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Database: UniProt
Entry: A0A1S3NRQ1_SALSA
LinkDB: A0A1S3NRQ1_SALSA
Original site: A0A1S3NRQ1_SALSA 
ID   A0A1S3NRQ1_SALSA        Unreviewed;      2056 AA.
AC   A0A1S3NRQ1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE            EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN   Name=LOC106580884 {ECO:0000313|RefSeq:XP_014017886.1,
GN   ECO:0000313|RefSeq:XP_014017887.1, ECO:0000313|RefSeq:XP_014017888.1};
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_014017886.1};
RN   [1] {ECO:0000313|RefSeq:XP_014017886.1, ECO:0000313|RefSeq:XP_014017887.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014017886.1,
RC   ECO:0000313|RefSeq:XP_014017887.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion
CC       degradation (UFD) pathway and regulation of DNA repair. Part of the
CC       ubiquitin fusion degradation (UFD) pathway, a process that mediates
CC       ubiquitination of protein at their N-terminus, regardless of the
CC       presence of lysine residues in target proteins.
CC       {ECO:0000256|RuleBase:RU369009}.
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|RuleBase:RU369009};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369009}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000256|ARBA:ARBA00004642, ECO:0000256|RuleBase:RU369009}.
CC   -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC       {ECO:0000256|ARBA:ARBA00006331, ECO:0000256|RuleBase:RU369009}.
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DR   RefSeq; XP_014017886.1; XM_014162411.1.
DR   RefSeq; XP_014017887.1; XM_014162412.1.
DR   RefSeq; XP_014017888.1; XM_014162413.1.
DR   STRING; 8030.ENSSSAP00000104143; -.
DR   PaxDb; 8030-ENSSSAP00000104143; -.
DR   GeneID; 106580884; -.
DR   KEGG; sasa:106580884; -.
DR   CTD; 9320; -.
DR   OrthoDB; 1093891at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000087266; Chromosome ssa20.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00078; HECTc; 1.
DR   Gene3D; 3.30.720.50; -; 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   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR045322; HECTD1/TRIP12-like.
DR   InterPro; IPR004170; WWE-dom.
DR   InterPro; IPR018123; WWE-dom_subgr.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR   PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF02825; WWE; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00678; WWE; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF117839; WWE domain; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50918; WWE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369009};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transferase {ECO:0000256|RuleBase:RU369009};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          794..870
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          1659..2056
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1038..1143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1470..1499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1809..1843
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1038..1059
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1082..1096
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1097..1137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2023
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   2056 AA;  227039 MW;  FFE650F433F34429 CRC64;
     MSNRPNSNPG GSLRRSQRNT AAAQPQDHTV AGRLQSEQVK HKANSPPESR RPKSKASKAA
     PSSASGQSRG HSSRSSLSLS VASFVLQDDP EAAGTSEREP TGHQSKTEGT TRGLKRNSAP
     DLNTYTPTPA KKSKSNPPPR DHTTEAKKGP AKSSKKRPLA PELPTGCGQS KKSGASGASP
     TLKRKKADSL PCLSSTAGSL PNRTDGRSAK PTKLASKSAA SAKAGCSTVT DSSSSASTSS
     SSSTGTNSAT AAQGARLKQG KDQNKARRSR SASSPSPRRS TRDKEQAKTS VSSKFEWAAR
     FSPKVNLPKP KLSLPSSSKT ETASKPGPSG LQAKLASLRK STKKRSESPP AELPSFRRST
     RQKTTGSCAS TSRRGSGLGK RGAAEARRQE KMADSDNNQD GANSSAARTD EAPQGASGTA
     SSSVTGAVGM TTSGESESDD SEMGRLQALL EARGLPPHLF GPLGPRMSQL FHRTIGSGAS
     SKAQQLLQGL QATGDESQQL QAAIEMCQLL VMGNEETLGG FPVKSVVPAL ITLLQMEHNF
     DIMNHASRAL TYMMEALPRS SAVVVDAIPV FLEKLQVIQF IDVAEQALTA LEMLSRRHSK
     AILQAGGLAD CLLYLEFFSI NAQRNALAIA ANCCQSITPD EFHFVSDSLP LLTQRLTHQD
     KKSVESTCLC FARLVDNFQH EENLLQQVAS RDLLTNIQQL LVVTPPVLSS GMFIMVVRMF
     SLMCSNCPCL AVQLMKQNIA ETLRFLLCGA ANGSCQEQID LVPRSPQELY ELTSLICELM
     PCLPREGIFA VDLMLKKGSA QATEGAIWQW RDDRGLWHPY NRIDSRIIET AHQNGEDEIS
     LSTLGRVYTI DFNSMQQINE DTGTARGIQR KPNPLANPTT GGHQEVRRED ARAQLMKEDP
     ELAKCFIKTL FGVLYEVYSS SAGPAVRHKC LRAILRIIFF ADAELLKDVL RNHAVSSHIA
     SMLSSQDLKI VVGSLQMAEI LMQKLPDVFS VFFRREGVMH QVKNLAESEA FLTSPPKACT
     SGTASLCTIS TANTTAATTA TPDLGSPSFQ HSMDDSLDLS PQGRLSDVLK RKRLPKRGPR
     RPKYSPPRDD DKVDNQAKSP TTTQSPKSSF LASLNPKTWG KLGTQTNSTN SEPSRTAGVS
     GLARALPKDS VSNNRDKIKA WIKEQACKFV ARYFNTENID GSNPALNVLQ RLCTATQQLS
     LQMDGGVECL VEICSIVSES DVSSFEIQHS GLVKQLLLYL TSRSDRDLVS RDVRLKRFLH
     VFYGCPIPGM EPAGRLEPSE NGPLLSLVRK MNNCLSQMEQ FPVKVHDFPS GNGNGSRGSQ
     ALKFFNTHQL KCQLQRHPDC TNVKQWKGGP VKIDPLALVQ AIERYLVVRG YGRIREEDED
     SDDDGSDDEI DESLAAQFLN SGSVRHRLQF YIGDHLLPYN MTVYQAVRQF SLQAEEERES
     TDDEANPLGR AGIWTKTHTI WYKPVREDED GTKDVVGGKR GRAQTAPTKT SPRNAKKQDE
     LWHDGVCPSV ASPLEMYLMS EPPESITFDD PSLDVNLLLR VLHSISSYWF YLYDNAVSKE
     IIPTSEFINS KLTAKANRQL QDPLVIMTGN IPTWLTELGK TCPFFFPFDT RQMLFYVTAF
     DRDRAMQRLL DTNPEINQSD SQDSRVAPRL DRKKRTINRE ELLKQAESVM QDLGSSRAML
     EIQYENEVGT GLGPTLEFYA LVSQELQRAD LGLWRGEEVA LSNPKGSQEG TKYMFSSRGL
     FAVPFGRTTK PAHIAKIKMK FRFLGKLMAK AIMDFRLLDL PLGLPFYKWM LRHETSISSH
     DLVNIDPGVA KSIQHLEDII RQKKRLEQDR SQTRETLQQA LESLNMNGCS VEDLGLDFTL
     PGFPNIELKK GGKDIPVTIY NLEEYLRLVV YWTMNEGVSR QFESFREGFE SVFPLHHLQY
     FYPEELDQLL CGSKSETWDV KTLMECCRPD HGYTHDSRAV RFLFDVLSSF DAEQQRLFLQ
     FVTGSPRLPV GGFRSLNPPL TIVRKTFEST ENPDDFLPSV MTCVNYLKLP DYSSIEIMRK
     KLLIAAREGQ QSFHLS
//
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