ID A0A5N6KQ03_9ROSI Unreviewed; 485 AA.
AC A0A5N6KQ03;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 02-APR-2025, entry version 17.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=FH972_021677 {ECO:0000313|EMBL:KAB8338732.1};
OS Carpinus fangiana.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Betulaceae; Carpinus.
OX NCBI_TaxID=176857 {ECO:0000313|EMBL:KAB8338732.1, ECO:0000313|Proteomes:UP000327013};
RN [1] {ECO:0000313|EMBL:KAB8338732.1, ECO:0000313|Proteomes:UP000327013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cfa_2016G {ECO:0000313|EMBL:KAB8338732.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAB8338732.1};
RA Yang X., Wang Z., Zhang L., Hao G., Liu J., Yang Y.;
RT "A chromosomal-level reference genome of Carpinus fangiana (Coryloideae,
RT Betulaceae).";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates.
CC {ECO:0000256|ARBA:ARBA00003976}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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:KAB8338732.1}.
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DR EMBL; VIBQ01000010; KAB8338732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6KQ03; -.
DR OrthoDB; 9977870at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000327013; 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:UniProtKB-UniPathway.
DR CDD; cd20335; BRcat_RBR; 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; IPR001841; Znf_RING.
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 SMART; SM00647; IBR; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000327013};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 155..353
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 159..203
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 95..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 52707 MW; DE265159039E2C83 CRC64;
MAEPQQHVDR GEDHESAVSL LAMQLDNLNT LLSDLPEGQN NEDVDLRAVL LAQREEVESS
LASTRDRALC ISISKAVETD GPLISLAQAH ELHQKPTDTH ADEAEPTMQP AEDSDSHGSG
QHVDVHPDRL IEHLWSYNIV PQPPLDEASA GTPTAELECS VCLEKNPATQ SYNSPCGHVY
CHVCLRRVFH EATLNGPYLE PYCCDTPIPL ATVNTLVGPS ILAKHQLATL EHSSTDRTYC
ANTHCASFIP PHLTHKTLAT CHNCHHRTCI LCKSTSHPGA VCDRTADDPI LQLADQEGWR
RCYQCRTLVE LETGCYHMTY LLPLLLLFIR SHQTNTPQLP LRRGVLLPVR RPLADLRVPA
LHHPPKRHPP ASMTAGSTSL GGSSAASASA GCRASSASAG GAGCVPAASA MWRFDGVEDA
RHESREGRNW EEGSRAVNCV GQGLKMADCV YIEHTIEQSR NNLQVWGHGS GSAPLTSLSG
RQADA
//
