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Database: UniProt
Entry: A0A3B4YTC3_SERLL
LinkDB: A0A3B4YTC3_SERLL
Original site: A0A3B4YTC3_SERLL 
ID   A0A3B4YTC3_SERLL        Unreviewed;       757 AA.
AC   A0A3B4YTC3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE            EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000031486.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000031486.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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         ECO:0000256|PIRNR:PIRNR001569};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR   AlphaFoldDB; A0A3B4YTC3; -.
DR   Ensembl; ENSSLDT00000032383.1; ENSSLDP00000031486.1; ENSSLDG00000024154.1.
DR   GeneTree; ENSGT00940000155563; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261360; 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; 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:SF300; E3 UBIQUITIN-PROTEIN LIGASE SMURF2; 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   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; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 3.
PE   4: Predicted;
KW   Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR001569}.
FT   DOMAIN          1..104
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          144..177
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          242..275
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          288..321
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          423..757
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          173..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        725
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   757 AA;  86539 MW;  C8951F342A7D2FC1 CRC64;
     MSNQGVRRNG PVKLRLTGLP DPFAKVVVDG SGQCHSTDTV RNTLDPKWNQ HYDLYIGKSD
     SITISVWNHK KIHKKQGAGF LGCVRLLSNA INRLKDTGYQ RLDLNKLSPN DSDTVRGQIV
     VSLQSRDRIG TGGPVVDCSR LFDNDLPDGW EERRTASGRI QYLNHITRTT QWERPTRPAS
     EYSSPGRPLS CIVDENTPIS TNGATPTTAL PPSDGDQRAQ ERRVRSQRHR NYMSRTHLHT
     PPDLPEGYEQ RTTQQGQVYF LHTQTGVSTW HDPRVPRDLS NVNCEELGPL PPGWEIRNTA
     TGRVYFVDHN NRTTQFTDPR LSANLHLVLN PSPNGSRGGI ESQNVSRQNQ LKDQAQQALV
     SPGQLPEEAE CLTVPKYKRD LVQKLKILRQ ELSQQQPQAG HCRIEVSREE IFEESYRQVM
     KMRPKDLWKR LMVKFRGEEG LDYGGVAREW LYLLSHEMLN PYYGLFQYSR DDIYTLQINP
     DSAVNPEHLS YFHFVGRIMG MAVFHGHYID GGFTLPFYKQ LLGKPITLDD MESVDPDLHN
     SLVWILDNDI TGVLDHTFCV EHNAYGEIIQ HELKPNGKSI PVTQDTKKEY VRLYVNWRFL
     RGIEAQFLAL QKGFNEVIPQ HLLKAFDEKE LELIVCGLGK IDINDWKSNT RLKHCTPDSN
     IVKWFWKAVE SFDEERRARL LQFVTGSSRV PLQGFKALQG AAGPRLFTIH QIDASTNNLP
     KAHTCFNRID IPPYEHYDKL YDKLLTAIEE TCGFAVE
//
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