ID K1VKE6_TRIAC Unreviewed; 788 AA. AC K1VKE6; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 29-MAY-2024, entry version 62. DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569}; DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569}; GN ORFNames=A1Q2_06060 {ECO:0000313|EMBL:EKC99641.1}; OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Trichosporonales; Trichosporonaceae; Trichosporon. OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC99641.1, ECO:0000313|Proteomes:UP000006757}; RN [1] {ECO:0000313|EMBL:EKC99641.1, ECO:0000313|Proteomes:UP000006757} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC99641.1, RC ECO:0000313|Proteomes:UP000006757}; RX PubMed=23193141; DOI=10.1128/EC.00264-12; RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.; RT "Genome sequence of the Trichosporon asahii environmental strain CBS RT 8904."; RL Eukaryot. Cell 11:1586-1587(2012). 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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885, CC ECO:0000256|PIRNR:PIRNR001569}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}. 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:EKC99641.1}. 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; AMBO01000367; EKC99641.1; -; Genomic_DNA. DR AlphaFoldDB; K1VKE6; -. DR STRING; 1220162.K1VKE6; -. DR eggNOG; KOG0940; Eukaryota. DR HOGENOM; CLU_002173_0_0_1; -. DR InParanoid; K1VKE6; -. DR OMA; DNYTIQI; -. DR OrthoDB; 5480520at2759; -. DR UniPathway; UPA00143; -. DR Proteomes; UP000006757; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter. DR GO; GO:0000209; P:protein polyubiquitination; IEA:TreeGrafter. DR CDD; cd00078; HECTc; 1. DR CDD; cd00201; WW; 3. DR Gene3D; 2.20.70.10; -; 2. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1. DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1. DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR024928; E3_ub_ligase_SMURF1. DR InterPro; IPR000569; HECT_dom. DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR11254:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1. DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF00632; HECT; 1. DR Pfam; PF00397; WW; 3. DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1. DR SMART; SM00119; HECTc; 1. DR SMART; SM00456; WW; 3. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1. DR SUPFAM; SSF51045; WW domain; 3. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50237; HECT; 1. DR PROSITE; PS01159; WW_DOMAIN_1; 3. DR PROSITE; PS50020; WW_DOMAIN_2; 3. PE 4: Predicted; KW Ligase {ECO:0000313|EMBL:EKC99641.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006757}; KW Transferase {ECO:0000256|PIRNR:PIRNR001569}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|PIRNR:PIRNR001569}. FT DOMAIN 1..64 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 214..247 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 308..341 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 366..399 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 455..788 FT /note="HECT" FT /evidence="ECO:0000259|PROSITE:PS50237" FT REGION 87..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 238..263 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 277..311 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 104..211 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 277..307 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 756 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1, FT ECO:0000256|PROSITE-ProRule:PRU00104" SQ SEQUENCE 788 AA; 88701 MW; 4F249DDBE0A0CDBE CRC64; MKRTLNPYWN ENFDITVKDS SVVVVQIFDQ RKFKRRDQGF LGVINIKVSD VLDLELGGQE MLTKDLKKGS DNTPVNGKLI VYLSTQTSTP ITNPGPTPSA RPAAINTGGE SSTNSLNANN TSTPEPDSPA THNPRDSFAT GGSTTSNPTT ATTTTPSTTA INTNSTATMN SQQPSQTSPV APSQNHQQSA ISAVAGGAGS AGNTQFDSHS DQLGPLPHGW ERRIDHLGRQ YYVDHNTRTT TWSRPSSDQQ SNTNNAANST GVARAHHNTR LTAEDMLGAN TTGGSQTPNQ GQPTTIGSTN QATTVGSGPL PAGWEQRFTP EGRPYFVDHN TRTTTWVDPR RQQLLRVMAP NQPGVTVQQQ SVTTLGPLPS GWEMRLTSTA RVYFVDHNTK TTTWDDPRLP SSLDQNVPQY KRDFRRKLIY FRSQPALRSN TGQCHVKVSR NNIFEGSYTE IMRQTPNDLK KRLMIKFEGE DGLDYGGLSR EFFFLLSHEM FNPFYCLFEY SAHDNYTLQI NPNSGVNPEH LNYFKFIGRV VGLGIFHRRF LDAYFIVAFY KMILKKRISL ADLESVDASL HRSLTWMLEN DITDIIEETF SITEEHFGEM VTVDLKENGQ NIEVNEDNKK EYVDLVTEYR ISRRVSQQFE SFMSGFNEII PQELINVFDE RELELLIGGM SEIDVDDWQK HTDYRGYNPS DEVIEWFWKI VRSWPAERKS RLLQFTTGTS RIPVNGFKDL QGSDGPRRFT IEKAGEITQL PKSHTCFNRI DLPAYKTYES LEQKLTIAVD ETEGFGQE //