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Database: UniProt
Entry: A0A1D2NJZ4_ORCCI
LinkDB: A0A1D2NJZ4_ORCCI
Original site: A0A1D2NJZ4_ORCCI 
ID   A0A1D2NJZ4_ORCCI        Unreviewed;       620 AA.
AC   A0A1D2NJZ4;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0000256|ARBA:ARBA00017908};
GN   ORFNames=Ocin01_01090 {ECO:0000313|EMBL:ODN05590.1};
OS   Orchesella cincta (Springtail) (Podura cincta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX   NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN05590.1, ECO:0000313|Proteomes:UP000094527};
RN   [1] {ECO:0000313|EMBL:ODN05590.1, ECO:0000313|Proteomes:UP000094527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Mixed pool {ECO:0000313|EMBL:ODN05590.1};
RX   PubMed=27289101; DOI=10.1093/gbe/evw134;
RA   Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA   Smit S., van Straalen N.M., Roelofs D.;
RT   "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT   in the Genome of the Collembolan Orchesella cincta.";
RL   Genome Biol. Evol. 8:2106-2117(2016).
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:ODN05590.1}.
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DR   EMBL; LJIJ01000020; ODN05590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D2NJZ4; -.
DR   STRING; 48709.A0A1D2NJZ4; -.
DR   Proteomes; UP000094527; 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; 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; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR   PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 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:UP000094527};
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          30..78
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          347..385
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          111..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  68515 MW;  271E750A4F325AC1 CRC64;
     MTSAVTAQLI LIQGDGQHFQ RVIDLSNAHV SIGRAQTCDV VWGSLQISRQ HATLEYVISK
     WYIRDTSTNG LSVNGNKLGK GELFMLKDQD IISFIPTGAV RYRFKYVSAG STPLSRPNTS
     LGQNSLISPL PSTSNANAAS SSRISSSLEH RSASSVEAIS DHNHSDSEDS NHSESLLSLG
     NPEEYLYGFS GDELSQSPAV VDSEEDGPVG AVPKRKHHED SSDNDNRPTD RKKKKMLYTS
     SEDESSKDAY LKSEYSKATS SNGSPFKAMS EDQVNKCDDL EILKAQLKSC LQKLGTTEVE
     LGMLQMDRNI EREEFRRKEK DAESSNEAFK EEMFKKILEL MESELSCSVC NEVFIQATVI
     ECGHTFCSFC IHEWSRKKQE CPICRKRFAS RSRHIEVENF ILKMFESFSG EIASKRKASI
     KEREDQVKKA AEDAARAATA HQSRGTGGNF HAFIQSTAER YVDFLAELHQ INEILAPRPN
     SARGGAAGSD RRRSARIQER VVGDGAPPTG EPEVLRAPGR RRGGRTRAAT RAAVLVPSVP
     AAPRIQLGRV DAANLDVNAP IPIVTLNDSV DDGLGAARAA MRAPPLRFPN HFINYVRRIP
     MNLMEVPFNA IRDGNRPNNQ
//
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