ID A0A026W567_OOCBI Unreviewed; 2061 AA.
AC A0A026W567;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN ORFNames=X777_09894 {ECO:0000313|EMBL:EZA51217.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA51217.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA51217.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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; KK107405; EZA51217.1; -; Genomic_DNA.
DR STRING; 2015173.A0A026W567; -.
DR OMA; AEPLSQF; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053097; 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; 3.30.2160.10; 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 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:UP000053097};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 772..848
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1703..2061
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..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..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2027
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2061 AA; 225799 MW; 15903F9CAEE38F4C CRC64;
MADQQDQLSS GGSVEKASAS ADTSKPRGKN SSSGSSNYRK RQNTGAISDT VEEKRRRQAI
SDPQTSQVHS NTAHAHSVDS SREESRVRGE RRNHGTGLES YPDTDWRPHH KIHQASYSSS
SSSARVRSVA RTNLSELNLT PTDCVASRTR SRTPQNPQAL TQGSSSYDLS LATGYSSRKT
STYNLVASSS ATSITSHPST SRGRGGQRMS ECLEGFVSAV KALFPISTQT YHQEDSKSHG
GAATCSATSS STSSQVLGVK SSIRVGNAAS NSVESGGGAL AHDGAGTSGI ASTATTNPPV
SAAASANSAH PHSTHKHLLR SRAKASVEQS KELPSSNKTS GKHHKKDSTT GSCSSSRHRS
SSRVRKPVVE SGSGLGTVMS GNDSISATSV SSSVPGSQLV STTGEEESAS TATSATASGG
PSGMSGTTGD SESDDGEVGR LQALLEARGL PPHVFGALGP RMQHLLNRSM GASSAAKAQQ
LLAGLQAVED EGEQLQAVMN MGEILVMGNE DTLTGFPVKQ VVAALINLLG IEHNFAIMTH
ACRALTYMME ALPRSSTVVV DAVPVFLQKL ESIECMDVAE QCLTALAMLS RRHSKTILHA
GGVSACLKFV DFFNITAQRA ALTITANCCQ NLHPDDFHLV VDSLPLLTSR LTKERRVFQH
DPVMLHKIIN AELLQNLQQL LMITPPVNST NNFITVLRML SVISNRCPDL AQLLLQQNIA
FTLSYLLTGS LEVKTEDVEL VPHTPQEWFE ITCLIEELMP PLPTDGIFSV NSLLERTSNQ
QETVQWEWRD ERQCFHPFST IDSRIIEMAF QNGEDEICLS SLGRTYTIDL TVMKQINEDI
GMARSIFRRV NANPTEGKSP TCSSSMDVVP PVIETNEWLV SFIRTLFSVL YEVYSSSAGP
AVKCKCLRAL LRMVYYASTD LLKDVLKNQV VSSHIAGMLA SQDLRIVIGA LQMASILMKR
LPQVFGVHFH REGVLHQVRQ LADPEVPLGV SPPKCPSGTS LPSPQPGPSN TPLSSTAMLS
SSSATSPVVS PSSNGNILFG TIASSCQYKP NISASLEPHR TELSGSVEEP STPQSAHLRI
GDVLKRKRQN KKGRFSRLGG TTTPQQAQQP ESLFTGFTPK NNRFLGNLNP ARWGRKSSSS
STSSDKRDSS SSTNLSKPPS NPSLTGGNRD KAKAWVREQA AQFLARYQDD APCSHPALTV
LARLTAAIQR LQSNELDEML SALTELRDIV LESDISPFEM NYSGLIKALL NYLTTTDAPG
NRYDRLRMFW KLFAESTMQQ NNDIMDLNPG AFGALVAKLN SCVAQLEQFP VKVHDLPAGS
GAGRGGTSAL KFFNTHQLKC NLQRHPDCNN LKQWKGGTVK IDPLALVQAI ERYLMVRGYG
RIRDADSMVS DDDNSEDDID DTLAAVVISQ GSAKHKLQFL IGDVVLPFNM TVYQAVRQFG
CSGVDHSEAE ADSEPPLGHD AVWVQTHTIY YRPVPEEDAA TSPKSGSTSQ GSSRKGKGKS
TKISSKRKED SLWLEGTIPP QHCPLAPYLS PTLPSSVTIT DASLDGLCLL RLLHALNRHW
GILFPHLKSM SLLSSQDFIN NKIAAKASRQ LQDPLVIMTG NLPSWLQQIA TVCPFLFPFE
TRQLLLYATS FDRDRALQRL LDSAPELSGS DSQERVTPRL ERRKRTISRT DILKQAEQVI
QDLASSKALL EVQYVNEVGT GLGPTLEFYA LVSKELQRAD LDLWHGSSNP TENGYVNPVH
GLFPTPIPWN TKVSHLAKLK TKFKFLGKFM AKAIYDSRML DLPFSLTFYR WLLGEEHTLT
LADLAYVCPD VHRTLSKLQE VVRRKEAMEK DQTLRPHEKA QLIESLDLDS CPISDLGLVF
ELPGYENIEL RKGGSEISVT IHNLDQYIKL VVYWFLYEGV FRQMEAFREG FESVFPPSQL
RLFFPEELEA VFCGHAQTGG QWDVKTLAEC CRTDHGYTPD SRAIRFLFEV MSKYNSEEQR
QFIQFVTGSP RLPVGGFKSL TPPLTIVRKT FDPSMKTDDF LPSVMTCVNY LKLPDYTTLE
IMREKLRIAA QEGQHSFFHL S
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