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Database: UniProt
Entry: A0A0A2I6S9_PENEN
LinkDB: A0A0A2I6S9_PENEN
Original site: A0A0A2I6S9_PENEN 
ID   A0A0A2I6S9_PENEN        Unreviewed;       389 AA.
AC   A0A0A2I6S9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Transcription initiation factor TFIID subunit 13 {ECO:0000256|ARBA:ARBA00040136};
GN   ORFNames=PEX2_075630 {ECO:0000313|EMBL:KGO59583.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO59583.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO59583.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO59583.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TAF13 family.
CC       {ECO:0000256|ARBA:ARBA00038392}.
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:KGO59583.1}.
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DR   EMBL; JQFZ01000094; KGO59583.1; -; Genomic_DNA.
DR   RefSeq; XP_016600753.1; XM_016744833.1.
DR   AlphaFoldDB; A0A0A2I6S9; -.
DR   STRING; 27334.A0A0A2I6S9; -.
DR   GeneID; 27680253; -.
DR   HOGENOM; CLU_706171_0_0_1; -.
DR   OrthoDB; 1326266at2759; -.
DR   PhylomeDB; A0A0A2I6S9; -.
DR   Proteomes; UP000030143; 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: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:SF5; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 13; 1.
DR   PANTHER; PTHR11380; TRANSCRIPTION INITIATION FACTOR TFIID/SUPT3-RELATED; 1.
DR   Pfam; PF02269; TFIID-18kDa; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT   REGION          83..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   389 AA;  42704 MW;  E924AF06E67A99F5 CRC64;
     MCMNSPFCAA VKSSPVTWAK KQNCDTYSAH HVRQTHGPNA QAGIVFPAGP EPVGITATFY
     ANSATCLAEL IHWIAYSEHI NPKSESSLPD SSRRHTDSKP SSTNSERILS DSKRSSPDSE
     HTNSNFKHRL TNYKSLLANP EKLFPTSKNL ISKLSPNWYF NEQDTTLIRA GYEPQWTPDP
     PDTTSTSTEK GRKAPATKVA NKPTMAEPRA RMARHKGQMN FQNELRLLLL AYGDPSPHPS
     FSNEPLPETV RVLDEIVTDF VLELSHGAAQ VAHHARRQKI KVEDFRFALR RDPNKLGRVQ
     ELLRMERELK EARKAFDQND DQVAKEAGKK GAAAAAAAAA AGEDPLAAEA AAAATVTKKS
     KGKGKRGAAT RRGSDATEES VSKKRKTIG
//
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