ID A0A3B4E5D1_PYGNA Unreviewed; 2047 AA.
AC A0A3B4E5D1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000030439.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000030439.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion
CC degradation (UFD) pathway and regulation of DNA repair. Part of the
CC ubiquitin fusion degradation (UFD) pathway, a process that mediates
CC ubiquitination of protein at their N-terminus, regardless of the
CC presence of lysine residues in target proteins.
CC {ECO:0000256|RuleBase:RU369009}.
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|RuleBase:RU369009};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369009}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642, ECO:0000256|RuleBase:RU369009}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331, ECO:0000256|RuleBase:RU369009}.
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DR RefSeq; XP_017541627.1; XM_017686138.1.
DR Ensembl; ENSPNAT00000018494.1; ENSPNAP00000030439.1; ENSPNAG00000017370.1.
DR GeneID; 108413549; -.
DR CTD; 9320; -.
DR GeneTree; ENSGT00940000156517; -.
DR OMA; AEPLSQF; -.
DR OrthoDB; 1093891at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.720.50; -; 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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369009};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 783..859
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1650..2047
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1800..1834
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2014
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2047 AA; 225539 MW; 24CE54B1BE74A108 CRC64;
MSNRPNSNPG GSLRRSQRNT AAAQPHDHTL TGRNSLSLSV LDPDSEAAGS SGQQEQREGS
GVSISSISVS RALKRNSASE HNSTGSYSPS PAKRPKAQSE SSRAGPSDPP GAPEPKSKSK
KRRLAPEPPP RAVSRKSSPG PGPSGASSTS SSSNKRKKAD ASSSSSSSSS SSSSSSSLGG
PPPPRSEAGR PAKPSKLASK PAASAKAGCS AVTDSSSSSA SSSSASSSSS SSAAAGVNSS
APLQGARLKQ GKDQSKSRRS RSASSPSPRR SSRDKEQPKP AGSSKFEWTS RFNPKVNLPK
PRLSLPGSSK PESSSKPGPS GLQAKLASLR KSSKKRSESP PAELPSFRRS TRQKTTGSCA
STSRRGSGLG KRGAADTRRQ DKMADSDNNQ DGANSSAART EEAPQGASAS SSVAGAVGMT
TSGESESDDS EMGRLQALLE ARGLPPHLFG PLGPRMSQLF HRTIGSGASS KAQQLLQGLQ
ATGDESQQLQ AAIEMCQLLV MGNEETLGGF PVKSVVPALI TLLQMEHNFD IMNHASRALT
YMMEALPRSS AVVVDAIPVF LEKLQVIQFI DVAEQALTAL EMLSRRHSKA ILQAGGLADC
LLYLEFFSIN AQRNALAIAA NCCQSITPDE FHFVADSLPL LTQRLTHQDK KSVESTCLCF
ARLVDNFQHE ENLLQQVASR DLLTNIQQLL VVTPPVLSSG MFIMVVRMFS LMCSNCPTLA
VQLMKQNIAE TLRFLLCGAS NGSCQEQIDL VPRSPQELYE LTSLICELMP CLPREGIFAV
DAMLKKGSAH TTEAAVWQWR DDRGLWHPYN RIDSRIIETA HQNGEDEISL STLGRVYTID
FNSMQQINED TGTARGIQRK PNPLANPNSG GHLEVRGEDA RAQLMKEDPE LAKCFIKTLF
GVLYEVYSSS AGPAVRHKCL RAILRIIYFA DAELLKDVLR NHAVSSHIAS MLSSQDLKIV
VGSLQMAEIL MQKLPDVFSV YFRREGVMHQ VKNLAESETF FTSPPKACTS GTASLCTTTI
TTATTTTASN VTPDLGSPSF QHSMDDSLDL SPQGRLSDVL KRKRLPKRGP RRPKYSPPRD
DEKVDNQAKS PTTTASPKSS FLASLNPKTW GKLGAQTNST NSEQSRTAGV SGLARATPKD
SVSNNRDKIK AWIKEQASKF VERYFNSENV DGSNPALNVL QRLCTATEQL NLQVDRGVEC
LMEICSIVSE SDVSSFEIQH SGLVKQLLLY LTSNSDRDVV SRDQRIKRFL HIFYNCPMPG
QEPLYRLEPT ENGQLLALVH KMNSCLSQME QFPVKVHDFP SGNGNGSRGS QALKFFNTHQ
LKCQLQRHPD CTNVKQWKGG PVKIDPLALV QAIERYLVVR GYGRVREEDE DSDDDGSDDE
IDESLAAQFL NSGSVRHRLQ FYIGEHLLPY NMTVYQAVRQ FSLQPEEERE STDDEANPLG
RAGIWTKTHT IWYKPVREDE DGCKDAVGGK RGRAQTAPTK TSPRNAKKQD ELWHDGVCPS
VSNPLDVYLI SEPPEGITFD DPSLEVILLL RVLHSISRYW FYLYDNAVCK EVISTSEFIN
SKLTAKANRQ LQDPLVIMTG NIPTWLTELG KTCPFFFPFD TRQMLFYVTA FDRDRAMQRL
LDTNPEINQS DSQDSRVAPR LDRKKRTINR EELLKQAESV MQDLGSSRAM LEIQYENEVG
TGLGPTQEFY ALVSQELQRA DLGLWRGEEV TLANPKGSQE GTKYMFSSRG LFAVPFGRST
KPAHVAKIKM KFRFLGKLMA KAIMDFRLLD LPLGLPFYKW MLRHESSISS HDLVNIDPGV
AKSIQHLEDI IRQKKRLEQD QSQTRETLQQ ALESLNMNGC SVEDLGLDFT LPGFPNIELK
KGGKDVPVTI HNLEEYLRLV VYWTLNEGVS RQFESFREGF ESVFPLHHLQ YFYPEELDQL
LCGSKSETWD VKTLMECCRP DHGYTHDSRA VRFLFEVLSS FDAEQQRLFL QFVTGSPRLP
VGGFRSLNPP LTIVRKTFES TENPDDFLPS VMTCVNYLKL PDYSSIEIMR EKLLIAAREG
QQSFHLS
//
