ID A0A2A9NX34_9AGAR Unreviewed; 1868 AA.
AC A0A2A9NX34;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 03-MAY-2023, entry version 18.
DE RecName: Full=Transcription initiation factor TFIID subunit 2 {ECO:0000256|ARBA:ARBA00017363};
GN ORFNames=AMATHDRAFT_140606 {ECO:0000313|EMBL:PFH52313.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH52313.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH52313.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH52313.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) 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; KZ301980; PFH52313.1; -; Genomic_DNA.
DR STRING; 703135.A0A2A9NX34; -.
DR OrthoDB; 1342632at2759; -.
DR Proteomes; UP000242287; Unassembled WGS sequence.
DR GO; GO:0005669; C:transcription factor TFIID complex; 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; 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 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:UP000242287};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1262..1334
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1642..1714
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1752..1826
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1184..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1844..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1384
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1845..1860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1868 AA; 209626 MW; 45F9BBFD320D682D CRC64;
MDTRINNLRE HVRRGFSIYR LHINNNFVYT SHQKVVLEID FAGSIWGYTE ITIVPSSSEL
RTIHLHSRQC TIHSVTVGGH TAEFVHSDPL NHISMGPPNE AQDCHRHPEL KRKLYSAYQE
CDEGELSIAI PKEISLKQSG HSSVGPVISE AATPEPQTPG FSHATHTLPE FSPIVVNIAY
SLRNPVDGLE FVLPTESYPY RVPHAYTNAS SPDSARCWVP CIDNVWERCT WEFEFVVPRY
LEERTSLEDD DESNSLSPTV VVCSGDLVEQ VAHPNNSNKT IFLFSQSILT SAQHVAFAAG
RFHMYSIPPD SSADDASGAA QPLMYAFCLP GYENILPTST SFLRSAMSFY STDFGSFPFG
SFKVVFVDQM ASQRFDSATL SIVTNDLLFG EDAIEQALET RHALGHALAC QWISINILPK
NWSDLWLING LALYITGLYM RKLLGNNDYR LRLKKDMMRV LEWDIGGMPP ICQPQVLEPP
DAAIIPFINL KAPLVLHILD RRLCKSGTSL GLSRVLPKVF LSAISGEMPN NALSTHAFLR
TCRKVSGVDP RSFAEQWIYG SGCPSFGFSA SFNRKKMAVE ITMRQEAPAF KAMENNEVSK
ALMKPVPFFE GQMTIRIHEA DGTPYEHVLD IRSPFKRYEV PFNTKYKRVR RNTKRYLARQ
AAAQAAAEGD SEAAEAIGMV DMGFGLEIWE KEQERENWKV ADWTEDDETV MSGATYEWIR
IDADFEWIAN MKFEQPDFMW VSQLQRDRDV VAQLEALYAL AEKPTAIVSS TLTKTVLVSN
YYFRIRSEAA LALVNCAIRR LDFLGLFHLF KLFLRYCYEP EDPNQDLFDH TYVPKPNDFS
DFAEYFVRKV TSLINAISRV RFENGKSPSV VRRFLIDQLR YNDNTINPYS DGFYISSIIS
SAACANVSTA PPERGELLPS EVRNEHSAED LELVKQTLGE VDRYRSMDRL IPSPHNAVTV
AALEFYMVLC IANLLPNHPR LFFPLTREGN YTQVRIAAFD GLFLTKWYVP QIMRYILAVM
ANDSSRVIRR HVAKNVCHSL ALLMHMGEMK SNLKETESLL IEEDGSVPEK AKESKRSEMD
MMIKVLRKDR EVGKNEVLRE FLMPIALAPD VDHEVRWCIL KLADLLIRPV DETPPTVKIH
IPVQEVPQLQ AVKLPTKPPR TIKSSGPPSK SPLVPFTPST KLKLPTSPAL DAGAKTPIVP
SPDVSRRTIT VPSVAVSLSK NPKLKGRPPL PESKPVHALK AQAGGMSLND LRACRNALKK
LKSNKHAFLF NQPVDPIRDH APNYFDIVKD PMDLSTMGAK LEEGMYKDRF TFQADFRLMI
SNAKLYNAPG TYVHNEAIAL ETFFEKQWTI INKTLEAADR AHPPPPTGVT PQRRVLPPVP
KPFAKPSQNH TFNPQSSRKR PPTGAPLATD PTPSTSRPTI KLKVNAQQGL ATGSQPSEDS
VATLKPRARK AKTSDAPFLD AVEAAALEPP PPYVDDGSHD ILQEVIAIER EKREQQHRSA
IEKEREKSLT NGSSGKRKKS DISIDEDDIL TLATPSKKER VSPTGPGGPK SRIVVPPASS
KLPPAPTQNK SKKGKQTELV SIASKPTMDV PQVSAKGKEK ENSSSSSTPA PAPQIIRNKK
SPVVQTTPIN EKKCRELLKV LQKIPDAGIF LRPVDPVLDG CPTYLDEIHF PMDFGTMSTK
LNEGKYNTME DFRKDIELVF SNCRKFNPPR TFPVTCADTV EKAFKKEWPK LIERKLSWTE
KRGLQGVMTN LVKDPISWVF REPVDPVILG IPTYFDVIPR KDARDLRTIR QKLDNDKYDT
VEAFDADIEL MIQNAIKFNG ADSEVGLIAT SLRQKFTELV GSWKTGSSKK RKEGEKSTSQ
PAKKIKTS
//
