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Database: UniProt
Entry: A0A150UZJ4_9PEZI
LinkDB: A0A150UZJ4_9PEZI
Original site: A0A150UZJ4_9PEZI 
ID   A0A150UZJ4_9PEZI        Unreviewed;       131 AA.
AC   A0A150UZJ4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Transcription initiation factor TFIID subunit 12 {ECO:0000256|ARBA:ARBA00017484};
GN   ORFNames=M433DRAFT_70905 {ECO:0000313|EMBL:KYG43780.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG43780.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG43780.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG43780.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TAF12 family.
CC       {ECO:0000256|ARBA:ARBA00007530}.
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:KYG43780.1}.
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DR   EMBL; JPDO01000283; KYG43780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150UZJ4; -.
DR   STRING; 766039.A0A150UZJ4; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR   GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR   GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR   CDD; cd07981; TAF12; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR037794; TAF12.
DR   InterPro; IPR003228; TFIID_TAF12_dom.
DR   PANTHER; PTHR12264; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 12; 1.
DR   PANTHER; PTHR12264:SF21; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 12; 1.
DR   Pfam; PF03847; TFIID_20kDa; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          18..87
FT                   /note="Transcription initiation factor TFIID subunit 12"
FT                   /evidence="ECO:0000259|Pfam:PF03847"
SQ   SEQUENCE   131 AA;  14493 MW;  D0EAC24473BD25E5 CRC64;
     MARPPPFTLE GEGDRVLSKR KLDELVRQVT GGAEDGFLTP ELEELVLQYV DDFVDDVITS
     ACRLAKNKPS QTLDVKDIQI VLERNYGIRI PGYSLDEART VKKFQPAPGW QSKMQAIQTA
     KTLGGVSKGD S
//
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