ID W1PDF0_AMBTC Unreviewed; 399 AA.
AC W1PDF0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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_s00012p00250160 {ECO:0000313|EMBL:ERN07957.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN07957.1, 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; KI393609; ERN07957.1; -; Genomic_DNA.
DR RefSeq; XP_006846282.1; XM_006846219.2.
DR AlphaFoldDB; W1PDF0; -.
DR EnsemblPlants; ERN07957; ERN07957; AMTR_s00012p00250160.
DR GeneID; 18436197; -.
DR Gramene; ERN07957; ERN07957; AMTR_s00012p00250160.
DR KEGG; atr:18436197; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_040377_0_0_1; -.
DR OMA; HAESHCA; -.
DR OrthoDB; 469114at2759; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd16667; RING-H2_RNF126-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR010543; DUF1117.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF234; OS05G0110000 PROTEIN; 1.
DR Pfam; PF06547; DUF1117; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 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 182..223
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 52..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 43221 MW; 10B789F427B71403 CRC64;
MSSSPSNSSS YWCHRCNRFV QVSSDPICPD CQSGFVEEMS SRRRRSIPAA MYMVGNNPNP
NPNPNPNPHS EPRRRSRTNA DRTPFNPVIV LRGPSDGADG AENGSFELYY DDGVGSGLRP
LPTSMSDFLM GSGFERLLDQ LTQLELNGGA GRCEPPPASK QAVESMPTVK IVSSHVSMES
HCAVCKDPFE LGSDAREMPC KHIYHQDCIL PWLSLRNSCP VCRHEMPPES HNEIDRNRSS
ETVPENGEEE TVGLTIWRLP GGGFAVGRFS GGSPAVSGRH PVVYTEMDGG FNSNGVSRRV
SWGSRVSRPR QSGGIGNAFR SFFSFFGRLG RGSSSNSNSR SNLSSAGSGS GSPALSSSAS
SRSSSENGSS RRSRSVFSRS SRRRGGAWDI ETGASLPRW
//
