ID A0A0V0VBE0_9BILA Unreviewed; 2070 AA.
AC A0A0V0VBE0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
DE Flags: Fragment;
GN ORFNames=T09_9985 {ECO:0000313|EMBL:KRX60818.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX60818.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX60818.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX60818.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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|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 -!- 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:KRX60818.1}.
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DR EMBL; JYDN01000054; KRX60818.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
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; SSF81995; beta-sandwich domain of Sec23/24; 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 Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 586..662
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1759..2070
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1135
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2037
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX60818.1"
SQ SEQUENCE 2070 AA; 228771 MW; 40F23869D90CB719 CRC64;
LLCRRNGNRM DKSSRPPKRL SKSSRVQVGR PVADRAESNL ESEQTSSIKP IRKKAKIQQT
TEQSGENSKN GASGSRTGPS SSSASLSSAG ESSRSLADLV DYFPSVSTDK RITRSFIHRP
KKEAKFDRQL RNTQTIFIIS QGDTFCRTQQ QQQQQQQQQP PQPTTSGVQK SKSSRLSNRQ
AQAQSASHTS KTDLNEMESN SRSQGGKKKG KAQKPNATKS GHATSSAASD ANNPGNTSDP
NFNTDLRTSY ASILGTFGPR VTNLLLRGSS SGNERIESLL SSMQKHEDSS TQLQALIELC
NILVMSNEET LGSNFPFKEL IRVLTRLLQT EHNFDIMTHA CRALTYLMEA SPRIGSALMD
AVPCLLSKLQ RVECIDVAEQ ALTALELLSR RLGKNILNAN GIECCLMFID FFPLASQRSA
LHIVSNCCYH LTEKDFDYLA NSLPILTQRL KSQDKKTVEL MCVTFARLVE NLIHSPDKIQ
KICEHGLLSN IQQMLIAVPP VISSGTLVNV IRMMHLICRS CPTLTVSLVS SSFVFILRFL
LTGSTEEKSE SRELLSRTPQ EMYELVLLIG ELLPSLPTEG LFEVDSLLQP HGNIGDAATW
SFKDERGVWR SYSHSDSRVL ELAYQTKEEE ISLSILGQSY VIDLIQMTQI CEETGSSLPI
QRKPKEINAQ SGTSNANVVT PENDPRVVLL KDAPIHYEEI VQSIFPLLYD IYSSVGGSAV
RHECLRCFLK MIYHGNVKMI DRILETVPIS NLIAGLLCSH DFKSIVCALQ LAKVLLEKKR
KYFTVCFQRE GVTNHLKNLS VHLKQANAFT IAYGDTADLS ARFGLQMAGS GIAGAAAPGG
GSSSFTGFST APNYSPMLES LMMNGARVIP LSGSGRNLSL SFPFFGSPSS GSGSSQRRVS
LNSLFGFASG TLGSRATSPT FSLSEQLEAS AANTAMALAG ASSSAAVGVA GSLFNYTADN
IHLIQAAGSS LAVLPTAVAG STSGSANASA VLANHQQQQL HHHLSQHQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQQQQQS QQSTAKNTRG RGRMKKSSTP GFSSGEVRSN PRGGSPLRKT
VSTGRGSGNF LGSIGLHRWN TRSGFGALKP PTPPLSSSNT VAHHHHHHHH HHHSTALHSN
DSQSQEFLSS HANYWKSISD KVSAWAEVTA KALLDDYFKE GDGNGVANYY GQATAKKLCE
IAQKFAEKAD EGFDDLVEVL HSDVTCYELL QSGLIEELSK YLTQGNWQHA LPNRLRLFCS
KLFGVRVKTP TESEVPEVFI EDEESGKRLI TMLVMCISQL EQFPVKTHDL SWGQSGGGLR
GLNAFRFLHS QQIKCQPVRH PSETKLRQWK RGVIKVDPLC PISTIERYLI LKGYGKPKTN
PGDDDSSNDE EDGTELTEDD AEALLNVASI ANGVHRLQLL IHDRVLPYDM TIFQALRQYG
GKSSNVTSDG LVVSEWIGPD MWMATNRIAY RLLPENDTSG GGSAGSSKEA ASTSGVSGSC
GASSTTGAGT SRGRRGGKGS GGGKKRSPTA ASNATPVYKE PENILLAQLK QPMNVTTYDP
CLKALGLLRV VFSIARYWWI LYEKSALVRC SAPLVPLTAF HVSKIAAKIS RQLQDPLIIL
SDHLPYWVEQ VAYHCPFILP FDVRRSLFNV VALDHDRALQ HLLESAGESS SYNSADRLAP
RLERRKVCIP RQNILKQAET VFNNMNHSRA VLEVQYENEV GSGLGPTLEF YALVAHNLQR
ADLHLWRGTV NRDRPLAEGV NEYIHSDTGL FPDLLNPGNS EEVIRRFRLC GKLLSRALLD
GRVLDIPLNV LFFKWLLQEE KFLCATDFND LDPAFAASMH FLKTLLLKGR LGSEESRERV
RAEIEDMQID FVVPGRENVE LKPGGKNIAL TLENLSEYID LVAFWMLHAG VVRQMDALRE
SFGSIIQLKC LKMFLPEEME LLISGCNDST DTWEVQSLLQ AIHPDHGYTP ESPQIRWLAE
IMSNYTLKER RDFLQFLIGS PRLPVGGLKH LNPPFTVVRK LCDCGNTDKL LPSVMTCVNY
LKLPEYSDRE LMRERIRTAV EYGRYAFHLS
//
