ID J9E8Z2_AEDAE Unreviewed; 2138 AA.
AC J9E8Z2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
DE Flags: Fragment;
GN ORFNames=AaeL_AAEL017357 {ECO:0000313|EMBL:EJY57371.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EJY57371.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EJY57371.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EJY57371.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EJY57371.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EJY57371.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EJY57371.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EJY57371.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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; CH477215; EJY57371.1; -; Genomic_DNA.
DR RefSeq; XP_011493146.1; XM_011494844.1.
DR STRING; 7159.J9E8Z2; -.
DR VEuPathDB; VectorBase:AAEL017357; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR eggNOG; KOG4276; Eukaryota.
DR PhylomeDB; J9E8Z2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000682892; 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; 3.30.2160.10; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 444..521
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1806..2138
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1711..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1777..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1711..1732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2105
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 2138
FT /evidence="ECO:0000313|EMBL:EJY57371.1"
SQ SEQUENCE 2138 AA; 234409 MW; F3B7F13508F3AB56 CRC64;
GSHRGGGSGS ASANLHSAGS SSGATAKGSS SKGASSYSSS VLTANNNNST SLGSLAAGYD
PTAAAPGPSN SAMANDGSRA AAAAPHPDSE SDDSEVGRLQ ALLEARGLPP HLFGALGPRM
HHLLHRTMGA NSSSKAQQLL QGLQCQDESQ QLQAAIEMCQ MLVMGNEDTL AGFPIKQVVP
ALITLLRMEH NFDIMNNACR ALAYMLEALP RSSGTVVDAI PAFLEKLQVI QCMDVAEQSL
TALEILSRRH NKSILQANGV SACLTYLDFF SINAQRAALA ITANCCLNLH AEEFHFVKES
LPLLARLLAQ QDKKSVESIC TAFYRLVDSF QHDPTILQEI ASMELLKNCQ QLLVVTPSVL
NSGTFTNVVR MLSVMCANCP DLAITLLKND IASTLLYLLT GSAEPVTADV ELVPRSPSEL
YEITCLIGEL MPRLPTDGIF AVDSLLERTQ ANVQDAVQWQ WKDDRGVWRP YSSIDSRMIE
AAHLNSDDEI SLSTLGRTYT IDFHSMQQIN EDTGTTRAVQ RKINHALLAQ QQGTVVINTG
GIPGGVTISS ETGEVTPNCS VGTGSVNLAT RPPNATRDAR IACLKEERGL AAEFIKNLFS
VLYEVYSSSA GPSVRYKCLR ALLRMVYFAN GDLLREVLKN QLVSSHIAGM MASNDLRIVV
GALQMAEILM QKLPEVFGMH FRREGVVHQI TQLTDPTIPI CAAPSPKSGA QSAPSSATIH
PNNTFDFDSA IASSSKSGTQ AIAIVGGAGP HVKNLNSAMM MASKISMSMP STSSNLLHSP
TSAANLPGTS SSFTAINLNT SAKALHHNHH HHQQMSTSTL HLESLATNMQ PNIPGAIATP
NNGNILLNAI YSSAIPINQQ ASHHHQSESA VATTVAASHH DTRSHSPGQL KVSDILKRKV
PPKRKSQSSS KSKSRHDDAG SHSVASGSNM AGSSGSSTTS SVMQELINKA TTLGSSSGRN
TPSSSSRSRF SGASSKTTSF LASLNPARWG RQSSSSSSHH SSTSFAKDGS NALAKSQSNS
NLIAAGNREK ARQWIREQAI TFVNRYSTDN AGATSGSLHP ACSILSRLTG KSNYEYQRVS
RHCFQQYQRS IEQKLKRHPK SFWKYVNEQR KESGFPSSME WNGRTATCLQ EICQLFSSKF
ASLDGNQVDC LLALKELRDI LIESDISPFE VNHSGLIRAM LTYMANDANQ LVERADRLRM
FLHVFANLPL DANFSSNVSP AINSAPFSAF VAKLNGCVTQ LEQFPVKVHD FPAGVGGRSN
TSALKFFNTH QLKCNLQRHP ECTNLRQWKG GTVKIDPLAL VQAIERYLVV RGYGGIRVDS
EEDSEEDIDN IDAAAMISMG GLKHKLQFLI GEHVLPYNMT VYQAIRQYSP LVNDQSETDT
DTETPIGKWF PPTFFYKCLK FLFSRRIRKK NVCNLSIVSL FQLQEAPAFG SSSTPYITAR
ASKSGQSSSS RKNSKNSQSK IMRRKPEFWI DGIAPPIISS LMPFLTSKLP DVVSVQDASL
DALCMLRIIN ALNRHWATLY FSVPQSHIIP QIEFIHSKIA AKASRQLQDP LVIMTGNLPQ
WLQQIAAACP FLFPFETRHL LFYAVSFDRD RALQRLLDTT PDLNSADTSE RVTPRLDRRK
QIVYSGMLRE LIIFFCDFGH SKALLEIQYE NEVGTGLGPT LEFYALVSTE LQRCDLGLWN
DSDSYKNNNN QQSSSIADNI VKSSLNQIDD DTTNAATTTN RSSLSPMATR HQHHQHQQQD
SDHNVSDGSF VISNDNSLNM LIEQSDNLLL SSNPQQAELE NNQTPPPMTQ QHSLVSPASG
AGGSSGTVSY VNAPHGLFPI PLSKTAKTSQ ISRLKYKFKF LGKFMAKAVM DSRMLDLPYS
IPFYRWLLAE ENSIGLPDLD QVAPEVQVTL LRLNEIVKQR DLIQADLTLD AMEKTEKIEA
LDLDGCPIAD LGLDFVLPGH PNIELRRGGR DTAVTIHNLH QYISLVTHWF LVEGVSRQFE
ALREGFDSVF PVNRLRMFYP EELENVFCGS GLNAASHQRW DVRMLAECCR TDHGFSQDSQ
AIQYFYEILS TYNREEQRLF LQFVTGSPRL PTGGFKALTP PLTIVRKKMD GNQNPDEYLP
SVMTCVNYLK LPDYSSREVM RQKLKLAASE GSMSFHLS
//
