GenomeNet

Database: UniProt
Entry: A0A182UYW9_ANOME
LinkDB: A0A182UYW9_ANOME
Original site: A0A182UYW9_ANOME 
ID   A0A182UYW9_ANOME        Unreviewed;       922 AA.
AC   A0A182UYW9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=BED-type domain-containing protein {ECO:0000259|PROSITE:PS50808};
OS   Anopheles merus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM006030-PA, ECO:0000313|Proteomes:UP000075903};
RN   [1] {ECO:0000313|Proteomes:UP000075903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles merus MAF (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEM006030-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM006030-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A182UYW9; -.
DR   STRING; 30066.A0A182UYW9; -.
DR   EnsemblMetazoa; AMEM006030-RA; AMEM006030-PA; AMEM006030.
DR   VEuPathDB; VectorBase:AMEM006030; -.
DR   VEuPathDB; VectorBase:AMEM21_006544; -.
DR   OrthoDB; 3440249at2759; -.
DR   Proteomes; UP000075903; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR   InterPro; IPR008906; HATC_C_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR003656; Znf_BED.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR46481:SF4; ZINC FINGER BED DOMAIN-CONTAINING PROTEIN 39; 1.
DR   PANTHER; PTHR46481; ZINC FINGER BED DOMAIN-CONTAINING PROTEIN 4; 1.
DR   Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR   Pfam; PF02892; zf-BED; 4.
DR   SMART; SM00614; ZnF_BED; 4.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50808; ZF_BED; 4.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00027}.
FT   DOMAIN          6..56
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   DOMAIN          106..156
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   DOMAIN          199..249
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   DOMAIN          293..342
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   REGION          150..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   922 AA;  103607 MW;  254CE4DFF1AFEE7A CRC64;
     MSKPSRFISS VWKHFERLGD RAKCQFCQNT FSFSTGSTAN LKRHLARKHP TDPLEEMYAE
     VAESEPSSPP EETNGEQTWD DGIEGILIPK VECVMPQVET KPKPQQLVSS VWKHYDRDGS
     TAKCHHCPRV ISYSHGSTSN LKKHLIRKHP DASLDPEPTP GDELAGEQGE DDPSSPSQWS
     EGIEGIVVPK KEQATPGGKT YADIWNHYDR DGTMATCHYC YRSIAFSAGS TSNLKKHLTR
     KHPMVTVQSR PAKKRQSLER KVKLPQSPTP LNDYFDEDSI LPAVGLQPRN RPKPTSSVWN
     HFDRSGTTAK CRICLRVLTY AGTTSNLRKH ILRQHPTLTL GKQEMTRIHH VTLPTPPQRH
     RDSADDTERP PFTVKPFVSA SPGESSDSEQ QQQQPALKPL TEARLAKMHE SILLMICRGN
     HTFAMVEEEA FQALFKQYSH REFEMCSKFT FKRVWLPQVY GKVQSRVKAE LATARAISLG
     VNSATSVNHE SVLSVTAYFI DQNGQLSNAL LDFARCTPSH GGENVAAQLG EVMKLFEIDG
     RVLSIVTDND DASMTQAVET LNIPHVACFA HSIDPIVMLT LNSTIQGTLD EVRHVVAQIR
     SSAKAREVVE GTENCARVTT LKLDVPNDWH STLDMLGRFV ACKEAILACS AELNIACKLE
     GKDWLMIEQS SRVLQELATA MHEVSADKLV TISKPCVLYQ LLVHRLEGMA VEQNVLMDVS
     ALAATLRDSI RECCAYVRSS PLLTQAVMLD PRYKAEGFMQ DEECLQKTYE NIVEEIAALQ
     SDGGEGGLPM ELDKESETEQ SRTTEEALYQ LFETHKHSKH DGSALKVSAQ YELDYYLKAK
     HLQRKGDPLE WWERNKHFYP NLYKLASKRL CTPAACVSAS GCCAKAEVEC RERKNRLLPK
     RIQQMVFLKY NHHRYQADVG DD
//
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