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Database: UniProt
Entry: A0A384AHI0_BALAS
LinkDB: A0A384AHI0_BALAS
Original site: A0A384AHI0_BALAS 
ID   A0A384AHI0_BALAS        Unreviewed;       719 AA.
AC   A0A384AHI0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=SMURF1 {ECO:0000313|RefSeq:XP_007186780.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007186780.1};
RN   [1] {ECO:0000313|RefSeq:XP_007186780.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007186780.1};
RG   RefSeq;
RL   Submitted (JAN-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_007186779.1; XM_007186717.1.
DR   RefSeq; XP_007186780.1; XM_007186718.2.
DR   AlphaFoldDB; A0A384AHI0; -.
DR   STRING; 310752.A0A384AHI0; -.
DR   KEGG; bacu:103001429; -.
DR   CTD; 57154; -.
DR   InParanoid; A0A384AHI0; -.
DR   OrthoDB; 5480520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261681; Unplaced.
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; cd08382; C2_Smurf-like; 1.
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:SF293; E3 UBIQUITIN-PROTEIN LIGASE SMURF1; 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; 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; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000261681};
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          222..255
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          268..301
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          382..719
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          148..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        687
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   719 AA;  81815 MW;  28834FF7BBF88EF0 CRC64;
     MKDSGKLLCA KNLAKKDFFR LPDPFAKIVV DGSGQCHSTD TVKNTLDPKW NQHYDLYVGK
     TDSITISVWN HKKIHKKQGA GFLGCVRLLS NAISRLKDTG YQRLDLCKLN PSDTDAVRGQ
     IVVSLQTRDR IGTGGSVVDC RGLLENEGTA YEDSGPGRPL SCFMEEPAPY TDGTGAAAGG
     GGCRSVESPS QDQRLQAQRL RSSEVRGSLQ TPQNRPHGHQ SPELPEGYEQ RTTVQGQVYF
     LHTQTGVSTW HDPRIPRDLN SVNCDELGPL PPGWEVRSTV SGRIYFVDHN NRTTQFTDPR
     LHHIMNHQCQ LKEPSQPLPL PSEGSVEDEE LPAQRDERDL VQKLKVLRHE LSLQQPQAGH
     CRIEVSREEI FEESYRQIMK MRPKDLKKRL MVKFRGEEGL DYGGVAREWL YLLCHEMLNP
     YYGLFQYSTD NIYMLQINPD SSINPDHLSY FHFVGRIMGL AVFHGHYING GFTVPFYKQL
     LGKPIQLSDL ESVDPELHKS LVWILENDIT PVLDHTFCVE HNAFGRILQH ELKPNGRNVP
     VTEENKKEYV RLYVNWRFMR GIEAQFLALQ KGFNELIPQH LLKPFDQKEL ELIIGGLDKI
     DLDDWKSNTR LKHCGADSNV VRWFWQAVET FDEERRARLL QFVTGSTRVP LQGFKALQGS
     TGAAGPRLFT IHLIDANTDN LPKAHTCFNR IDIPPYESYE KLYEKLLTAV EETCGFAVE
//
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