ID A0A654FK11_ARATH Unreviewed; 812 AA. AC A0A654FK11; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 08-NOV-2023, entry version 17. DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483}; DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483}; GN ORFNames=AN1_LOCUS16604 {ECO:0000313|EMBL:VYS61171.1}, C24_LOCUS16483 GN {ECO:0000313|EMBL:CAA0388034.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702 {ECO:0000313|EMBL:VYS61171.1, ECO:0000313|Proteomes:UP000426265}; RN [1] {ECO:0000313|EMBL:VYS61171.1, ECO:0000313|Proteomes:UP000426265} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. An-1 {ECO:0000313|Proteomes:UP000426265}, and cv. C24 RC {ECO:0000313|Proteomes:UP000434276}; RA Jiao W.-B., Schneeberger K.; RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases. 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}. CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family. CC {ECO:0000256|ARBA:ARBA00035113}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CACSHJ010000089; CAA0388034.1; -; Genomic_DNA. DR EMBL; CACRSJ010000106; VYS61171.1; -; Genomic_DNA. DR RefSeq; NP_191783.1; NM_116089.3. DR AlphaFoldDB; A0A654FK11; -. DR EnsemblPlants; AT3G62240.1; AT3G62240.1; AT3G62240. DR GeneID; 825397; -. DR Gramene; AT3G62240.1; AT3G62240.1; AT3G62240. DR KEGG; ath:AT3G62240; -. DR OMA; NANRIPH; -. DR OrthoDB; 3059402at2759; -. DR Proteomes; UP000426265; Unassembled WGS sequence. DR Proteomes; UP000434276; Unassembled WGS sequence. DR ExpressionAtlas; A0A654FK11; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro. DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro. DR CDD; cd16615; RING-HC_ZNF598; 1. DR InterPro; IPR041888; RING-HC_ZNF598/Hel2. DR InterPro; IPR044288; ZNF598/Hel2. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR001841; Znf_RING. DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1. DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1. DR SMART; SM00355; ZnF_C2H2; 4. DR PROSITE; PS50089; ZF_RING_2; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; 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 5..46 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT REGION 300..326 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 341..372 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 392..425 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 437..576 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 648..812 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 306..326 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 358..372 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 410..425 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 437..506 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 518..576 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 676..690 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 709..729 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 730..748 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 812 AA; 90224 MW; 5D0BB49CF38A6CC7 CRC64; MDDSCAVCAD NLEWVAYGSC GHREVCSTCV VRLRFVLDDP RCCICKTESP IVFVTKALGD YTRTINDFST FPSAPREGRV GAFWYHEDTQ AFFDDLDQYR MIKAMCRLSC GVCDKTEDKP REGGPRHHRQ RIKSVEQLKG HLYHKHKLHM CGLCLEGRKI FICEQKLYTR AQLNQHIQTG DSEVDGSESE RGGFAGHPMC EFCRNPFYGD NELYTHMSTE HYTCHLCQRS QPGQYEYYKN YDDLEIHFRR DHFLCEDDSC LAKKFTVFQN ESELKRHNAI EHGGKMSRSQ RSAALQIPTS FRYSRGNDQE NRRGRPRSFR REPGDEEYNL AVHAALRLSE SEYSRQEPAP PPSSAPPGFS ENNNIHVDDT DPLIQPMESL STTDMEPSSR YLQAVGSFGG GGSRLGESAF PPLSGQQSSG QNVESLPTNT MAARLRRQTN RTSTASAIAS PSQGWPVINR GPGQASITSG GNHSSSGWPA IGRTPVQASS SSVQSRSHNR VSQPRPLASA VPQAARNANR IPHSSSAPNL SDTRSLQPSH SDFPPVSSAV VQNRKTSSTT TQGSSNTQPP PDVQSANKSL IEKMRSALGH DEDVFVAFRN ISGQYRQGSI DAKTYLEYVQ GYGLSHLVID LARLCPDPKR QKELIDTHNA SLREEDSKDN GRSAAQSSSQ PKESQSSKKN KGKAVKVVDP KETLADNFMD TVRRLQSSQN PQEEEEEAIS KDKNTYRSDK GKSQVVGTDS SSTGSKQQRK KTSKFHRVRL GDGSMAALLD LNNSTRESEQ ESKDSNSNSN QNQTGGLPVR GVWRKGGANL FS //