ID A0A139WAN5_TRICA Unreviewed; 2920 AA.
AC A0A139WAN5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=AUGUSTUS-3.0.2_16227 {ECO:0000313|EMBL:KYB24996.1};
GN ORFNames=TcasGA2_TC016227 {ECO:0000313|EMBL:KYB24996.1};
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:KYB24996.1, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:KYB24996.1, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB24996.1,
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:KYB24996.1, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB24996.1,
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KQ971380; KYB24996.1; -; Genomic_DNA.
DR EnsemblMetazoa; TC016227_003; TC016227_003; TC016227.
DR InParanoid; A0A139WAN5; -.
DR OMA; IFANCRI; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007266; Linkage group 10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd08664; APC10-HERC2; 1.
DR CDD; cd14402; UBA_HERC2; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR021097; CPH_domain.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR037976; HERC2_APC10.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR22870:SF398; E3 UBIQUITIN-PROTEIN LIGASE HERC2; 1.
DR PANTHER; PTHR22870; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF11515; Cul7; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF06701; MIB_HERC2; 1.
DR Pfam; PF00415; RCC1; 5.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM01337; APC10; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS51416; MIB_HERC2; 1.
DR PROSITE; PS50012; RCC1_3; 5.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 REPEAT 541..592
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 593..644
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 647..698
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 699..750
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 751..802
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 1178..1254
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1864..1937
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 2676..2727
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 2731..2905
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT REGION 1306..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1526..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1934..1954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2920 AA; 325836 MW; 229CE794F21435A9 CRC64;
MSRFETTLRP QPRLDLKWLK TDLQSVLTEE DTLVNCWNNL VADGEVTGAF SDGLLNSAGV
TARKGEFGKY YCNQKVLTCT CCDGICGPST GCNCQPCQKL DEETALTEVK EPLPSTEALL
GQWAWMPQPS LEQLSQFVLS LNNEQKVLCA EAASSTLSAR RLYYRLIVLK RYFVALNRVP
HSVDFEHGLI TSRKSNSELL QTRNLVKLSK RAWNLEPAIA LARVGSRAAL NFAFAFLRKA
WRLGEDIDLC REDIDLCSEL LTESLEALQM LPVATLFHQS DVSPVWLEVV ERSSKFLRQV
ITGDISGSRQ NFAIPLEDQH TSLNLLMELG IQKGTLSSIL DIVLLLLNLW DKQTNLNDNR
SNVQMASAPL LPFLKRFSQI PHALPEFHEK DTTEENLSTT QTYLSFVELP EDDTVEIDLK
QAASFIMAHL DRLAEPHIPP LSFNKSNFYY NGQRVFGWGW FSWIFGVGPQ NCDTLSELTI
KQICCSDRTI LILTQTGKVF FMYYSSDTQC PQEMTALDDK EVIKIAAHPE GKHYLALTKD
YEVYSWGNGD GGRLGHGDTS TKEEPTLIQA LKGKDIIDVE CGGTYSAAIS ANGALYTWGR
GNYGRLGHGT AEDCLTPTMI SALSDEHIIK VACGSFYAHT LCITSQGKVY SWGDGDYGKL
GRGGSDGSKL PRLIEKLQNV KIVQVYCGAQ FSVALSEDGH VYTWGKGEGW KLGHPTEENV
RFPEMVEVLR DRKVVGVSLG VSHVLALTDQ GEVYGWGKNE NKQICDSSEL FVQQPRLIEA
LKGQKVVGVC CGPAQSFAWT DDNERTPKTA VPFVIDLGEQ TFKLIENLLE VVLTNTIAQD
KECIAVSALN LLHLQLHCII SNNLDTKTLG IGANSKLLNS LKTQVVCLAS ASDILPSVQS
AAQNALQAGW SVLLPTANGR ARILSSLLLN TDSETKMCKS GHRFMTDLLV WSLMADGGLE
TALNEALGLD ISELTESEEN FEPSTSHITI PLLYLIKQLI RNGSAQTQTF LRELGTCGKM
GAQRNVPSPS LKLLSRFQRL LIGRIFSKEL ECQDACETLL VKYLECFSGH VTASLNVAYE
MCLLTPKNFL YVLQILKSDI IGILLPELIT SLILLESEVE MFLTSVNWLT LFGEMIKSLD
KLCRLSPDVE SFDIDDISWR GVSQTRPNPY CHKPFDDLPL IRKADLDNHN MDGGLWVLIN
NKVYDVQDFR CDSSTINELL QKYAGKDASQ LFNSSPYHLS VLQMMENYVV GNYCQPEPEL
PQNNLDCLNV YSTLFDTERN LGYLLGIASN VWLNARFLRA GLQVDQPPNP YGEEKGESRS
TNSTTENTPT EPRVNESQRI SKKFQLPIER INSFINALAE SRLSDSYVIS FLAVVEQFSK
QNNFLTRVDF SFEHPIEEIG RVLYAVLLKH LGLGYVVLPI LDAYSSQPNV KLPKAIAEMI
KLVHNTKWSL IKMRQELNKS YKEICIPLLE KCRFLLYDVR PSISVEMEAF KKVNILYKEP
RVRTLVKKVI KDLKCGRHTS EIQKPEDIVN ATIQSQSERH KSNEDVSKSA MKKTTSDGKI
SESKSETDDV NNEIKNGAQK VVTEASKAEQ RNTKSLEDLE EKWNVEKIEN DTRSEQSEEE
KEKKLENEIA LSGIVSKLTE KQMRKVCSEN LELMSAIVDF VVQETCDVEI LRKAMYYQVK
RCKIRKQGLW MINRLLHDNY LLTSVKYAII NGYLNLNSPS STTQHCLDNI QLVTPFMKTE
ILLSQLSVTE WCIENLRNYI LRDVPVKTGK TKGGNKVTLN LGTYTLLRDV PRARMILAIM
GILASNRYIA LELSPLVNSG VISSVLALLK QTGCDQSIVR KVSEFYVLYA DIIDNNKPKT
SCLSGPELAS LMKLGTKVVR GADWKWGDQD GSPPGEGRVI GELGDDGWVR VEWANGTTNS
YRMGIEGKYD LALASPPSPV TTDTDTEEPS DHTSQIVKDN QLIKLLRDAS INFLRNVSVS
AGLANENLHQ TTMHGLSSLF CATLSASNTS EWCNLTLIRS IAQTQQICRA FSTKPWINML
LGFLSASSLV GNELNLPKQI FSVRFLHTVL QSWDMDNSEI PTLLEKLLNI LGKIILTCSY
DTGNKPQTTT KSLVLLTQSH SSTLAQEIIH LLRSLHGLVG WNQVLNAILG QKLNLAAYFL
SDTCLMSMIN DGNTSDQQHY MVIACLNVIG AWDVRPRIGG VAEVESLQGT IVRVTPKGKL
CVQMHETGDS RKVPINSLKL LPQLEFNFDR MPLSESLVKT WASLLLNRQS SALNNHEKKP
QHGQVNAAYL RTQQNTLSAL NATRMLNSNQ YKLRKVLKHQ INGMDQSQEQ QSIEEELNQQ
PILLIQKLLA KATQPSPLKP GFSRQEMQLA ALNLSQYLAA EGNFAVSASG GGDKTTPKFC
TRCNSEVPTP NSECSVKSVV SEKKRKQSEE LPVHPMVGQI VEMGFPKRAV EVAIKSLAIG
PESLTTPESI VTWLLEHPET AISDTDSSSS VCESDTESVS YDNGNAMQPF VQFGDEFSSS
QTYLRRSQFL SNDEYAMYVR DNVEVGMLVR CCKSYEEVQL GDIGKVVKVD REGLHDLNLQ
VNWQHRVSTY WVRFIQVELL GFPPSVPSPS TLKVGDKVRV KSTVSTPRYK WGHVTHDSIG
VVAGISPNGQ NVQVDFPKQQ NWLGLVSEIE VVPSCHEGVA CNGCCVVPIS GPRFKCKVCD
NFDYCENCFY TKRNHKHSFN RMNEPGGVEI YAGKAGKYCR HDTFEGEGEL ISDWGKCVRN
VTVSSKYAAK FEIPGSIWQS CGSQGKHWIR LEIYPDVVIK SLKLGVDPAD NSYMPSVIVV
NGGSTLNSLQ ELNVINVKSH DTSVTLLTNL DKYYSIIEIN IAKCRNNGID CKIHGMTILG
MRRQSYGELK TSVSFLANDW DLNQEQIPGP STSANVGRCQ
//
