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Database: UniProt
Entry: A0A368FCY0_ANCCA
LinkDB: A0A368FCY0_ANCCA
Original site: A0A368FCY0_ANCCA 
ID   A0A368FCY0_ANCCA        Unreviewed;       644 AA.
AC   A0A368FCY0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=BED zinc finger {ECO:0000313|EMBL:RCN29468.1};
GN   ORFNames=ANCCAN_24775 {ECO:0000313|EMBL:RCN29468.1};
OS   Ancylostoma caninum (Dog hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN29468.1, ECO:0000313|Proteomes:UP000252519};
RN   [1] {ECO:0000313|EMBL:RCN29468.1, ECO:0000313|Proteomes:UP000252519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Baltimore {ECO:0000313|EMBL:RCN29468.1,
RC   ECO:0000313|Proteomes:UP000252519};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Ancylostoma caninum.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCN29468.1}.
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DR   EMBL; JOJR01001936; RCN29468.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368FCY0; -.
DR   STRING; 29170.A0A368FCY0; -.
DR   Proteomes; UP000252519; 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   InterPro; IPR008906; HATC_C_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR003656; Znf_BED.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR46169:SF24; BED-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR46169; DNA REPLICATION-RELATED ELEMENT FACTOR, ISOFORM A; 1.
DR   Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR   Pfam; PF02892; zf-BED; 1.
DR   SMART; SM00614; ZnF_BED; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF140996; Hermes dimerisation domain; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50808; ZF_BED; 1.
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:UP000252519};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00027}.
FT   DOMAIN          1..56
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   REGION          47..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..644
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   644 AA;  73097 MW;  D18746DBD06B73D4 CRC64;
     MSTVWNYYKR MVEAGSNSEL AICKFCSRSF NIPKSRTTTN LLEHIRRKHK EEAEESTSTF
     TGDNDSTNNN QPKLEEMFKR KMNLAVRKKI DRKVVNFIAN ASVPLNVVTH PSFKDLLGTL
     NNSYTVPSRA SIERLMREQV QCIDESNKKL FADEDVNIAI TADSWTSKNA SCSLLAITGH
     ALGKDFEDRR NVILDCVPLE EESHTSEIIA AKVLETLARL GITTERISFV VADGAAVMVK
     MASDLGLPYI HCCAHLVNLA VSASMNYPMS AQALRKVKSI VSRLNKSGKM KKMFRRYLKE
     EQLPDVIPMN DAPTRWSSTY FMLCDVLNAL PAVEKLMHAH RMAPFEDEEI RVLKAMKVFL
     QPFQTMTSQV CFQSSCISMF IPVGKLLITE TEKNLVDARR EGLHFGEQLL EKTKQYFAKW
     FNNQHLRLAA LCDPRFAHLD TVLTREEWRQ TVDHFISMKV SSARSEETKE TVTKQQSARK
     ESSVWSLLTS PKSTDAPSKT VRLKEEGLQV ELQQYSIFLN GDEARPDPAE DPIAWWRSHR
     DRFPLLAETV PRFLVAPCTS VDTERLFSSA GIIYGNKRRG RLSGKNARLL LMINASGKNE
     TCRPSKAWSQ RDIERYGNVG DMADVYSTSD DDVEDEEDSS EELE
//
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