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Database: UniProt
Entry: V5GHZ1_KALBG
LinkDB: V5GHZ1_KALBG
Original site: V5GHZ1_KALBG 
ID   V5GHZ1_KALBG            Unreviewed;      1838 AA.
AC   V5GHZ1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Transcription initiation factor TFIID subunit 2 {ECO:0000256|ARBA:ARBA00017363};
GN   ORFNames=PSEUBRA_SCAF5g02419 {ECO:0000313|EMBL:EST05572.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST05572.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TAF2 family.
CC       {ECO:0000256|ARBA:ARBA00010937}.
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DR   EMBL; KI545891; EST05572.1; -; Genomic_DNA.
DR   RefSeq; XP_016290561.1; XM_016438704.1.
DR   STRING; 1365824.V5GHZ1; -.
DR   GeneID; 27421400; -.
DR   eggNOG; KOG1474; Eukaryota.
DR   eggNOG; KOG1932; Eukaryota.
DR   HOGENOM; CLU_002317_1_0_1; -.
DR   OMA; REFLMPI; -.
DR   OrthoDB; 1342632at2759; -.
DR   Proteomes; UP000019377; Unassembled WGS sequence.
DR   GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd04369; Bromodomain; 2.
DR   CDD; cd09839; M1_like_TAF2; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 3.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR037813; TAF2.
DR   PANTHER; PTHR15137; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR   PANTHER; PTHR15137:SF9; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 2; 1.
DR   Pfam; PF00439; Bromodomain; 3.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 3.
DR   SUPFAM; SSF47370; Bromodomain; 3.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 2.
DR   PROSITE; PS50014; BROMODOMAIN_2; 3.
PE   3: Inferred from homology;
KW   Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          1252..1324
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          1596..1668
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          1706..1780
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          123..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1181..1232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1349..1567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1801..1838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1183..1199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1434..1452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1546..1566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1821..1838
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1838 AA;  201395 MW;  7A8091E499357A8F CRC64;
     MSKQRGTAAY RGFTVSHQRV VLDLSFSGTV VGFTEITILP THRSLRTIHL NCRQASVQSA
     SINSHPAEFS YADHVTGATI TDTRDVHRYP ELKRRVYAAA SDGVNGELSI LIPPDVSVQS
     SRAGSRAVSM APDDAPTPGG SASTELTPIM VRVDYFIKDP TDGLQFMRPT ADSPYRVPHL
     FTIASSPDAA RCWVPCVDSL WERCTWEFEL IVPKSLSTAD EDEEAANGRA GTSALEQAAT
     TGVDTSDPDS EVVVVCTGDL MEQVTHPNNP SKTVFCYTQA VPTSVQHIAF AAGPFHIMRI
     EAGNHKGVQA PNGVVSDVTA GAPAVVDDSG QPEILAFCLP GREDELRTSV SFTRHALDFF
     SQQYGSYPFG AFRMVFVDEP PQDCTTQSMM AICSNDLLHP TSVIDQAIEN RQVLSHAIAF
     QWVGINIIQA TWADTWLVNG LSLYMNGLFL RRLMGNNEYR FRLKKDLDRL CAWDIGMPPL
     YEAGSFEPPD PATLPFVNLK APLVLHILDR RLRKMGASVG LGRVIPKVFL QAMTGEMTNN
     MLSTQHFLRT CRKVSGADLR LFTEHWIRGS GCPRFICSAN FNRKKLLIEM HIRQEVPAAQ
     FAAARPSDAL AANAVPLFEG QMTVRIHEAD GTPYEHVLEI KGPAKRYEVP FNTKYKRVRR
     NTKRFQARQA AAAAAAQGDQ EAQEAIGLID LGFGLGMWED EKAREEWKVA DWTEEDEEKM
     SSAPYEWIRM DADFEWLASI HFEQPDYMWV SQLQRDRDVV AQVSAVHALA QMPSLVTCSM
     LTRTVLVNKY FYRVRSEAVH ALVHCAIPQL DNLGLFHLLK LFRTSFCHDS PDEASIENPL
     DVPCIPRAND FSDAADYFLQ RALIHAISRV RNPDGRTPPQ VKRFLINLLR YNDNSTNHFV
     DDFYLAGAIN ALASAFIPVE SSLAGTQDTA AANEESFLLS HAIAEVERLQ ELDRLVPSYH
     NVITLASLDF QVAMMLANLK ARDLQLFFTY TRQGNFTPVR IAALNCLLLV GNLDHRIIAR
     YCFALLRLDE NRTVKRALAR ALCEGLAVGM STGVFGGGGL RGPEALLIEE DSGHVNAAEK
     ARDAQLEAML KTLKKEIGRS AGVREGFMSA LLAPNIDAEA RWALLKVAEL LFRPAEEKDL
     PLQHKVQLRV RMPSAQNTID AGALESPSIS KIKLIRQSTA AAGDETVPKT PSSAAATNGP
     RVAFETPEKP AAEAPDRKKI KPKKIKPLAP GQASGMSFAD LTACRNTLKK LMQNKFASIF
     LNPVDPVRDQ ATDYFDVIKE PMDLGSILNK LDSGQYKDRH ELRADFELML RNAKAYTPDE
     KAWAHKQAAG LEKVFHPLWN RMEKTLEQSA ARQKAAQDAV LANEQSAALP DSPERFSPSK
     PDASPAAGPA SASNGDVREA STPSSAVPKL SLKFKLKSKL GGEDSPAPVS TPTPKPKTFN
     LEPASTPSST LKLKKPLIKL KRGNDSEAAV PATPSPRPPS ATPDAPPQSV DDDILEALGE
     SVPKASKVKS KKPPTKAAAS PSPAPPTSVS PSSKKSKPAH SPVPVTPVSN GMTKSSSSSG
     TPSSDIAKWA ETDPVGATAN MPMNGKKCKV LLQILKKSPF SVFFRYPVDP IRDGLPTYLD
     EIKHPMDLST MEKKLNQASY TTMSSFAADV ELIFANCRQF NPPGTEPCQH ADELEKLWRK
     EWAKTVTPKL EANEKRALVG LINRLKTHQS SLLFREPVDP VALGIPTYFD VIPKKDARDL
     SLIEGKLKGD KYDSFASFDA DVKLMLKNCY TFNALDPGIM EIAKAFETYY KREFGHAKQQ
     AGISGGSAAG GGGATTPGKR KLSVTPANGG SSKKVKSG
//
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