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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//