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Database: UniProt
Entry: A0A226ESD6_FOLCA
LinkDB: A0A226ESD6_FOLCA
Original site: A0A226ESD6_FOLCA 
ID   A0A226ESD6_FOLCA        Unreviewed;       559 AA.
AC   A0A226ESD6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0000256|ARBA:ARBA00017908};
GN   ORFNames=Fcan01_05173 {ECO:0000313|EMBL:OXA59984.1};
OS   Folsomia candida (Springtail).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX   NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA59984.1, ECO:0000313|Proteomes:UP000198287};
RN   [1] {ECO:0000313|EMBL:OXA59984.1, ECO:0000313|Proteomes:UP000198287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VU population {ECO:0000313|EMBL:OXA59984.1,
RC   ECO:0000313|Proteomes:UP000198287};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXA59984.1};
RA   Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT   "The genome of Folsomia candida.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CHFR family.
CC       {ECO:0000256|ARBA:ARBA00005797}.
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:OXA59984.1}.
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DR   EMBL; LNIX01000002; OXA59984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226ESD6; -.
DR   STRING; 158441.A0A226ESD6; -.
DR   OrthoDB; 337585at2759; -.
DR   Proteomes; UP000198287; Unassembled WGS sequence.
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   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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR   PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF13639; zf-RING_2; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          74..122
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          314..353
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          246..280
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        13..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  62222 MW;  5A2B779233563A11 CRC64;
     MPREGDDDTS SRAGSIVDVT STPPIATSHP RLPAAQGEPQ VQDNAFTTAQ LSLADNTTGD
     NDVPAVILLR RKDMLFGRAA TCDVSLNSLQ ISRRHCSLEY RNDKWFIRDL STNGITVATK
     KVIKDQLHPL NHQDIVQLVP TGALTYRFTE TNKENQQLIC NASNPITIED DQESLLSLKH
     EEDEGLPSIE VVDHANKKQQ NEQDSVMLLD DSMSSASTKK TNSPSKRPFS AFALESSPPF
     LEIKSNKKQK TDIHHLSLQL QRIKAENEVL RVERVIEREE YKQKRDLEVL FFKEQYKEEV
     NKKLQDILES EFSCCICSCV FVEPSISPSC GHTYCHHCIS EWLKKKPECP ICRSPINTPP
     KKHIEMGNYI NKVYEFAGND VKEKRDIQIK DRQKEKEAAK NVLRMAAPHP MPQGFMFDLE
     LLNAAMNGRG GGGRRGRRNN TAAVAAAAAA AAAGGGAGNA PPPPHRRSAR RGRNQNNNPA
     TGGLPGGGAQ VPGYQMIPGM LNMNPPGPPH RGAGHNHPFF HVPAMPQNMT HQAMHNHFPQ
     LFNNNQFEPF LHNDVLMID
//
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