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Database: UniProt
Entry: A0A2P5ETT7_TREOI
LinkDB: A0A2P5ETT7_TREOI
Original site: A0A2P5ETT7_TREOI 
ID   A0A2P5ETT7_TREOI        Unreviewed;       545 AA.
AC   A0A2P5ETT7;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   18-JUN-2025, entry version 25.
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=TorRG33x02_151890 {ECO:0000313|EMBL:PON88960.1};
OS   Trema orientale (Charcoal tree) (Celtis orientalis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Trema.
OX   NCBI_TaxID=63057 {ECO:0000313|EMBL:PON88960.1, ECO:0000313|Proteomes:UP000237000};
RN   [1] {ECO:0000313|Proteomes:UP000237000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) 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:PON88960.1}.
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DR   EMBL; JXTC01000099; PON88960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5ETT7; -.
DR   STRING; 63057.A0A2P5ETT7; -.
DR   InParanoid; A0A2P5ETT7; -.
DR   OrthoDB; 10009520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000237000; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; IPR048962; ARIH1-like_UBL.
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   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; PF22191; IBR_1; 1.
DR   Pfam; PF21235; UBA_ARI1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:PON88960.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237000};
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          113..338
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          117..170
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   545 AA;  63449 MW;  445C4F5F4BE7B3FF CRC64;
     MESPETSLKP FDENDAVAGV FFDRFVREEE TSEAGQQNYV ILNEAEIRHR QEDDILRVST
     ALSEPRAAAI VLLRHFNWNL SKLFDNWFDD EDRVRNEVGL FRSPIVAQFS PDCTITCGIC
     FESYNNSMSR SSSSSSMVWA SCGHPFCRDC YGGYITKSVN DDGPGCLLLR CPDPSCAAAV
     GEDMIGTLTM DNSVKLKYSR YLLRSYVEDS YRRRKIKWCP APGCDYAVDF FDFVGNCRRG
     FDVYCRCSFN FCWNCNEEAH RPVDCDTVAK WNMKNKDESE NANWILVNTK PCPQCKRVIE
     KSHGCNHMRC APPCRYEFCW HCLGEWTSKT FHSCNKFLPE ATTADENEMK RREVVKASLV
     KYTHYYNRWA ANLRSRQKAV EGLRLVQVEY LDKLSFFYGQ ERPLLRFLTE AWQQIIRCRR
     VLQWTYAYGY YFPQHQWTKQ QFFEYLQGEA EFSLERLHYC AEKELEKYVN GEGTVQEFID
     YRLKLAELTS VIGNYFKNLV RALEDGLTEV ESNGSYWSCE LCSFVNSLPT ARCQMCYHSP
     VAVNL
//
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