ID A0A2C9LKD2_BIOGL Unreviewed; 1386 AA.
AC A0A2C9LKD2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=Transcription initiation factor TFIID subunit 2 {ECO:0000256|ARBA:ARBA00017363};
GN Name=106056616 {ECO:0000313|EnsemblMetazoa:BGLB031942-PA};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB031942-PA, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB031942-PA}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB031942-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 RefSeq; XP_013068884.1; XM_013213430.1.
DR STRING; 6526.A0A2C9LKD2; -.
DR EnsemblMetazoa; BGLB031942-RA; BGLB031942-PA; BGLB031942.
DR KEGG; bgt:106056616; -.
DR VEuPathDB; VectorBase:BGLB031942; -.
DR OrthoDB; 11119at2759; -.
DR Proteomes; UP000076420; 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; cd09839; M1_like_TAF2; 1.
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; 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; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 273..502
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 1000..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1086
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1337
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 156865 MW; D72086D6289D97B3 CRC64;
MKKDSKYEIS RLFKVSHQIL CINSINFENR SLVGYVELTI WPTVPDLTEI RINSKQCIVY
RVSVDKKWDA EFSYFDPSLN ICQGNAVKRN IDYFHKCQMN AINAVDPDLG CGELIITFPK
EVLPTISALG SFQICVEFGL KEPQGGVHFV VPDMPGTMAE RSAHMFTYSL ENQSRLWFPC
MDTFSEPCTW KIEVTVDRDM TAISCGDLVG VEFTEDLLEK TYHYFLSTPV AAPNIALAVG
PFEILVDPKM HEVTHFCLPK LMPVLKHTTS YIHQAFEFYE ELMSSRYPYS YYKQVFVDEA
YCEVSTYSTM SILSTNLLHP TNIIDQTMAS RQLMATAVAQ QFFGSFIAME SWSDAWLTKG
ITGYLSYLFS KRTFGNNEYR NWVFRDLLEV SEYEQQMGNV VLDPTKHGSN HHFHIQSPHT
LSPRYIEMFC KKARLVMRML EIRIGTELLL QVLNKLLSLA YNASQQPFSF SSWSNMLLST
SSFLKIIYTV TGKDIEPFIE QWVYQGGCAR FIGSFVFNRK RNVVELEIKQ DLAPGAMKYV
GSLNVTIQEL DGSFNHQFKI EENKTKFEIT CHSKSRRNKK KKIPLMTGEE VDMDLTAMDA
DSPVLWLRLD PDMHLLRTVT FEQPDYMWQY QLRYEKCIVA QFEAIDALGK FPTPPSRLAL
TDTIENEECY YRVRQDACYC LAKWSDNYYR AALVEALSAS LTPAVTNVSL ITGQIVTAAA
LSPEMKLVVE EVVRSLNIEK LMPCYKFTVT VSCLYTIRTL QKLGHLPIES DVFKDYTQVG
IFRDVRVAAI TCLVDFIRGD VTGEHLNWIL DFIENEKDPY LKHHTVTCLT QNPPFRRSER
SALNIEPLVE RLWEMMCHTS HDSRLRCGLA DLYFILYGRQ RPTCLPVPEI VKMGQKDKKS
KMESLCLQIN ADDLSVSEPA PSSIAIWNPE LSNIFASPVH EPAMVENSAP ATVKVNLDLD
ITDDFTDRSS VDVTMHSEDQ SNVIEEAVVT ETVELESDLE SEVTPNLSRP SVQIDLSQGL
SRHDSISRLS EDSLSNSPPP VSKGHPDDVI VSLDNIIKHD PIIPGKLFQP PSPPPTYHPD
QPVRVELSPP PVTLEEVKSP LSPPPASPDS RSSPGYIIED ESAQEKQARI SGDVTQENME
DIKPVVEDLT TEMVEEKQLT VITEDQTDAK IELSPATPTQ LVVDFKKEIK EESQPSPPQS
SSPPQTPQPP PSAPTPQFSF ASVYQQIPPL PIKHSVSLDT ETPSSSLTLK RKLSVPSYQS
SPEPETKKIP PLIVSTSVSG GTTILSPNSA KPSLKTTLYL NTSAASTSES RDKSHHKSKK
KKKKNKHKHK HKHKHDRGDK HERGDKHDKH KPRERLLLDL SEIARASRDS PTVRPTTEQE
EESSSE
//