ID A0A3Q2E0Q2_CYPVA Unreviewed; 909 AA.
AC A0A3Q2E0Q2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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 Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000024839.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000024839.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_015254847.1; XM_015399361.1.
DR AlphaFoldDB; A0A3Q2E0Q2; -.
DR Ensembl; ENSCVAT00000003176.1; ENSCVAP00000024839.1; ENSCVAG00000000773.1.
DR GeneID; 107100739; -.
DR CTD; 619412; -.
DR GeneTree; ENSGT00940000158905; -.
DR OMA; PPYQDYE; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265020; 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; cd04033; C2_NEDD4_NEDD4L; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 4.
DR Gene3D; 2.20.70.10; -; 3.
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:SF282; E3 UBIQUITIN-PROTEIN LIGASE NEDD4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 3.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
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; 4.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 6..126
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 191..224
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 350..383
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 431..464
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 482..515
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 574..908
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 154..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 876
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 909 AA; 104708 MW; 0C93EF25D07870CA CRC64;
MMAAVPASQI RGLQADEEES RILKVKVISG IGLAKKDILG ASDPYTRLSL YDPINGEITS
LQTKTIKKTL DPKWNEEFYF RVFPRKHRLL FEVFDENRLT RDDFLGQVDV PLNQIPTENP
NSQRPYTFKD FLLHPRSHKS RVKGHLRLKM TYLPKNSGSE EESADPTEET EHGWEFLGQD
TSGPRQSQLL PPLPPGWEER QDNLGRIFYV NHVTRTMQCH RPTIQESNGE SHRPQNYNVD
AEHALNTRRQ ISDHDETTIP HEPPESWEII AVDESTLYPR NNHVPPSHEP PAFSSLSNES
SNHRASRSSA RELRSAQNNH TSNSNHSSLR ESASVREELP VSPVSPPTSA QLPPGWEEKR
DKKGRRYYVN HNTRSTTWVR PVFQISPEET AAAPTGSAQP QNLGSLSQPQ LRPGESSQSR
PTAEATTPET GSLPPGWEVR SAPNGRPFFI DHNTKTTTWV DPRLKVPVQM RRTGSLDPND
LGPLPPGWEE RVHSDGRIFY IDHNTKTTQW DDPRLQNSAI TGPAVPYSRD YKQKYDYFKK
KLIKPSDIPN RFELKLKRSS VLEDSYRRIL GVKRPELLKA RLWVEFEGEK GLDYGGVARE
WFFLMSKEMF NPYYGLFEYS ATDNYTLQIN PNSGLCNEDH LSYFKFIGRV AGMAVFHGKL
LDAFFIRPFY KMMLQKPITL QDMESVDSEY FNSLKWILEN DPEDLDLRFT IDEELFGETH
QHDLKPDGSE IVVTNENKDE YIDLVMQWRF VNRIRKQMTA FKDGFFELIP KDLIKIFDEN
ELELLMCGLG DVDVNDWRQN TKYKGGYCGD HVVIQWFWKT VLLMDAEKRI RLLQFVTGTS
RVPMNGFAEL YGSNGPQLFT IEQWGTSDKL PRAHTCFNRL DLPPYESFEE LREKLNIAIE
NAQGFDGVD
//
