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Database: UniProt
Entry: V4AJ63_LOTGI
LinkDB: V4AJ63_LOTGI
Original site: V4AJ63_LOTGI 
ID   V4AJ63_LOTGI            Unreviewed;       555 AA.
AC   V4AJ63;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0000256|ARBA:ARBA00017908};
GN   ORFNames=LOTGIDRAFT_232629 {ECO:0000313|EMBL:ESO93576.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO93576.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESO93576.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
CC   -!- SIMILARITY: Belongs to the CHFR family.
CC       {ECO:0000256|ARBA:ARBA00005797}.
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DR   EMBL; KB201891; ESO93576.1; -; Genomic_DNA.
DR   RefSeq; XP_009055775.1; XM_009057527.1.
DR   AlphaFoldDB; V4AJ63; -.
DR   STRING; 225164.V4AJ63; -.
DR   EnsemblMetazoa; LotgiT232629; LotgiP232629; LotgiG232629.
DR   GeneID; 20248994; -.
DR   KEGG; lgi:LOTGIDRAFT_232629; -.
DR   CTD; 20248994; -.
DR   HOGENOM; CLU_036129_0_0_1; -.
DR   OMA; MDEQLTC; -.
DR   OrthoDB; 337585at2759; -.
DR   Proteomes; UP000030746; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   CDD; cd22663; FHA_RNF8; 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; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
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; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS50158; ZF_CCHC; 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:UP000030746};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00047}.
FT   DOMAIN          28..78
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          368..406
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          537..553
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          117..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          170..346
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        117..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  63722 MW;  95C2A787FF106A34 CRC64;
     MTEMLPCLIR VGENVKKYKL FILDKDEVTV GRSPDVTYCI LSGMISRCHA FFRKSPDNTW
     TVSDNKSLNG IFVNDKRIEV DKAVSLNDGD KLQLGVTNKE KKEEFIFRFS LSSRVKRSRK
     ESEESNRPNH KRSRQDSIDG IKLTQKSPEC DNHVSSSQPD LESSSVNSPY KLYEQKMEEY
     KKQEEEKRKE YEEKLQSMKK MLEAKEFEQN EMRKALEKQK EEKLESEAKL KSALELQQEE
     MEREKTELKQ QMQDELEKQL KNKEQSLIEQ LRVQQDTLIS EKAKVEESLK QEMEKAIEQK
     NKQLENELTL QRDKLQKVID SKELEQKVLE NQLEETKAEN IKTKEAMLCA RGDVLNNFKD
     LMETELQCSI CSELFVQSTS LNCSHSFCAL CIEQWMAVKK ECPICRSPIT SHMRSIVLDS
     YIDKMVEQLD DELRQSRKEL VDGRKEEYKK LQEKKKAEVP GGSGAGRGRG GRARRRGGGS
     SGGNLNATPT TPSRRPIIIS DEEEAGEVTD SDISNSSDND SSDVEGDPDA YYGGYGRCYT
     CGRSGHWANG CPDNW
//
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