ID I3KD48_ORENI Unreviewed; 1649 AA.
AC I3KD48;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=HECW1 {ECO:0000313|Ensembl:ENSONIP00000019043.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000019043.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000019043.2}
RP IDENTIFICATION.
RG Ensembl;
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR RefSeq; XP_005460517.1; XM_005460460.3.
DR STRING; 8128.ENSONIP00000019043; -.
DR Ensembl; ENSONIT00000019060.2; ENSONIP00000019043.2; ENSONIG00000015132.2.
DR GeneID; 100707125; -.
DR KEGG; onl:100707125; -.
DR CTD; 23072; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000158294; -.
DR InParanoid; I3KD48; -.
DR OMA; SGSQNCE; -.
DR OrthoDB; 5480520at2759; -.
DR TreeFam; TF313938; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005207; Linkage group LG9.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd08691; C2_NEDL1-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.2840; -; 1.
DR Gene3D; 2.60.40.150; C2 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 InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037795; C2_HECW.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR032348; HECW_N.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF79; E3 UBIQUITIN-PROTEIN LIGASE HECW1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF16562; HECW_N; 1.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 185..318
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 888..921
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1061..1094
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1314..1649
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 367..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1617
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1649 AA; 184148 MW; 149A85F4759299A7 CRC64;
MIHRQVILSQ NLYQNRFLGL AAMASPTRSS QTRQRCKDAV RHSYGPESFA VNGLNQDAFM
LGLSRSTSDT DLVSPDARST LTISSSHYTI GQSEDLVITW DIKEEVDAGD WIGMYLVDET
LSENFLDYKN RGINGSHKGQ IVWKIDSSSH FSDPETQVCF RYYHGVTGAL RATTPSVIIK
KGSAPVLKPV VSPEVNHGLG NRRLINFNLS DLQAVGLKKG MFFNPDPYLK LSIQPGKHSI
FPSLPHHGQE KRSRVVCNTV NPKWSTERFN FVSLPTDVLE IEVKDKFAKS RPIIKRFLGK
LSVPVQRLLE KHAIGDRVVS YSLGRRLPTD HVCGQLQFRF ELTSSIHPDD EEVSLVIEAA
CPEGGHAADV NHAADAPDDD TLSVGPDMPD LPLDAPPDPE TLPDAASAPK EVQPAEKEQA
EATSQEEQGS VEEETTVREE PLAPEPQVEQ AEGESAEQQQ EGGVEGQQEK GEVEQGEGTA
AQAEEEVTAE GKEAVDEAQS EPHSDCAVAE MTHDEATAVE APPEENTASQ EAPVDPAEEA
PQEAGEGGER SCAPCSCQSL LSNYNSNAHS RRKTRPCSLP VSELETVIAS ACGEPETPRS
HYIRIHHLLH SLPSAQHRPP SQEEEQSGEG ENTDSTLETN ATSPTLKTSK EQEGQEDDEE
EDTSQSPSQV LGCPGPCCRR SLPRSLSIER LSELNQLLEG EGFGGGHPAV RRISPSCPES
EEGDSSNGGG RRAGGSAHRA PGESECEFCD TSCYSTSCYS TSCYSTSCYS NSGYEGRGRF
CSHTRLSSVE SNRLSSSTVF SSQEEEDEES AFESVPEGNH GPDRQEQGGA ERRTGRWKET
RSGEQGDPAV AGPSDQNSIG SGFSPPVGYL PVLRPSHDLN HFPAATDQAL PPNWEARIDS
HGRVFYVDHV NRTTTWQRPS QATKCNHGIP RSGSTHQMEQ LNRRYQNIQR TMATEESGGS
QRTERSSSTE TDPDSTQTGP ASPVNQQKIS HLLQSPAVKF ITHPEFFTVL HSNYAAYRMF
TSSSCVKHMI LKVRRDARNF ERYQHNRDLV VFLNKFADSQ LELPRGWEIK TDPQGKSFFV
DHNSRATTFI DPRIPLQNGR LPGHLAHKQH LQRLRSYSAG EASDVSRSRG ASLMGRPGNS
LVAAIRSQHY ADSQQLSAPS YNDKIVAFLR QPNIFDLLQE RQPSLTRNHA LREKIHYVRT
EGNQGVEKLS CDADLVILLS LFEEEIMSCV PTHPIHHNLS FSPRCSPASS PQNSPGLQRA
RAPAPYRRDF EAKLRNFYRK LEAKGYAQGP GKIKLLIRRE HLLEGTFNQV MAYSRKELQR
NKLYVTFLGE EGLDYSGPSR EFFFLLSQEL FNPYYGLFEY SANDTYTVQI SPMSAFVENH
LEWFRFSGRI LGLALIHQYL LDAFFTRPFY KALLRLATDL SDLEYLDEEF HQSLQWMKDN
DITDILDLTF TVNEEVFGQV TERELKSGGA NLQVTEKNKK DYIERMAKWR VERGVVQQTE
ALVRGFYEVV DSRLVSVFDA RELELVIAGT VEIDLGDWRN NTEYRGGYHD GHIVMRWFWA
AVERFNNEQR LRLLQFVTGT SSVPYEGFAA LRGSNGLRRF CIEKWGKVTS LPRAHTCFNR
LDLPPYPSYT MLYEKLLIAV EETSTFGLE
//
