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Database: UniProt
Entry: A0A179FMK8_METCM
LinkDB: A0A179FMK8_METCM
Original site: A0A179FMK8_METCM 
ID   A0A179FMK8_METCM        Unreviewed;       684 AA.
AC   A0A179FMK8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Transcription initiation factor TFIID subunit 12 {ECO:0000256|ARBA:ARBA00017484};
GN   ORFNames=VFPPC_07960 {ECO:0000313|EMBL:OAQ66401.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ66401.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ66401.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ66401.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(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:OAQ66401.1}.
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DR   EMBL; LSBJ02000004; OAQ66401.1; -; Genomic_DNA.
DR   RefSeq; XP_018143488.1; XM_018286743.1.
DR   AlphaFoldDB; A0A179FMK8; -.
DR   STRING; 1380566.A0A179FMK8; -.
DR   GeneID; 28850737; -.
DR   KEGG; pchm:VFPPC_07960; -.
DR   OrthoDB; 22237at2759; -.
DR   Proteomes; UP000078397; Chromosome 4.
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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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   Initiation factor {ECO:0000313|EMBL:OAQ66401.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein biosynthesis {ECO:0000313|EMBL:OAQ66401.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          569..643
FT                   /note="Transcription initiation factor TFIID subunit 12"
FT                   /evidence="ECO:0000259|Pfam:PF03847"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  71751 MW;  67945CC365A1DE0A CRC64;
     MNPAQGQVPQ QGQAQGQPGA AGQQQRITPM YQPSQIRSLP MLSEDEKNKY EQGLRGLWNK
     ANNSPANSPD QIAAKQKIIE FSKMLIGKIQ QRRSQAQQQQ AQQGQQGGQV PARPPSAQQN
     PTGQAAGAPS AAQAQQKPQP VPAAGQGSQG QAPSAAASGA AQGQNAQGAT AGAAAAAAQR
     PKIPDQIMQH VNKIVFRAPA QLANKPPAEV AKWIEDLKDK YSRALFTMDS SKAKVAGMEK
     IFKDRNDAGK PLQNEELRQY QIRREQQLKL YQDAHKWVES VRKQQEGLQA NQQQAGAQAG
     QNGTAAAPPA NQQTNTQATP NAAQNNAQAA TQNVAASMNA AVEAAKNQQN LAAASRPSPA
     NGTSTPIPTA AQNQPRPVPQ AAQQPQGQPQ VKTEQPHPPP VNTAQAQAVA QAQATARVPT
     PQSATPVTAG GPTRALSHSA AMTLANQRAA NTPGTAQGQS QPAAGTGVGG AVNQGAVVPG
     AVQQQQQQGH PHAHPTQTQT GFQAKMPIPK QLPEKATAVP QGVTVGGGVT AGRPTMSQGS
     GTLGGVMNQP PVARIPAYSH DAEGDHVLSK KKLDELVRQV CSGSGDTQDG NLLTPEVEES
     VLNMADSFVD NVLHSACRNA KERGSKVLEI RDIQLVLERT YNIRVPGYSS DELRTVRKVQ
     PSPGWIAKMS AVQAAKVMPG KGDP
//
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