ID A0A4Y0BF30_ANOFN Unreviewed; 1058 AA.
AC A0A4Y0BF30;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=NR LBD domain-containing protein {ECO:0000259|PROSITE:PS51843};
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:AFUN018646-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:AFUN018646-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN018646-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000256|ARBA:ARBA00008092}.
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DR AlphaFoldDB; A0A4Y0BF30; -.
DR STRING; 62324.A0A4Y0BF30; -.
DR EnsemblMetazoa; AFUN018646-RA; AFUN018646-PA; AFUN018646.
DR VEuPathDB; VectorBase:AFUN018646; -.
DR VEuPathDB; VectorBase:AFUN2_002157; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR CDD; cd06940; NR_LBD_REV_ERB; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001728; ThyrH_rcpt.
DR PANTHER; PTHR24082:SF508; ECDYSONE-INDUCED PROTEIN 75B, ISOFORM B; 1.
DR PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00546; THYROIDHORMR.
DR SMART; SM00430; HOLI; 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR PROSITE; PS51843; NR_LBD; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
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}.
FT DOMAIN 59..306
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 331..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 112671 MW; 9D21A687D67340DE CRC64;
MAEELPILKG ILKGVVSYHN APVRFGRVPK REKARILAAM QQSTQNRGNQ RALASELDDQ
PRLLASVLQA HIETCEFTRE KVTAMRQRAR DCPSYSMPTL ACPLNPAPEL QSEQEFSQRF
AHVIRGVIDF AGMIPGFQLL TQDDKFTLLK AGLFDALFVR LICMFDTSIN SIICLNGQVM
RRDTIQNGAN ARFLVDSTFN FAERMNSMHL TDAEIGLFCA IVLITPDRPG LRNVELIERM
YTKLKACLQT VISQNRPDKP EFMQELLRTM PDLRTLSTLH TEKLVVFRTE HKELLRQQMW
SAEEDQGAVL DAKSPASWSC DGNQVEVEIA KSPMSSVSST ESTETSSSSS SSSSSSSSEY
HHLHHHHHHH NGGISSAASA AAPLLAATLS GACPIIRHRA SSGSSAEDDL IGGTAQHLAQ
NGLTITPVIR SVGSSSSASS ASSASSHLHH HHHHHVSRYR KLDSPTDSGI ESGNEKHDNP
SPQQQQQQQQ QQQQQQQQQQ QQQQPSHHPH HHHLLLHPKP ASSSVSSGSS SCSSPRSSLE
DPTLEDNNSS STNQGKTLLA RHASVENMPV LKRVLQAPPL YDTNSLMDEA YKPHKKFRAM
RHRESEAEAA SSSTMSASSS SSSSTSSSSS SPIVATVLAS SSSPRPAAIQ PHQQHQQQSS
VVTAAAPSPP QHHQSQLHMH LTRPQTQSHQ SSSSATGFLQ SSSARSSPQP PIGGAQQQQQ
QQHHHTYSSL SSTHSVLAKS LMEEPRMTPE QMKRTDIIHN YIMRESAQEQ QNYIKQQQGG
LLVCGPTANG VFQRASPHLT VSAVSPAPSS SSSSSSSSSS SSNSPAASSA PNGCPFGGLS
STSSTSGRWQ QVIHGSSAAA SVITTTGHRA QQTPSPGSLT PPDTSSSSSS SSSLSVVSSP
PSAASPSSSS STSIRYFQSP HSTMTSPAPP ASPSSVVVAP PLTPSPRLIE LKVDIGSSAA
SGSATVVTSL EPSQQPLNLS KKSPSPAPVG VVSVVQRPMV PTASSSSSTS PSPISPVAAA
ATTVVVATSS SSSSSSNGPN SSSATASNPT IHKILLEA
//
