ID A0A0C9N6H1_9FUNG Unreviewed; 2383 AA.
AC A0A0C9N6H1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 03-MAY-2023, entry version 38.
DE RecName: Full=Transcription initiation factor TFIID subunit 2 {ECO:0000256|ARBA:ARBA00017363};
GN ORFNames=MAM1_0327c09720 {ECO:0000313|EMBL:GAN10183.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN10183.1};
RN [1] {ECO:0000313|EMBL:GAN10183.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN10183.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-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}.
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; DF836616; GAN10183.1; -; Genomic_DNA.
DR STRING; 91626.A0A0C9N6H1; -.
DR OrthoDB; 1342632at2759; -.
DR Proteomes; UP000053815; 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; 6.
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; 6.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 6.
DR SUPFAM; SSF47370; Bromodomain; 6.
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; 6.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1308..1380
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1543..1615
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1769..1841
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1881..1951
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 2120..2192
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 2266..2338
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 112..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1974..2018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2057..2101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2213..2250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1660..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2071..2085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2383 AA; 266460 MW; 3B07846A65AB18B2 CRC64;
MKASCNEGLA ELTVQPLNNK LTNIRINCRQ CKIEKAFVND IPVEFEYNDA VSDLTLGANT
SISHHQVYKS RYMNALRDAD EGELIVKLPA NCINQVSESE AQSINKTTTF LNSQPEFKPQ
TPQQSTAADG STSTAAIATT APAQPEEVEP TYNTIVIRIE YTLEDPRNGV VYVQKDDEIA
PYRSNHVYTV NQPLPGATRS WLPCIDRISE RCTWDMEFIV PRKDDGAAVP EYDGEGSFDE
VNGIMVVCSG DIIEQVIHPT DNSKKIVHYN LSVPTPAPFI GFAIGPFEMI KLSPSQLQEE
VMTAADLDEN QQQSLMAEIN MMSNIYAFAL PGLEEELSVS CSFLMHAMHF YTQEYGSYPF
SDYKLVFVED TWADTASSAS LAICSSRLLH PVEIIDQIYS TRRELSQALA RQWFGIYIVQ
KSWPDTWLVR GLANLMGSLF IKRHLGNNEY RLRLKKDMEL CCMLDVNRPP VYNPALPYPL
DPEDLDFIEL KAPLVIYMLD KRMCKGGGTL GLSRVLPKIL VSAMSGELAQ NAISTHYFLR
LCRKVSGFDT KVFAEQWIYR SGCPKFSFSF LFNRKKMVVE IFMRQENTNT PLALSQEQSG
GGIDGSTANY QELMAPLFTG NLTVRIHEAD GTPYEHILDI QSTEHKFEVQ FNTKYKRIRR
NTKRFLAKQA AAAAAVAEEE QENEEGGDGT TVLGIIPSLG LGMPIFEDPT QKKDWKIIEW
GQDEEDTSGA ASAMFDWIRL DAEFEWLCVC EFKQPDYMWA AQLTKDRDVV AQHEAIDALK
HMPSLPTSTS LLRAVLDPKC FYKIRMEAAY GLASCAKANL NWVGLHQLNK MFQKRYCFPV
SSFAQQHMGQ DDLPITNSIP KPNNFSNLPD YFIQKATVVA FSQIRDERGL TPVRIRQFLL
DLLKYNDNIG NEFSDCYYVA TLVSSLGDSL IPASDKPNAI EMDDFEGEQV TAAAKAEIER
FRTLDYVIPT YHNIITVTCL RTMTKLMLKN LLPVNIPMFM QYTRYGNYLE VRLAAIDSLF
ILCGLSDHTL NQYLLDVVKE DPCVYVSHYV ARAMLAWLGL AMRESSDAPV VTNRFVEEFA
EEEGRVVIDD ERGPLEKTPQ QQFQASIESL RKRFENDTVL QENLWNLLNS SENTKLDHCI
RKYLLQFCEY VFKPIDVGLK VTIRVPTLPP THDMGEDTSE PSTPTSNPVI RFSKPKQKPE
EKASKSHKKA NSIVIKTEAL SQQVPEAATA ATTASSITTT ASPISVDSSE HMDVEHVEPT
LDFPPFQPME RTPSPPPPPP PPKVKHKKVD SATAEELKKC RRVINKLNKS SAALPFTVPV
DEELDGAPGY YQMITHPMDL GQIKSKVENK EYKLFSQFED DVRLMLSNCF KYNGPGTFVY
NAGMELEATF EKELSNLRGK ADEETQNMTI VESPVTTPRA VHSSLPPSSL STSVATAPAG
STAPAPSSIV IKPPKPAKTK SFSTVVSSAP PVQPQQTDYF SVSPSVSSPG PVQSPVERKK
SMTPVVDVYN ASPKTKTPSV EPKSNYDRMT EKEKMSAVLN KTMSSDHAYE FLRPVDPIKQ
GIPQYTKIIK HPMDLGTIKS RLVNHQYPNA LAMDSDMRLM FRNCYTFNPP KTYVYEKSKQ
LEEDYNKVWK AYFGSVRRGS TTTDKKPKEK HITPPVASPV VVSPNGSSIS SNTVPTIKIK
TSTSSSSSAA KPPKTPKPPK SHPAGHSDAV PLTPSYDAHS DHKASSPSIS SSSSSHPTTD
KPSKPKAVFN PAMTESNQKR CERIYKKLYS HQTCQPFYEP VDAVALNIPL YYTVIKRPMD
MSTIRKKLDQ GQYQTVWEFE LDVRQIFWNC NAFNDNESWV AKQCVALEAF FNQIWSAEFA
LPNALKGEEL KLAQKVINKL TLHDQAALFN VPVDLESLPD YAQKIKYPMD LRTIWEKLES
GKYTSLKAVD QDVRLVFKNC FTYNAPGTYA SDAGKKLEKY YHNISREMRH RIAAGSGGAP
TGSAVSASPK RPHSASPAPP KMTASASTLS TDAAPAPKKI KVVHTKPTVG ATHSPSPAIP
SQSDYMDVDV ASSAIAKSPS VVRSPSVTKP SPVPKSSPVP KPSKPSMSPS IAVRSPANDA
PVKLHPSLQA KMESLVHKLM NRKESYGFHT PVDPVAFNIP HYPRLIKHPM DFGTMLTNLQ
QGQYKTVKEF ESDMRLIFTN CYTFNGFDHV LSQNAKILEQ ILNKEGPNLR RKEEQLKNAA
SGSPSSSHHA HGHGHKSSSS SSDIPRSVSP TEAELRKYQS VLDKIQAHPS YYAFGAPVDA
ELLGIPTYHE IVRRPMDFGT IRHRYMSGGY DNANQLLRDV KLVFYNCYLF NLPDDVVTQM
GRDLQTEFNR LSRARGLRTI SVDDTAREAA EARPDIPPME TYN
//
