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Database: UniProt
Entry: A0A267GTA1_9PLAT
LinkDB: A0A267GTA1_9PLAT
Original site: A0A267GTA1_9PLAT 
ID   A0A267GTA1_9PLAT        Unreviewed;       658 AA.
AC   A0A267GTA1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=BOX15_Mlig020114g2 {ECO:0000313|EMBL:PAA89253.1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA89253.1, ECO:0000313|Proteomes:UP000215902};
RN   [1] {ECO:0000313|EMBL:PAA89253.1, ECO:0000313|Proteomes:UP000215902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DV1 {ECO:0000313|EMBL:PAA89253.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:PAA89253.1};
RA   Berezikov E.;
RT   "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT   model organism for stem cell research.";
RL   Submitted (JUN-2017) 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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAA89253.1}.
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DR   EMBL; NIVC01000158; PAA89253.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A267GTA1; -.
DR   STRING; 282301.A0A267GTA1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000215902; 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:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 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; 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:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 2.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 4.
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:UP000215902};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1..108
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          166..199
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          231..264
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          308..621
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        621
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   658 AA;  75057 MW;  A1D0A31B8D334EF2 CRC64;
     MTSATDNNAF QLSIVINSAK FPGGQMSKTP SKLYCKLLVD GSQLATTQVK RKTWAPVWNE
     DHTVLVRPRS KLQFNVNRVN TFGRHSLVGH GTLDLHHELE ASGGLLRNRP VLVELRLDAD
     VASSQRTGEL VATLSCDQVN LAGGVGGQRQ RRSTTASEVI SPDAGEALPA GWERRLDPQG
     RVYYVDHNTR TTTWQRPSNQ LLHAQAVYQT WLREQDYGQF QGRFVGDDQL GPLPPGWERR
     ADQSGRVYYV NHKDRSTQWE DPRQGAIRSK ASEFRRLCSD RSQPGQFQLC VSRNNLLEDS
     FRQVAAADPA ALRKRLFVRF QGEEGLDYGG LAREWFFHLS HELMNPMYCL FEYTSTNNYC
     LQINPASEVN PEHLLYFHFV GRFVAMALFH GCFIDNGFSL PFYKRILGQP LSLKDIEAID
     NSYYNSLVFI RDSDLDECEL GLYFSASYEV LGEKREHELK PGGANIEVTN ENKLEYIRLV
     VDWRFSRSVE RQTEYFLNGF NEVVPLQLLR SELRVDARDL EVLLCGMHAI DVDDWERNTK
     YKNCEAGCQQ VRWFWQAARA MDQARRTRLL QFVTGTCRLP VGGFSHLLGS NGEQQFCIEL
     LSACRQLRCR EVTPVSTGST CRPTRHSSSC RRNCCLPLTR PRASLRNDFT PKLLTACL
//
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