ID J9IV17_9SPIT Unreviewed; 4061 AA.
AC J9IV17;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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_16035 {ECO:0000313|EMBL:EJY85977.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY85977.1};
RN [1] {ECO:0000313|EMBL:EJY85977.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY85977.1};
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 -!- 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:EJY85977.1}.
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DR EMBL; AMCR01002593; EJY85977.1; -; Genomic_DNA.
DR EnsemblProtists; EJY85977; EJY85977; OXYTRI_16035.
DR OrthoDB; 178167at2759; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd14270; UBA; 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; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 2.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:EJY85977.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1243..1285
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 3728..4061
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 2087..2125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2147..2257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2673..2706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2728..2758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2774..2848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2881..2917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 50..104
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2087..2119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2163..2229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2242..2257
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2673..2695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2774..2825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2891..2917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4029
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4061 AA; 468319 MW; 3DF886C6D580BD8E CRC64;
MKFDLTSFDE NALKNNSKTD LQTQELVNMY LRLREILKEQ NQITASNVTE EEKNEKIQLL
EAEFTEILQN LVNISLKMTA RANLQHIKDI FNAVSERLEK LTQENQSDKL LLYLRALGIF
VGNYVGQERI QNTKVLTDIL ANEEDIIIQI LAIKILQSIS TKKSPDNAQK IIYIAQAPNL
LRSKEHQVTL LELLEQSKPQ DTLDFDIEKV SYGLNERITL ETISISKEEI LESKLKSSEL
AKDIAAKYSQ DNDKFTLKLQ TKIQWFKFQH SYNSSRQIVI AIMDAIYVSY GIIDQIRHAE
FANFLRDHYI NQSIEILQKS SDTEVVFSVL LTMIQAFAKG QGNLVSLDTL TKAPIIRNSP
SQQDQNETDQ RPILTKMLED VASVILTEDE FSNVKKQPSP KVFNGLVIIN DRIQYQVVIL
VLTIIRLMQA QHRGTAHYND VVNQIIGSLL KIVQDEPENK LYNFNPSVSF VAAQILKYIV
RPRLEEHNEI IAKFEKRLLF EVKHLEEEFY TWNDEENQRK IVDQRDRQQI IKTLLQLLAD
LVSRDQSGLG MSRKIMEGQL IQQFQSLLQY NNEEKGYLVD DILSKFYMLI GSICSDNPAQ
IPVLIKNSVI PELLQSFENR LPLSQDVFDT TLYGINQFSI HEEGQTLILG SNIFKSMLER
VTDPKLSQYL MTDQMIFRLY LGNVFDRNQQ FKEIAKEMVL KYIDVVKKFV KEQAIKFIQT
YRRTDLSEEE KITESSKGVS PSENQQIVAA LVMIHSFSFI SNDNLAHNRH SQEIMGGAVY
NQVLDLYKST VMIPSLKDYQ THFEKSLKIL IENQNYPLQV QSFADNLKSQ TDQFLNLVGM
PLYQLDDFDF QQKDENAELK PIEELDLENI ARYLTKGEHI MFQLSKIHNM IKLSFFLHTQ
TFNILIQNQQ MIKVSKVIFY IQKILQKQKA NYFIEQMEYL AQNQDSEEYK KCGQYLLKKY
SQDDTDTLEE RRERITKIKN YLYIDLITSF QAKRILKLRE KYFSDYFHKF QTQSFQMRNP
QAKEALEKNQ FFIGKLAYKA SKLFAKKQFE KIEIIPGSQS LLKALFQLAQ HLVEFWQKVQ
QCQLEGSSFY MFVKKGGLDN LIECFEWLSD ALPKIDQNFQ QVYVFLFDEA CSHLKLIFQA
LVNTRNSEAS INSLMNANMG TDYENAKNLY QTFYTILCNK LLHLNDPQSQ NIIQKLQHQR
SPYLQEIVIN LLKNSSKSFA SCPFLKDGIR NERDQYGRRN RNLADPVQVE LIMTMGMSFN
RDRVNQALIQ THNNLDNAVN LLLEWQMQEQ LGIGEGEQAQ QVNDELSSGQ SDDDYNQDMS
EAYMNLDGKF SEVKQKVKKA PKVTENEFSE TVKKAQQIGF KWIIESQQDP QFEYIKTSFR
DFIVTQMLSE KTELIQRQMY SEIDKIFKQN LSSFIEKLQN YKPKDQAGQD NDKDMEDINT
ISEEKQNECL QKASFSLQND INLILKLINN NKQYLKESII KSDAFIKISH LVQIMNRNFN
SSGLRRFLED DGQFGQFQRL LHDALVFSFT VVQLSQLQVN IYQSSKVQVE SCSKKMQIYQ
AKVPVADALN THTEILSAYL EQLQDEKKLK FKNAIAQTAS VLVLKILTGS QNLFNFNQQI
VQEKSLHLFD LLGKIQSTKP VNSMIQNSTL ILQIEDQKIL QAQMDKLSLR AMYLKYEYES
KNTEDHKIDS QSHIKSKAGF NNFLKYFSVI QQRDVATFKQ VLKDDFEVQT IKKLNQLSQD
QATIQIKEGK FSEIKKQIIK ERGQLKQLTK TFDFKNDKQA KLLIQQSKKI LLSTLNESFQ
QSIKTIITRV SDKSTALLDQ FSLFNQSQIN QQICLLPQDQ NKPLNLNQEQ TQMETLGQLT
LAYPAVTVPI LQSHPQPKRS FANWLIKDYI VSLMLIRKLK KVNLPISQPE AMEVSQESKN
YELSYKLITN IQPLASKISV LVNNLTSYNH LMNINEQAVK HQLRTKFMVE ALHVLQKAIK
DKSLHQLMQK SLIFSSLMVI ECLINFQDPT IQNRQVISQD NFINSIRVAI QRDATNKDSQ
LPGSLIRVID ELMGDVIDVT LDSNSLVIQK VVSILNVLAE FINNEKKKEE KKGKDKRGSP
KLSKGNPLEE EKKDQSSLSD QQRQEVARDL GGMIDPLSIA DRQAFHSDNV GGAGFQNIQN
QQDQESDDDE DDDGIMMDDD VEDEMNIDDG GNADDEEDED DDDGEDGDDM DDADGDEEDI
YDDDDDDLQA NAIVIGRNNA IFEEEDEEDM DDDDEGLDDE DEQIIIEENR AWGAGAVAGG
RIPQRLNDIL NPVDAAQANV DARGRAYIRF HDMNVDFQRR GAPPGNVVGS NWTEEEAEVQ
RILTQMRAHQ QPIVPPPAQI QNNPWDIQER VIYRANRDAP IADRQQAVVA SCFIDKMYEG
LKPISEREYL DIVQQNKQML LDELFEDQKA SNDGLQGKEK EVIESLVNAR QAINNIHRRI
EDMNDIMFDM EIPPLGNEFG GPVGARAVDM GMFHNDPMGG AAPFGIGNPL LDPLFMRPPQ
AFVDHNGLPV PVPGGYGNLF GGGAGLPPNP SGLDRQDNAL FNHYFRNQSQ VQTNLNDELG
QQLLETMDVQ FQEEKVPEVE KDKPKTEKLP TEQIIGLNMD MSNDQLLSGF FAPIINRNAP
AGGLIPSSVA NNNNNVIPPF DIGQALNIAN NLQQQQQQVP QQNAGGSPRF HRVPSQNEIQ
QERERVEERQ RELREIIERQ HQDIQQIISQ QNRQESASQD VQMQDEQQQI QQQNQNAIQP
VQDQINQINI SDDVPQQEQI QQQQQQPIQA SADQIMVEDQ QQQDDSISAF DDQVQQQNVQ
QPPVQVEEEK KQEQVQEPVA SSDDNKTFGY DNDLLIAHGL DPMILLELPE ELRVELLSTI
ELPPPQNPPV AQEQAQQQPR QDQQNQQEEQ KQQQPANQEN DIANELGLDP EFLANLPEDM
QLELIQNAQF RERNLGNQQQ QPPQREAEQM DIASFIATVV DPALRREIFS NMDEATVATL
PPNLMAEARR VQEQMRNERH RFRDNFDNVD RRVRGLLEQI DPRYNMGGGL NRDDQGGMFG
RARYGGGRAE EQKQKPQVGG KTLEEAVLAR HQQLFEEMSN EDFVSLLTYQ LTNDEKILEQ
LLLILMENQS VECSMIPCLQ NLIKIHSNGL PVIRNKVLNA ITFLLKSIAT NDEEAFKAIY
PNNTQLNLDS QKKKSALILI GCLRLLLRTN RSLMKHILKG LFVKDEKQNA AGTSTIKNNQ
MLKKQHKYNQ SLQQKVQEPQ KQDEISAFQE DQIMTTSSSQ KQNTSQVLPA LAEIFYLIRT
DMFKTNKSLL RNLSMLIHQI LKQFDIALEE LEQSNSTISS ETVQSLAEVL SLDSLDQTLM
EDLGEFLFQI SKKKRENFDL ISSYCHERAM NLVDSLTQRL SQVVQNFNEM KGRISPGKMQ
IMENYSPSQF GGESIYEEEK SEQMMIDTST NPLNELQRQT STAEVRNLSI KLQDEDEKLL
KQQLKMSDQS EMLLRILKLF NLFYEKFFAQ IKQDSLDQEI PTEEQNKDNI LQMVDYIHSI
YKNEKMTLFV KLVSTVMKIV YKTNIEAFEN LTQLLFCVFG QYFPEMILSV KDEEEQTKLQ
KQSSQGNQQS KYQIKMMSLD ESQGRQNKVV IFRNQNYFNN RVQEISSFCL GNKRLINKLI
KSKPNVFNVE LEGLIKYMPN LLDFDNKRVF FKRELSKLKK NQGYQTIQLF IRREDIFMDS
YAQISIRQPE EMKGRMQIQF TGERGQDAGG LTRDFFIELS RQMFNPMYSL FVLSSSGSTY
YPNPKSYIQA DHLRYFKFIG RVVGKALLEE CLLECYFVKS FYKIITGEPL MVADLEDFDN
EFYNNLKWCI ENDIATLETT FVVEQDHFGR TQDYDLIPNG STIPVTNENK SMYIEKLVHF
KLYKCIQQQI DAFLEGFYEM IPKDLIGIFN HKELELLISG LPNFDLNDLK QNTEYLGYNA
QSPQVLWMWD ILETFDNEDR AQFLQFVTGS SKVPLDGFKG LMGMRGPQKF TIAKIKTDDI
LRLPSGHTCF NQIDIPEYPS KEIMHERVLT AVKETKGFGF A
//
