ID W1NIZ3_AMBTC Unreviewed; 332 AA.
AC W1NIZ3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=AMTR_s00009p00263210 {ECO:0000313|EMBL:ERM95169.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERM95169.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(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};
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DR EMBL; KI397501; ERM95169.1; -; Genomic_DNA.
DR RefSeq; XP_006827753.1; XM_006827690.1.
DR AlphaFoldDB; W1NIZ3; -.
DR STRING; 13333.W1NIZ3; -.
DR EnsemblPlants; ERM95169; ERM95169; AMTR_s00009p00263210.
DR GeneID; 18423090; -.
DR Gramene; ERM95169; ERM95169; AMTR_s00009p00263210.
DR KEGG; atr:18423090; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_072423_0_0_1; -.
DR OrthoDB; 415856at2759; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF238; RING_U-BOX SUPERFAMILY PROTEIN; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 282..324
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 132..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 38218 MW; 60433E85C577537D CRC64;
MGSYNNIGYR LSTDVCSVST VQSHQNVVIR VFVKKRTIFT NLTSQDADFL DSIDFFALEL
ATSITQHLQT QERAYMYLLL ALVEHIPIPL QIIRGLSWEI ACQACDNARS LDQPNIQVQL
RFFIDIKHER EIAEGDHSEP ETEYETRQEE EELPEAETEY EDLQEVEEIL EAETEYEDPQ
REEEIPEAET EYEAPQEEEI PEAEMHELGI LMELELELGI FMEVTSQYIF EGEFRQMETD
NLEHLIGIEA SSQVDCTPRT VARSIVDSLA KADIKAEEEV LCTVCLCNIN ASDGDGRVLP
CSHMYHEDCI YEWLKSRNSC PVCRFEFPAN LP
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