ID A0A433U5B7_ELYCH Unreviewed; 1034 AA.
AC A0A433U5B7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 02-APR-2025, entry version 22.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=EGW08_003254 {ECO:0000313|EMBL:RUS89007.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS89007.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS89007.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS89007.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS89007.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RUS89007.1}.
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DR EMBL; RQTK01000069; RUS89007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433U5B7; -.
DR STRING; 188477.A0A433U5B7; -.
DR OrthoDB; 6152076at2759; -.
DR Proteomes; UP000271974; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000271974};
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 615..842
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 129..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..143
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..180
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 116833 MW; 16D3F77D983E7D0E CRC64;
MVLKKSNSGL NSGATQHVRR GGFIDPRTHL RHTSLYGSIE VSVEMPTIEM ADEVDACLEE
INGYLDFTWP RFPSSRKGWN RTSSVSCDKG GNWQLKQRLH DLMKDIEFLR YVSGTIDIHF
TEISENLAKG RSETSSTKTK TSSQILKEFE SEENEREKAR LAREGVQSKK RQTYHGRGVQ
RRYQSTLNKQ SDRNDNQRVD ESASELKPTL TFTFHNPCAV DARASKLCKD GDKYDRWYCQ
GLKSLKKSKG FVNGMRSENR DFTHNVIKDT EGLHFRDQQR TLNVDDVSFS EIEACEDCSD
PSYTFSLGDF ITKNKAMKRK HTSRKSEHVP LPSKEAIFWD KSKHPKGSYI YIEPDSDSSL
LDSSWEVIEI PVAGDLENDC QADFPNNGED KADRENIHGA SVELHSKPME ISAEDVTQEQ
ENVSKSFTEC FVGVQASMPG DGITLFPETL DRLQLHGRSN VTVGDSLPHC FSISPSHHSL
NKPYIVARRA SKDGKTWLFS LQGSSELKRE HFRSKLSRLH QSDEKISLVQ AIKVAEEVLN
SGEDCQEVVD IDSGDTGHAE SKDSELDAWV DLASKFMQEV SIHTVEEAAE KMILPSAQPK
RSGVESKHGA PNISEDIECG VCFSPCNLYG KSEEESAMML LSCGHLHCIG CWRAHVYHSI
NSGAPKISCM TNGCDAVLDE TTLKTLAPVS MVTLWQARLR DRLLQSSQHT SWCPHARCGH
VAISRGTPLK KQFGSPLVCR CLRSWCSNCQ EDPHWPVSCD QMAAYKKLLS KAGKDSYLPV
AQISFVIDMK KCPKCKYPIE KFQGCPSMVC RMCWHNFCWN CLQSTEKHNV YTCKVSPSSN
FITFQLHNKL LYDFPIEYFI ESLQTNKQRE LLRQKRNWLH TLRGSLQSKF SLHRLLSSRK
VGGFSSHVAV TSTLELIDEV LAFMKRAFTH IELFYILLGF AELNKTKSAA RLVAATNRKV
SRLHFIVDRL STHIVGRSLS HISSMNKQAR ILLKTGSSTL DELFGLAPQL QNVSKDVATA
WIAEIDPSKH LHYK
//
