ID A0A0B1P7X8_UNCNE Unreviewed; 1863 AA.
AC A0A0B1P7X8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=EV44_g2098 {ECO:0000313|EMBL:KHJ33465.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ33465.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ33465.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(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 -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHJ33465.1}.
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DR EMBL; JNVN01001413; KHJ33465.1; -; Genomic_DNA.
DR STRING; 52586.A0A0B1P7X8; -.
DR HOGENOM; CLU_000366_1_1_1; -.
DR OMA; AEPLSQF; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000030854; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00078; HECTc; 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 PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KHJ33465.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030854};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1507..1863
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..215
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..790
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1830
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1863 AA; 204918 MW; DE7AF43C74CB41B8 CRC64;
MDQRINSTPV FDSERRTSSN ATSRVTRAAA RQAAGFLESA NHFTGAPPVA LPNRISETAR
KRKVPTLEPD RAPSPVPVAQ EVTRTSISRR PKRQKVAAET NHTIPTPTLA VAASSRRKKG
HNTVVMSNPG ESAGPSTDHT MVSPGPKRKL TRSKKNNQDS SINTPSSSRR FKKTNTGIKE
AEQLMTSNPI ENSHPPEGDD GSVEEEDEEI TRHYEGQDDD EDSFGSFGGP GGASHGLSST
LRALSTMMSG VSTRLRDILK NLRQKGEPSL QLIALQDLSE ILLVSTEDNL SGHFSPDAFV
KELVTLLQPS ELDEENTEMM LLACRCIANL MEALPSSVAN VVYGGAVPVL CQKLLEIHFI
DLAEQALSTL EKISVEYPAS IVREGGLTAC LTYLDFFATS TQRTAVTTAA NCCRNIPNDS
FTVIRDVMPI LLNVLGSNDQ KVVEQGSLCV SRVVESFRYH PAKLEELVST DLLKAILRLL
LPGTTNLVGS NIPTQFLRVI SITAKASPTL ATELLKMNVV ETIYQILTGV SPPGPSEDAA
SKLDSVIIMQ ALIHRSREQV IETLNVICEL LPGTPRETDL FTESSNINSS LTPDEIPISC
SRKHSSREKR LELLEGCKKE VKRFAVILFP ILTDAFCSTV NLSVRQKVLS AQLKMLSNLD
EEILIEALQS VPYASFLAAI LSQKDHLSLT VYALRAAELL LRRLDQIYRY QFYREGVITE
ISKIANSKGD GHPITRPEIM YEAIDATVSN SSNTTAKISE KSEQLDEVGT EDNDSLDGDE
RGDNDNDELP DDTSPSPSSS HGSTMSLDGP SNRISDTLCL KNFIVQRAKA FLDAHENEKS
SQDMKKKASK ILNDLQTLAL NIESHYLHRA SGNGNGNGTE LFSSLASYFD GDLLESVTSA
ELLNSEIVRV LLDVFNNKDE RLSNDARSSF LEAFMGRSVA RKFKPTNTES PATPFSVLIR
KLQDLLSRSE HFEVVTVHQN SFDGNKSSAA SMLAKQIRLK LVADENSEIP RPYRNIMVSI
HAIATFKALD DYLRPRISVS ERSRGSRARD GLSGALAALA AAGMPNPFAG AGHSRLTDHE
PVTTNTTSPV TPSLQKTDSK TMHSISSASG RQALITKSQR SISRRPNRSF AQKELLGAPP
DDDGLTPTLE CADEKGLTTE NDSNDSTALD TIVGNLDDEI GDGSNLDTAA VNLEIVASEK
ITARKEGGSR LATPPQAPNR GDSSIQPPTA LATLIAQSTA RPISYAAAIQ ATPQDWHIEF
SLGDQVIPNE TTIYRAVHSG AHAIEEHGTR SVWSSIHSIR FKRVSGPPPP EISSLSNTPE
TNLDRTVSGI PASLDKHQAT SSILRLLNIL HDLNSNIDDV LAENKDTLKL NVEPLSQFVN
TKLTAKLNRQ LEEPLIVASN CLPSWSEDLA RCYPFLFPFE TRHLFLQSTS FGYARSMTRW
QNAQSADESR RDRHRDERTF LGRLQRQKVR ISRSKILESA IKVMELYGAS QSILEVEYFE
EVGTGLGPTL EFYSTVSKEF SKKKLKLWRE TDCNNTDEFA FGARGLFPAP MSEEQATTEN
GKRILHLFKM LGKFVARSMI DSRIIDVSFN PTFFRIGDAS KAVSPSLGAV KTVDPQLAKS
LKLIKKFVTG KKAIDENPNL TPAQKVREAE QLRVDGARID DLGLDFTLPG YSSIELLSNG
SQVSVSIDRV EEYLNKVIDM TLGSGVQRQI NAFRTGFTQV FPYSALSAFT PDELVMLFGR
VEEDWSLETL MDSIKADHGF NMDSKSIKNL LQTMSELDLT ARREFLQFTT GSPKLPIGGF
KSLTPMFTVV RKPSEPPYTS DDYLPSVMTC VNYLKLPDYT NLEVMRERMT TAIREGQGAF
HLS
//
