ID A0A162AR71_DAUCS Unreviewed; 543 AA.
AC A0A162AR71;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 18-JUN-2025, entry version 41.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=DCAR_0206205 {ECO:0000313|EMBL:WOG86986.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:WOG86986.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:WOG86986.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:WOG86986.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
RN [2] {ECO:0000313|EMBL:WOG86986.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:WOG86986.1};
RA Iorizzo M., Ellison S., Senalik D., Macko-Podgorni A., Grzebelus D.,
RA Bostan H., Rolling W., Curaba J., Simon P.;
RT "Draft title - Genomic analysis of global carrot germplasm unveils the
RT trajectory of domestication and the origin of high carotenoid orange
RT carrot.";
RL Submitted (MAR-2022) 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}.
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DR EMBL; CP093344; WOG86986.1; -; Genomic_DNA.
DR EnsemblPlants; KZN04673; KZN04673; DCAR_005510.
DR Gramene; KZN04673; KZN04673; DCAR_005510.
DR KEGG; dcr:108209852; -.
DR OMA; ICFESLP; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000077755; 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:UniProtKB-UniPathway.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd22583; Rcat_RBR_ARI7-like; 1.
DR CDD; cd23141; RING-HC_ARI6-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; 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 SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 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:UP000077755};
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 REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..40
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..543
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 62020 MW; 33FEC0E1AE5AF0C1 CRC64;
MGSEDDMHDC NDLEEFYSSS DNDVENDSDN DYVYDNDSDD ASPKLVSIRQ QKNYIVLKEE
DIRRRQEDDI VRISAVLSIP RVAACMLLRQ YKWSVNNVHE AWFSDEDGVR KAVGLVEEQA
VKSQNDRELI CEICFEPYPV DKINSAACGH PYCGTCWAAY ISTSINDGPG CLTLRCPDPS
CNAAVSQDMI NTLVSSEDRE KYYRYLRRSY IEDNRKTKWC PAPGCDCAIE FDVGSGSHDV
SCLCSYSFCW NCTEEAHRPV DCETVSKWIL KNTAESENMN WILANSKPCP KCKRPIEKNQ
GCMHMTCTPP CKFEFCWLCL GVWAEHGERT GGFYACNRYE AAKQEGAYDE SEKRREMAKN
SLERYTHYYE RWATNQSSRQ KAVADLHQMQ TVHLEKLSEK HKVPESQLKF VVEAWSQIVE
CRRVLKWTYA YGFYLPEDEL AKRQFFEYLQ GEAEANLERL HQCAEKELQN YLGDGTSEDF
NSFRTKLAGL TSVTRNYFEN LVRALENGLS DVNSTGASSM KPSSKFVAGS SNAKSGKNSS
SKI
//
