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Database: UniProt
Entry: A0A8K0HZV1_COCNU
LinkDB: A0A8K0HZV1_COCNU
Original site: A0A8K0HZV1_COCNU 
ID   A0A8K0HZV1_COCNU        Unreviewed;       591 AA.
AC   A0A8K0HZV1;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   18-JUN-2025, entry version 15.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=COCNU_02G012690 {ECO:0000313|EMBL:KAG1331301.1};
OS   Cocos nucifera (Coconut palm).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Arecaceae; Arecoideae; Cocoseae;
OC   Attaleinae; Cocos.
OX   NCBI_TaxID=13894 {ECO:0000313|EMBL:KAG1331301.1, ECO:0000313|Proteomes:UP000797356};
RN   [1] {ECO:0000313|EMBL:KAG1331301.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spear leaf of Hainan Tall coconut
RC   {ECO:0000313|EMBL:KAG1331301.1};
RX   PubMed=29048487;
RA   Xiao Y., Xu P., Fan H., Baudouin L., Xia W., Bocs S., Xu J., Li Q., Guo A.,
RA   Zhou L., Li J., Wu Y., Ma Z., Armero A., Issali A.E., Liu N., Peng M.,
RA   Yang Y.;
RT   "The genome draft of coconut (Cocos nucifera).";
RL   Gigascience 6:1-11(2017).
RN   [2] {ECO:0000313|EMBL:KAG1331301.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spear leaf of Hainan Tall coconut
RC   {ECO:0000313|EMBL:KAG1331301.1};
RA   Yang Y., Bocs S., Baudouin L.;
RL   Submitted (JUL-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:KAG1331301.1}.
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DR   EMBL; CM017873; KAG1331301.1; -; Genomic_DNA.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000797356; Chromosome 2.
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   CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR   CDD; cd22583; Rcat_RBR_ARI7-like; 1.
DR   FunFam; 1.20.120.1750:FF:000005; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR048962; ARIH1-like_UBL.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   Pfam; PF21235; UBA_ARI1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS01358; ZF_RANBP2_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:UP000797356};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KAG1331301.1};
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          130..343
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          134..178
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..48
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  67288 MW;  87BB595F49A549A4 CRC64;
     MDSEDDMHDA NDLESLDDDF YSGETAMGSD DGDAGYDFVD NESDDSEDIT SHRQQQNYTI
     LSEVDIRQHQ EEDINRVSIV LSISRSAACI LLRHYNWSVS KVHDEWFADE ENVRKAVGLL
     ENPVEMQNAR ELSCGICFEN YPHNNMSTAA CGHHFCGSCW RGYIGTSISD GPGCLMLRCP
     DPSCSAAVGQ DMINILATDE DKEKYSRYLL RSYIEDNRKT KWCPAPGCDF AVEFVMGSGN
     YDVCCNCSYN FCWNCTEEAH RPVDCGTVAK WILKNSAESE NMNWILANSK PCPKCKRPIE
     KNQGCMHITC TPPCKYEFCW LCLGAWSEHG ERTGGFYACN RYESAKQEGA YDESERRREM
     AKNSLERYTH YYERWATNQS SRQKALADLH SMQTEKLEKL SDRQSQPESQ LKFIIEAWLQ
     IVECRRVLKW TYAYGYYLPE HEHAKRQFFE YLQGEAESGL ERLHQCAEKE LQVYLDAETP
     MKDFNDFRTK LAGLTSVTRN YFENLVRALE TGLKDVGSSN SQATCSKTSS SKCLGGKSKI
     GKIKAGGTTS RSGGPSRSLD ESNLWSCDQC TYVNPRSTNT CQMCEHRRCT T
//
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