ID   A0A8B9XM57_BOSMU        Unreviewed;       942 AA.
AC   A0A8B9XM57;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   29-MAY-2024, entry version 13.
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:ENSBGRP00000021359.1};
OS   Bos mutus grunniens (Wild yak) (Bos grunniens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=30521 {ECO:0000313|Ensembl:ENSBGRP00000021359.1, ECO:0000313|Proteomes:UP000694520};
RN   [1] {ECO:0000313|Ensembl:ENSBGRP00000021359.1}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   Ensembl; ENSBGRT00000024636.1; ENSBGRP00000021359.1; ENSBGRG00000013430.1.
DR   GeneTree; ENSGT00940000154635; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000694520; Chromosome 18.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:TreeGrafter.
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; 2.
DR   Pfam; PF00397; WW; 4.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 2.
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:UP000694520};
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          348..381
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          380..413
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          455..488
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          495..528
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          587..942
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          153..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        910
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   942 AA;  106693 MW;  970A82308D96F1C6 CRC64;
     MATASPRSDT SNNHSGRLQL QVTVSSAKLK RKKNWFGTAI YTEVAADGES KKTAKSSSSS
     NPKWDEQLTV NVTPQTTLEF RVWSHHTIKA DALLGRATVD LKQALLIHNR KLERVKEQLK
     LCLETKNGVV QTGELTVVLD GLVIEQENIT NGSSSPAIEV QQNGDALHED REPSARTTTR
     LAAEDTNGID NCVPTNTVVQ NSCCSYVVNG DNTPSPSQVA ARPKNTPAPK PLTSEPANDT
     VNGDSPSSVP TDNASSTGTA IGSGEPALSS NCTSTPVEDP PVQETLTSSE NNECIVSNSA
     AFGSEAQSTL DPSTSSSASS SAFEAAKLRQ PDGCVEPVQQ QSGGANTETL PSGWEQRKDP
     HGRTYYVDHN TRTTTWERPQ PLPPGWERRV DDRGRVYYVD HNTRTTTWQR PTMESVRNFE
     QWQSQRSQLQ GAMQQFNQRY LYSASMLAAE NDPYGPLPPG WEKRVDSTDR VYFVNHNTKT
     TQWEDPRTQG LQNEEPLPEG WEIRYTREGV RYFVDHNTRT TTFKDPRNGK SSVTKGGPQI
     AYERSFRWKL AHFRYLCQSN ALPSHVKINV SRQTLFEDSF QQIMALKPYD LRRRLYVIFR
     GEEGLDYGGL AREWFFLLSH EVLNPMYCLF EYAGKNNYCL QINPASTINP DHLSYFCFIG
     RFIAMALFHG KFIDTGFSLP FYKRMLSKKL TIKDLESIDT EFYNSLIWIR DNNIEECGLE
     MYFSVDMEIL GKVTSHDLKL GGSNILVTEE NKDEYIGLMT EWRFSRGVQE QTKAFLDGFN
     EVVPLQWLQY FDEKELEVML CGMQEVDLAD WQRNTVYRHY TRNSKQIIWF WQNKWGRERR
     ASAGDSADAA PGKFVKETDN EVRMRLLQFV TGTCRLPLGG FAELMGSNGP QKFCIEKVGK
     DTWLPRSHTC FNRLDLPPYK SYEQLKEKLL FAIEETEGFG QE
//