UniProt: V4C6V4

Database: UniProt
Entry: V4C6V4_LOTGI

LinkDB:  V4C6V4_LOTGI 
Original site:  V4C6V4_LOTGI

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (1)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (23)   

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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};
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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
//

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