ID   A0A3B3C823_ORYME        Unreviewed;      1252 AA.
AC   A0A3B3C823;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Zinc finger BED-type containing 4 {ECO:0000313|Ensembl:ENSOMEP00000013749.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000013749.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000013749.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A3B3C823; -.
DR   STRING; 30732.ENSOMEP00000013749; -.
DR   PaxDb; 30732-ENSOMEP00000013749; -.
DR   Ensembl; ENSOMET00000021480.1; ENSOMEP00000013749.1; ENSOMEG00000015204.1.
DR   GeneTree; ENSGT00940000161365; -.
DR   OMA; NEMSVEC; -.
DR   OrthoDB; 3139403at2759; -.
DR   Proteomes; UP000261560; Unplaced.
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   InterPro; IPR008906; HATC_C_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR003656; Znf_BED.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR46481; ZINC FINGER BED DOMAIN-CONTAINING PROTEIN 4; 1.
DR   PANTHER; PTHR46481:SF6; 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   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   SUPFAM; SSF140996; Hermes dimerisation domain; 1.
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          192..249
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   DOMAIN          360..417
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   DOMAIN          532..588
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   DOMAIN          632..689
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   REGION          91..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1115..1139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1252 AA;  140569 MW;  49C5780791A0908B CRC64;
     MDGEEEVPHM SEDLIIESNG LIESKKREAK ASCLKIEGQD GYVFKSYSIH PHDDDEDPKS
     LACSSTLDKD ILPCFHFTSQ MDKRLEIDLA CNTGPSSPNT DTEGNAETEK YENGNESSEL
     AREDIEDANG MEDEPQDDER LAFGSSIGPF ATKDVDDYSN LLSGYTSTLY DVAMDAVTQS
     LLSSIRGHAN PRKKSPAWNH FCISPRDNTK AICLYCMKEF SRGKNEKDLS TSCLMRHVRR
     AHPTVLLQDG ADVSLSNLSS SLPSPFLPFP PSSPKNGDLT NCIFTPASKN SSPSTSSAEN
     SDPSSKETLP KVEPKLESCA NADTVYGSLL PSHSIENNVE EMSDGGSERL PGTPKGSNSR
     RRSAVWKHFY LSPADNSKAV CIHCMNEFSR GKNGKDLGTS CLIRHMWRAH KEVVIEENGQ
     GNHIPPPYTN PPSLLSRTQL LDSFEVKKES PLLPSSPETI ADELPQSIEE SMDIKEECEE
     VMQLSGQDSS LNFFKTQEED LPLTSSPCEL FDGPGASQDH SVFQQNKKIM KRVKSEVWHH
     FIVSPVDQLK ALCRYCPCVI SRGKRGDFGT SCLMRHLTRR HPDVLKNQKS TDEKESSPHP
     YNNFAMMDTV SAKETESPVT EAKAQSTPAF SKKTSKLWNH FSISPADPTK VVCLHCNRTI
     SRGKKTTNLG TSCLFRHMQR FHGHVLESNN AISGDAQDAE IHVKQEVMET SVYETEQNCE
     RFDEEHPVAK KITKLVAEML ALDLQPSAVV ENAGLNRLLE YLKPQYSLPS SSYFTSTAIP
     DMYEKVKEVV LTHLKEAEGG VVHFTTSIWV SSQTREYLTL TAHWATYESS VRPQGQDFHC
     SALLSVSQID CDQDMHDIPK QLEYLWDTWI TSSGLKRGFT LTDNITIQHT LEEHGHPIME
     CFGHTIDLIV SEAIKSQRMV QNLLSIARKI CERVHRSAKA KEKLVELQRV HQLPENQLVQ
     DVPSKWRTSF FMLERLVEQK NAIDEMSIEC NFREIISCDQ WEVMLSVCNA LKPFEVACRE
     MSTHTATLGQ VIPLIHILSR KIDLLFDETV GIDNMLKSLK EALVSRMSAT LHDQRYTWAT
     MLDPRYKTSL FTEEEAEQCK QDLIRELDSS SSTSAEAESL LPNGCSDDPA SCSSSHSNAD
     DLWSLMPDVR QRTKNEEKPK SSEEAVLEYL EEDILDQSCD PLDYWNLKKF LWPDLAKVAA
     RYVGCPPSIV PSETLFSTAS VNCALNQPRP MLDNIEGLLF LKVNLPLIYF QY
//