ID A0A0M3HRU6_ASCLU Unreviewed; 1687 AA.
AC A0A0M3HRU6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 2.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
OS Ascaris lumbricoides (Giant roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0000509901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0000509901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (MAY-2016) to UniProtKB.
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|RuleBase:RU369009}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331, ECO:0000256|RuleBase:RU369009}.
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 WBParaSite; ALUE_0000509901-mRNA-1; ALUE_0000509901-mRNA-1; ALUE_0000509901.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000036681; 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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
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 375..449
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1316..1687
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 439..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1655
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1687 AA; 186856 MW; A26BF7CF54FBBC74 CRC64;
MVLGVCTRVL FPVGWLTHMG KEVSVVRNMV VTLKVVLCGA LIRLAPASCL VCCARRTLDV
DVRVVTIMEG LRSSNEIRQA EAASELAEML LLGNEESLPN LPVKDIVHAL IALLQKEHNF
ELMLTAARCI SNMLEALPRA LPIVIDAVPY LLEKLKRIEC IDVAEQSLMA LEVMSKRNGK
NIMAAGGIAA TISHVDFFSV PSQRLAFQIA ANCASFVTVN DFAQVRESLA DLTQRLLIED
KRCLESICVL FCRLVDNVRG HADKLREVAG QNHALLKNVQ QLLLVQPCAV GPNTFQALVR
MLRHMAAKCS DLAVALINMD FARTIRFLII GTEGGDRSLE MVNRPSQQLQ ELVFLAGELL
PRLPSDGVFA IDSVMIRPHA SFHEIPPAQW FWKDDANQWQ PFNNFDSRMA YSTNETEISL
QINGSVYRMD LQRMVQQNHA TGNERSIQRR APQPPQKTKA SQPEEDRRLE LLKNDASTLN
QVVQMLFPIL VEIDGSSSGP ALRYESLRVM LRMIYPSETT HLKEVLNEVP LAGHVASALA
SPRSKDLCIV ASALQLVHLV LDKLPELYVP LFRREGVAHE VEKLSKIKSD SPVNMPPVRS
SPSVIASARE GSSVMRTRSG LKTRASLASS ASEDHPARMI FLASVVILVV CLISLHAKQS
SSRSRSSTQP PVGVDTASTS AEGTTRVIVS PSGGRHRRKA SPESPISKKE SRRKGSSSNF
LHSLRLPSFR MPGTSSSHNP HEAASSSAGT SANAATSSQA GTSRSRIVFP YGGGSASNYS
TILMHSASNS GHTSFPLSVA SSTSHVSSLN HQQKEKVRQW IRKEAEYLLS THFSPSTGGD
SSTASTITRM GAVASALITE KDVGSAPLSE LKTIMLENDV SAFELSHSGV LSALIEYLTS
TSPSLQPPRK LRLKRFAAVF MSLNPDNLRP LDESGSWAAF EALVTKLLAS VAQLEQFQVK
VSDMGGILTG SSAGALRGAQ ALRFFQTHQI RCNLRRHPAC RELKEWRHGH GSIKVDPFTS
ISAIERYLLD RGVGYVRGED SSGDEDASDD DEMPSEGSLS AQTGPQRRID ILINDEKIPG
HMSILQAIRQ YSPAMMGDGS DQLAIATGLW VNTHTLYYRA ASIPPPPETN HEAVPSKSPA
TRNERKERKN KIDEKLWIEG EVPVYESPLE RYLTGALPVE IDDPCVSSLI LLRCLYALNR
FWWSLFEDED VPPTTHAPLL PPTSFHSAKL NAKMARQLSD FLSVATQQIP KWTMDLVKAA
PFIFTFASRR NLLYCTAFGR DRALMHLVNQ TDGGHSDGES GRLTPRLERR KVSVRRDDLL
RQAEQTMNHL GHSRAMLEVG FEGEAGTGFG PTLEFYSTVS REIQKASLRL WHGRSVTMPA
ENIDSPQVEY TISEGGLYPA AHGSQNVKQR DARLKKFEFI GRLLAQALID ARMLDLPLNP
VFFKWLCGED KSFGLADLEI FDKTLYQSLR SLALTGAEDF ESLEQYFTLP GDESFELVKG
GKNRSVDCTN VMQYIKLVAH WELVEGVRRE MEAVRRGFES IINISDLSSF TPDEMEELFC
GCSEATWTRT WSEAALQTAI KPDHGYSHDS EQIRWLIHML SSFDYQQQRK FLQFVTGSPK
LPVGGFRSLN PPLTVVKKSG GYGNGDEELP SAMTCYNYLK IPAYSSYEVF KQRFDVALRF
IYSFHLT
//
