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Database: UniProt
Entry: S8E416_9LAMI
LinkDB: S8E416_9LAMI
Original site: S8E416_9LAMI 
ID   S8E416_9LAMI            Unreviewed;       258 AA.
AC   S8E416;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=M569_07753 {ECO:0000313|EMBL:EPS67027.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS67027.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS67027.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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:EPS67027.1}.
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DR   EMBL; AUSU01003345; EPS67027.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8E416; -.
DR   OrthoDB; 67404at2759; -.
DR   Proteomes; UP000015453; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46077; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR   PANTHER; PTHR46077:SF1; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
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          10..51
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   258 AA;  30045 MW;  8A0B0DF506E390E4 CRC64;
     MAGSLGGKRC PICLGGLETR SPSVILPCGH AYCVGCIRRW SDVKCNCPLC NYDFRSWWLC
     RSSVGYGEEE ASPIGRSQKN GSRRRDELLR RRRYQSYERR RIVRRSREDS VGETRSRILP
     KQRSFRRRVD DTPAIVAERT RQWRSSIYRS RLRGVLPPQK HVAEEKESTL KRIGPWIRRE
     LQALLDDPDP TVIVHVVVSI FNAGKLENLR DDQVDDEFLA PLRRFLHDQT EAFWNELICF
     SESRLSIEAY DTVAVYES
//
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