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Database: UniProt
Entry: A0A182RHJ3_ANOFN
LinkDB: A0A182RHJ3_ANOFN
Original site: A0A182RHJ3_ANOFN 
ID   A0A182RHJ3_ANOFN        Unreviewed;      1673 AA.
AC   A0A182RHJ3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 2.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Bromodomain adjacent to zinc finger domain protein 1A {ECO:0008006|Google:ProtNLM};
OS   Anopheles funestus (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN005705-PA, ECO:0000313|Proteomes:UP000075900};
RN   [1] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA   Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA   Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA   Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT   "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT   Middle East: occurrence data, distribution maps and bionomic precis.";
RL   Parasit. Vectors 3:117-117(2010).
RN   [2] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA   Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA   Besansky N.J.;
RT   "A chromosome-scale assembly of the major African malaria vector Anopheles
RT   funestus.";
RL   Gigascience 8:0-0(2019).
RN   [3] {ECO:0000313|EnsemblMetazoa:AFUN005705-PA}
RP   IDENTIFICATION.
RC   STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN005705-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR   STRING; 62324.A0A182RHJ3; -.
DR   EnsemblMetazoa; AFUN005705-RA; AFUN005705-PA; AFUN005705.
DR   VEuPathDB; VectorBase:AFUN005705; -.
DR   VEuPathDB; VectorBase:AFUN2_011354; -.
DR   OrthoDB; 1382023at2759; -.
DR   Proteomes; UP000075900; 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   CDD; cd05504; Bromo_Acf1_like; 1.
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; IPR037325; Acf1_Bromo.
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; 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; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00475}; 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          22..130
FT                   /note="WAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51136"
FT   DOMAIN          396..461
FT                   /note="DDT"
FT                   /evidence="ECO:0000259|PROSITE:PS50827"
FT   DOMAIN          1188..1238
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1553..1623
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          233..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          810..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1007..1081
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1258..1515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1648..1673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          322..379
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        235..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..825
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1038
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1063
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1258..1309
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1310..1324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1339
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1363..1381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1451..1466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1673 AA;  190091 MW;  F473A19F8EB42631 CRC64;
     MPLLRRQVLQ KTSTAERLRD SEEVLFCQPT GEIFSNYEDY FHRIMLISSM VWSCAMTGRP
     NLTYSEALES EKAARKLLKT FPDAVKGPFL LVASHTQRTS INEMHEDVYG FVKDHLFKGE
     IVDAMDLTRK AFRRAVISDV LVDNTQGAGP VMYQVTADDN MTSRVWNVTP GNLKRDRSTL
     TRDKCKLFLK QHVEAGPGGQ LRIKADSLVK FVTEQGWTDE QVFLGQAPNF EQSKRLKQNA
     ERSEVSGASK PTKKKAPVEK TTKITTVDGD KQQQQEEKPK KAKKQATKNV EKKGPAKVKQ
     KSSTGKQQSI AKYIEKTIEP EILDAKAKKM AEEIALQKLK LEQEALAKKR LEEEKALLLQ
     QAALALKRYN AVLEDQELTD QRPMPPVRSV RPLITSKHFG NFVFILEFLN SFSDLLAIRS
     KFSGGLTMHL LERALILREV NGPLSDIFQV LLGAIFTQQL EEENEVEVGY ERVENLALKR
     QTVPEQARAR DTVLWCEKHY CTKLSEMPID STTVSELLRL HFLSSGALVE EKATKHRYYN
     RGGYSNADDP GLRLVRDYPH ILRALSSHSV YQLSIGDIIQ ILCCLIHQLL TYSGVRELVE
     ERVDRARSAR YNYQNNRYAQ RRLTVKTGSQ KNQARDDMKR ELTAFEGDTE AREEHRKKLM
     ERLEEQCNRI DAEAQRQMKI LQTESGRLKE DFFDYQIYLG SDRCFRNYWL FESLPGLFVE
     HDRTYAGRCL DQPTPNIPGL AWCAQEQRKK YITKAIMRCA GTDGVAGLLD AKAIAGADPN
     QPDNGGRDPE VYEQLLTQGS AELERIEQQT AQTKALNSRA NSEEPRTEGG LNGEPTVVPA
     ANTIPLPPPS NRELLMCTAQ PADCPVHTEK HAQTVSWGYY ATADELDALI RSLNVRGARE
     KQLRETLECE RDLILTHIEK CPIDKLSVNE SDRAAVLCEI VSRNQKRYDA PNFSSDPGTD
     PNEILEAAFL ENLLELEAKI TVGYLGVMRV RDRDKWRTAL EACTYDPQTD KPLQWGPKRL
     AKQEETNGKE KQEQDTEQQQ PQDVDEDHDE HPTDNDSGRD SLERLLSDAS NPGHNLPDTT
     VSLLDDTLDS DEIAFPLHES ETLRQRVHAL ARALLQVAQC IDQKFLRHPF GPKKEHKDRT
     VMLQKQYQGL KNLVQWEVSL MRSTCFSQLF LHYNVLYDAI QWSRSAERIC CMICRRKGDP
     GLTLLCDECN RACHTYCLKP KLKEVPAGDW YCMRCRPENF KEKRAPAKKK KIFKWVEDME
     EEEEDESDEA SKQEENEAEE EDEEEEEGEE EEEMDQDEGG EEAEEEQAEM EDMVQRKNVD
     GEDSPSEDSD SEDDKEDDGS DEEYRMRKSK QPVTKAKSRA KTKPTIVVTS SGRSSRSAAA
     TNGAAYRDEE AEEDDDSYDE REERRKRRNL TLPNGAVALR ADSKRSGAAL RTRRATSVSS
     TKRKRTQNEE SDVSPSGNTS KRPRRSGLTN GGRKMSVSPA AAAGSDEDAA GKKPRTSARS
     TKGQRRSSVY VGEEEEETVA RLKMGSAARR SRRTGEDLPL NSVALYTLID DILKHPSSWP
     FNRPVSAKEV PDYYAVIKNP MDFARIKSKL NMGDYKINEQ MLSDVQLVFR NCDLYNTDET
     DVYRIGRELE QYVVKRCKEL TLPFQPSDMQ KSGLHQKVPT SKPINGVAGP HGK
//
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