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}.
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; 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
//