ID A0A182P4V8_9DIPT Unreviewed; 825 AA.
AC A0A182P4V8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Transcription initiation factor TFIID subunit 13 {ECO:0008006|Google:ProtNLM};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI001945-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI001945-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI001945-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR AlphaFoldDB; A0A182P4V8; -.
DR STRING; 199890.A0A182P4V8; -.
DR EnsemblMetazoa; AEPI001945-RA; AEPI001945-PA; AEPI001945.
DR VEuPathDB; VectorBase:AEPI001945; -.
DR OrthoDB; 4270836at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd07978; TAF13; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045140; SHCBP1-like.
DR InterPro; IPR003195; TFIID_TAF13.
DR PANTHER; PTHR14695:SF4; PROTEIN NESSUN DORMA; 1.
DR PANTHER; PTHR14695; SHC SH2-DOMAIN BINDING PROTEIN 1-RELATED; 1.
DR Pfam; PF02269; TFIID-18kDa; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 4: Predicted;
FT REGION 603..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 93241 MW; 7B3FF75C76D52966 CRC64;
MEVYEFKKNF LTRLLETTSV LNGGGTNIPA SAIRSEWINL VEVAVEPTGW QALWKASRPV
CEQLGVKYPL VVLGTVDQVL FDELKASFLI EAIQDDDVQL PEEQITVDLE ELWPLREQNN
PALNVNITAE CIDKLRFFYQ HLWMPWDNDT EDEHGWIDKH LESRIRFCHD LKNKTMSRQL
SSHALALLAE ARYIQRKRTF IEQELSEAVG EEEEEEEDNE ASILKDDRSG ELLQLNLRLN
TIKNEINILE NPVMRNVFEK VRFGAIKDGK GSAALMAYIV TQAVPIDEQL TYLQRVKTLI
EPKLSVKMCD SLQHALDHCS PDSAIYLPPA TRQDIKFLEY LNSDGSFRGV SDVSFVEDFD
KASKMNPTIA SKNDDSVLLT IDGDFTLENI QLDCSNVRTG VVIKKGNIVF RNCCFTGDPN
SSTKQGIVIF GNCTITFDRC LIKEFSTGIY SNHDCTINLI NSTISHCMTG LETLDQCQIA
FRSTSVTHCT LYGVLLEDFN DDGAVDRTGS GAGGGSQVYE DYNTIERQEF TFEGGCEFRD
NAKGNFVIRK GFSERFNSSC FVDEDESQLH DMEDGLEESV CNTTNVSFCD DYLEASKLSS
TKHIVPPAMD KSDREEQSAS DTGVSGSLSQ SEDDLSATGY HENSTQIVRD VERSSVRDVK
KSEQSSESDD CDESEARKAT SSYSNTYLKP RNMAQNPPEE GFDQAEFEDD ELGEVQIETS
SGRKRLFSKE LRCMMYGFGD DQNPYTESVD LLEDLVVEFI TEMTHRAMEI GRTGRVQVED
IVFLVRKNSR KYARVKDLLT MNEELKRARK AFDEIKYAGA EAKIK
//