ID A0A1U7ZY04_NELNU Unreviewed; 1599 AA.
AC A0A1U7ZY04;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=LOC104594745 {ECO:0000313|RefSeq:XP_010253502.1,
GN ECO:0000313|RefSeq:XP_010253503.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010253503.1};
RN [1] {ECO:0000313|RefSeq:XP_010253502.1, ECO:0000313|RefSeq:XP_010253503.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
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DR RefSeq; XP_010253502.1; XM_010255200.2.
DR RefSeq; XP_010253503.1; XM_010255201.2.
DR STRING; 4432.A0A1U7ZY04; -.
DR GeneID; 104594745; -.
DR KEGG; nnu:104594745; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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:SF10; E3 UBIQUITIN-PROTEIN LIGASE UPL4; 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 Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1217..1599
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1566
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1599 AA; 177717 MW; 7A9E24C58011A88F CRC64;
MESRGRKRAE LVDQLPADKR ACSSSDFKPG SSSSSVQTQM ASTNSASEAP DCEMETSSSA
SVSGRSEGEA EKDSAYGSCD SDGLDDPEQR HRSFREYHPR RSSSDQAKFK RILSSLADDA
GPSSQVVALT ELCDVLSFCT DDSLSSFTAD SFAPILVNLA KNESNPDIML LAVRAITYLC
DVLPRSSGFL VRHDAVPALC ARLMAIEYMD LAEQCLQALE KISRDHPLAC SQAGAIMAVL
NYIDFFSTSV QRVALSTVAN ICKKLPSDCS SSFMEAVPIL CNLLRYEDRK LVESVAICLI
RIVERVGHSS DMLDELCKHG VIHQVSHLVA LNSRTTLSQP IYIGLIGLLA RLASGSVLAV
RTLIELNISS TLKQILATYE LSHGMPHPHI GDMHSSQVHE VIKLLNVLLP PLPRNNEDIP
LVSDKERILV DQPELLQQFR IDILPVLIQV VNSGANSYVC YGSLSVINKL VYFSRSDMLL
DLLKNTNISS FLAGVFARKD HHILISALKI AKTVLEKLPD ACFSSFVKEG VVYSIDALLM
PERSPEIMFP TSTDIELSSG SNQKLAARDD PRCLCYALDS DQFPSSSEKG NCKLERNSVY
TLAKKIKATY FATESHDSKI GMTETLQKLR TICTLLIDKV NIPMNDFTND QHEECLYGIL
HQIMIELNGG EPMSTFEFIQ SGIVKSLVNY LSCGQHMKEE VDQNVISIKY HFVLKRFEMF
SMLSLMSVGG FWKDMPLANL TQKLLSAFSS LEDFPVILNH VSKSRNTYAS IPSGHCTMHP
CFKVRFVKEE GEACLCNYPG DILTVEPFTS FDAIEGFLWP KISGTTDEHH TSVCQPLVQC
KSVLLPLPSD TRSPQGKDLN FVGEINSISS GVPEVQENQG NMSPPIKRAV DMIEGNPTTS
HLVHTEPGSR IQDLQYSPEM DSDLKLVDSS NASASTSTSS GKECMEGRKC PTSCGNSDDP
TKLVFHLEGR KLDRALTLYQ EILNQHVKAE NDMIVGPKFW NQVYKITYRK ATDLEKCDSQ
DSCHGSSISS ALNKLGTCWK DVPFLSGMLV SKLPCDLEKS NPTYDMLVLL KSLEGLNRSA
FHLMSHERRC AFAEGRSNNF DDLRVNVPSL PQSEFVSCKL TEKLEQQMRD PLAVSVGGMP
SWCAQLMAAC PFLFGFESKC RYFQLKAFGS SRVQPHPWPQ SATSNSNTSN DRQQHAVLLP
RKKFQVRRSH ILDSAAQMMD LYANHKAILE VEYSEEVGTG LGPTMEFYTL VSHEFQKAGL
GMWREDHSTP TAGKGLDDNS SGFVAAHLGL FPRPWSPSLS ADKTLVSEVI KKFVLLGKIV
AKALQDGRVL DLPFSKAFYK LILEKELCIY DIQSFEPEFG RTLLEFQALV DRKKNLNSIS
EKGTNFISDS CFRDTRIEDL CLEFTLPGYP DYVLGSEPGN KIVNMDNLEE YVSLTVDATV
NSGIIRQVEA FKSGFNQVFP IKSLQIFSEE ELERLLCGER DAWASNEIVD HVKFDHGYTS
SSPPVINLLE IIQEFEHDQR RAFLQFVTGA PRLPPGGLAA LNPKLTIVRK HCSEWVDGDL
PSVMTCANYL KLPPYSSKER MRERILYAIT EGQGSFHLS
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