ID B0X0Z0_CULQU Unreviewed; 2335 AA.
AC B0X0Z0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN Name=6046054 {ECO:0000313|EnsemblMetazoa:CPIJ012812-PA};
GN ORFNames=CpipJ_CPIJ012812 {ECO:0000313|EMBL:EDS38382.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS38382.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS38382.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ012812-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ012812-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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DR EMBL; DS232249; EDS38382.1; -; Genomic_DNA.
DR RefSeq; XP_001863312.1; XM_001863277.1.
DR STRING; 7176.B0X0Z0; -.
DR EnsemblMetazoa; CPIJ012812-RA; CPIJ012812-PA; CPIJ012812.
DR KEGG; cqu:CpipJ_CPIJ012812; -.
DR VEuPathDB; VectorBase:CPIJ012812; -.
DR VEuPathDB; VectorBase:CQUJHB008565; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR HOGENOM; CLU_000366_2_0_1; -.
DR InParanoid; B0X0Z0; -.
DR OMA; THFDISH; -.
DR OrthoDB; 1093891at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
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; 3.90.1750.10; 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 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; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000313|EMBL:EDS38382.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 880..957
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 2254..2311
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1848..1876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2127..2166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2194..2216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1857..1872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2127..2150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2194..2214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2335 AA; 250032 MW; FC2268B53254424A CRC64;
MADSVVTEGH HHHQQQQQQQ QHHRNHQQQS AASSSNAGSS SSSRRSRARS SQTAATSQKH
HQRVVVVNTA EQQPATANRK RKLEDATTTH STPSPVAFRT RSRTVSKEVP LAGAPVDVRN
KRHSHGGSTS HESTKIASSA HATSSHSSGR ATLIASPSVA STVFCQSSAS STTAVAGPSG
SGSSSSRGAI EKRKRKKSGQ LSKQLVEQYL QEEPAERRRS KSGQQKQQVS GEEGRSLRST
HHQQEVGGGL TGAAVPKKRQ KVGDQHQQPD GTAGSHKAPN LGARLARSSG GREPHQQQQH
HFGAGGGHLS SSAAAAGGSQ GHLPSGLLRR SSRGKGSHQS GTTGSCVSSN TANPSQQQQQ
QQPQSSSQSS RSGSHRGGGG GSSGSTSGNL HNSSAGTSGT KGSSSKGSSS SNNNNSTSLV
GSVAAAATAP GPSHSAMASD GSRNNNNEHH HQQQQQNSSS SSHPFIKLHK TTSLGSSSAQ
SSAGTSSAID VNMLNMANAA GATASNSANL GGAAGAAAAV PHPDSESDDS EVGRLQALLE
ARGLPPHLFG ALGPRMHHLL HRTMGANSSS KAQQLLQGLQ CQDESQQLQA AIEMCQMLVM
GNEDTLAGFP IKQVVPALIT LLRMEHNFDI MNNACRALAY MLEALPRSSG TVVDAIPAFL
EKLQVIQCMD VAEQSLTALE ILSRRHNKSI LQANGVSACL TYLDFFSINA QRAALAITAN
CCLNLHSEEF HFVKESLPLL ARLLAQQDKK SVESICTAFY RLVDSFQHDP TVLQEIASME
LLKNCQQLLV VTPSVLNSGT FTNVVRMLSV MCANCPDLAI TLLKNDIAST LLYLLTGSAD
PVTTDVELVP RSPSELYEIT CLIGELMPRL PTDGIFAVDS LLERTQANVQ DAVQWQWKDD
RGVWRPYSSI DSRMIEAAHL NSDDEISLST LGRTYTIDFH SMQQINEDTG TTRTVQRKIN
HALLAQQQGT MIITAGTLAT LSTAASLSSE TGEPSAVGTG CVNLATRPPN ATRDARIACL
KEERGLAAEF IRNLFSVLYE VYSSSAGPSV RYKCLRALLR MVYFANGALL REVLKNQLVS
SHIAGMMASN DLRIVVGALQ MAEILMQKLP EVFGMHFRRE GVMHQINQLT DPSIPICAAP
SPKSGAQSAP SSATIHTTHT TFDFDSAIAS SSKTGTQAIA IVGGAAGPHV KNLNSAMMMA
SKMSMSMPST SSTLLHSPTN VMPGTSASSS GSFTAINLNA STKAALHHTN HHQQMSTSTL
HLESLATNMQ QQQQQPTSIP GAIATPNNGN ILLNAIYNSA IPTNQPGHHH HHAVAHHHQP
EAGSSKQSHL YQTHPHFSDT FAYNAEQGIL TSPLSVPSGA GATLVATSAV AASHHDTRSH
SPGQLKVSDI LKRKVPPKRK SQSSSKSKSR HDDAAGSSAA AAAAAMSSGS TTTSAAGSST
TSSVMQELIN KATTLGSSSG RNTPSSSSSS RSRFSGASSK TTSFLASLNP ARWGRQSSSS
SSHHTTTTSA FGKDASGNAL AKSQSNSNLI AAGNREKARQ WIRDQSITFV SRYSSDGGAA
GAGGSAGSLH PACSILSRLT GAIQKLDGHQ EDCLGALKEL RDILIESDIS PFEVNHSGLI
RTMLGYMANE ANQLVERADR LRMFLHVFAG LPLDANYSSA VAPPSLNAAP FGAFVAKLNG
CVTQLEQFPV KVHDFPAGVG GRSNTSALKF FNTHQLKCNL QRHPECTNLR QWKGGTVKID
PLALVQAIER YLVVRGYGGI RVDSEEDSEE DIDNIDAAAM ISMGGLKHKL QFLIGEHVLP
YNMTVYQAIR QYSPLVNDQS ETDTDTETPI GSASIWVQQH TIYYRPVEEE SGAAGSGSKS
GAANSSRKNS KNSQSKIMRR KPEFWIDGIA PAIASPLVPF LVSKLPEVVT VQDASLDALC
MLRIINALNR HWATLYFSVP QSHIIPQTEF IHSKIAAKAS RQLQDPLVIM TGNLPQWLQQ
IAAACPFLFP FETRHLLFYA VSFDRDRALQ RLLDTTPDLN SADTSERVTP RLDRRKRAIS
REDILKQAES IIQDFGHSKA LLEIQYENEV GTGLGPTLEF YALVSTELQR CDLGLWNDSD
SYKNNNNQQS SAIADNIVKS SMNQIDDDTA TANTNSSRSS LSPTAATRHH HQQQQDSDHN
VSDGSFVISN DNSLNMLIEQ SDNLLLSQNP QQAELENNQT PPPPTQQQHS LLSPAAGSAG
AGAVSYVNAP HGLFPIPLSK TAKTSQISRL KYKFKFLGKF MAKAVMDSRM LDLPYSIPFY
RWLLAEENSL ALSDLDQVAP EVQVTLLRLN EIVKQRDLIQ GDPGLDAMEK TEKNL
//