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Database: UniProt
Entry: A0A0V0S8K5_9BILA
LinkDB: A0A0V0S8K5_9BILA
Original site: A0A0V0S8K5_9BILA 
ID   A0A0V0S8K5_9BILA        Unreviewed;      4388 AA.
AC   A0A0V0S8K5;
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=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=HUWE1 {ECO:0000313|EMBL:KRX23049.1};
GN   ORFNames=T07_9508 {ECO:0000313|EMBL:KRX23049.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX23049.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX23049.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX23049.1};
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00034494}.
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:KRX23049.1}.
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DR   EMBL; JYDL01000027; KRX23049.1; -; Genomic_DNA.
DR   EMBL; JYDL01000027; KRX23052.1; -; Genomic_DNA.
DR   STRING; 6336.A0A0V0S8K5; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd00078; HECTc; 1.
DR   Gene3D; 3.30.720.50; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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   InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR   InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR025527; HUWE1/Rev1_UBM.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR004170; WWE-dom.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF06012; DUF908; 2.
DR   Pfam; PF06025; DUF913; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF14377; UBM; 3.
DR   Pfam; PF02825; WWE; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   SUPFAM; SSF117839; WWE domain; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS50918; WWE; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1744..1820
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          4052..4388
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          764..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1423..1465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1540..1568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2004..2027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2424..2534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2733..2783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2923..2965
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3396..3442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3724..3798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3922..3954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1423..1456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1541..1565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2424..2516
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2733..2751
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2923..2938
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3396..3438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3732..3750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3751..3798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        4355
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   4388 AA;  491821 MW;  278A742DF22EB80A CRC64;
     MYMTLVPMLS VQSYLNKAVN CGNSEEELEM KIDVTSVRKQ TAQAPSDCLK QISEILSADE
     SSIADFLINV KTWSWSKSEL CHWIPVLNRF DDFLAQACVR KEDNEWRLHC DQRQEKLVIG
     ILQFTALLFE NTFSRDIYNS MEHIVVLLES SSISILAATL NLINVFSKRS TFLSRLSKDL
     HEELKARMLA IVETWGGPEF GLTLSICCRR DVEIPSALTT LTFDVDDDEI NLTNPKNDND
     KGSSRRTIRF VEVHKQKRTP AQWMQELISK GITLPADKKF LLFHRLRVAY AFGNFETRLL
     MVICRLKAVA ISVYISSFTD FEYRLLNTGL VIQMLDVLKL PDLPELMAVR AEVFRTLGTF
     FSHVRTGIWT EVVDPLGLTF FHGFLPTLTR SCVNELLEHS SNSPVKYPHY FSTALFSFLY
     YLAKYDRNGA QALTTSGTVE VLLKVVSSSA ARGEGLTFVT RAVRIIEMTL TPTDSMTFQN
     LNGIQTFIHR LSDEIDHCRC ALGHPLSSSD DSSIHAPGTS GSNVPQQSND ALKGKPLLPF
     AISSDAQALS FQSAALIKSL LSFMKKIIQD PQFSESVRHI MDSNFSNCLS HIIQNSLFYG
     PSLFLLAMSC VASFILQEPS QLSQLQERGL TTEILEALFR NEIPTSREIV SSLPNIFSAL
     CLNERGVSQF LSYSPFKTLF TLLISPNYLN ALRRVRSLED VNNTAFILGS MIDQLLRHQP
     RLKSDAIHAV VEVCICDHVD ADDRLLRQLA VMYKCRGVTC AEEADVSGRN RRRPQFPTEH
     PLPFSRLGNN DSDQSDPDDS ESGPVPSLVL SSPNGNSSEN NSNRNDLSNE QVIPLVDYFE
     NVLKFLHGLF NRNQNDEHAR LFLNLGGMYS LVDLIGCGNI PVDYMGGQLY YLLATICRQL
     YVVTHNPLIF EGIFSSALDR ARAVKNIFSY HSKNADRPDV RHSVLVKHFP DGVQTVESTV
     YSSSQFSAVF DLFNHIYVLS CMLTTIFQQG ENRAIILKTV NEFPLVETLI KVHLVLLLEM
     GCVASATEEA VRRNGPVSVS QFMKDGHTLD AKSFPGANDI LSMQLLRRAV MNELPNDSTT
     CNHSKKSTAL RCFPMELYFC ERLILQLKFF FGRLAKLTQT NRPGIPGRRF AQFADRTAVT
     VEGDKAMTHL VKTLCSINKV TISSKNLDAC LYICTATLEL LSDIFLDYEH LHVTPVIEFF
     QRVSTFQMLQ NLSNIVDSDR LWLGKDKYGK SCGSDARGFI SDVLVLIDKL IRGKHFDHRS
     ESEGRSSFPN TPHPVIISSL SKFMYKALIS LWHRLPSSPK LKSDEALSAL SRITLHALRY
     ESRKIEERKS SEKSSVVQAE VEVIPEISQI VNPVHLQQLM DVGFSQQLAT EALSRLPNVD
     QAAEYCLYAS SNRALVQHGN QADVGDDEEQ LRQAIALSLM TMSSPGGEQQ QQRPPETQAA
     AASSSSSSSN QRGVDFVPEI RQQPSREEIN ATIEDLLTGT GTQMMDIAES SLASIGSFPP
     LFEQIERQLE MEMEMELELE MEPRTSGRNI LAPVISAGSN AAQMPPASSS HKTQLPKQAS
     KAASQSVVPK EHDERSEAFL RFAEKDLLPS SILLLKRSPK MAAALTPLFS IVITLFGFKS
     VKTYLLIFCN RLCSVVTTTM NEIEQMMEDN SEVDRSTTIL SDSRFEFEEL STLLNLLHRL
     FVQFQVPMAI MLHETKLLAK FEEFIVLIGL KKKNGTFLSF MSKRSQAWLA YILRILELHV
     YTCEVVDRLL AIPKCRNYVW KFWDRQWYCY SPSVNRKIND AFMAGDQYVY FLQGRRTYRI
     DFFLMIQFCY ETNIIRKVIC LRPENSDKNS ADNSTPVTYC YHPFLNYVDM ATFKKEDLGS
     CDKEILLNVA VEMIGSSVHA ETLRGILRII LLLTRDHSRT KYIVFHGTIK RLFALDESQK
     FVGVEDMVML LLRHIIEDPD YLQNLMEKII ASLLTGHMAI SNYTSTELKE FSCLLCLLEP
     FACRDMNLFA KAFKRTAKIN IASNENRTNA NNTSNNSGSN SNNNSNNNAG AAAPSTVCLE
     LSCATPSVVN SRSPHLKPAA FELIKTLLEY IMTKQKSSVS SVVKDSRAEM KPSSSRLFQR
     ESAEGESQLA GSLLFPKPLV MLYLAEIIQC YPDAASVVVN FRLNESGSLN TSDNRSPLAH
     ILDVLIEGEY EEWKCKGQTF VDGVKAVFGS LAACVHCEES QVAVVSEIKA ALARALALNN
     NERKHKILDN LMSLLCHIVE VCPLSEVQIP KDSKLPPPQN TRFKSILRWF VKKRLLVDLA
     RIPHSLDLSD GQSVLTVNCM LKALDEISRQ HFYPSRSRST GTPAINYLTS NGQAGRRSLI
     RISETVDSSG HDYVFLNLAS ANGRGNNLFT VFDSEFPTLR SLDGDFSSDA FFDREDTIEV
     AQEPPQGNGN DNFPEFIVHN LAADDDEEDD DEDDEDDEDE DVEEEEIDIN EEVGEDEEEE
     EADHGDDHEV GEEEEEEEAD NDDSEYEAVE DDVNEEDDDD DDDDDDDDED EDDELANSFR
     DTSYVEENNN NAISSNDLAG SIGALGDLLR QTLSSNSNGV RDVINQLSSE GREERWHHDV
     PSITIEPDVE FGYRTLGRNR GGQHRSALPR IVQLNRQSAF RIRVTEPMPI VDTDDIFWRD
     FFSEAVRPAE RFVMFQRSLT DTLRSINFGS RLNVTNSSEA NMPMTTEICG FFTRIMQEGS
     LLEMDSTYLA WLGVREDILK ALEKRRDDEL SRKQAEALSA ADSEDKSKKS ENNNTSGTAS
     QDEPGQMRAM VTGDHPRDSA NSSQLAESFI NQDRNDIEQE ISWVSVADGQ VLFEGSRQQV
     VDNSQRLFQQ QQAEQEQQAV ANNDANPEIP IVANNAFLEA LRQAQEHFET PGRLDMPDPD
     ALQEACNMLL MTGGLSETPE QRQDQQLDPL PEPDLVQGRV AAEEQQQLQQ QEPQENVESN
     ADAAVAADAT TAAPETAETE ELTEEQRRIR DILGDTPIPE GVDRAFLAEL PENIRAEVIA
     EQWRLLRLQQ QSRSAEGTDG SAPPAISMDF LVALPPELQE EVIAQHRISS QQQNNPDGQM
     DLATFFETLP APLRRQILSD ADESQMAFFP SHIAAEARHI QLTFNNRETG RPRHYHVVRT
     GRNGQRGDNS VRPRHGIRLA RRPVPADMRS LRQQLANWNR DTASYTRTQF GGHTGSKSAT
     TNTTLSTRSS ALFDRESLTC LLVLLFVDDS RLSTARLTRI LRTVCAHPGT REWLLRALVS
     ILQRTWMSVD LIGGSTLGGV RPSDPEFGDL SSYTFSPTPS RSTVVARSSH RRNEAAGAAG
     GLHLSSANSE NKGWLSMTMT SKLGNCVEVF RISKPTASGG KRALLFPQLT PVLLHPLVVP
     AVTTAVINTI AAIAKSYSHS FFPQLRKLLN SQSNAANTSD SASASVAEAG STAQQSGAAR
     QGDEQQPQSA SKTPTLRRRS SSAVDRIRSD FWDILTKLNN ASSANSRTKH SPKIVSFGFP
     DTTAQCGVED SLFGQLVLFL RHPVIVERQG LQSILLSTLQ HVTSTSLAQI SDTILDQGVF
     LEEQLKLLID VLVRDSSSGD NRNDARLILV RCAAALGPAT RRRIFELLFE AARELAGALR
     KELIVLLEEM RSLKNNEPGT SAQFVASSSS SSALLPARGR MIDRFTGTTL VVSSTSPAKA
     PNFACSQELQ CPSMELLSKK NSMQTCLLRV INSILSMKHS MKKFDERDPN FEQDVTSFDF
     ELQDSEEVID ESDMSAGDRD RDRRNGSSQE EGRQETTAAV EPAPATTTTT AGTDASSTTV
     TASSAATTTT TTSDESSTAT VAAPVTPVTS AVVEVSDSNA PFVTVTSTSI TALSSGDGSS
     NNELVGEETQ RPVFELEVQP LTVSMQVDNL WDLLSECLTL LDESADPHAV LILQPAVEAF
     FIIHGDDKKH MNELCTLLQS STRPDSDTLT ESSASNSAQP FSDMTVSSND AMKSSDPHFR
     NLPLDVQMFI RFAEKHRTVL NQIIRQSKTP LNTGPFSVLI NYTRILDFDI KRRYFRLELE
     RVDQTFRADD TPVRVKRDRI FQDSFRELFR LRPSEWKSRF YILFEGEEGQ DAGGLLREWF
     SVITREIFDP NYALFMTASG DSVTYTINPS SYINREHLQY FKFIGRLIAK AIYDNKLLDC
     YFTRAFYKHI LSKPVKYTDI ESEDPSFYQS MVFLLENPVS TLGYDLTFSL EVEEFGVREI
     RDLKPEGRTV LVTDANKMEY VRLVCQMKMT GAIRQQLNAF LEGFYDIIPR RLISIFNEQE
     LELLISGLPI IDIDDLQQNT EYYKYNKNSL QIQWFWRAVR SFDHAERAKL LQFVTGTSRV
     PLQGFAALPG MHGAQRFQIH RDDRSVDRLP AAHTCFNQLD LPPYETYDKL RHMLLLAINE
     CSEGFGFA
//
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