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
//