ID A0A059AP42_EUCGR Unreviewed; 1767 AA.
AC A0A059AP42;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=EUGRSUZ_I014101 {ECO:0000313|EMBL:KCW55519.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW55519.1};
RN [1] {ECO:0000313|EMBL:KCW55519.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW55519.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KK198761; KCW55519.1; -; Genomic_DNA.
DR RefSeq; XP_010028722.1; XM_010030420.2.
DR EnsemblPlants; KCW55519; KCW55519; EUGRSUZ_I014101.
DR Gramene; KCW55519; KCW55519; EUGRSUZ_I014101.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR OrthoDB; 1093891at2759; -.
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; IPR000225; Armadillo.
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; SM00185; ARM; 3.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1467..1767
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 534..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1707..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..985
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1734
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1767 AA; 190477 MW; D5801414E872FEFB CRC64;
MDRDGGVEDD DNDSEGGVGI LHQNLTSASS ALQGLLRKLG AGLDDLLPSS AIASASSSHQ
TGRLKKILTG LRADGEEGRQ VEALTQLCEM LSIGTEDSLS TFSVDSFVPV LVGLLNHESN
PDIMLLAARA LTHLCDVLPS SCAAVVHYGA VSCFCARLLT IEYMDLAEQS LQALKKISQE
HPTACLRAGA LMAVLSYLDF FSTGVQRVAL STAANMCKKL PSDAADFVME AVPLLTNLLQ
YHDAKVLEHA SVCLTRIAEA FASSPDKLDD LCNHGLVTQA ASLISTNNSG GAQASLSTPT
YTGVIRLLST CSSGSHLGAK TLLLLGISGI LRDILSGSGV SANGSVPPAL TRPPEQIFEI
VNLANELLPP LPLGTITLPV SSYLFVKGPM LRKSPTSNSG KQEESNGNAV EVSTREKLLN
EQPELLRQFG MDLLPVLIQI YGSSVNGPVR HKCLSVIAKL MYFSTSEMIQ SLLSVTNISS
FLAGILAWKD PHVLVPALQI AEILMEKLPE TFSKMFVREG VVHAVDQLIL AGNSSSGSAS
ADKDNDSVTG TSSRSRRYRR RSGSSNPEGT SIEESKNSLS INVGSPPGSI EIPNVNSNLR
TTVSACAKAF KDKYFPSDPG ATDVGVTDDL LHLKNLCMKL NAGIDDQKMK AKGKSKNSGS
RLPDNSANKD EYLNGIISEM LAELSKGDGV STFEFIGSGV VGALLNYFSC GYYSKDRITE
ANLSRLRQQA LRRYKSFVSV ALPYGNGEVA VAPMTVLVQK LQNALSSLER FPVVLSHSAR
SSSGSGRISS GLSALSQPFK LRLCRAQGEK SLRDYSSNVV LIDPLASLAA VEEFLWPRVQ
RSDSGQKPSP SGGNSESGAT PAGAGASSPS SSTPATRRHS TRSRSSVNIG DTAKKEMAQE
KSSSSSKGKG KAVLKPTQEE GRGPQTRNAA RRRAALDKDA QMKPENGDSS SEDEDLDISP
VDIDDALVIE DDDISDDDDD DHEDVLRDDS LPVCLTDKVH DVKLGDSAED SATNPATSDS
QTNPPSGSSS RAAVSRPSDS ADFRGGNTFG ARGAMSFAAA AMAGLGSANG RGFRGGRDRH
GRPFPSNSEP PKLIFTAGGK QLNRHLTIYQ AIQRQLVLDE DDDERFAGSD FASGDGSRLW
SDIYTITYQK PDGQGDRASG GAAPSKSAKS GSSSSYSDVQ SQRMSLLDSI LQGELPCDLE
KSNPTYNILA LLRVLEGLNQ LASRLRAEIV RNDFAEGRTS SLDRLSTSGA KVSLEEFMNS
KLTPKLSRQI QDALALCSGS LPPWCSQLTK ACPFLFPFET RRQYFYSTAF GLSRALYRLQ
QQQGAEGHGS ANEREVRVGR LQRQKVRVSR NRILDSAAKV MEMYSSQKAV LEVEYFGEVG
TGLGPTLEFY TLLSHDLQKV GLEMWRSTSS EKRAVGVDLN EQSNGKSTST DSAVEDRDTV
VAPLGLFPRP WPPNADVSDG SKFSKVIEYF RLVGRVMAKA LQDGRLLDLP MSSAFYKLVL
GQELDLHDII SFDAEVGKVL EELHALVCRK QFLESSSDHN RGAIADLHFR GARIEDLCFD
FTLPGYPDYV LKSGDETVDI NNLEEYLSLV VDATVKTGIA RQMEAFRAGF NQVFDISSLQ
IFTPHELDYL LCGRREMWEA ETLAEHIKFD HGYTAKSPAI LYLLEIMGEF TPEQQRAFCQ
FVTGAPRLPP GGLAVLNPKL TIVRKHSSTA STVPTNGTGP SESADDDLPS VMTCANYLKL
PPYSSKEIMY KKLLYAINEG QGSFDLS
//
