ID A0A0L9V717_PHAAN Unreviewed; 538 AA.
AC A0A0L9V717;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HKW66_Vig0141340 {ECO:0000313|EMBL:KAG2397630.1},
GN LR48_Vigan08g155400 {ECO:0000313|EMBL:KOM50727.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM50727.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN [2] {ECO:0000313|EMBL:KOM50727.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:KOM50727.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2397630.1, ECO:0000313|Proteomes:UP000743370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2397630.1};
RA Xiang H.;
RT "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL Submitted (MAY-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 -!- 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; JABFOF010000005; KAG2397630.1; -; Genomic_DNA.
DR EMBL; CM003378; KOM50727.1; -; Genomic_DNA.
DR RefSeq; XP_017433724.1; XM_017578235.1.
DR AlphaFoldDB; A0A0L9V717; -.
DR STRING; 3914.A0A0L9V717; -.
DR EnsemblPlants; KOM50727; KOM50727; LR48_Vigan08g155400.
DR GeneID; 108340707; -.
DR Gramene; KOM50727; KOM50727; LR48_Vigan08g155400.
DR KEGG; var:108340707; -.
DR OMA; WGDCFER; -.
DR OrthoDB; 2943236at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053144; Chromosome 8.
DR Proteomes; UP000743370; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd22582; BRcat_RBR_unk; 1.
DR CDD; cd22584; Rcat_RBR_unk; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR11685:SF457; TRANSLATION TERMINATION INHIBITOR PROTEIN ITT1; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF13456; RVT_3; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 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:UP000053144};
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 295..519
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 299..343
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 538 AA; 61626 MW; 7701F0B83435BD63 CRC64;
MDFREDFTFL SEQRREFATA EVIESDLEFA FDLQLQEALE ASLALNPSSS SAVIEQPTVD
ELNATSVQSE ELARVECEMK DKEQSEREMQ KMREDLCRRI HDEKVARDIL TISEADWQQW
GDNFEKPFGE GSSSSGRTET EEGWVRVYLK GLVSEENVRG EKVVLSGIGF AICDRSDNLI
FEVSKSVIEN GTSKVAVEIK ALIEAFNMVL ALELKRIVYY TDYYPLLQYV RGNWSAKQRK
IAMLVDQVHL LQRKFTYCDS RLLARNDVKF AFKLARDAIV SQSMRPSGPG STRSLNENCA
ICLEDTDVSQ IFSVDGCQHR YCFSCMKQHV EVKLLHGMVP KCPHEGCKYE LLVDSCQKFL
TQKLTDIMRQ RQAEASIPVA EKVYCPYPRC SALMTKTEVF EYSKNLIGES ELSGPKKCLK
CHGLFCFNCK VPWHSGMTCF MYKTLNPNPP AEDLKLKFLA SRSLWRQCVK CNHMIELAEG
CYHMTCRCGS EFCYNCGAEW KDKKATCSCP LWAEDNIWME ERDLDETDDD DDVFGGWL
//
