ID W1NJG4_AMBTC Unreviewed; 401 AA.
AC W1NJG4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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_s00008p00200880 {ECO:0000313|EMBL:ERM95369.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERM95369.1, 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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KI397486; ERM95369.1; -; Genomic_DNA.
DR RefSeq; XP_006827953.1; XM_006827890.2.
DR AlphaFoldDB; W1NJG4; -.
DR EnsemblPlants; ERM95369; ERM95369; AMTR_s00008p00200880.
DR GeneID; 18423288; -.
DR Gramene; ERM95369; ERM95369; AMTR_s00008p00200880.
DR KEGG; atr:18423288; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_040108_0_1_1; -.
DR OrthoDB; 462403at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd16461; RING-H2_EL5-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044600; ATL1/ATL16-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46913; RING-H2 FINGER PROTEIN ATL16; 1.
DR PANTHER; PTHR46913:SF1; RING-H2 FINGER PROTEIN ATL16; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM01197; FANCL_C; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..193
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 89..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43764 MW; CBD4E6BAC4A9F330 CRC64;
MALFTTKWVE SLDCLKTAIC YGDESCIHDH CFYPPPPPPP PPPLSESHPS TTPSTLVIAI
VTLLTSAFLL ITYYAIFVKY CSFRNSRNSN QPHDHHENND QENNQNQNQN QEPPIHHIWY
ITTVGLEESL IKSITVCKYK GGDGLIEGAD CSVCLSEFNE GEEVRLLPKC SHAFHLPCID
TWLRSHTNCP LCRAPIVSNS DAPTSQDQNG DGVLVSGEIS QQNESYVVVP SGGSEGSSSV
GAGTEDERER GKVGESVAER GRDMTKVGES GAERGRDMTK VGNLERERRG GMGKAGNSNV
SCGFYVLRHL GSAHRLGESM REVKAEAPQA MRRSFSMDFP NGICLSSSDD GGKNQRNGKL
LRDGSEALSF QKGPVAVIRS FSSGKFGFSR HSRGRSSVLP L
//
