ID A0A8T1NPQ7_CARIL Unreviewed; 566 AA.
AC A0A8T1NPQ7;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 02-APR-2025, entry version 13.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=CIPAW_13G106600 {ECO:0000313|EMBL:KAG6631681.1};
OS Carya illinoinensis (Pecan).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Carya.
OX NCBI_TaxID=32201 {ECO:0000313|EMBL:KAG6631681.1, ECO:0000313|Proteomes:UP000811609};
RN [1] {ECO:0000313|EMBL:KAG6631681.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG6631681.1};
RA Platts A., Shu S., Wright S., Barry K., Edger P., Pires J.C., Schmutz J.;
RT "WGS assembly of Carya illinoinensis cv. Pawnee.";
RL Submitted (DEC-2020) 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:KAG6631681.1}.
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DR EMBL; CM031821; KAG6631681.1; -; Genomic_DNA.
DR Proteomes; UP000811609; Chromosome 13.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
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; cd22582; BRcat_RBR_unk; 1.
DR CDD; cd22584; Rcat_RBR_unk; 1.
DR FunFam; 1.20.120.1750:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000230; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.420.10:FF:000076; RBR-type E3 ubiquitin transferase; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF13456; RVT_3; 1.
DR SMART; SM00647; IBR; 2.
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:UP000811609};
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 316..533
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 320..364
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 543..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 64565 MW; 7D3385BA246D5346 CRC64;
MDNSTEAQYY DGDLPYLFSD HRLELELMAA EELDSDLDLA FRIQLEEALA ASLAFHPSAS
TSTSSNFLVD SHLTSESDGF SKISGLQSDE LARFEQEVED LEISGAEVLR LTGELRRQIL
NERAAREILR IEEEDWRDWS VNYEKPFDYG EGSSKSKSLA ESDEVFGLYF KGIVSEERVR
GETTVLAGIG VAICDSRGKL ILEVSKPLLG NGKSKNAAAA KALIEGLNAA LGLELKRITI
YCDYHPLYQF IIGRWLPRQR KISELVDEVT ILEEKFIYFN PKMVARNDIK YAFELARDAI
VSQISSPAES SQAKNLTKNC VICLEDTDIG RMFSVDGCLH QYCFSCMKQH VEVKLLHGMV
PKCPHEGCKS ELVVESCRKF LTPKAIDTFS QRLREASIPV TERVYCPYPR CSTLMSESGV
LEYAKDFLDV ERTGARKCMK CHGLFCITCK VPWHSNMTCH DYKMLNPLPP SEDVKLKSLA
TRNLWRQCVK CNHMIELAEG CFHMTCRCGN EFCYNCGAEW KNKQATCSCP LWDEDHIWLE
QDRQFDEEDE EEDEDDEYYD SDLDFY
//
