ID V4C6V4_LOTGI Unreviewed; 1824 AA.
AC V4C6V4;
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=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=LOTGIDRAFT_159405 {ECO:0000313|EMBL:ESO97374.1};
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:ESO97374.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO97374.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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; KB201305; ESO97374.1; -; Genomic_DNA.
DR RefSeq; XP_009051971.1; XM_009053723.1.
DR STRING; 225164.V4C6V4; -.
DR EnsemblMetazoa; LotgiT159405; LotgiP159405; LotgiG159405.
DR GeneID; 20238044; -.
DR KEGG; lgi:LOTGIDRAFT_159405; -.
DR CTD; 20238044; -.
DR HOGENOM; CLU_235321_0_0_1; -.
DR OrthoDB; 443445at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd22585; Rcat_RBR_DEAH12-like; 1.
DR CDD; cd00590; RRM_SF; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685:SF340; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51873; TRIAD; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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}.
FT DOMAIN 1600..1818
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 60..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 663..725
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 82..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1824 AA; 207895 MW; FF68E6EA6ADA22D3 CRC64;
MAYLFDGACD LNIDFLKGNS FLPIQGIWLS MCDNLLLNRD PYAPPGNYCP KNKLVNDMSR
PNKGAQFCPG NSRGGRGGGR GRRSHTSRDR GDHGNPNDRF RDEGRNFHRQ DSRDSNLYGN
DSRRDRDYGP DYRTRDGDMN YGQNRRQSPN RYRRHSPNRD YRHDRRDSPN RDYRYDDNRD
YRQDTRQSPN RDRRHSPNRD YRYDRRDSPN RDYRYDDNRD YRQDTRQIPN GDRRHSPNRD
YMHNRSNKPN TDYRRDNRQQ QQPIFDGYSL PPSYQMIHNQ PSFPLPLPGQ PLLPNPVPPL
MSFTSPPPPL YYAFPNMPIH DTNLIRLDST SNQSLASNSS RQSTPPQFPN KGSKDGFQGR
ARGRGRGRGQ GRGRGQGRGR GQGRDARRRE SSTTSSKGDC ELDSFGSDVS REPEKIAPKT
EKKETFLFFI FKGKSDESFD YGAYLKSRTG SLTSIEYDIQ AIMKTGNSKV VLGLFHSKAS
ANKVIKYFRK TNSSSEIEVL CYTRDLLPPI YHDLAHVNLE KKIKKTKIQE KEASKGQESA
QATKKKTKKK KKVESTPEIH ETTLYLSIDD ALKSQDAVGF IRARMGTGTI YPFQLVSSVL
SEDGSSTNIE IKVQSEAIAD IVIRQLEESN TNSPTNVVCS LIPISTESTS KREMIQQVLS
GIKTKSKQRI EHHELKINDA NNRLEEFVIS PNISVKEYNR KVAERDAIKA KLEELKSQKL
EYQNYFEKIT ADISKSENIE NFKEYIQQLS KQFSIECCRL DTALPIYARR SDILSCIANN
QGDFVESPSQ DALNSALKTL VQLNAVKDGK ITDHGNWLAK VPFEPRLSSI VKKGFDKGFV
YDALVLASLI SSGGSLFYRG GSDSEKDNSD LVKTQFCQHQ GDCFTLLEVY KVWIAQTDDK
RNKWCFDNYV NNKVIRGVFE TVSEISGILK RELGIEVKKE FSQDQGLAES FQKIILLAFT
ENIAHFTGHR KAGYFVPSLD QQVFIHPSSS LKVLNDSSEW VVFCNVLRTS TDFITTVTPV
REEWIQGMMK LHFDIENVKS KRISIVHTEY FGSSSFSMFV GPRFTKLRKY EEMLTQICGC
IVMIDADRDR GEVRFYTSSL NETAKQVIAK WRHEAIQPVL MKTEEFQLGS KRTRTGGVRI
VLGKGGEGTL LLMPLDYRSV YITKPNCKTS SKENIKEKFS KFGEIVDCWE YKRPDGRWGC
VTFSSDVAAR LAVKETENDN VDVAIPDIKQ SERRITVKID VNDASTGLIL RRLPPNTKEA
EIKESLCNSL SFISEEAKAN IQRVSVVREK VQATSVDDID NIKRAISVYI SNYVNGQTGF
VVDVVKPKKN TDINFVAYAK FYSAEDGYLA CRGLNGVMRI NNQPVTMIPD VSSSINISQQ
VYRIMKSSID EAVEALHKTL DFKFHEKELN NGRVILNLYS KSSSDLAQTR AILDGILKGE
VIECWRNENY RHLFLRHGRQ FVQKVEEKTQ TVIIMDERTN SIRIFGPMAK FATAQMELQN
YRNDILNGGW KEIDLRGPRR PRGLMKTLIK QYGLTLENLV EDSGLQSILL NHKRQTVKII
GESGAVEKAC QLIDGLSDSL LETFHYANNS ESAAGEPGDE LPECCACICP IDSLAELYRL
ENCSHAYCLG CFKQQIQVAI QSKDLPILCS EESCQEPFTW VDFKHSFTKV QIDPRALIRA
AVTKFMLKSG RGTYHHCLTP DCPVIYKTNT ENTQYICEEC GIRICSSCHI EYHDGLSCAM
YKSQERDKEE IEAYLRSHAD TIKPCPQCEF PIEKNRGCNH IVCHACKVDF CWLCTATFVS
ADECYDHLHQ KHGGIADIGD ILYD
//