ID E2BP13_HARSA Unreviewed; 1346 AA.
AC E2BP13;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=PHD finger protein 20 {ECO:0000313|EMBL:EFN82605.1};
GN ORFNames=EAI_00897 {ECO:0000313|EMBL:EFN82605.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN82605.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN82605.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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DR EMBL; GL449511; EFN82605.1; -; Genomic_DNA.
DR STRING; 610380.E2BP13; -.
DR InParanoid; E2BP13; -.
DR OMA; FCIHRKK; -.
DR Proteomes; UP000008237; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20104; MBT_PHF20L1-like; 1.
DR CDD; cd01396; MeCP2_MBD; 1.
DR CDD; cd20386; Tudor_PHF20-like; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 6.20.210.20; THAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR043449; PHF20-like.
DR InterPro; IPR006612; THAP_Znf.
DR InterPro; IPR038441; THAP_Znf_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15856:SF51; MBD-R2; 1.
DR PANTHER; PTHR15856; PHD FINGER PROTEIN 20-RELATED; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF20826; PHD_5; 1.
DR Pfam; PF05485; THAP; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00980; THAP; 1.
DR SMART; SM00333; TUDOR; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00309};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008237};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 1..85
FT /note="THAP-type"
FT /evidence="ECO:0000259|PROSITE:PS50950"
FT DOMAIN 515..588
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 662..687
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 129..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1346 AA; 153444 MW; ED564428D148DE35 CRC64;
MARKCCVRSC EADVREARAK GLPLHKFPKD AVLKDRWLAS GGFEKSFKPT PGQVVCHRHF
KRADYEAAAR GHKFLLKRGS VPSVFADYDN HPDPVIISVK SSTSYAQEDL DLINSEILNL
EHSVSPLLSE ARTPKSDSCG EQCYSRPESS TDSLNPPDNS ELIDTGYKMT TLKEETVTMM
KDKSMENSDS KVNTVAMQLG IVEPGIIKTV AKDLMIKEEL KDIKLSDDKE FDKTEEIKPK
VLNKDGLKFY PGAKLEAKDF SEKWQVLLKI MYSAKVVETD WDEREVLIHF DKWNSRFDEW
IPMDSSRLRV LQTPPKETKV RDFSVGERIL ATWADGRKYP AKVNAVLSND RYDVLFDDGY
GKIVKSSKMT KIAATPTKQL SELEGYIGSK QERRDKKRKH TIMELFHTNS RKRIKTDSDK
TPKKVETVVK ESGESSLETK IELDGTMYGP CFEPDTNLLK GFDTNIAKIK SYSKKSKKEL
PKIDTDHEED VGPEWIDGEP QGTESYIVDG NDGPRRSIII SDKRLPPGWE KHFTQRKAGT
SAGKWDVLFI HKQTGKKFRS RNDIRVFMEN QGQLDFDPEK FDFCIHRKKR NVHRIKQEIT
PEVPKKIKTL LPKTKALATP ESTSLIASTP DIPPTASTPT TSATDSAVFI GGLRVEMEDS
AYKCPKEGCN KNFRKENLLQ MHIKHYHPEY SKFLGSTPKV EDLAYARTIG ESIEDIIPKK
STPFLEKINK IGKKKSLPDK LSSNLLQPVL NPVQPTSPSI SAPLISELEE EIDQSEKCSD
LQKDDVKIET MSPMSNHSME IDDDIEKKRE NACAMSPTTL FDMKVKEEKT QVGIKTLLPV
RPSTTSESQK IDKTKPVDEI MHIERTKNSK KRQSEYSMHL PAKGKKRHDL IDSFGDLDDS
ALDVDGPTAL MYRYSRRKSD SKSDENSQNS QLNDSRIEKG DPLKGDTSKT DINNDAEESE
GVMMMINGEM VKVEQLRREE IINCTCGFME EDGLMIQCDL CLCWQHGHCN AIEREKDVPE
KYICYICQHP YRQRSSRKYF HDQDWIKEGK LPSLPNRTRD QYMINQRTAM LKRSYDLVGA
LLQIQQILHS LRVKINVAQQ KDHPKLYLWA KNWEKTNIPK VDFEPVPVME ITKSGVDFID
TGVENLRRIE PKTEIKLPLK DDQDEKSIAS DSELMKILEE DSTHSDESRV TGKREGLINS
KDSHILLDAL TNSNSDMKQR NVDADIKTEN IENLSSNSLI NDDQPESNIV QVEDEVTAPL
QPFIPEPEAP IDPAECRMRL LEHIEHFQNH IESRLSSIDA QVCALEAMDM EELEELPNPH
MQSRLKQTVQ MLLRDLNTVR KLAALC
//
