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}.
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 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
//