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Database: UniProt
Entry: A0A0D0ABF3_9AGAM
LinkDB: A0A0D0ABF3_9AGAM
Original site: A0A0D0ABF3_9AGAM 
ID   A0A0D0ABF3_9AGAM        Unreviewed;      1835 AA.
AC   A0A0D0ABF3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   28-JUN-2023, entry version 33.
DE   RecName: Full=Transcription initiation factor TFIID subunit 2 {ECO:0000256|ARBA:ARBA00017363};
GN   ORFNames=CY34DRAFT_799120 {ECO:0000313|EMBL:KIK47610.1};
OS   Suillus luteus UH-Slu-Lm8-n1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX   NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK47610.1, ECO:0000313|Proteomes:UP000054485};
RN   [1] {ECO:0000313|EMBL:KIK47610.1, ECO:0000313|Proteomes:UP000054485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK47610.1,
RC   ECO:0000313|Proteomes:UP000054485};
RG   DOE Joint Genome Institute;
RA   Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA   Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA   LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA   Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN835145; KIK47610.1; -; Genomic_DNA.
DR   STRING; 930992.A0A0D0ABF3; -.
DR   HOGENOM; CLU_002317_1_0_1; -.
DR   InParanoid; A0A0D0ABF3; -.
DR   OrthoDB; 1342632at2759; -.
DR   Proteomes; UP000054485; 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:UP000054485};
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          1608..1680
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          1718..1792
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          130..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1150..1236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1370..1391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1404..1594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1809..1835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1178..1192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1197..1224
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1374..1390
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1418..1438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1451..1476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1517..1531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1573..1589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1813..1827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1835 AA;  204672 MW;  A67911218DD3EC7B CRC64;
     MQREHNRRGF SISHQKVVLE IDFSGSLWGY TEITLIPTNP NLKTIHLHSR QCTIHSVSVA
     SHPADFVHHD PLAQINISNP QDCHTYPELK RKIYSALAEG DEGELSIAIP KEVSLRQTGH
     ANHSLLNGHF SEAATPEPHT PGPSSHTPAP SPEFMPVVIH IDFSLRSPVD GIQFVLPTDS
     YPYRVPHAYT TPSSPDAARC WVPCIDSLWE KCTWEFEFVV PRYLEEPDPG HRGENGDFEE
     SQESIPTVVV CSGDLVEQVA HPNNSNKTIF LFSQAVLTSV QHVAFAAGPF HVHPIPTELT
     SEDTSGISQP LMHAFCLPGH EAMLHSSISF LRSAMNFYST EFGSYPFGSY KVVAVDEMPV
     QRFDSSTLSI ITVDLLHGED SIEQVLETRQ ALSHALACQW MGINIQQKTW SDTWLVNGLA
     LYITGLFVRK LLGNNEYRYR LKRDMQRVVE WDNGSMPPIC QPQHNDPPDS MTLPFVNLKA
     PLVLHILDRR LGKSGTSLGL PRVLPKIFLS AMSGELPNNA LSTHSFLRTC RKVSGIDLRS
     FAEQWIYGSG CPAFGFSASF NRKKMAVEIT MRQDSPAYKA LEHNEVSKLL HKPVSFFEGQ
     MTVRIHEADG TPYEHVLDIR SPFKRFEVPF NTKYKRIRRN TKRYLARQAA AQAAAEGDAE
     AAEAMGLIDM GFGLEIWEKE KERENWKVAD WTEEDEQVMS GATYEWIRMD ADFEWIAAIA
     FEQPDFMWVS QLQRDRDVVA QLEAVNALAK QSTAIVSSTF TKTVLVSNYY YRIRCEAAMA
     LVHCAIRKLD FLGLFHLFKL FLRYCYDPED PNQDLFAHTY VPKPNDFSDL AEYFVRKSLV
     NAISQVRFEN GKTPSVVRQF LVDQLRYNDN TANPYSDAFY ICTMISAVAC ATVSIAPPER
     GELLREEVRS EHTSEDANLM KQAVDEVSRY RSMDRLIPSP KNVVTTAVLE FYLILTTANL
     IPNDLRVFFP LTREGNYTQV RLAAFDGLFM SKWYTPAIMR YVLAVMANDP SRVVRRHVAR
     GACQSLALLV SMGEMKNSIK DTESLLIEED GSLPEKSKEA KKSEVDMMIK VLRKDREIGK
     NEVLREFLMS IALAPDIDQE VRWGIIKLAD IVLRGVEETP PKVTIHLPPT PVTEIPPSLP
     VVKVLPKVSR PLKSGGPPAR APTVTSPAPK LKITPGGIQA RGSSSSATAP AIPTPPVCTG
     SMAPPPVPAK AKSKPKPKPM NGVRPPHIPK AQSAGMSLND LRASRNALKK LKIHKSALLF
     MQPVDPVRDH APNYYEVIKN PMDLSTMGAK VEAGMYKDRF AFEADFRLMI ANAKQYNPSG
     TYAHTEAIFL ETFFEKLWNR IQKTLEAASK NTEPAPENLP TIIVKKPGTA ASKPPVVSAP
     PPPPPQAESE APARPIIKLK VGGPQVKAPQ AEPSKKVVEP KALQKPKQPR KPKAVDEAPP
     PYVDDGSHDL LQEVIAIERE KDEEKRTRKT KDPVRESPPP ARASGSGPPG KRRKTSADDN
     GSEILMLAPS LSRKEKSGAP SLGSSTPAAE PSVTPVPAPK VSLGKPKKEK AVNPRDSESA
     PEPPRTSIKG KEREVASSST PTPSKPRKIQ ASAPLNEKKC REILKALLRV PESIIFAQPV
     DPERDGCPTY YEEIKHPMDF GTMTQRLNEG KYSTMEDFQK DVELVLSNCR KFNPPTTYPV
     NCADVVEKVF RKEWAKVIEK KLSWTEKRSL QTLMTQLVKE DVSWVFREPV DPVLLGIPTY
     FDVIPKRDAR DLRTIRQKLD TDKYDSSDAF EADINLMIQN AITFNGADSE VGFIAVAVRD
     RVKELFGGAK ASTGTKKRKD GEKGTPQPSK KVKLG
//
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