ID A0A836DQM2_9ROSI Unreviewed; 330 AA. AC A0A836DQM2; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 22-FEB-2023, entry version 6. DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483}; DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483}; GN ORFNames=IMY05_010G0037600 {ECO:0000313|EMBL:KAG5236343.1}; OS Salix suchowensis. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Salix. OX NCBI_TaxID=1278906 {ECO:0000313|EMBL:KAG5236343.1, ECO:0000313|Proteomes:UP000664337}; RN [1] {ECO:0000313|EMBL:KAG5236343.1, ECO:0000313|Proteomes:UP000664337} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XY12 {ECO:0000313|EMBL:KAG5236343.1}; RX PubMed=32257231; RA Wei S., Yang Y., Yin T.; RT "The chromosome-scale assembly of the willow genome provides insight into RT Salicaceae genome evolution."; RL Hortic Res 7:0-0(0). 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily. CC {ECO:0000256|ARBA:ARBA00024209}. 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:KAG5236343.1}. 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; JAEQKX010000010; KAG5236343.1; -; Genomic_DNA. DR AlphaFoldDB; A0A836DQM2; -. DR Proteomes; UP000664337; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro. 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; SM00184; RING; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175}; KW Reference proteome {ECO:0000313|Proteomes:UP000664337}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00175}; KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}. FT TRANSMEM 40..61 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 134..176 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" SQ SEQUENCE 330 AA; 36348 MW; 1116F3A63DF6CB0B CRC64; MDLVISKSYG AQSPPPLTSP VDSSSIFGPR TQSSDTSFPV LAIAIIGILA TAFLLVSYYI FVIKCCLTWH RIDLLRRFSL SRNRNHEDPL MAYSPAAIES RGLDESVIRS IPVFKFKKEG DNVGNFGERS FTECAVCLNE FQEAEKLRRI PNCSHAFHID CIDVWLQSNA NCPLCRTSIS STTRFPMDHI IAPSSTPQDA NPYTESVMGG DEDYVVIELS NHNSTDQTLL AAQERLNSGE LSVRSISPSP RKMEQRVGHK KARNLSKVLF NGLVGRSAAL FINSRDSAAE QAVTEVSPAE DCSGRARRAF FSFGHGRGSR SSVLPVSLEP //