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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//