ID E2BD42_HARSA Unreviewed; 2064 AA.
AC E2BD42;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN ORFNames=EAI_02899 {ECO:0000313|EMBL:EFN86384.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN86384.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN86384.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL447563; EFN86384.1; -; Genomic_DNA.
DR STRING; 610380.E2BD42; -.
DR InParanoid; E2BD42; -.
DR OMA; AEPLSQF; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008237; 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 CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.720.50; -; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000008237};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 790..866
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1718..2064
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2031
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2064 AA; 225955 MW; 4DB1D105B869DFE2 CRC64;
MADQQDQSSS GGSVEKASAA ADTSKVRGKG SSSGYSGYRK RQSTSAISDT VEEKRRRQIT
GDPQTSQVVS NTAHTHSTDS SKGEVRLRGE RRSHGAGLES YPDTNWRSHH KVHQTNYNIG
SSSTRVRSAA RTSLPELNLT ATDCVASRTR SRTPQNPQVL TQGTSSYDLS LSSGYSRKTA
ATFSDVVPSS STTSLTSHPS TSRGRGLRMS ECLEGFVSAV KALFPISTQT YHQEDSKSHG
GATCTSSSTS SQASSQGVKS SVRVGNAASN SVESGGGALA HDGAGTSGIA STATANPPVS
ATVSANPAHP HSTHKHLLRS RGKTSNEQYK ELPSNNKNSG KHHKKDSTTG SCSSSRHRSS
SRVRKPPVVE SGSGGLSSAM SGSDSISATP TSVSSSVPGS QLVSTTGEEE SASTATSATA
SGGPSGMSGT TGDSESDDGE VGRLQALLEA RGLPPHVFGA LGPRMQHLLN RSMGATAAAK
AQQLLPGLQN ADDEGEQLQA VIGMGEILVM GNEDTLTGFP VKQVVAALIN LLGIEHNFVI
MTHACRALTY MMEALPRSST VVVDAVPVFL QKLESIECMD VAEQCLTALA MLSRRHSKTI
LHAGGVSACL KFVDFFNITA QRAALTITAN CCQNLHPDDF HLVVDSLPLL TSRLTNQDKK
SVECVCQAFS RLVDSFQHDP VMLHKIINAE LLQNLQQLLM ITPPVNSIGN FITVLRMLSV
ISNRCPDLAQ LLLQQNIAFT LSYLLTGSLE VKTEDVELVS RSPQEWFEIT CLIEELMPPL
PTDGIFSVNS LLERTSNQQE TVHWEWRDER HCCHPFSTID SRIIEMAFQN GEDEICLSTL
GRTYTIDLTV MKQINEDMGM ARSIFRRVNA NPTEGKSPTC SSSMDVVPPV IETNEWLVSF
IRTLFSVLYE VYSSSAGPAV KCKCLRALLR MVYYASTDLL KDVLKNQVVS SHIAGMLASQ
DLRIVIGALQ MASILMKRLP QVFGVHFHRE GVLHQVRQLA DPEVPLGVSP PKCPSGTSLP
SPQPGPSNTP LSSTAMLSSS SATSPVVSPS TNGNILFGTI ASCQHNTNIA ASLEPHRTEL
SSNVDEPNTP QTHLRIGDVL KRKRQNKKGR FSRLGSATPQ QAQQPESLFT GFTPKNHRFL
GNLNPARWGR KSSSSSSTSD KRDSSSSTSL SKPPSNPSLT GGNRDKAKAW VREQAAQFLA
RYQDDAPCSH PALTVLARLT AAIQRLQSNE LDEMLSALTE LRDIVLESDI SPFEMNYSGL
IKALLNYLTT TDAPGNRYDR LRMFWKLFAE STMQQNNDIM DLNPGAFGAL VAKLNSCVAQ
LEQFPVKVHD LPAGSGAGRG GTSALKFFNT HQLKCNLQRH PDCNNLKQWK GGPVKIDPLA
LVQAIERYLM VRGYGRIRDA ESMVSDDDNS EDDIDDTLAA VVISQGSAKH KLQFLIGDVV
LPFNMTVYQA VRQFGCSGVD HSEAEADNEP PLGHDAVWVQ THTIYYRPVP EEDATTSPKS
GSSSQGSSRK GKGKSTKISS KRKEDSLWLE GTVPPQRCPL APYLSPSLPP SVTITDASLD
GLCLLRLLHA LNRHWGILFP HLKSMSLLSP QDFINNKIAA KASRQLQDPL VIMTGNLPSW
LQQIATVCPF LFPFETRQLL LYATSFDRDR ALQRLLDSAP ELSGSDSQER VTPRLERRKR
TISRTDILKQ AEQVIQDLAS SKALLEVQYV NEVGTGLGPT LEFYALVSKE LQRADLDLWH
GSSNPTENGY VNPVHGLFPA PIPWNTKVSH LAKLKTKFKF LGKFMAKAIY DSRMLDLPFS
LTFYRWLLGE EHTLTLADLA HVCPDVYRTL SKLQDVVRRK ETMEKDQTLR PHEKTQLIEA
LDLDNCLISE LGLVFELPGY ENIELRKGGS EIPLVVHWFL HEGVFRQMEA FREGFESVFP
PSQLRLFFPE ELEAVFCGHA QTGGQWDVKT LAECCRTDHG YTPDSRAIRF LFEVMSKYNS
EEQRQFIQFV TGSPRLPVGG FKSLTPPLTI VRKTFDSSMK TDDFLPSVMT CVNYLKLPDY
TTLEIMREKL RIAAQEGQHS FHLS
//
