ID A0A3B6MN30_WHEAT Unreviewed; 3631 AA.
AC A0A3B6MN30;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5D02G118000.1};
RN [1] {ECO:0000313|EnsemblPlants:TraesCS5D02G118000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5D02G118000.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5D02G118000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
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}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
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DR STRING; 4565.A0A3B6MN30; -.
DR EnsemblPlants; TraesCS5D02G118000.1; TraesCS5D02G118000.1; TraesCS5D02G118000.
DR Gramene; TraesCS5D02G118000.1; TraesCS5D02G118000.1; TraesCS5D02G118000.
DR Gramene; TraesCS5D03G0282500.1; TraesCS5D03G0282500.1.CDS; TraesCS5D03G0282500.
DR OMA; YASSIQV; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019116; Chromosome 5D.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd14327; UBA_atUPL1_2_like; 1.
DR Gene3D; 6.10.250.1630; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal 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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF398; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF06012; DUF908; 2.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF14377; UBM; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1291..1332
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 3290..3631
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 923..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1783..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2072..2204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2324..2590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2688..2718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2923..2966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3170..3200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2078..2128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2129..2162
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2163..2177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2178..2204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2451..2466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2476..2493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2504..2518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2527..2555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2572..2589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3174..3198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3598
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3631 AA; 401884 MW; 345035B7F0C3AAB9 CRC64;
MAAAAMAAHR ASFPLRLQQI LSGSRXXXXX XXXXXXXPAK VKAFIDRVIN IPLHDIAIPL
SGFHWEFNKG NFHHWKPLFM HFDTYFKTYI SSRKDLLLSD DMSESEPLTK NTILQILRVV
QIVLENCQNK TTFAGLEHFK NLLASSDPEV VVAALETLAS VVKINPSKLH MNGKLISCGA
INSHLLSLAQ GWGSKEEGLG LYSCVVANER NQLEGLCLFP ADMENKYDGT QHRLGSTLHF
EYNLAPVQDS DQANDKSSNL CVIHMPDLHL RKEDDLSILK QCIDKFNVPP EHRFALFTRI
RYAHAFNSPR TCRLYSRISL LSFIVLVQSS DAHDELTSFF TNEPEYINEL IRLVRSEDIV
PGPIRALAML ALGAQLAAYA SSHERARILS GSSIISAGGN RMVLLSVLQK AISSLSSPND
TSSPLIVDAL LQFFLLHVLS SSSSGTTVRG SGMVPPLLPL LQDKDPSHMH LVCLAVKTLQ
KLMEYSSPAV SLFKDLGGVE LLSQRLHVEV QRVIGVAEIT SVLASDTSKS EDDHLYSQKR
LIKALLKALG SATYSPANPA RSQSSNDNSL PMSLSLIFQN VGKFGGDIYF SSVTVMSEII
HKDPTCFPAL KELGLPDAFL SSVTAGVIPS CKALICVPNG LGAICLNNQG LESVRETSVL
RFLVETFTSR KYLIPMNEGV VLLANAVEEL LRHVQSLRST GVDIIIEIIN KLSCPRGDKI
TEAARAEEKT DMETDVEGRD LVSAMDSGTD GTNDEQFSHL SIFHVMVLVH RTMENSETCR
LFVEKGGLQT LLTLLLRPTI TQSSGGMPIA LHSTMVFKGF TQQHSTPLAR AFCSSLKEHL
KNALQELDTV FRSCEVTKLE KGAIPSLFIV EFLLFLAASK DNRWMNALLS EFGDVSRDVL
EDIGRVHREV LWQISLFDEK KIEPEASSPS ANEAQQVDAA VGDTDDNRYT SFRQYLDPLL
RRRGSGWNIE SQVSDLINIY RDMGRAATDS HRVGADRYPS TGLPSSSQDQ PSSSSDANAK
SEEDKKRSEH SSCCDMMRSL SYHINHLFME LGKAMLLTSR RENSPINLSP SVVSVASNIA
SIVLEHLNFE GHTISPEREI TVATKCRYLG KVVEFIDGIL LDRPESCNPI MVNSFYCRGV
IQAILTTFEA TSELLFAMNR PPSSPMETDS KTGKEEKDTD CSWIYGPLSS YGAAMDHLVT
SSFILSSSTR QLLEQPIFSG TVRFPQDAER FMKLLQSKVL KTVLPIWAHP QFPECNLELI
SSVTSIMRHV YSGVEVKNNV SNIAARLAGP PPDENAISLI IEMGFSRARA EEALRQVGTN
SVEIATDWLF SHPEEPPEDD ELARALAMSL GNSDTPVQEE DDRTNDLELE EVNVQLTSMD
EVLSSCLRLL QAKETLAFPV RDMLVTISSQ NDGQNRVKVL TYLIDHLKQC LVASDPLKNT
ALSAFFHVLA LILHGDTAAR EVASKAGLVK VVLNLLCSWE LEPREGQTTK VPNWVTSCFL
SVDRMLQLEP KLPDVTELDV LKKDNSPTQT SVVIDDSKKK DSESSSSVGL LDLEDQEQLL
RICCKCIQKQ LPSGTMHAIL QLCATLTKVH VAAISFLESG GLHALLSLPT SSLFSGFNSV
VSTIIRHILE DPHTLQQAME LEIRHSLVTA ANRHANPRVT PRNFVQNLAF VVYRDPVIFM
KAAQAVCQIE MVGDRPYVVL LKDREKEKSK EKEKDKLVDK DKSSGVATKI TSGDMVMASP
VSAKGKQSDL SARNMKSHRK PPQTFVTVIE HLLDLVMSFV PPQRAEDQSD GSSSMDMDID
SSSAKGKGKA VAVTHEESKQ AIQDATACLA KNAFVLKLLT DVLLTYASSV QVVLRHDAEL
SSTRGPTRTS GGIFNHILQH LLPHATKQKK ERKPDGDWRY KLATRGNQFL VASSIRSSEG
RKRICSEICS IFVEFTDNTG CKPPMLRMDA YVDLLNDILS ARSPTGSSLS AESVVTFVEV
GLVQCLTKTL QVLDLDHPDS AKIVTGIVKA LEVVTKEHVH LADFNAKGEN SSKTVLEQNN
VDSSSNRFQV LDTTSQPTAM VTDHRETFNA VHASRSSDSV ADEMDHDRDI DGGFARDGED
DFMHEIAEDR TGNESTMDIR FDIPRNREDD MAEDEDDSDE DMSGDDGEEV DEDDDDEENN
NLEEDDAHQR SHADTDQDDR EIDEEEFDED LLEEEDDDDE DEEGVILRLE EGINGINVFD
HIEVFGGSNN VSGDTLRVMP LDIFGTRRQG RSTSIYNLLG RASDQGVLDH PLLEEPSMLL
PQQRQPENLV EMAFSDRNHE NSSSRLDAIF RSLRSGRNGH RFNMWLDDGP QRNGSAAPTV
PEGIEELLLS QLRRPMAEHP DEQSTPAVDA QVNDPPSNFH GPETDAREGS AEQNENNENV
DIPAVRSEVD GSASAGPAPP HSDELQRDAS NASEHVADMQ YERSDTAVRD VEAVSQASSG
SGATLGESLR SLDVEIGSVE GHDDGDRHGA SDRTPLGDVQ AATRSRRPSG NAVPVSSRDI
SLESVREIPP NTVQESDQNA SEGDQEPNRA TGTDSIDPTF LEALPEDLRA EVLSSRQNQV
TQTSSEQPQH DADIDPEFLA ALPPDIREEV LAQQRAQRLQ QQSQELEGQP VEMDAVSIIA
TFPSEIREEV LLTSPDTLLA TLTPALVAEA NMLRERFAHR YHSGSLFGMN SRNRRGESSR
RGDIIGSGLD RNTGDSSRQT ASKLIETVGT PLVDKDALNA LIRLLRVVQP IYKGQLQRLL
LNLCAHRESR KSLVQILLDM LMLDLQGSSK KSIDATEPSF RLYGCHANIT YSRPQSSDGV
PPLVSRRVLE TLTYLARNHP NVAKLLLFLQ FPCPPTCHTE TLDQRRGKAV LVEDGEQQSA
FALVLLLTLL NQPLYMRSVA HLEQLLNLLE VVMLNAENEV NQAKLESSAE RPSGPENATQ
DALEDASVAG SSGVKPNADD SGKSSADNIS DLQAVLHSLP QAELRLLCSL LAHDGLSDNA
YLLVAEVLKK IVALAPFICC HFINELSRSM QNLTVCAMNE LHLYEDSEKA ILSTSSANGM
AVLRVVQALS SLVTSLQERK DPELLAEKDH SDALSQISDI NTALDALWLE LSNCISKIES
SSEYTSNLSP TSANATRVST GVAPPLPAGT QNILPYIESF FVTCEKLRPG QPDAVQEPST
SDMEDASTSS SGQKSSASHT SLDEKHTAFV KFSEKHRRLL NAFIRQNSGL LEKSFSLMLK
VPRLIDFDNK RAYFRSKIKH QHDHHHSPVR ISVRRAYILE DSYNQLRMRS PQDLKGRLTV
HFQGEEGIDA GGLTREWYQL LSRVIFDKGA LLFTTVGNDL TFQPNPNSVY QTEHLSYFKF
VGRVVGKALF DAQLLDAHFT RSFYKHILGA KVTYHDIEAI DPAYYRNLKW MLENDISDVL
DLTFSMDXXX XXXXXXXXXX VTDCELIPGG RNIRVTEENK HEYVDRVAEH RLTTAIRPQI
NAFMEGFNEL IPRELISIFN DKEFELLISG LPDIDLDDLK ANTEYSGYSI ASPVIQWFWE
IVQGFSKEDK ARFLQFVTGT SKVPLEGFSA LQGISGPQRF QIHKAYGSTN HLPSAHTCFN
QLDLPEYTSK DQLQERLLLA IHEANEGFGF G
//
