ID A0A090LEC5_STRRB Unreviewed; 950 AA.
AC A0A090LEC5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Transcription initiation factor TFIID subunit 3 {ECO:0000313|EMBL:CEF68126.1, ECO:0000313|WBParaSite:SRAE_2000278400.1};
GN ORFNames=SRAE_2000278400 {ECO:0000313|EMBL:CEF68126.1,
GN ECO:0000313|WBParaSite:SRAE_2000278400.1,
GN ECO:0000313|WormBase:SRAE_2000278400};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF68126.1};
RN [1] {ECO:0000313|EMBL:CEF68126.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000278400.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF68126.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000278400.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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DR EMBL; LN609529; CEF68126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090LEC5; -.
DR STRING; 34506.A0A090LEC5; -.
DR EnsemblMetazoa; SRAE_2000278400.1; SRAE_2000278400.1; WBGene00262998.
DR WBParaSite; SRAE_2000278400.1; SRAE_2000278400.1; WBGene00262998.
DR WormBase; SRAE_2000278400; SRP06470; WBGene00262998; -.
DR OrthoDB; 248379at2759; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd15522; PHD_TAF3; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46452; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 3; 1.
DR PANTHER; PTHR46452:SF1; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 3; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Initiation factor {ECO:0000313|EMBL:CEF68126.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein biosynthesis {ECO:0000313|EMBL:CEF68126.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 874..925
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 217..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 106687 MW; 97505E1888D8869F CRC64;
MVECPMDPLT QGPEECIRDE VTKTMAIILE DIGFSGVTVE ALTELIRLFE TYFCTLSKRT
ISFANLANRA EPSVNDVFHS LKTMHNKVSE ISDFVKQIDM PKRDLYHGLP FIVERNQVVS
REKPPKEDIV EDLDKVEEEN IAPSEDNEEN QKNIETNIVE KTTKSKFLTL FKGQKVTDLG
FEIVSTKKPK PPPEPIKVEN KDIEESVKIK FPKRDIPKVD TSRNSNNTCK SPKVSEMASS
SKPPLTNFPL LGNLNLNDLA NQTFLQQLMA NYSATAAMFG IGKIPPDAAT QLNLLAQCDM
ISKLVSHNFS FQKVQNNAQS IDQAIQRFVS GNINIQEQQP YNNHQQKGPQ TQQFSQFTQQ
KSKQSCKEDS IDMTIENVLK NVTASPTATF IPSQVKVPSK KVNKIKEDHS KSATDSSGLK
FDTPTSSISK IGGSNQNSVN KFNDSSFLNI SSTMPLAEST PKIGYNKEFN KQTPVLPKII
NKSVQLTETD KEREKREKRE RKEKKREKKR RKREERERLL QTLNSSEIDK KVGQTNMPNK
NLQPLTIDVK SSDNSDAASI SSLFTPVEKK LPIKLTFKRT NSSVTSPTVL TATPLTSQLA
DSKVNEDLKV KVKPINDTTN TSTIVGRQND EIKQVKSIEP DNLNVDKKKH KKEKGTLKVE
NNVSFPSTNP DMLKSKIKKK DKDKKKITEP PTIPTVIGSF NDNGSDYIRN LKEKMAKENK
IQASTSSSHC INKDKSKESS IVVDKESSPI KRPMTPISFS RPGSGPLDIE KEERGKSQVK
NILNNFGVSP TKNKDKKEKK KKSNDGLSFN IKKSNSFKQS SGGKMSNLFP LHKKSPSLNE
DSGKTMLLPL NETPPGPITL PSISGNGGDD EERLWICPKC HVAYNEDAEM VGCDTCECWY
HFHCVGLIVA PAEHESWFCE DCLKKEKNKD RKRKNSKDLN KTTKITVYNP
//
