ID A0A1S3KUX6_SALSA Unreviewed; 1265 AA.
AC A0A1S3KUX6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=LOC106562216 {ECO:0000313|RefSeq:XP_013982415.1};
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_013982415.1};
RN [1] {ECO:0000313|RefSeq:XP_013982415.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013982415.1};
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR RefSeq; XP_013982415.1; XM_014126940.1.
DR AlphaFoldDB; A0A1S3KUX6; -.
DR STRING; 8030.ENSSSAP00000020576; -.
DR PaxDb; 8030-ENSSSAP00000020576; -.
DR Ensembl; ENSSSAT00000155140; ENSSSAP00000119810; ENSSSAG00000005199.
DR GeneID; 106562216; -.
DR KEGG; sasa:106562216; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000087266; Chromosome ssa11.
DR Bgee; ENSSSAG00000005199; Expressed in pharyngeal gill and 15 other cell types or tissues.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; IPR035892; C2_domain_sf.
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:SF282; E3 UBIQUITIN-PROTEIN LIGASE NEDD4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 4.
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:UP000087266};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 553..586
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 713..746
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 787..820
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 838..871
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 930..1264
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 89..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1232
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1265 AA; 143476 MW; 261616FCF3D32A92 CRC64;
MAHRLRLHFA SRRSNTDPLS ESLSSHGEES VLCVSTRSPT ESLAHSSVQM KVIPGQLALA
LPPLSPEYGN LQRYSSVFIP KVNTGSVSKK STLQISLQPR GKLNGELENS TEGGEPGVGE
LGSGSGSDGV SCSSSTASDA GYCSSSSSIF EPELPDQRRA SHERSLPRRK ARVPLRRCSS
LVIFPRSPCN TPPASPVSPV ALPALPPARG SYQTSHQLQL SPSEPPQEDE TGTSKASIAT
AMNGLRLSKS SFPSAEFRDA RPMVHFNIPL PDKPKDKMEE CEKTDHSATL DRPCRDKADH
SANLDQHSSV LLHFAHQRPM SGKASRNRTT VNVECPECPE SPTHPSEGEC GPRHIKLFRS
TSACFLPSTK LSEKSHSASL ADNGNGQENH CHHALQRSFS LEVPYHNTGI SCHVSNQKLS
NSPHVHIHVS HGYGARVSSP VIDVNTNHKR DHIQKSPARK TTTRDDFLGQ VDVPLHQIPT
ENPNIERPYT FKDFLLHPRS HKSRVKGHLR LKMTYLPKNN SEDAAEQTED MDPSWEFLEG
QDMSGPRHNH LLPAMPPGWE ERQDNLGRTY YVNHETRTTQ WHRPIVQDSQ VEAEQRQNIH
MEAQQSFTAR RQISDQEDSN DRQESPESWE IITEDESTFY NSQRSPPPPH SPLEFHSFCD
ELSRFQASGA TSGNRRTSLQ LQGPSSHSSR RGSAQTLTVE EHPVHPVLLA TSAGLPPGWE
EKQDSKSRPY YVNHNSRITT WTRPLIQITS EAAAQAVLSQ NATVYQPPML SPEGSPQHSP
GSQRECGFMP AGWEVRNAPN GKPFFIDHNT KTTSWEDPRL KIPVHMRRRP SLDPTDLGPM
PPGWEERVHS DGRIFYIDHN TKNTQWDDPR LQNSAITGPA VPYSRDYKQK YEYFRKKLKK
PADIPNRFEM KLRRNAVLED SYRRILSIKR ADFLKARLWV EFEGEKGLDY GGVAREWFFL
ISKEMFNPYY GLFEYSATDN YTLQINPNSG LCNEDHLSYF KFIGRVAGMA VYHGKLLDAF
FIRPFYKMML QKPITLQDME SVDSEYFNSL KWILENDPID LDLRFTIDEE LFGQTHQHEL
KPGGSEIVVT DDNKKEYIHL VMQWRFVNRI LKQMTAFKEG FYELIPQDLI KIFDENELEL
LMCGLGDVDV NDWRENTKYK NGYCPNQPVI LWFWKTVLLM DAEKRIRLLQ FVTGTSRVPM
NGFAELYGSN GPQLFTIEQW GTRDKLPRAH TCFNRLDLPP YESFEELREK LHIAIENAQG
FDGVD
//
