ID A0A2P7YUD9_9ASCO Unreviewed; 783 AA. AC A0A2P7YUD9; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 02-OCT-2024, entry version 29. DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569}; DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569}; GN ORFNames=C7M61_001383 {ECO:0000313|EMBL:PSK39584.1}; OS [Candida] pseudohaemuli. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis; OC Candida/Metschnikowiaceae. OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK39584.1, ECO:0000313|Proteomes:UP000241107}; RN [1] {ECO:0000313|EMBL:PSK39584.1, ECO:0000313|Proteomes:UP000241107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B12108 {ECO:0000313|EMBL:PSK39584.1, RC ECO:0000313|Proteomes:UP000241107}; RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N., RA Cuomo C.A.; RT "Candida pseudohaemulonii genome assembly and annotation."; RL Submitted (MAR-2018) 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=2.3.2.26; 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:PSK39584.1}. 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; PYFQ01000002; PSK39584.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2P7YUD9; -. DR STRING; 418784.A0A2P7YUD9; -. DR EnsemblFungi; C7M61_001383_t1; PSK39584.1; C7M61_001383. DR VEuPathDB; FungiDB:C7M61_001383; -. DR OrthoDB; 5480520at2759; -. DR UniPathway; UPA00143; -. DR Proteomes; UP000241107; Unassembled WGS sequence. DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi. DR GO; GO:0022626; C:cytosolic ribosome; IEA:EnsemblFungi. DR GO; GO:0010008; C:endosome membrane; IEA:EnsemblFungi. DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblFungi. DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi. DR GO; GO:1990306; C:RSP5-BUL ubiquitin ligase complex; IEA:EnsemblFungi. DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:EnsemblFungi. DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:EnsemblFungi. DR GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblFungi. DR GO; GO:0006325; P:chromatin organization; IEA:EnsemblFungi. DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IEA:EnsemblFungi. DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi. DR GO; GO:0007005; P:mitochondrion organization; IEA:EnsemblFungi. DR GO; GO:0070651; P:nonfunctional rRNA decay; IEA:EnsemblFungi. DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:EnsemblFungi. DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:EnsemblFungi. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi. DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IEA:EnsemblFungi. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi. DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:EnsemblFungi. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:EnsemblFungi. DR GO; GO:0010794; P:regulation of dolichol biosynthetic process; IEA:EnsemblFungi. DR GO; GO:0032443; P:regulation of ergosterol biosynthetic process; IEA:EnsemblFungi. DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IEA:EnsemblFungi. DR GO; GO:0010796; P:regulation of multivesicular body size; IEA:EnsemblFungi. DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:EnsemblFungi. DR GO; GO:0019220; P:regulation of phosphate metabolic process; IEA:EnsemblFungi. DR GO; GO:0032880; P:regulation of protein localization; IEA:EnsemblFungi. DR GO; GO:2000203; P:regulation of ribosomal large subunit export from nucleus; IEA:EnsemblFungi. DR GO; GO:2000232; P:regulation of rRNA processing; IEA:EnsemblFungi. DR GO; GO:2000238; P:regulation of tRNA export from nucleus; IEA:EnsemblFungi. DR GO; GO:2000235; P:regulation of tRNA processing; IEA:EnsemblFungi. DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IEA:EnsemblFungi. DR GO; GO:0034517; P:ribophagy; IEA:EnsemblFungi. DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; IEA:EnsemblFungi. DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:EnsemblFungi. DR CDD; cd08382; C2_Smurf-like; 1. 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; IPR050409; E3_ubiq-protein_ligase. 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; 2. DR SMART; SM00239; C2; 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 Reference proteome {ECO:0000313|Proteomes:UP000241107}; KW Transferase {ECO:0000256|PIRNR:PIRNR001569}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|PIRNR:PIRNR001569}. FT DOMAIN 1..105 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 195..228 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 306..339 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 361..394 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT DOMAIN 450..783 FT /note="HECT" FT /evidence="ECO:0000259|PROSITE:PS50237" FT REGION 130..183 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 221..285 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..254 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 260..285 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 751 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1, FT ECO:0000256|PROSITE-ProRule:PRU00104" SQ SEQUENCE 783 AA; 89074 MW; 4C6756F9DE3F3C7B CRC64; MTKVNVKVVA AESLYKRDVF RQPDPFAVIT VDGDQTITTK TAKRTLNPYW NESFLLSASE DSILAIQVFD QRKFKKKDQG FLGVVNVRVG DVIDLSLSGS EETITRDLKK SNENLAVSGR VIIVLSHNTN PSSAPAANGS AAPAPRASSS ARNSVPNSTP AASSAPPAAA NGNGNSNGNG EQFTKQYSSF EDQYGRLPPG WERRTDNFGR TYYVDHNSRT TTWERPTLDQ SETERGQQRE NHTEAERRQH RGRTLPGEAP QSPTLPSAST STSNNVTVNS TGANTPVSPA AAVSMAATGG TTRGLGELPT GWEQRFTNEG RPYFVDHNTR TTTWVDPRRQ QYIRTFGPNT TIQQQPVSQL GPLPSGWEMR LTNTARVYFV DHNTKTTTWD DPRLPSSLDQ NVPQYKRDFR RKVIYFRSQP ALRILPGQCH IKVRRDHIFE DSYQEIMRQT PEDLKKRLMI KFDGEEGLDY GGVSREFFFL LSHDMFNPFY CLFEYSSHDN YTLQINPNSG INPEHLNYFK FIGRVVGLGV FHRRFLDAFF VGALYKMMLR KKVNLQDMEG VDAEFYRSLQ WILDNDITDI LDLTFSAEDD KFGEIVEVDL KPGGRDIEVT EENKAEYVEL ISEWKIHKRI ELQFQAFIDG FNELIPQELV NVFDERELEL LIGGLAEIDV EDWKKHTDYR GYQETDQVIQ WFWQCIKEWD SVQKARLLQF TTGTSRIPVN GFKDLQGSDG PRRFTIEKAG EPNQLPKSHT CFNRVDFPPY TSYESMKQKL TLAVEETVGF GQE //