ID A0A3B4FJ17_9CICH Unreviewed; 806 AA.
AC A0A3B4FJ17;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN Name=NEDD4L {ECO:0000313|Ensembl:ENSPNYP00000009833.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000009833.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000009833.1}
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; A0A3B4FJ17; -.
DR STRING; 303518.ENSPNYP00000009833; -.
DR Ensembl; ENSPNYT00000010070.1; ENSPNYP00000009833.1; ENSPNYG00000007418.1.
DR GeneTree; ENSGT00940000156873; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261460; 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; 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; 2.
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:SF310; E3 UBIQUITIN-PROTEIN LIGASE NEDD4-LIKE; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 4.
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 90..123
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 281..314
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 392..425
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 443..476
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 535..805
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 773
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 806 AA; 92328 MW; B2014EAECA671CE2 CRC64;
TRDDFLGQVD VPLSHLPTED PAMERPYTFK DFLLRPRSHK SRVKGYLRLK MAYLPKQGGH
EEEGGDMREE AEGWDESADS GSQRPQQLLP PLPQGWEEKV DNLGRTYYVN HNNRTTQWKR
PSNVDVISEI ESDNQQRQIH QEAHRVFRSR RHISEDLENE HLEPRDLDNS WELITEEDND
SLAQSLPGPS SVLTPQHTPT PITQEFSEDL NLRLSLTPDT NGEVPGPSSA LSQLSNRLRS
SSMTDGVSDQ AQAPPLTPYL LCSLSALGQS PSSTAYTLTT PGLPPGWEER KDAKGRTYYV
NHNNRTTTWT RPVVQLTEDG ASTSAAAASG GASPQVRRPR SLSSPTVTLS TPLEGANNIQ
VRRAVKDTLS NPQSPQPSPY SSPKSQHKTQ QSFLPPGWEM RIAPNGRPFF IDHNSRTTTW
EDPRLKYPVH MRNKNSMEPG DLGPLPPGWE ERVHTDGRTF YIDHNTKNTQ WEDPRLQSPA
ITGPAVPYSR EFKQKYDYFR KKLKKPADIP NRFEMKLHRN NIFEESYRRI MSLKRPDVLK
ARLWIEFESE KGLDYGGVAR EWFFLLSKEM FNPYYGLFEY SATDNYTLQI NPNSGLCNED
HLSYFKFIGR VAGMATYQVD LKPSGSDMVV TNDNKKEYID LVIQWRFVNR VQKQMNAFLE
GFTELIQIDL IKIFDENELE LLMCGLGDVD VNDWRQHTVY KNGYCPNHPV IQWFWKVVLL
MDAEKRIRLL QFVTGTSRVP MNGFAELYGS NGPQLFTIEQ WGTPDKLPRA HTCFNRLDLP
TYESFEDLRE KLLMAVENAQ GFEGVD
//
