ID H3AEM6_LATCH Unreviewed; 1188 AA.
AC H3AEM6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Zinc finger BED-type containing 4 {ECO:0000313|Ensembl:ENSLACP00000008097.1};
GN Name=ZBED4 {ECO:0000313|Ensembl:ENSLACP00000008097.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000008097.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000008097.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AFYH01182131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006007424.1; XM_006007362.2.
DR RefSeq; XP_006007425.1; XM_006007363.2.
DR RefSeq; XP_006007426.1; XM_006007364.2.
DR RefSeq; XP_014350873.1; XM_014495387.1.
DR AlphaFoldDB; H3AEM6; -.
DR Ensembl; ENSLACT00000008163.1; ENSLACP00000008097.1; ENSLACG00000007168.1.
DR GeneID; 102363153; -.
DR KEGG; lcm:102363153; -.
DR CTD; 9889; -.
DR eggNOG; KOG1121; Eukaryota.
DR GeneTree; ENSGT00940000161365; -.
DR HOGENOM; CLU_006260_0_0_1; -.
DR InParanoid; H3AEM6; -.
DR OMA; NEMSVEC; -.
DR OrthoDB; 3139403at2759; -.
DR TreeFam; TF322818; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000007168; Expressed in chordate pharynx and 2 other cell types or tissues.
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 Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00027}.
FT DOMAIN 118..175
FT /note="BED-type"
FT /evidence="ECO:0000259|PROSITE:PS50808"
FT DOMAIN 287..344
FT /note="BED-type"
FT /evidence="ECO:0000259|PROSITE:PS50808"
FT DOMAIN 463..519
FT /note="BED-type"
FT /evidence="ECO:0000259|PROSITE:PS50808"
FT DOMAIN 565..622
FT /note="BED-type"
FT /evidence="ECO:0000259|PROSITE:PS50808"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 133153 MW; E40E586D291F3047 CRC64;
MDCKKRRENS PKAESNFDPD KINNIKCEQD DFDNAENGSE LNRVDAKDQE ENFMTTDSGD
EQMENREQSL IGSSGRYLPT ENEEEYGSLF SQYTSTLYDV AMEAVTQSLL STRNMSSRKK
SPAWNHFFIS PRDSTKAVCM YCMKEFSRGK NEKDLSTSCL MRHVRRAHPS VLVQENGSTS
GISPFSSPTL LSSIQSPESM CHNSGAASGK PTKKSVSKLS SLEKLTEEPL SVVSSEETIT
DVSVSEKCTK DETSVIPSPY PANNHCDETV ETVPERTTPT PKNAGSRRRS AVWKHFYLSP
IDSTKAVCIH CMNEFSRGKN GKDLGTSCLI RHMWRAHRSI VLQENGTTSS IPVPYSSPPT
LVPSLLSSGA GDPNSLSTSP GKLVTEPTSV SSSPDRLPNE MHSKLCSGDV TIEETVTPSS
EDAEESYTMT SSEKATEAPA PVVPFLDKDT NSVFQENKKI MKRLKSEVWH HFSLSPVDNL
KAICRYCNCI ISRGKKGDVG TSCLMRHLYR RHPEVVGSQK NVTDASLANS PYATLASAEC
SSSKITDLPT MVASDKQMIF PLSSKKTSKL WNHFSICSAD STKVICMHCG RTISRGKKPT
NLGTSCLLRH LQRFHSTVLE NSDNVSETVL TSCSSDLQMS SNTCSQGSSF FDETSDKFSD
SHPVAKKITN LVAEMIALDL QPFSFVDNVG FSRLLEYLQP QYSLPSPSYF SRTAIPDMYE
NVKQIIVSHL KEAESGIVHF TAGIWMSNQT REYLTLTAHW VTFESAVRTQ GEDYHCSALL
NVSQIDCDYN GISIQKQLEY LWETWIVSSG LHVGFTVTDN QGIGKTLNES EHSSVQCFGH
TINLIVSEAI KSQRMVQNLL SIARKICERV HRSAKAKEKL SELQKEYCLP QHQLIQDVPS
KWNTSFHMLE RLIEQKRAID EMSIECSFRE LISCDQWEVM QSVCHALKPF EAASREMTTH
MATLSQVIPM IHILNRKIDL LFEETMGIDN MLKSLKEAMV SRFSSTLYDP RYIFATLLDP
RYKTSLLSEE EGEQYKKDLI NELEMLNCNS NECKPVSNGC DVKSLPSNKL HGGGDNLWAL
MGDIRKTSDT KETAKTPEEM VFAYLQEEVV DHTCDPLTYW NLKKSSWPLL SRLAVRFLGC
PPSIVPTERL FNTSSESSSS LNHSRLITEH LEKLIFLKVN LPLIYFQY
//
