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Database: UniProt
Entry: J9IXR0_9SPIT
LinkDB: J9IXR0_9SPIT
Original site: J9IXR0_9SPIT 
ID   J9IXR0_9SPIT            Unreviewed;      1911 AA.
AC   J9IXR0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   13-SEP-2023, entry version 43.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=OXYTRI_21726 {ECO:0000313|EMBL:EJY80883.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY80883.1};
RN   [1] {ECO:0000313|EMBL:EJY80883.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY80883.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
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   -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC       {ECO:0000256|ARBA:ARBA00006331}.
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:EJY80883.1}.
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DR   EMBL; AMCR01007353; EJY80883.1; -; Genomic_DNA.
DR   EnsemblProtists; EJY80883; EJY80883; OXYTRI_21726.
DR   OrthoDB; 1093891at2759; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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   PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE HECTD1; 1.
DR   PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:EJY80883.1};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1526..1911
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1020..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1077..1108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1136..1166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1178..1205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1178..1194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1878
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1911 AA;  221553 MW;  E411AAB49031495D CRC64;
     MEDQLDQLES NLNQLQQMAQ NQMFNLGVDN YGWQPAFTDY KQILEQLKTG DDMLIYEGLI
     NLSNQLSMAQ ENTLTTFPLE QYVPVFMDIL KKPPLSDLSN ESNMFVIQCL TNLMDIFPSV
     WNTIVQHGAI KSIAEVLERS MGFIDLNEAC IKCLEKISLE NPYGILTSGT IGLCLNMMDF
     FEISTQKRIL NMIVNISRHS ATEQDLNDHI IPIMPFLGML LQSRGDHAQQ KIETVCNIVL
     GVCHSITRFL SPHSQFDKVQ AQYENIGQSG IIDGILQRLQ DYCVFDVQQQ NEPSLIQQTK
     PKSLSNQAIE HILKTLTLCC KHSINLNIMI VSFDIFRLVE QFLPSSEDLK NIHFNSDKFP
     FILDTLNLID ALLPEREESL QSENDKSKLA LEQAKKEFYL HSEQQKVLFI AEKILPKVFS
     VYENNIQTIM RNRSLRVIDK MILLFDDELL NNFIEPYSFA KFIYSNLRSK SPSQIQICLQ
     MISKLMRTNP QTYTLPLMRE GVTTFINKLA SKEAIQQALG INMDEVEKVV NPLDDAKDRE
     EVLARARQVI LQRGLDNQDH ESLAQYEQTI QKYLEATRKQ SSQQPDKLKI ELAEKIITIA
     SSLQNKYFEN EEFKSKLNEW YGEEFKLITT LKNLANDIIE ESKQEVFNFE RVKALMKQLA
     EVLTSKRQVM NYEFKESGLL KALDLFLTSS PKQVQLFMEK EKVGEEVKHS EEMMMSQMAR
     NSQNISKKEA RAFIQRLKVF THCMLNSQND KKPINELITL CHSLLSQSEN FLFEQQGDPM
     AHPYGQGGFS NFSEDPNQSV NALRQLTKRT RVNLIYDPKK AFLKKQEPVQ KDSQGLLEPP
     SLLTSKANSH HPAFMQLGGA RRPSQDEQHS KVFMKRNFLF NELQQVLISV EQCASLHLLE
     DFLRNKVRTV DDVKQLKVPT SYYSAGLKKP TGSMPESAKV IIDKALQRVR QMMENSGSKD
     QLREDADDFA NRISDDLVNS SDISDLEQQD VLRHLENLIL HMIDEVYADQ ESQYDDMMRD
     DLLAGGHGDA ERDEAEDREF EQKVFEYQRM IEQLRAQFRL KKQAKIDAEQ HTIGRITQSL
     PVLEKSKGTN EQPNQQQEEL KQSQQPTEEI STLLDTEMQS DDVVEKEKVV QTWLEEMKDE
     EEEEQKQTAS QKREDVEMTD EEEEVQKHML EQLQRSRQQF EKNQQRREVE LTVEEQDDNS
     SQDPENIKET LQMDLDDLIK ASGDDIEFEF YFMGQLIQQN QTIYEIFKQA EARQTHQEQQ
     ILGFSAPFGG NSGLGGYGSS KESTNIYFLI KDKRDEIQLS RKDSLLEFSQ RRERTRSEAV
     NDISVSAVNS IVQQLIEKEF QVFNQESLFK YKSAEKQQEM KQLESSLKIL KVMHFVCKNI
     QLFSNQGIKF IINSNELFEE QKDDMFSDLS LQIGISQLHQ NVFHHHKLDS YILKSIQDPY
     ALIGGAISDT LQQIFKNCPF LFPFQTRQLF FKLISFIGSI DMNRSIYFLR QFLKQKLGKL
     PPEDKNSAVK FQKQKIIVDR NRLIDSAFSL IKQINKRAFL EIQYKDEIGT GLGPTLEFYC
     LISNDIKNVE LLMNGQKQSI WRRNMIDNSL FPAPISVHSI KTEELQKIYE IFRLTGVMMA
     KSISDDRLID LPISSLLWDL LLGKKMSIFD LERIDRDFFK VFAELQQLAN QKKELDKQVF
     MDPESKMRQL NTLRTSQGAK VEDLSLVFLL PGYENIELKQ NGRNTDVNLD NVQEYIDLVM
     HHQFHESVKI QIQAFKKGFN SIFPLETLKP FSTQYELEDM ICGVQRNDED WTNTQKLFQN
     VIPAHGYHSK SQEYMNFIMF MSQLDHEKRR KFLRFVTGSP RLPNGGFSSL DPKLTVVLKK
     PLNPKESPDD ILPSVMTCQN YIKLPSYSSF EKLIERFEMA FNEGTNNFTL S
//
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