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Database: UniProt
Entry: W5M5I9_LEPOC
LinkDB: W5M5I9_LEPOC
Original site: W5M5I9_LEPOC 
ID   W5M5I9_LEPOC            Unreviewed;       887 AA.
AC   W5M5I9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE            EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
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:ENSLOCP00000003647.1, 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:ENSLOCP00000003647.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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; AHAT01010575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01010576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01010577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01010578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01010579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5M5I9; -.
DR   STRING; 7918.ENSLOCP00000003647; -.
DR   Ensembl; ENSLOCT00000003654.1; ENSLOCP00000003647.1; ENSLOCG00000003079.1.
DR   eggNOG; KOG0940; Eukaryota.
DR   GeneTree; ENSGT00940000160726; -.
DR   HOGENOM; CLU_002173_0_1_1; -.
DR   InParanoid; W5M5I9; -.
DR   OMA; EIDMADW; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000018468; Linkage group LG23.
DR   Bgee; ENSLOCG00000003079; Expressed in ovary 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:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; 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:SF396; NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP2; 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|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001569};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR001569}.
FT   DOMAIN          1..121
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          314..347
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          344..377
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          420..453
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          460..493
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          553..887
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        855
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   887 AA;  100411 MW;  DA1577C59DCA8DDA CRC64;
     MASASSSRSG VGQSSEKSQL TLKVLSAKPQ SPKSPSRHSR LNSFVEVTAD GLSSETKKTG
     KRCGHPELQW NEDLTLNVTP QSHLDLKLWS CHALRNELLG IASIDVYDTL KSNNGKMENV
     QLNLALQTEN KGSLVPGGEL TVCLDGLAVD LGSLPNGSAV TDKPQQSDGH GIRRTQSEDS
     PPSSSGSCSG PRGRSHRHSA GMARGGPVAN GDPAVNGEHS PGARSRRRQT GKALSSNTGL
     GTPGKAEVAA NGTEDGRRSP TCQTPPPSAA LSTSTTPCAG TPSSGSDAPQ GDTGETGGTP
     TPDQASAAPE QNMESLPPGW EQRVLPNGRI YYVDHNTKTT TWERPLPPGW EKRVDQRGRF
     YYVDHNTRTT TWQRPTAESV RNYEQWQSQR SQLQGAMQQF SQRFLYQSIG MRALQRTKLS
     LLNSGWYEKR QDNGRVYFVN HNTRTTQWED PRTQGMIQEP PLPPGWEMKY TNEGVRYFVD
     HNSRTTTFKD PRPGFDSGSK QGGSPGAYDR SFRWKYHQFR FLCHSNALPS HVKISVSRQT
     LFEDSFQQIM NMKPYDLRRR LYIIMRGEEG LDYGGIAREW FFLLSHEVLN PMYCLFEYAG
     KNNYCLQINP ASSINPDHLT YFRFIGRFIA MALYHGKFID TGFTLPFYKR MLNKKPTLKD
     LESIDPEFHN SIMWVKENNL EECGVELYFA QDMEILGKVS THELKTDGEN ELVTEDNKEE
     YIRLLTDWRF TRGVEEQTKA FLDGFNEVVP LEWLRYFDEK ELELMLCGMQ EIDLTDWQKN
     TIYRHYTKNS KQIQWFWQVV KEMDNEKRIR LLQFVTGTCR LPVGGFSELI GSNGPQKFCI
     DKVGKETWLP RSHTCFNRLD LPPYKSFEQL KEKLLFAIEE TEGFGQE
//
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