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Database: UniProt
Entry: A0A1S3STJ6_SALSA
LinkDB: A0A1S3STJ6_SALSA
Original site: A0A1S3STJ6_SALSA 
ID   A0A1S3STJ6_SALSA        Unreviewed;       505 AA.
AC   A0A1S3STJ6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000256|ARBA:ARBA00015618, ECO:0000256|RuleBase:RU367101};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU367101};
GN   Name=LOC106611702 {ECO:0000313|RefSeq:XP_014067664.1};
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_014067664.1};
RN   [1] {ECO:0000313|RefSeq:XP_014067664.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014067664.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Ubiquitin-protein ligase which is mainly involved pre-mRNA
CC       splicing and DNA repair. Required for pre-mRNA splicing as component of
CC       the spliceosome. {ECO:0000256|RuleBase:RU367101}.
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC         ECO:0000256|RuleBase:RU367101};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367101}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU367101}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000256|ARBA:ARBA00004642}.
CC   -!- SIMILARITY: Belongs to the WD repeat PRP19 family.
CC       {ECO:0000256|ARBA:ARBA00006388, ECO:0000256|RuleBase:RU367101}.
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DR   RefSeq; XP_014067664.1; XM_014212189.1.
DR   AlphaFoldDB; A0A1S3STJ6; -.
DR   STRING; 8030.ENSSSAP00000085153; -.
DR   PaxDb; 8030-ENSSSAP00000085153; -.
DR   Ensembl; ENSSSAT00000213464; ENSSSAP00000154066; ENSSSAG00000068788.
DR   GeneID; 106611702; -.
DR   KEGG; sasa:106611702; -.
DR   OMA; AHKTWEE; -.
DR   OrthoDB; 130592at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000087266; Chromosome ssa09.
DR   Bgee; ENSSSAG00000068788; Expressed in sexually immature organism and 16 other cell types or tissues.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-KW.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000974; C:Prp19 complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:UniProtKB-UniRule.
DR   CDD; cd16656; RING-Ubox_PRP19; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR013915; Pre-mRNA_splic_Prp19.
DR   InterPro; IPR038959; Prp19.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR43995; PRE-MRNA-PROCESSING FACTOR 19; 1.
DR   PANTHER; PTHR43995:SF1; PRE-MRNA-PROCESSING FACTOR 19; 1.
DR   Pfam; PF08606; Prp19; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00504; Ubox; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   PROSITE; PS51698; U_BOX; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367101};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367101};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW   ECO:0000256|RuleBase:RU367101};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW   ECO:0000256|RuleBase:RU367101};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367101};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|RuleBase:RU367101};
KW   Transferase {ECO:0000256|RuleBase:RU367101};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU367101};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   DOMAIN          1..73
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REPEAT          261..302
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          354..388
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          389..430
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          472..505
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ   SEQUENCE   505 AA;  54731 MW;  0CEFCFD42A6D394C CRC64;
     MSLVCAISNE VPEHPCVSPV SNQVFERRLI EKFIAENGVD PMNGQPLSEE QLIDIKVSHP
     IRPKAASATS IPAILKSLQD EWDAVMLHSF TLRQQLQTTR QELSHALYQH DAACRVIARL
     TKEVTAAREA LATLKPQAGL VAPQAMPASQ PAAGGAGGEP MEVSEQVGMT PEIIQKLQDK
     ATVLTTERKK RGKTVPEELV RAEDLSKYRQ VASHAGLHSA SVPGILCMDL CPSDTNKVLT
     GGADKNVVVF DKKEEQIIAT LKGHTKKVTS VIYHPSQSVV FSASPDSTIR VWSVTGGNCV
     QVVRAHEASV TGLSLHATGD YLLSSSEDQY WAFSDIQTGR VLTKVTDEAA GVALTCAQFH
     PDGLIFGTGT ADSQIKIWDL KERTNVANFP GHSGPVTSIA FSENGYYLAT GAQDSSVKLW
     DLRKLKNFKT IALDNNYEVK SLVFDQSGTY LAVGGSDIRV YICKQWSEVL NFSDHSGLVT
     GVAFGDNAQF LSSAGMDRSL KFYSL
//
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