GenomeNet

Database: UniProt
Entry: A0A1W4WEU7_AGRPL
LinkDB: A0A1W4WEU7_AGRPL
Original site: A0A1W4WEU7_AGRPL 
ID   A0A1W4WEU7_AGRPL        Unreviewed;       565 AA.
AC   A0A1W4WEU7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0000256|ARBA:ARBA00017908};
GN   Name=LOC108732370 {ECO:0000313|RefSeq:XP_018318638.1};
OS   Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC   Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX   NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018318638.1};
RN   [1] {ECO:0000313|RefSeq:XP_018318638.1}
RP   IDENTIFICATION.
RC   TISSUE=Entire body {ECO:0000313|RefSeq:XP_018318638.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the CHFR family.
CC       {ECO:0000256|ARBA:ARBA00005797}.
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DR   RefSeq; XP_018318638.1; XM_018463136.1.
DR   AlphaFoldDB; A0A1W4WEU7; -.
DR   STRING; 224129.A0A1W4WEU7; -.
DR   EnsemblMetazoa; XM_018463136.1; XP_018318638.1; LOC108732370.
DR   GeneID; 108732370; -.
DR   KEGG; apln:108732370; -.
DR   InParanoid; A0A1W4WEU7; -.
DR   OrthoDB; 337585at2759; -.
DR   Proteomes; UP000192223; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   CDD; cd00060; FHA; 1.
DR   CDD; cd16535; RING-HC_RNF8; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR15067; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR   PANTHER; PTHR15067:SF8; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192223};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          26..74
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          391..429
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          274..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  62692 MW;  11710407F72F7C5E CRC64;
     MEKAILTNYG TSKAFSTPIV LSNEKYGLGR GLQNDCVFDD VSISRNHCTI EKSGKEWIVI
     DRSSNGTLVN GILVGRLKAH VLQNGDVVTL GSNTQFQFIK RNSAPEPVTE SNKSSLSEEE
     IINITDATLT KVEQPNLRLS PSLEDEFNIP MDVEGNSNID KHITNENNSS VKSGTVNESN
     HKSQLPHCIE HKVNMTSTSD VPKTTLISIN PTSYKGFFSS FVINSNVNKK SITLPSISQP
     SFAQNTLPGA TATTSTAIPS WLIGVVSQKV NQQSQKSKCS ITKSPKSARL KSSITSPPKT
     YSNTKKGSKK KSTEANDQPS CSKDFPQAKV ESRNAEGIKE NIPKDLPQAK DELKNVNDIK
     EKITKEDTEP KPGCSKSSET KLHAVQDELQ CIICTEMFIK AVTLSCSHTF CKFCIDEWKK
     KKTACPICRA PICSILPTLV IDSFIEKILE NADEETKLQR SKLIADRESQ QASGSKDYRG
     KEKSATDVFD EAFAHDAIIL SSDSDMNSYD SDAETMSYYD DDSDNGRILR MQRLRNNFVD
     RVKEHLERSL YNQIQLISIL NDTLY
//
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