ID A0A8T2T3W3_CERRI Unreviewed; 565 AA.
AC A0A8T2T3W3;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=KP509_15G024600 {ECO:0000313|EMBL:KAH7404412.1};
OS Ceratopteris richardii (Triangle waterfern).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Parkerioideae; Ceratopteris.
OX NCBI_TaxID=49495 {ECO:0000313|EMBL:KAH7404412.1, ECO:0000313|Proteomes:UP000825935};
RN [1] {ECO:0000313|EMBL:KAH7404412.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Whitten #5841 {ECO:0000313|EMBL:KAH7404412.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAH7404412.1};
RA Marchant D.B., Chen G., Jenkins J., Shu S., Leebens-Mack J., Grimwood J.,
RA Schmutz J., Soltis P., Soltis D., Chen Z.-H.;
RT "WGS assembly of Ceratopteris richardii.";
RL Submitted (AUG-2021) 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:KAH7404412.1}.
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DR EMBL; CM035420; KAH7404412.1; -; Genomic_DNA.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000825935; Chromosome 15.
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 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:UP000825935};
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 136..349
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 140..186
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..558
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 64115 MW; 79FF1E8250590445 CRC64;
MDSEDDMHDA LGSASESEQD DEKDFMPSDD DAHDSAESDY GFDDNGVDDD LQSVSGRSQS
NYSVLSEKDI RLRQEEAIEN VVTILHISPV EASILLRHFK WSVSKVNDEW FTDEDAVRER
VGLLSKQPGE ARREPKDITC GICFESYPPE SMKAMMCRHN FCYSCWKGYI HTAINDGSGC
LSLRCPDPNC HAAVGEDMVR SLVSDEDRTK YTRYVLRSYI EDNRKAKWCP APNCEFAVEF
TLGGGPFDVV CKCGYSFCWN CREEAHRPVD CDTVAKWILK NCAESENMNW ILANSKPCPK
CKRPIEKNQG CMHMTCTPPC KFEFCWLCLG AWSEHGERTG GFYACNRYET AKQEGVYDEA
ERRREMAKNS LERYTHYYER WATNESSRAK AAADLARMQA EQIEKLSDTQ CQPVSQLKFI
TEAWLQIIEC RRFLKWTYAY GYYLPENEVG KRHFFEHLQG DAETALERLH QCAEKDLQVF
LEGDNPNPSF NDFRTKLAGL TSITKTYFEN LVGALENGLS DVDSKVVTKV SSSSSKPSAS
SKGRSKSKAG TSKSGTSRIG DDVNH
//
