ID A0A3B3UHL9_9TELE Unreviewed; 869 AA.
AC A0A3B3UHL9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000012251.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000012251.1}
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 RefSeq; XP_014895555.1; XM_015040069.1.
DR AlphaFoldDB; A0A3B3UHL9; -.
DR STRING; 48699.ENSPLAP00000012251; -.
DR Ensembl; ENSPLAT00000019993.1; ENSPLAP00000012251.1; ENSPLAG00000015519.1.
DR GeneID; 106952138; -.
DR KEGG; plai:106952138; -.
DR CTD; 100331274; -.
DR GeneTree; ENSGT00940000157014; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261500; 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; cd04021; C2_E3_ubiquitin_ligase; 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:SF445; E3 UBIQUITIN-PROTEIN LIGASE; 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; 1.
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; 4.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
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..100
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 292..325
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 324..357
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 404..437
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 444..477
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 535..869
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 142..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 837
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 869 AA; 99142 MW; 8C6905EB71B64630 CRC64;
MKAQLQVTVL SAKLKENKKN WFGPSPYVEV AVDGESKRTE KCNNTHSPKW KQALTVIVTP
VSKLIFRVWS HQTLKADILL GMATLDIGTV LKANDLKLCE VVQTLQLCFD RDPQDIVGDL
SICLDGMQVD PEAFALAERE QAPLTNGNAK QNGNTSNRSS RDTSPSSDSD DWVIVPNGLA
VSDRGSPSLS AEGSTSSRPP RPARPPPPTP HKPAASPSSS SSSSPSELSE APASDGSSQA
SASGGSDHPN DAGARAATAV SSQTTSAPKP GGAVTAAPAT TATPRVNPIS NTPLPPGWEQ
RVDQNGRVYY VDHIEKRTTW DRPEPLPTGW ERRVDPMGRV YYVDHMTRTT TWQRPTQESV
RNYEEWQNQR SQLQGAMHQF NQRFIYGLQD QFAATSTKEF DPLGPLPHGW EKRTDTNGRV
YFVHHPTRTT QWEDPRTQGL LNDKPLPEGW EMRFTVDHIP YFVDHNRRTT TYIDPRTGKS
SFENGPQITY VRDFKAKVQY FRFWCQQLSM PQHIKITVSR KTLFEDSFQQ IMSFHPQDLR
RRLWIIFPGE EGLDYGGVAR EWFFLLSHEV LNPMYCLFEY AGKDNYCLQI NPASYINPDH
LKYFKFIGRF IAMALFHGKF IDTGFSLPFY KRILNKPLAL KDLESIDPEF YNSLIWIKDN
NVEECGLEMF FSVDKEILGE VSTHELKPDG GNIPVTEDNK EEYIRLVAEW RLSRGVEEQT
QAFFEGFNEV LPQQYLQYFD AKELEVMLCG MQEIDLVDWQ RNTIYRHYAR SSKQILWFWQ
FVKEMDNEKR MRLLQFVTGT CRLPVGGFAD LMGSNGPQKF CIEKVGKENW LPRSHTCFNR
LDLPPYKSYE QLKEKLMFAI EETEGFGQE
//
