ID D6WYJ4_TRICA Unreviewed; 914 AA.
AC D6WYJ4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN Name=AUGUSTUS-3.0.2_06704 {ECO:0000313|EMBL:EFA08997.2};
GN ORFNames=TcasGA2_TC006704 {ECO:0000313|EMBL:EFA08997.2};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA08997.2, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:EFA08997.2, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA08997.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [2] {ECO:0000313|EMBL:EFA08997.2, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA08997.2,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(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|PIRNR:PIRNR001569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR EMBL; KQ971362; EFA08997.2; -; Genomic_DNA.
DR RefSeq; XP_008197286.1; XM_008199064.2.
DR AlphaFoldDB; D6WYJ4; -.
DR STRING; 7070.D6WYJ4; -.
DR EnsemblMetazoa; TC006704_001; TC006704_001; TC006704.
DR GeneID; 103314102; -.
DR KEGG; tca:103314102; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_1_1_1; -.
DR InParanoid; D6WYJ4; -.
DR OMA; QWDRPRH; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007266; Linkage group 8.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0060322; P:head development; IMP:iBB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd08382; C2_Smurf-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 3.
DR Gene3D; 2.60.40.150; C2 domain; 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 InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF395; E3 UBIQUITIN-PROTEIN LIGASE SMURF1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 5.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 3.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..118
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 172..205
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 365..398
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 413..446
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 577..914
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 146..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 882
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 914 AA; 102508 MW; E429E64831AFB215 CRC64;
MSNAPTSRRN GAQKIRLTIL CARNLVRKDL FRLPDPFAKI SVDGSGQCHS TEFVKNTLEP
KWNSHYDLYI GRNDSITISV WNHRKVIKKQ GSGFLGCVRI VNSHIQRLRD TGYQCLDLGK
ACPADSEPVK GQIIISLLSR DGPCSGTPLA VVGPQGELRG PTDRDSSPSN NDDLPPGWEE
RRTENGRPYY VNHITRSTQW IKPQSTNKTR RRSTHQNDNN NTNNENTIGG TQMGVQEILN
NNTGETLTPS SSTSPVSPVV SPQKTTSTPQ TTDNRNNFIT LSPTSTSVIP APNNISCNAP
NGENTNVVSP QMGQGQGQRA IVRSERRQRS AEERRDGSSR RRSGRNNRNS GGTTAQGPVT
QNSKLDLPPG YELRTTQQGQ VYFYHIPTGV STWHDPRIPK DLAPLSLALD HLGPLPPGWE
MRQTASGRIY FVDHNNRTTQ FTDPRLNTQI LNNILRRASA TSTTTPTTRT TPTTTTASTT
SPSTSTTTVT TTTTTTAVPQ NPAPLSPPPR TRIVEELPQS LLNDCDHLPK YRRDLVAKLK
TLRAELTALQ PQSGHCRLEV SRNEVFEESY RLIMKMRPKD MRKRLMVKFK GEEGLDYGGV
AREWLHLLSR EMLNPQYGLF QYSRDDHYTL QINPDSAVNP EHLSYFHFVG RILGIAVFHN
HQLEGGFTLP FYKQLLNKPI TLQDIEGVDP ELHRSLTWML ENNIDGVLDT TFSVENNSFG
IVKVHELKPS GATIPVTEDN KREYVKLYVN YRFMRGIEQQ FLALQKGFTE LIPPSLLRPF
DERELELVIS GIGSIDIADW RSHTRLKHCT PETPVVQWFW QVVESYSEEM RARLLQFVTG
SSRVPLQGFK ALQGSTGAAG PRLFTIHCID CSPQNLPKAH TCFNRIDIPP YDSYQTLADK
LTQAVEETCG FAVE
//
