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Database: UniProt
Entry: A0A1R3IYK6_COCAP
LinkDB: A0A1R3IYK6_COCAP
Original site: A0A1R3IYK6_COCAP 
ID   A0A1R3IYK6_COCAP        Unreviewed;       620 AA.
AC   A0A1R3IYK6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   02-APR-2025, entry version 35.
DE   RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1 {ECO:0000256|ARBA:ARBA00017887};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=CCACVL1_08847 {ECO:0000313|EMBL:OMO87651.1};
OS   Corchorus capsularis (Jute).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO87651.1, ECO:0000313|Proteomes:UP000188268};
RN   [1] {ECO:0000313|EMBL:OMO87651.1, ECO:0000313|Proteomes:UP000188268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC   TISSUE=Whole seedling {ECO:0000313|EMBL:OMO87651.1};
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.;
RT   "Corchorus capsularis 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:OMO87651.1}.
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DR   EMBL; AWWV01009187; OMO87651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3IYK6; -.
DR   STRING; 210143.A0A1R3IYK6; -.
DR   EnsemblPlants; OMO87651; OMO87651; CCACVL1_08847.
DR   Gramene; OMO87651; OMO87651; CCACVL1_08847.
DR   OMA; CAMCTEA; -.
DR   OrthoDB; 10009520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000188268; Unassembled WGS sequence.
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   FunFam; 1.20.120.1750:FF:000027; 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; IPR054694; Parkin-like_IBR.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
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; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22605; IBR_2; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00547; ZnF_RBZ; 2.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 2.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188268};
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:PRU00322}.
FT   DOMAIN          141..350
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          145..191
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          303..346
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          567..591
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..19
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..49
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  70079 MW;  1A0882EB3E58D9AF CRC64;
     MAASDNEYLS DNDDGEDDSF CYYGAESGDE SLQDAGIDDE GELPDDEEAE RVPQGLHDNR
     VVLTEVDIRQ RIKDDIDEVK NHIDEVSSVA SNISKDEASI LLLHYNWSVS KVHDAWFLDE
     NEAREKAGLP VKPLVELSDH DEILCGICFD TYPFDGIKST GCGHPYCNEC WGSYIKTAIA
     DGPGCLFLRC PEPSCNAAVT KDLVGLFASE EEKSKYSNFL VSSYIEENKW IKNCPGPGCE
     NAIEFDAGIG NKDVFCSCTH SFCWNCTEGG HRPVDCETVK KWMAKNSSEA ENVNYILAFT
     KPCPKCKKPI EKNLGCNHMT CRAPCHHQFC WICLENWKDH RWNYSCNRFN KADENKRKKA
     KDYLERYTHY YERWATNQNS MKRAIADMKR VEVVETEILG EVQVQPASQL SFLTEAWQQI
     VECRKILAWT YAFGYYLADE DAAKKNLFEF LQGHAETSLE RLHHCAEKEL KPLLEQQSPV
     QFSEFRKKLC QLTRVTKHFF DNLVAGLENG LAEANSIDAP RPSKKPRRDY QSNKFANANY
     RADHQRFAFA SGAAATTSQS FQLPAMATGP WSCAYCTLVN DESATSCTVC GRGSWTCDIC
     TFANPRTVST CQMCSEADDI
//
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