ID D6WL15_TRICA Unreviewed; 999 AA.
AC D6WL15;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=AUGUSTUS-3.0.2_13531 {ECO:0000313|EMBL:EFA03528.1};
GN ORFNames=TcasGA2_TC013531 {ECO:0000313|EMBL:EFA03528.1};
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:EFA03528.1, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:EFA03528.1, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03528.1,
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:EFA03528.1, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03528.1,
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KQ971343; EFA03528.1; -; Genomic_DNA.
DR RefSeq; XP_008193676.1; XM_008195454.2.
DR AlphaFoldDB; D6WL15; -.
DR STRING; 7070.D6WL15; -.
DR EnsemblMetazoa; TC013531_001; TC013531_001; TC013531.
DR GeneID; 659647; -.
DR KEGG; tca:659647; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR HOGENOM; CLU_007287_0_0_1; -.
DR InParanoid; D6WL15; -.
DR OMA; HDAIGKD; -.
DR OrthoDB; 45541at2759; -.
DR PhylomeDB; D6WL15; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007266; Linkage group 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16726; RING-HC_MIB2_rpt1; 1.
DR CDD; cd16520; RING-HC_MIBs-like; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00184; RING; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 1..73
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 79..131
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 142..220
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 462..494
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 495..527
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 528..560
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 629..653
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 663..695
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 956..989
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 806..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 999 AA; 110121 MW; 25C5633527DE3553 CRC64;
MLTPGVRIVR GPDWSWGNQD GGEGFVGTVC EIGKSGSVGS PDKTAVVQWD NGTRTNYRVG
YLGKFDLLVI DNAQIGVKHP NIVCDGCKSQ GICGMKYKCC VCFDYDLCYM CYHGDKHDLD
HTFKRFDSAT ALGVDLPPRQ NGRKCELKGI FVGAKVVRGY NWEWGNQDGG DGKVGRVLDI
RGWDKESSRS VANVTWLSGS TNVYRLGHKG DCDIKFVEPA SGGFYYPEHL PILGHNIEQA
VARPVRSGPP PFSVGDKVKV VVSEEQLKTL QQGHGGWNPK MAEYIGKIGK VHRVTDKGDI
RVQYEGCHNR WTFNPVTLSK VNSVAVGDIV CLSTDIEKVK ELQKGHGEWI EIMKNSLGKL
GKILKIYSDG DLRVQLDGHA WTLNPQCVRI VPGSAAELAN TMQATQNQRQ EPSMEWHPAN
PADNQTNGVA DQLVRAAAQG HLETVQRLLE GVSRTMVDMR SGGKTALQVA AHQGHAAIVR
LLLHAGASVN ASDNDGDTCL HYAAFGNQPE VLDLLIKAGA DLNTANRSGC TALHIAAHKQ
PARCVQILLS AGADPNCTDL YGDTALHDAI GKDSYQVIEL LCAASGIDFT LRNKRGFNAL
HHAALKGKNF ATRKLLTQAR QLVDVKKDDG FSALHLAALN GHKEVVETLV HVGQADINLR
NNRNQTALLL AVSQGHCGVI ELLIKLKANI NAKDEDEDTA LHLVFIKKAH LNGEIRQEES
PDMFAIYESI GQVSEYRLAV TIACYLIQKG IDLDTLNSKG QSALSLLQDS SLQELLKSYK
PNLDSNQIQE NTQETLNLES LNLTEPRHSM DGYNLTDNTP KHSPARNLFD DSKSSRRSRR
EQKNEKILDI GGTSQENSPN HKNHYYQNEI VSSKPVECLV CSELSEENVR LEPCNHKPAC
EDCSSRMKKC LQCGSIVQKR ITKDGRVIPA KSRQPSAERM RYLECKIAEI EESHACSICM
ERKRNVVFLC GHGTCSKCAD TLKTCHMCRK TITKKIPIY
//
