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Database: UniProt
Entry: T1GGN5_MEGSC
LinkDB: T1GGN5_MEGSC
Original site: T1GGN5_MEGSC 
ID   T1GGN5_MEGSC            Unreviewed;       390 AA.
AC   T1GGN5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS   Megaselia scalaris (Humpbacked fly) (Phora scalaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Platypezoidea;
OC   Phoridae; Megaseliini; Megaselia.
OX   NCBI_TaxID=36166 {ECO:0000313|EnsemblMetazoa:MESCA002558-PA, ECO:0000313|Proteomes:UP000015102};
RN   [1] {ECO:0000313|Proteomes:UP000015102}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Durham, NC isolate 2 -- Noor lab
RC   {ECO:0000313|Proteomes:UP000015102};
RA   Hughes D.;
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:MESCA002558-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-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}.
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DR   EMBL; CAQQ02124450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAQQ02124451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAQQ02124452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1GGN5; -.
DR   STRING; 36166.T1GGN5; -.
DR   EnsemblMetazoa; MESCA002558-RA; MESCA002558-PA; MESCA002558.
DR   HOGENOM; CLU_708424_0_0_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000015102; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase 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   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
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:SF395; E3 UBIQUITIN-PROTEIN LIGASE SMURF1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015102};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          76..109
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          315..390
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          49..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        358
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   390 AA;  42804 MW;  E9C914BF707A1683 CRC64;
     MNKLENSRRN GAHKIRIVIQ RLELGQLNPS DDEVIRGQII ISLVSKDGPN SGNPVRIVDP
     SGDFRAPATP EESSEESLPE GWEERRTPEG RLYYVNHTTK TTQWNRPTAN QNGNVDENSR
     INGPSRSNTC TNLLNDSQSN NVDTLQLSPP QSARRHSAEI LTDIDLDCPT VIANGQSPQP
     QSDVNVVGGE SSKKTTNQQQ STSINENIEN QINNLNKTPR SHSANVPQVP KTSLSPTLDN
     LILESPQRPT TSQSVLNGNS PATPSNENGN AINTPTTTQS SNSNHRENSS SGRIRRSSRN
     LDESSSNSRR RSSRGTARVP LQGFRALQGS TGAVGPRLFT IHLTSDVPTQ NLPKAHTCFN
     RIDLPPYDNY QLMYDKLTQA VEETCGFAVE
//
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