ID A0A6J1L0M1_CUCMA Unreviewed; 590 AA.
AC A0A6J1L0M1;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC111499954 {ECO:0000313|RefSeq:XP_023007471.1};
OS Cucurbita maxima (Pumpkin) (Winter squash).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3661 {ECO:0000313|Proteomes:UP000504608, ECO:0000313|RefSeq:XP_023007471.1};
RN [1] {ECO:0000313|RefSeq:XP_023007471.1}
RP IDENTIFICATION.
RC TISSUE=Young leaves {ECO:0000313|RefSeq:XP_023007471.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
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 RefSeq; XP_023007471.1; XM_023151703.1.
DR AlphaFoldDB; A0A6J1L0M1; -.
DR GeneID; 111499954; -.
DR KEGG; cmax:111499954; -.
DR OrthoDB; 10009520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000504608; Unplaced.
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; cd22586; Rcat_RBR_ARI1-like; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR FunFam; 1.20.120.1750:FF:000013; 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; IPR054694; Parkin-like_IBR.
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; PF22605; IBR_2; 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:UP000504608};
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 115..329
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 119..167
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 540..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 68052 MW; F8D7C534B37AADF8 CRC64;
MEDCISSDED YYDSDRESLH GLENEDSEIQ WIPKSSATKV ITKECLLAAQ KEDMRRVMDM
LSLREYHART LLIHYRWDVE KLFAVLVEKG RHHLFATSGV TMIGNQSISS SEPSSMVMCD
ICMEEVHGND ATRVDCGHCF CNNCWTEHFI VKINEGQSRR IRCMAHKCNA ICDEAVVRNL
VSKRHPDLAN KFDRFLLESY IEDNKRVKWC PSTPHCGNAI RVEDDEFCEV ECSCGLQFCF
SCLSEAHSPC SCLMWELWIK KCRDESETVN WMTVHTKPCP KCHKPVEKNG GCNLVSCICG
QAFCWLCGGA TGREHTWSSI SGHSCGRYKE ESAQKAERAK RDLYRYMHYH NRYKAHTDSC
KLESKLKESI QEKISISEER ESMLRDFSWV NNGLHRLFRS RRVLSYSYPF AFYMFGDELF
KDEMTEEERE IKQHLFEDQQ QQLEANVEKL SKFLEEPFDQ YAKDKVMEIR MQVINLSVIT
DTLCKKMYDC IENDLLGSLE LGIHNIAPYK SKGIEKALEL SACWNSKTNT TIDKYLPSDC
STSGGLSERD RLSGLNSEEN GCSSRKRARA DVVTGNFFDL NLPAEVVDRN
//
