ID A0A0N4V3T3_ENTVE Unreviewed; 1370 AA.
AC A0A0N4V3T3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 1A {ECO:0008006|Google:ProtNLM};
GN ORFNames=EVEC_LOCUS4437 {ECO:0000313|EMBL:VDD89686.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000472901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000472901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD89686.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR EMBL; UXUI01007857; VDD89686.1; -; Genomic_DNA.
DR STRING; 51028.A0A0N4V3T3; -.
DR WBParaSite; EVEC_0000472901-mRNA-1; EVEC_0000472901-mRNA-1; EVEC_0000472901.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047171; BAZ1A.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR013136; WSTF_Acf1_Cbp146.
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; PTHR46510; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR PANTHER; PTHR46510:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS51136; WAC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000274131};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 1..86
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 389..456
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1111..1160
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1285..1355
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1174..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 322..353
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1181..1195
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1370 AA; 157176 MW; 51639C6A8C328CB7 CRC64;
MLSSMLWTCS ATRRTGLTYE EALESERTAM EALETIPDFF GAPVLYLVHA LSHRGRLDDL
VNDVYSFLKD RYFVGEKCTY TGERRKKTVR IMSVSFKGAD FTIFAGDLEA DSVRGEDETR
KIELLRIGAA EDYTYTVQII EEDGSEDDNG VREGVVYSQL SRPKSIASRA KLKLFLKNSC
DMMSRRQDVK EALVKDYGLD MLTWNEVFGG PVAQFPHTPM LQRGRSKGTL HVHTSEQERQ
CTSVKDLGLV SGDVISLDKK NRGRPRTFCG GEKRPAQELR GTPIIEKQQF ELQIMFQQAR
SAGMEDLSSW EQSEKLLSEE EIGDLKSAIR VAKEEKRRKE KEAKQRKREL YVEWKKPRDD
LLCDDLKVLT RILPLPKLKK LILPEWLNEK DFGDYLLIYQ FFQSYAELLP IQEVRGASDV
TFVDVITAVR SRDPSSACFV ELMHVLLLAK AERADEEDGD EGVLFVVDLS NKEELPVDAN
NDLENKVHGS RLRWVTRFHE RIRSTHGTLR NSIGFLPSAL FRSLSFLINH YSLGSLLELF
YFKGNIKVFI FCMSARHLPI DWMTMTEVLR LSLLSSGYFT GIGTHRFRLF SRGGIRCFED
EGYIFVMNNP RTMQKLAQGT VFDLLPEERL ALLQVLIHQL MSYHKFRSLS EERISAIAEL
RRDLKALRAW DASQEKKAKE ARLILEFVAE QVEENGEAIR SELTKRPNPS KSTNFLLSYL
TVSKDSVASR REEEAVKVVS KCFVKLFGLC YYGALHKTRI LLDGVAYEEL KNVEEIEAIR
GLQKEHYSAK ECSLLSKVYD LQCQMGYNQL GRDRAFRIYW VVDSLSLLLV EDQFAENENI
PSCETPTPLD KVDDGIYSKI STDEELRSML LSCTASDGCP VHCKRPRIRW SFVDTLETLE
SLIDACNLRG YRELELVENL KFLKSRLSNL VSRSAKKHCS GELCKGLMIS PNDPASVVST
FDWRQEFIEM LLDFEEKMEQ GGIGHLHLGG SSALRERWRE SLSKEFSTTE FLNGDIMVFD
EVVVTYDRLN DLSPVQHLAV AFLQIVQGVQ FKFLRMPFAT ADSKEKDAVN IPTTTFAQWQ
KSLLECNSIS SLALFYATLE PAILWNKSLL QAKCKVCRKR GVVDKLILCS RCDRCYHMDC
LRPRLSRIRE NWKCTDCVAI EKAKVAEEKR KRKSKQDEFE TYTEEDEDNQ STDSLLFDDD
VTSTEDQSSD CLELKRTQKG RIVKKVVYAE DSYSVGIRSN KKLCKGRMSN GNTGGNSRLS
MGLRESDHQN RNALRLMEHI IREAMKQESA WPFIDPVDAK EVPDYHQIIK RPMDLRTMMN
KIKQQLYNTP EEVVSDTRLM FENCRIYNKE GSIICGVSTI SYAVYSFFLG
//