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Database: UniProt
Entry: A0A1S3PYB2_SALSA
LinkDB: A0A1S3PYB2_SALSA
Original site: A0A1S3PYB2_SALSA 
ID   A0A1S3PYB2_SALSA        Unreviewed;       787 AA.
AC   A0A1S3PYB2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE            EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN   Name=LOC106588327 {ECO:0000313|RefSeq:XP_014032698.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014032698.1};
RN   [1] {ECO:0000313|RefSeq:XP_014032698.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014032698.1};
RG   RefSeq;
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   RefSeq; XP_014032698.1; XM_014177223.1.
DR   AlphaFoldDB; A0A1S3PYB2; -.
DR   GeneID; 106588327; -.
DR   OrthoDB; 5480520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000087266; Chromosome ssa02.
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; cd08382; C2_Smurf-like; 1.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 3.
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:SF300; E3 UBIQUITIN-PROTEIN LIGASE SMURF2; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 3.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 3.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 3.
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; 3.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 3.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR001569}.
FT   DOMAIN          1..117
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          157..190
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          256..289
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          302..335
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          453..787
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          342..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        755
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   787 AA;  89711 MW;  1004E6257B877C7B CRC64;
     MSNQGVRRNG PVKLRLTVLC AKNLSKKDFF RLPDPFAKVV VDGSGQCHST DTVRNTLDPK
     WNQHYDLYIG KSDSITISVW NHKKIHKKQG AGFLGCVRLL SNAINRLKDT GYQRLDLNKL
     GPNDNDTVRG QIVVSLQSRD RIGTGGPVVD CSRLFDNDLP DGWEERRTAS GRIQYLNHIT
     RTTQWERPTR PASEYSSPSG RPLSCVVDEN TPVMTPNGAA IGVLPSSGSD PRVQERRVRS
     QRHRNYMSRT HLHTPPDLPE GYEQRTTQQG QVYFLHTQTG VSTWHDPRVP RDLSNVNCEE
     LGPLPPGWEI RNTATGRVYF VDHNNRTTQF TDPRLSANLH LVLNPNGPGP NSPGPNGSRV
     AMESQSQNTN LSRQSNQLKE QQPPPQVPAL SPAQLPEEAE CLTVPKYKRD LVQKLKILRQ
     ELSNQQPQAG HCRIDVCREE IFEESYRQVM KMRPKDLWKR LMVKFRGEEG LDYGGVAREW
     LYLLSHEMLN PYYGLFQYSR DDIYTLQINP DSAVNPEHLS YFHFVGRIMG MAVFHGHYID
     GGFTLPFYKQ LLGKPITLDD MESVDPDLHN SLVWILDNDI TGVLDHTFCV EHNAYGEIIQ
     HELKPNGKTV SVSEDTKKEY VRLYVNWRFL HGIEAQFLAL QKGFNEVIPQ HLLKSFDEKE
     LELIVCGLGK IDIADWKSNT RLKHCTTDSN VVKWFWKAVE SYDEERRARL LQFVTGSSRV
     PLQGFKALQG AAGPRLFTIH QIDANTNNLP KAHTCFNRID VPAYEHYDKL YDKLLTAIEE
     TCGFAVE
//
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