17106 MW;  C74943C11F3D0933 CRC64;
     MEPRARIGKN RGQQNFSDLE LQQFLFGYGD DPQSLEPVKR ILDELLTDFI TELCFEAHRS
     AQVSGRQKIK LEDIKFACRK NPIYLGKIKE VQDKKAEIDA ARKLLDQNDD KISKSDVKAF
     DEIPLGEADD DIDGDIVTQT QHRGKSTGIG K
//
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