ID M7X5L9_RHOT1 Unreviewed; 1837 AA.
AC M7X5L9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Transcription initiation factor TFIID subunit 2 {ECO:0000256|ARBA:ARBA00017363};
GN ORFNames=RHTO_00059 {ECO:0000313|EMBL:EMS25631.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS25631.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS25631.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS25631.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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; KB722642; EMS25631.1; -; Genomic_DNA.
DR RefSeq; XP_016276750.1; XM_016413743.1.
DR GeneID; 27364072; -.
DR eggNOG; KOG1474; Eukaryota.
DR eggNOG; KOG1932; Eukaryota.
DR HOGENOM; CLU_002317_1_0_1; -.
DR OrthoDB; 1342632at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 3.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Initiation factor {ECO:0000313|EMBL:EMS25631.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein biosynthesis {ECO:0000313|EMBL:EMS25631.1};
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 1614..1685
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1721..1795
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 213..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1816..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..250
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1419
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1479
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1837 AA; 203430 MW; E9BC1F3D597CA624 CRC64;
MGKGFAITNQ KVSISIGLQG RIHGYTELTI VPTAADLRTV WLHARSLSIL SCSLRLPTVV
PLAFSHLPPS MPALTQPENI HTYPEMKRQI WRAENEGEEG ELGIAIPQGC IVRTSIGMGR
TPSTAPTPAK DGLLPRTDEF EPFTVAVEYE VTKPGIGLVV VGPDEANPSR FPHVFTSSIS
DIGARTWVPC SDSPRERCSW DLELVVPRVL ASAPPDKRKR DGPVPAEDGA NGTTAEEDEE
DEDEEDEEVD AEYPISVIAS GELVEQVVHP DRSDRVIWHF VQVSPVSVQQ VGWAVGPFVV
TEVRGTKKRA DGESREDDED EDGAAVQDDG PAIHALCLPG RESEMEYSVG VIRQAMEFYT
ATFGSYPFVT YAVAFVDSLA SASPTFHSAG LTILSSDILH PPSVIDQAYE TRHLLAHALA
VQWSGVNLIP RTPSDSWLII GIALHMTSHF VRHLWGNNEF RFRLKKDINR CVEQDIQFEP
ICVPARLTLP EPNQMQFIAL KAPLVLHILD KHLRKSGTSL GLDKVFPKIF LDAISGELTS
QANSLSTTSF MRTCRKLCGG SSEALKIFFD QWVYGSGCPT FEVTANFNRK KMAVELNVTQ
RCYAYAWSQK APCEAQGHLR PIPLFDGQMT IRIHEADGTP YEHVLTIQDS FKRHEVPFNT
KYKRVRRNTK RYQARQAAAT AAALGDIEAQ EDMGLIDLGF SLGMWEDEKE RERWRVADWT
EEDDLVMSQA TYEWIRIDAD IEWICIVKFT QPDFMWISQL QRDRDVVAQL EAIHALSSIP
SPIVSSNMCK TVLVSNYFFR IRMEAALALI SCATLEQQYL GLFHLFKTFQ TWYCFEPDVE
TKDPFGFRCI PKTNDFSDFT LYFMKKALVT AISMIRDERG QTPPVIQQFL VDLLAYNDNL
GNKYSDAFYI TSVMNALSHT LVNVVPRDLN GDTDQIAEVD SNENLAPAVQ EVERYLASDR
LVPSYHNAVT IAGIEFKLKL TLASLIPEDR MFFFNYTRDG NYPPLRIAAF DALLLLNPLQ
DVMALVRYLF AVMRDDSSRL VQRRLAESVL ESLPVLVAIH DLAAPDPNAD PAGDAKKERD
ELANVLKMLR KKPGRSMNYR TSLLQTLTSP DVDPEVRLCC LKICEATVRP EGEPIPKMRF
RLPPTPAPAP VPEAPPTPVQ TFPKLKLGGP ATPKVAIPPR IDEYTPVGAF DEFAQPYQPY
QEPIPPPPPP VIKPPKKPKD KVVKPPKPQA SQASGMPLAD VTACKSLLKK LLKDKKSFIF
RAPVDPVKAG ALDYFDKIKN PMDIGTMSAK LSAGVYPDRY AFRDDFKLII SNAKLYNGAF
SPIGELANDL DMMFDKHWER VEATLSRLEG GQPSYAAAPE LARLPKIPKH AIPPPPPPPL
DGYYGSPAPA PHAPTPIISL KLKAPAPPPP PPPLPAAADA SAPAPAATPA QSPPPPAQPQ
AQATPAPILA SPALPPLPSG PPSASPAGTP APPPVPKPTF KIKLGGASIK DATPKPPKAA
SFSPEVSYSP ASTTYPDSYD PALAGIGPPK QKKQRDVKLE KKKAKGPINY AEPPDLDFDD
ADSTVPVNPT PVAFAVPQRP EVLDTPRPPY PTKWVDPEGP VDIAKARNVL SKIRSLREAF
FFQYPVEPVG PLATYYDEIE QPMDLDTMSK KLDAGAYPNY SALFSDFDLI VANCEKFNTP
NTEPIWHVLL LDRAWRTEWE KANKLSYNTK RSLGAFLKKL MEDGSALPFN VPIADLAVQV
PNYHDYIPKE DGRDLQDLKR KLETDQYNSI EALEADFDLM VRNCYRFNGM ESQVSFSARE
LDGKFKAGIK RIKTDSLKQN KRAGSSGVGG VSKKQRI
//
