ID A0A0V1PC70_9BILA Unreviewed; 2100 AA.
AC A0A0V1PC70;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
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};
GN Name=trip12 {ECO:0000313|EMBL:KRZ93823.1};
GN ORFNames=T08_10210 {ECO:0000313|EMBL:KRZ93823.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ93823.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ93823.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ93823.1};
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:KRZ93823.1}.
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; JYDM01000023; KRZ93823.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054924; 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; 3.30.2410.10; 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:UP000054924};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2100
FT /note="E3 ubiquitin-protein ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006884084"
FT DOMAIN 618..694
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1789..2100
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 53..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1507..1564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1165
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2067
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2100 AA; 231921 MW; B4ED25A38ED464D8 CRC64;
MLENVFSLVL LINCYVVGTG TEWTKVQDRL SGCPIKLVYC RSSRVQVGRP VADRAESNLE
SEQTSSIKPI RKKAKIQQTT EQSGENSKNG ASGSRTGPSS SSASLSSAGE SSRSLADLVD
YFPSVSTDKR ITRSFIHSSK HRGLLLGDLN FLKVGYQLQF YERKIVWTGG LSQGDTFCRT
QQQQQQQQQQ QPPQPTTSGV QKSKSSRLSN RQAQAQSASH TSKTDLNEME SNSRSQGGKK
KGKAQKPNAT KSGHATSSAA SDANNPGNTS DPNFNTDLRT SYASILGTFG PRVTNLLLRG
SSSGNERIES LLSSMQKHED SSTQLQALIE LCNILVMSNE ETLGSNFPFK ELIRVLTRLL
QTEHNFDIMT HACRALTYLM EASPRIGSAL MDAVPCLLSK LQRVECIDVA EQALTALELL
SRRLGKNILN ANGIECCLMF IDFFPLASQR SALHIVSNCC YHLTEKDFDY LANSLPILTQ
RLKSQDKKTV ELMCVTFARL VENLIHSPDK IQKICEHGLL SNIQQMLIAV PPVISSGTLV
NVIRMMHLIC RSCPTLTVSL VSSSFVFILR FLLTGSTEEK SESRELLSRT PQEMYELVLL
IGELLPSLPT EGLFEVDSLL QPHGNIGDAA TWSFKDERGV WRSYSHSDSR VLELAYQTKE
EEISLSILGQ SYVIDLIQMT QICEETGSSL PIQRKPKEIN AQSGTSNANV VTPENDPRVV
LLKDAPIHYE EIVQSIFPLL YDIYSSVGGS AVRHECLRCF LKMIYHGNVK MIDRILETVP
ISNLIAGLLC SHDFKSIVCA LQLAKVLLEK KRKYFTVCFQ REGVTNHLKN LSVHLKQANA
FTIAYGDTAD LSARFGLQMA GSGIAGAAAP GGGSSSFTGF STAPNYSPML ESLMMNGARV
IPFGGSGRNL SLSFPFFGSP SSGSGSSQRR VSLNSLFGFA SGTLGSRATS PTFSLSEQLE
ASAANTAMAL AGASSSAAVG VAGSMFNYTA DNIHLIQAAG SSLAVLPTAV AGSTSGSANA
SAVLANHQQQ QLHHHLSQHQ 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 FVVPGRENIE LKPGGKNIAL
SLENLSEYID LVAFWMLHAG VVRQMDALRE SFGSIIQLKC LKMFLPEEME LLISGCNDST
DTWEVQSLLQ AIHPDHGYTP ESPQIRWLAE IMSNYTLKER RDFLQFLIGS PRLPVGGLKH
LNPPFTVVRK LCDCGNTDKL LPSVMTCVNY LKLPEYSDRE LMRERIRTAV EYGRYAFHLS
//
