ID   T1IAJ8_RHOPR            Unreviewed;       896 AA.
AC   T1IAJ8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE   Flags: Fragment;
OS   Rhodnius prolixus (Triatomid bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX   NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC013319-PA, ECO:0000313|Proteomes:UP000015103};
RN   [1] {ECO:0000313|Proteomes:UP000015103}
RP   NUCLEOTIDE SEQUENCE.
RA   Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:RPRC013319-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2015) 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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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DR   EMBL; ACPB03005975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1IAJ8; -.
DR   STRING; 13249.T1IAJ8; -.
DR   EnsemblMetazoa; RPRC013319-RA; RPRC013319-PA; RPRC013319.
DR   VEuPathDB; VectorBase:RPRC013319; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   HOGENOM; CLU_002173_0_3_1; -.
DR   InParanoid; T1IAJ8; -.
DR   OMA; PPYQDYE; -.
DR   OrthoDB; 5480520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000015103; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd04033; C2_NEDD4_NEDD4L; 1.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 3.
DR   Gene3D; 2.20.70.10; -; 2.
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; IPR024928; E3_ub_ligase_SMURF1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254:SF443; E3 UBIQUITIN-PROTEIN LIGASE NEDD-4; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 3.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 3.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 3.
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; 3.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 3.
DR   PROSITE; PS50020; WW_DOMAIN_2; 3.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015103};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
SQ   SEQUENCE   896 AA;  104295 MW;  D3FF4AC78ED944EC CRC64;
     LRLKVISGHQ LAKKDIFGAS DPYVRIDLNT INGDETIDSV LTKTKKKTLN PAWNEEFIFR
     VKPAEHKLVL QVFDENRLTR DDFLGMVELT LLNLPKEVDG RTVPTKQYIL RPRSARSRVR
     GYLELYHAYV LEDSVPLPDV DNAREREVEP GWEMLDRTNL AVSTSQVCIF VCDASLPPGW
     EERQDANGRT YYVNHVARST QWDRPTMKLQ IDRNLVHKLG KRLFWKEHRN VKYFSLLKFI
     LILHHFHDFT VCGFYLLIGD FYWTCENPPR LSCLHIHFNA FFVSSETGLY PYCFGVNKEK
     KIFKMFFMKT LRYHLQHISL FHDSNEIEPT KYWNQERRFP NSITKITGQS NLFSGAEMYQ
     LSCKSSINFL SFLFNCNLRM FLVINLSAII SLFYNSNENR NTSHQILESA ATEFQRRFHI
     SADEADSSRR RSSVLSCQGT EETCQGISSA DGLPEGWGLQ IAPNGRVFFI DHNSKATTWV
     DPRTGGNSSH IRNSVTADGD LGSLPEGWEE RVHTDGRIFF IDHNTRTTQW EDPRLANPQI
     AGPAVPYSRD YKRKYEYLKA QLRKPSNVPN KFEIKVRRHA ILEDSYRIIT NNASRPDLLK
     TKLWVEFEGE VGLDYGGLAR EWFFLLSKEM FNPYYGLFEY SAMDNYTLQI NPISGLCNEE
     HLNYFKFIGR IAGLAVYHGK LLDAFFIRPF YKMMLSKPIE LKDMESVDSE YYNSLLWIKE
     NNPTELGLTF SVDEDSLGHT CQRELKPNGA NIPLTEDNKD EYIKLVIEWR FVARVQEQMN
     AFLEGFNALV PLNLIKIFDE HELELLMCGI QNIDVKDWKN NTVYKGDYHP NHITIQWFWR
     VVLSFSNEMR SRLLQFVTGT SRVPMNGFKE LYGSNGPQMF TIEKWGTTDN YPRAHT
//