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}.
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; 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
//