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Database: UniProt
Entry: A0A1R3I3V9_9ROSI
LinkDB: A0A1R3I3V9_9ROSI
Original site: A0A1R3I3V9_9ROSI 
ID   A0A1R3I3V9_9ROSI        Unreviewed;       523 AA.
AC   A0A1R3I3V9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   02-APR-2025, entry version 32.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=COLO4_25250 {ECO:0000313|EMBL:OMO77266.1};
OS   Corchorus olitorius.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=93759 {ECO:0000313|EMBL:OMO77266.1, ECO:0000313|Proteomes:UP000187203};
RN   [1] {ECO:0000313|Proteomes:UP000187203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA   Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA   Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA   Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA   Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA   Shommy N.S.;
RT   "Corchorus olitorius genome sequencing.";
RL   Submitted (SEP-2013) 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:OMO77266.1}.
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DR   EMBL; AWUE01018977; OMO77266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3I3V9; -.
DR   STRING; 93759.A0A1R3I3V9; -.
DR   OrthoDB; 9977870at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000187203; 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:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd22582; BRcat_RBR_unk; 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   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; IPR012337; RNaseH-like_sf.
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   Pfam; PF01485; IBR; 1.
DR   Pfam; PF13456; RVT_3; 1.
DR   SMART; SM00647; IBR; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
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:UP000187203};
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          324..523
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          328..372
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          55..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..74
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  59426 MW;  85FFE0A879DFE150 CRC64;
     MAATVGSADS NPDPDDDLLS LLSRQHKELM AAHSLESDLD IAFNLQLQEA LSASLSLHTS
     HPPPPPPPPI PATPPSLNDT VFSLASKELS KTHQESLDHK RCLLETHKLK EDLNRRVHDE
     KFARLIARIP EEQWAEWGDS LERPFGEGCS KAMQCEDDDE YDIDDFSDDD ECEFRIYVKG
     LVSEEKVGNE KSKFAGIGVA ICDFRDNLIL EIKKPLVGDG LNKQAAELKA LIEGLNAALS
     LELNRVQFYC DYYPIYQYVT RRWPPKQRKI SMLVNQVLLL QRKFTYCSPK YVPRNDIKYA
     FKLAREAIDS QVTRPVEQNH VKTVKETCFI CLEDTGFGSM FSVDGCMHRY CFSCMKQHVE
     VKLLHGMVPK CPHEGCKSEL KVDSCGKFLT PKTVETLKHR IKEASIPVSE RVYCPYPRCS
     ALMSKSEVLG YTKDVLVGAE RSGARKCVKC HGLFCINCKV PWHSNMTCHD YKRRNPNPPA
     EDLKLKSLAT MNLWRQCVKC SHMIELSEGC FHITCSEGKT RWF
//
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