ID A0A2P7YUD9_9ASCO Unreviewed; 783 AA. AC A0A2P7YUD9; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 05-JUN-2019, entry version 8. 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] pseudohaemulonis. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Metschnikowiaceae; Clavispora; OC Clavispora/Candida clade. 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- CC cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor CC protein]-L-lysine.; EC=2.3.2.26; CC Evidence={ECO:0000256|PIRNR:PIRNR001569, CC ECO:0000256|SAAS:SAAS00628607}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|PIRNR:PIRNR001569}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00143; -. DR Proteomes; UP000241107; Unassembled WGS sequence. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR CDD; cd00078; HECTc; 1. DR CDD; cd00201; WW; 3. DR Gene3D; 2.60.40.150; -; 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 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; SSF51045; SSF51045; 3. DR SUPFAM; SSF56204; SSF56204; 1. 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 Complete proteome {ECO:0000313|Proteomes:UP000241107}; KW Reference proteome {ECO:0000313|Proteomes:UP000241107}; KW Transferase {ECO:0000256|PIRNR:PIRNR001569, KW ECO:0000256|SAAS:SAAS00628615}; KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR001569, KW ECO:0000256|PROSITE-ProRule:PRU00104, ECO:0000256|SAAS:SAAS00593691}. FT DOMAIN 1 86 C2. {ECO:0000259|PROSITE:PS50004}. FT DOMAIN 195 228 WW. {ECO:0000259|PROSITE:PS50020}. FT DOMAIN 306 339 WW. {ECO:0000259|PROSITE:PS50020}. FT DOMAIN 361 394 WW. {ECO:0000259|PROSITE:PS50020}. FT DOMAIN 450 783 HECT. {ECO:0000259|PROSITE:PS50237}. FT REGION 130 183 Disordered. {ECO:0000256|MobiDB-lite: FT A0A2P7YUD9}. FT REGION 221 285 Disordered. {ECO:0000256|MobiDB-lite: FT A0A2P7YUD9}. FT COMPBIAS 228 254 Polyampholyte. {ECO:0000256|MobiDB-lite: FT A0A2P7YUD9}. FT COMPBIAS 260 285 Polar. {ECO:0000256|MobiDB-lite: FT A0A2P7YUD9}. FT ACT_SITE 751 751 Glycyl thioester intermediate. FT {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 //