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Database: UniProt
Entry: W5MWB1_LEPOC
LinkDB: W5MWB1_LEPOC
Original site: W5MWB1_LEPOC 
ID   W5MWB1_LEPOC            Unreviewed;       908 AA.
AC   W5MWB1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE            EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN   Name=WWP1 {ECO:0000313|Ensembl:ENSLOCP00000012670.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012670.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000012670.1}
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   EMBL; AHAT01017486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01017487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01017488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5MWB1; -.
DR   STRING; 7918.ENSLOCP00000012670; -.
DR   Ensembl; ENSLOCT00000012694.1; ENSLOCP00000012670.1; ENSLOCG00000010335.1.
DR   eggNOG; KOG0940; Eukaryota.
DR   GeneTree; ENSGT00940000154635; -.
DR   HOGENOM; CLU_002173_0_1_1; -.
DR   InParanoid; W5MWB1; -.
DR   OMA; YNGRCEY; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000018468; Linkage group LG9.
DR   Bgee; ENSLOCG00000010335; Expressed in testis and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR11254:SF299; NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP1; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 4.
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   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR001569}.
FT   DOMAIN          1..114
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          333..366
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          365..398
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          440..473
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          480..513
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          571..908
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..290
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..334
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   908 AA;  102452 MW;  6005288C06F806D6 CRC64;
     MATASTRSDS SNRHNGRSQL HTTVSSAKLK RKKNWFGTAI YVEVATDGEA KKTAKSNSSS
     NPKWDERLTL NVTPHTKLDF KVWSHHTLKA DVLLGKATLD INQVLELHER KLENVREVLK
     LTLENKSGVI PTGELTVILD GLALDQDSLP NGNTDLTKVQ QNGNAIHENG GETSTRARSS
     STSGSSSGVD SQAPSTSSGQ SVSVFVNGDG TSSPLHGTTS PGNTPAPKPS DTETTDRTVN
     GDIPGCTPAM QDVLPSAGCL AGGCDAATST PVVNPAPAPS PPPPVPESPP MVATSGGAQA
     PSSSTSVSEA RANSSSAAEG GKPRQQTGSA STDPLPPGWE QRKDLHGRTY YVDHNTRTTT
     WERPQPLPPG WERRVDDRGR IYYVDHNTRT TTWQRPTMES VRNFEQWQSQ RSQLQGAMHQ
     FNQRYLYSAS MMSAENDPLG PLPPGWERRV DSNDRVYFVN HNTKTTQWED PRTQGLQNED
     PLPEGWEIRY TREGVRYFVD HNTRTTTFSD PRTGKSSVTK GPQIAYERSF RWKLAHFRYL
     CQSNALPSHV KITVSRQTLF EDSFQQIMAL KPYDLRRRLY VIFRGEEGLD YGGLAREWFF
     LLSHEVLNPM YCLFEYAGKS NYCLQINPAS TINPDHLSYF CFIGRFIAMA LFHGKFIDTG
     FSLPFYKRML NKKLTIKDLE SIDPEFYNSL IWISHKRDNN IEECGLEMYF SVDMEILGKV
     TSHDLKAGGT NLLVTEENKE EYIGLMAEWR FSRGVEEQTK AFLDGFNEVV PLQWLQYFDE
     KELEVMLCGM QEVDLQDWQR NTVYRHYTRN SKQIIWFWQF VKEVDNEVRL RLMQFVTGTC
     RLPLGGFAEL MGSNGPQKFC IEKVGKDTWL PRSHTCFNRL DLPPYKSYEQ LKEKLLFAIE
     ETEGFGQE
//
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