UniProt: T1JUR4

Database: UniProt
Entry: T1JUR4_TETUR

LinkDB:  T1JUR4_TETUR 
Original site:  T1JUR4_TETUR

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (14)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (2)   
   SMART (2)   
All databases (26)   

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ID   T1JUR4_TETUR            Unreviewed;      2410 AA.
AC   T1JUR4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE            EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur02g01890.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur02g01890.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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}.
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DR   EMBL; CAEY01000780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAEY01000781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAEY01000782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 32264.T1JUR4; -.
DR   EnsemblMetazoa; tetur02g01890.1; tetur02g01890.1; tetur02g01890.
DR   eggNOG; KOG0168; Eukaryota.
DR   eggNOG; KOG0170; Eukaryota.
DR   HOGENOM; CLU_486263_0_0_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0009966; P:regulation of signal transduction; IEA:UniProt.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
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; 2.
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; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Transferase {ECO:0000256|RuleBase:RU369009};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        368..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          448..524
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          2219..2410
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          14..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          890..963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1230..1316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1636..1680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1738..1811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2091..2125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1238..1289
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1290..1308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1738..1809
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2091..2105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2377
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   2410 AA;  264224 MW;  4989CC4DEFA8AB6A CRC64;
     MALVVLLELV GGSGDRGSSG GGGSSSSSSL PLSSLSSSGA LDSEPDDNEM GRLQALLEAR
     GLPPHLFSAL GPRVHHLLHR SMGNKTSSRA HQLIQGLQAQ GDEGQQLQAV MEMCQLLVMG
     NEDTLAGFPA KQAVPALIAL LQLEQNFDIM NHSCRALTYM MESLPRSSAI VVDAIPAFLE
     KLQFIQCMDV AEQSLTALEM LSRRHSKAIL HAGGVPACLS YLDFFTINAQ RAALSITANC
     CQNLTREEFS YVKDSLSTLG SHLVKYQDKK CLESLCLAFS RLVESFQHHP EILQQITENN
     LLSNIQQLLL VSPPIISTGT FVMVIRMLAT MCASCPQLAV QLLKLSEYCF LFLLYAYLLY
     YNLMACQFLL RFNFLFLYFF TNYIFFFYLH KILDIADTIR YLLVGSSATK EYIELTTRSP
     QELYEITSLI GELMPKLPTD GIFSVDGYWL KQTNVIPSGV TWQWKDDRGM WHNYSAIDSK
     MIEAAHLASE DEMSLTTMGR TYVIDFNSMQ QINEDTGTSR LIQRLVNNSD GTTSTSSIIW
     FRFIWSYDDD DIRCNISLSS RSSRSSIRNV NSSNNSSTPN NTPPNKMHNH NNSHSSMMKA
     MMMSNVNEND ARIQCLKEEP ELAESFIKSL FGVLYEVYSS SAGPSVRHKC IRALLRIIYY
     SSSDLLRIVL KNHAVSSHIA AMLPSSDLRV VAGAIQMVYI LMEKLPDIFA IYFRREGVIH
     QLKKLISNDG TIIGEASPIS AYIPSSSPNK SSTNIKIESR LQYQLQQQQQ QQQQQQNQHQ
     HKHQPQQQQQ KQQQQTGQST SSSPSSLIGQ SYVSSCFLES GSPLSNISPL QSFSSSCGMP
     HEVFTAQTND INMVNNNNIN NNNDNNQEST NATTNPIAIT TSAASNATIT ATSSPSSSKG
     STSGSPPASS SSSSSSSLSS NSNSNSCSSN SNSSSIGGVA GSIGGTSSNS NNSSSRSKNR
     GGIDSLSMHF NNCINSSSPL PLSNMHGNNR GVSGGDYDPM TANLSSHFFS TPYLSMPFFP
     YSGNSGTPSS GNSSAASSTP ATPNTNSTDA QTNYNNNNNN NNVLTPTSSN IIGPQRGLHN
     NLGLNAFGSG CPFGVTPSSS SSSPLSGSNT LGFGSSSGLS LNNNPTASTS TSSSSLGGGL
     PAAQAAAQAA AQAAAAAAAA AAAASAAATA TTTSRGSSRS SSKLSSAAAK TSSFFANLYP
     ARWRRWNTAG PNIIGSNAGS NLSNRKSMLI SQSQDQLGHH HHHHHHSHSH HHGHHSHGHH
     SHSHHHHSSH SPSSSSHSHH NHSHHSHHHL AGSSSSTSGS PRSPHSSHSS NGNKEKIRSW
     IREQAKAFVE KYFNNENEMN EAMSTLNRIN GAIEIFENSC DLEGLKEFRS VLLDGDISPF
     ELINCGIIGK LITHLTFTED GEEDRNMRIR RFLHVFLGTP VDDNTVINDE NELNLDTRPM
     SSLVSKLNAC ISQLEQFPVR VHDVIGTGTG NIRGTSALKF FNTHQLKCNL VRHRDCTTLK
     QWRGGPVKID PLALVQAIER YLLLRGYGRV KEDDDDGNSD DDNSDDDFED NMASVVMNQG
     QGRHKIQFLI DDRILPYNMT VYQAIRQFSG GAGNSQSIDG HETDTDFDGP MGNSNMWVTT
     HTIYYRSLND RLPSVSYPSA STSSTNSTPT STAGIIGTNT NTNNNNNNNN NNSRSSRSGR
     GTISAAALLS DITPISNMTN TVGSGSSSSS STPSSSVLNH HLTCSGNCAS NNGHSYSYPS
     TSTSSMTPSS STAISASSGI GSSGINTSNT TTYGRRAASK SANKNSTSNS PLSFPSSISL
     SSSSSSGSKK KDELWLEGKT PTISSIVYNY LIPSLPNCVN IEDSSLEVMS LLRILNALNR
     CWSWFYNLTI SSNPAIPQSE FVNSKLTAKA NRQLQDPLVI MTGNLPQWLS QIAYVCPFLF
     PFETRHLLFY ITSFDRDRAL QRLLDTTPGL NSSDTSERVT PRLDKRKKTV TREDILRQAE
     SVFHDIGNSK ALLEIQYENE VGTGLGPTLE FYALVSKELQ RADLDMWRGE AITSSSVIMP
     LSYSNDKLAT TGSPHYGSNE MMIDINQLLK NDVTKTNRKH CNTNLIQQNQ QNQNQNQNQN
     KNQNQNHQSH RHHQNQQHQQ QQQQQQQQQL LLQQQAQQAI QYIYSSEGLF PSPVGKSTKT
     TSLSKLKSRY RLLGKFMAKA LSDSRMERGV SGLNRESLTL SGVEIEDLHL DFTLPGFPQI
     ELRKGGKDMS VTLENIDQYL RLMVHWTMVE GVSRQMEAFR EGFESVLSLA QLQIFYPEEL
     EQLFCGCSHQ SWDLKTLIDC CHPDHGYTYD SRAIKYLFEV LSSFNGDEQR KFLQFVTGSP
     RLPVGGLKSL TPPLTVVRKT FEPGENPDNY LPSVMTCVNY LKLPDYSSIE IMREKLLFAA
     NEGQHSFHLS
//

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