ID O01965_CAEEL Unreviewed; 494 AA. AC O01965; DT 01-JUL-1997, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 3. DT 07-APR-2021, entry version 142. DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251}; DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251}; GN Name=ari-1.1 {ECO:0000313|EMBL:CCD61206.1, GN ECO:0000313|WormBase:C27A12.8}; GN ORFNames=C27A12.8 {ECO:0000313|WormBase:C27A12.8}, CELE_C27A12.8 GN {ECO:0000313|EMBL:CCD61206.1}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD61206.1, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC -!- CATALYTIC ACTIVITY: CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798}; 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; BX284601; CCD61206.1; -; Genomic_DNA. DR PIR; H87793; H87793. DR RefSeq; NP_491749.2; NM_059348.5. DR IntAct; O01965; 1. DR STRING; 6239.C27A12.8.1; -. DR EPD; O01965; -. DR PaxDb; O01965; -. DR PeptideAtlas; O01965; -. DR EnsemblMetazoa; C27A12.8.1; C27A12.8.1; WBGene00016158. DR EnsemblMetazoa; C27A12.8.2; C27A12.8.2; WBGene00016158. DR GeneID; 172284; -. DR KEGG; cel:CELE_C27A12.8; -. DR UCSC; C27A12.8.1; c. elegans. DR CTD; 172284; -. DR WormBase; C27A12.8; CE29680; WBGene00016158; ari-1.1. DR eggNOG; KOG1815; Eukaryota. DR GeneTree; ENSGT00940000155744; -. DR HOGENOM; CLU_009823_4_2_1; -. DR InParanoid; O01965; -. DR OMA; CKCGHVF; -. DR OrthoDB; 469819at2759; -. DR PhylomeDB; O01965; -. DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism. DR Proteomes; UP000001940; Chromosome I. DR Bgee; WBGene00016158; Expressed in multi-cellular organism and 5 other tissues. DR GO; GO:0005737; C:cytoplasm; IDA:WormBase. DR GO; GO:0005634; C:nucleus; IDA:WormBase. DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR031127; E3_UB_ligase_RBR. DR InterPro; IPR002867; IBR_dom. DR InterPro; IPR044066; TRIAD_supradom. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR11685; PTHR11685; 1. DR Pfam; PF01485; IBR; 2. DR SMART; SM00647; IBR; 2. DR PROSITE; PS51873; TRIAD; 1. PE 1: Evidence at protein level; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Proteomics identification {ECO:0007829|EPD:O01965, KW ECO:0007829|PeptideAtlas:O01965}; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCD61206.1}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 124..331 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS51873" FT REGION 1..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..27 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 28..52 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 494 AA; 57251 MW; 25BF128B84F805E3 CRC64; MSSDDEINMD DSDSSQGEID DGCMSDDDGI VLESREQNSS DYKDNGEPDN EVLNHDSLEA EMKKTITDVQ AVLQVKTGVC RILLHKYKWN KESLLERFYE HPDTTTFLID AHVIPRRQER LPAGDAECDI CCSLGELSGL SCNHRACTQC WKAYLTNKIA NNAQSEIECM APNCKLLIED EKVMFYITDP TVIATYRKLI VASYVETNRL LKWCPGIDCG KAVRVSHWEP RLVVCSCGSR FCFSCGHDWH EPVNCRLLKL WLKKCNDDSE TSNWINANTK ECPKCMITIE KDGGCNHMTC KNTACRFEFC WMCLGPWEPH GSSWYSCNRF DDSAAKNARD AQEVSRANLQ RYLFYYNRYM GHQQSLRLEG KLYATVKSKM EQMQTLSMSW IEVQFLRKAV DVLSECRRTL MFTYAFAFYL KRDNNAIIFE SNQKDLEMET EQLSGFLERD LDNENLVTLK QKVQDKYRYV EHRRKVLLDH CSEGADQELW VFNE //