ID G1QM19_NOMLE Unreviewed; 922 AA.
AC G1QM19;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 82.
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:ENSNLEP00000001985.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000001985.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000001985.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000001985.1}
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; ADFV01042782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01042783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01042784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01042785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01042786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01042787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01042788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003268315.1; XM_003268267.3.
DR AlphaFoldDB; G1QM19; -.
DR STRING; 61853.ENSNLEP00000001985; -.
DR Ensembl; ENSNLET00000002096.2; ENSNLEP00000001985.1; ENSNLEG00000001517.2.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000154635; -.
DR HOGENOM; CLU_002173_0_1_1; -.
DR InParanoid; G1QM19; -.
DR OMA; YNGRCEY; -.
DR OrthoDB; 5480520at2759; -.
DR TreeFam; TF323658; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001073; Chromosome 16.
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; 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:UP000001073};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..116
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 349..382
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 381..414
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 456..489
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 496..529
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 588..922
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 210..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 890
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 922 AA; 105130 MW; 9D1033B37492FC88 CRC64;
MATASPRSDT SNNHSGRLQL QVTVSSAKLK RKKNWFGTAI YTEVVVDGEI RKTAKSSSSS
NPKWDEQLTV NVTPQTTLEF RVWSHHTLKA DALLGKATID LKQALLIHNR KLERVKEQLK
LSLENKNGIA QTGELTVVLD GLVIEQENIT NCSSSPTIEI QQNGDALHEN GEPSTRTTAR
LAVEGTNGID NLVPTSTLVQ NSCCSYVVNG DNTPSSPSQV AARPKNTPAP KPLASEPADD
TVNGESSSFA PTDNASVTGT PVVSEENALS PNCTSTTVED PPVQEILTSS ENNECIPSTS
AELGSEARSI LEPDTSNSRS SSAFEAAKSR QPDGCMDPVR QQSGNANTET LPSGWEQRKD
PHGRTYYVDH NTRTTTWERP QPLPPGWERR VDDRGRVYYV DHNTRTTTWQ RPTMESVRNF
EQWQSQRNQL QGAMQQFNQR YLYSASMLAA ENDPYGPLPP GWEKRVDSTD RVYFVNHNTK
TTQWEDPRTQ GLQNEEPLPE GWEIRYTREG VRYFVDHNTR TTTFKDPRNG KSSVTKGGPQ
IAYERSFRWK LAHFRYLCQS NALPSHVKIN VSRQTLFEDS FQQIMALKPY DLRRRLYVIF
RGEEGLDYGG LAREWFFLLS HEVLNPMYCL FEYAGKNNYC LQINPASTIN PDHLSYFCFI
GRFIAMALFH GKFIDTGFSL PFYKRMLSKK LTIKDLESID TEFYNSLIWI RDNNIEECGL
EMYFSVDMEI LGKVTSHDLK LGGSNILVTE ENKDEYIGLM TEWRFSRGVQ EQTKAFLDGF
NEVVPLQWLQ YFDEKELEVM LCGMQEVDLA DWQRNTVYRH YTRNSKQIIW FWQFVKETDN
EVRMRLLQFV TGTCRLPLGG FAELMGSNGP QKFCIEKVGK DTWLPRSHTC FNRLDLPPYK
SYEQLKEKLL FAIEETEGFG QE
//
