ID A0A8T2STG5_CERRI Unreviewed; 612 AA.
AC A0A8T2STG5;
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_18G039300 {ECO:0000313|EMBL:KAH7365643.1};
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:KAH7365643.1, ECO:0000313|Proteomes:UP000825935};
RN [1] {ECO:0000313|EMBL:KAH7365643.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Whitten #5841 {ECO:0000313|EMBL:KAH7365643.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAH7365643.1};
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:KAH7365643.1}.
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DR EMBL; CM035423; KAH7365643.1; -; Genomic_DNA.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000825935; Chromosome 18.
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; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001876; Znf_RanBP2.
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 SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 3.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 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}.
FT DOMAIN 160..373
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 70135 MW; FC52D14484C73C30 CRC64;
MESEEDMLDA RSATSDDGFY PNNDDECDSD RMSMGYRYEE EDDDDGMDGD EDAYEDDFLQ
YGSDEDALHS GRPSYTGRQL PYTVLTEEAI TERQDAAIES VASVLSISRA QACLILRKHE
WCVSRVNEEW FADESRVRNC VGLIEKSIKP SMTGQRDIRE QIKCGICLEY HRIETMQACC
CDHYFCQSCW RAYAHTAICD GPGCLSLRCP NPDCNAAVGD ELILKLVLEE DKRKYRHYIT
RSYVEENRRA KWCPAPGCEY AIEFTPGGDI QDVTCNCGHN FCWNCSEEAH RPVECVTVER
WILKNSAESE NMNWILANSK PCPKCKRPIE KNLGCMHITC TPPCKFEFCW LCLGAWSEHG
ERTGGFYACN RYEAEKKEGK HDETERRREM AKNSLERYTH YYERWASNEQ SKAKALSDLK
QLQITQLEKL SDKHSLPMSQ LKFLVEAWLQ IVECRRVLKW TYAYGYYLPE NEATKKQFFE
YLQGQAETAL ERLHQCAEKE VKAHLDGDAS NVTFTDFRTK LAGLTSVTKN YFQRLVDAFE
NGLAEVKDST AVNTTVQASV KGKCSRSKAS SSRSNNASRV VDDEGHWYCR HCTFANTGCS
TTCSMCHLET MI
//
