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
//