ID A0A0V0S758_9BILA Unreviewed; 2122 AA.
AC A0A0V0S758;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 Name=TRIP12 {ECO:0000313|EMBL:KRX22611.1};
GN ORFNames=T07_2894 {ECO:0000313|EMBL:KRX22611.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX22611.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX22611.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX22611.1};
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:KRX22611.1}.
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DR EMBL; JYDL01000030; KRX22611.1; -; Genomic_DNA.
DR STRING; 6336.A0A0V0S758; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054630; 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:UP000054630};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 632..708
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1811..2122
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1586
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..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1184
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2089
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX22611.1"
SQ SEQUENCE 2122 AA; 234582 MW; 161FA3481ACAF8D1 CRC64;
LLCRRNGNRM DKTSRPPKRL SKSSRVQVGR PVADRAESNL ESEQTSSIKP IRKKAKIQQT
TEQSGENSKN GASGSRTGPS SSSASLSSAG ESSRSLADLV DYFPSVSTDK RITRSFIHSF
SHQEAIRVCV YACFLAALND FYVSSSKHRE LLLGDLNFLK VGYQLQFYER KIVWTGGLSQ
GDTFCRTQQQ QQQQQQQQQQ QQQQQPPLPT TSGVQKSKSS RLSNRQAQAQ SASHTSKTDL
NEMESNSRSQ GGKKKGKAQK PNASKSGHAT SSAASDANNP ANTSDPNFNT DLRTSYASIL
GTFGPRVTNL LLRGSSSGNE RIESLLSSMQ KHEDSSTQLQ ALIELCNILV MSNEETLGSN
FPFKELIRVL TRLLQTEHNF DIMTHACRAL TYLMEASPRI GSALMDAVPC LLSKLQRVEC
IDVAEQALTA LELLSRRLGK NILNANGIEC CLMFIDFFPL ASQRSALHIV SNCCYHLSEK
DFDYLANSLP ILTQRLKSQD KKTVELMCVT FARLVENLIH SPDKIQKICE HGLLSNIQQM
LIAVPPVISS GTLVNVIRMM HLICRSCPTL TVSLVSSSFV FILRFLLTGS TEEKSDSREL
LSRTPQEMYE LVLLIGELLP SLPTEGLFEV DSLLQPHGNI GDAATWSFKD ERGVWRSYSH
SDSRVLELAY QTKEEEISLS ILGQSYVIDL IQMTQICEET GSSLPIQRKP KEINAQSGGT
SNANVVTPEN DPRVVLLKDA PIHYEEIVQS IFPLLYDIYS SVGGSAVRHE CLRCFLKMIY
HGNVMMIDRI LETVPISNLI AGLLCSHDFK SIVCALQLAK VLLEKKRKYF TVCFQREGVT
NHLKNLSVHL KQANAFTIAY GDTADLSARF GLQMAGSGIA GAGAAAPGGG SSSFTGFSTA
PNFSPMLESL MMNGARVVPL SGSGRNLSLS FPFFGSPSSG SGSSQRRVSL NSLFGFASGT
LGSRATSPTF SLSEQLEASA ANTAMALAGA SSSAAVGSMF PYTADERQLI QAAGSSLAVL
PTAVAGSTSG SANASAILAN HQQQQLHHHL NQHHQHHQQQ QQQQQQQQQQ QQQQQQQQQQ
QHQQQQQQSQ QSTAKNTRGR GRMKKSSTPG FSSGEVRSNP RGGSPLRKTV STGRGSGNFL
GSIGLHRWNT RSGFGALKPP TPPLSSSNTV AHHHHHHHHH HHSTVLHSND SQSQEFLSSH
ANYWKSISDK VSAWAEVTAK ALLDDYFKEG DGNGVANYYG QATAKKLCEI AQKFAEKADE
GFDDLVEVLH SDVTCYELLQ SGLIEELSKY LTQGNWQHAL PNRLRLFCSK LFGVRVKTPT
ESEVPEVFIE DEESGKRLIT MLVMCISQLE QFPVKMHDLS WGQSGGGLRG LNAFRFLHSQ
QIKCQPVRHP SETKLRQWKR GVIKVDPLCP ISTIERYLIL KGYGKPKTNP GDDDSSNDEE
DGTELTEDDA EALLNVASIA NGVHRLQLLI HDRVLPYDMT IFQALRQYGG KSSNVTSDGL
VVSEWIGPDM WMATNRIAYK LLPENDTSGG GGGGSAGSSK EAASTSGVGG SCGASSTTGA
GTSRGRRGGK GSGGGKKRSP TAASNATPVY KEPENILLAQ LKQPMNVTTY DPCLKALGLL
RVVFSIARYW WILYEKSALV RCSAPLVPLT AFHVSKIAAK ISRQLQDPLI ILSDHLPYWV
EQVAYHCPFI LPFDVRRSLF NVVALDHDRA LQHLLESAGE SSSYNSADRL APRLERRKVC
IPRQNILKQA ETVFNNMNHS RAVLEVQYEN EVGSGLGPTL EFYALVAHNL QRADLHLWRG
TVNRDRPLAE GVNEYIHSDT GLFPDLLNPG NSEEVIRRFR LCGKLLSRAL LDGRLLDIPL
NVLFFKWLLQ EEKFLCATDF NDLDPAFAAS MHFLKTLLLK GRLGSEESRE QVRAEIEDMQ
IDFVVPGREN VELKPGGKNI ALTLENLSEY IDLVAFWMLH AGVVRQMDAL RESFGSIIQL
KCLKMFLPEE MELLISGCND STDTWEVQSL LQAIHPDHGY TPESPQIRWL AEIMSNYTLK
ERRDFLQFLI GSPRLPVGGL KHLNPPFTVV RKLCDCGNTD KLLPSVMTCV NYLKLPEYSD
RELMRERIRT AVEYGRYAFH LS
//
