ID A0A1S3PFZ4_SALSA Unreviewed; 961 AA.
AC A0A1S3PFZ4;
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=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038172};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038172};
GN Name=LOC106585154 {ECO:0000313|RefSeq:XP_014026527.1};
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_014026527.1};
RN [1] {ECO:0000313|RefSeq:XP_014026527.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014026527.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in the response to environmental stress.
CC Appears to act upstream of the JUN N-terminal pathway.
CC {ECO:0000256|PIRNR:PIRNR038172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR038172};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000256|ARBA:ARBA00008874,
CC ECO:0000256|PIRNR:PIRNR038172}.
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DR RefSeq; XP_014026527.1; XM_014171052.1.
DR AlphaFoldDB; A0A1S3PFZ4; -.
DR GeneID; 106585154; -.
DR KEGG; sasa:106585154; -.
DR OrthoDB; 152877at2759; -.
DR Proteomes; UP000087266; Chromosome ssa02.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06613; STKc_MAP4K3_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF17; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 3; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 2.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038172};
KW Kinase {ECO:0000256|PIRNR:PIRNR038172, ECO:0000313|RefSeq:XP_014026527.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038172};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038172};
KW Transferase {ECO:0000256|PIRNR:PIRNR038172}.
FT DOMAIN 16..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 623..934
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 444..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..466
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..496
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 961 AA; 107985 MW; 2A9DF7C4B0E74BEE CRC64;
MASTFDLSRR NPQEDFELIQ RIGSGTYGDV YKARHVTTGE LAAIKVIKLE PGEDFVVVQQ
EIVMMKDCKH SNIVAYFGSY LRRDKLWICM EYCGGGSLQD IYHVTGPLTE SQIAYVSRET
LQGLYYLHNK GKMHRDIKGA NILLTDNGYV KLADFGISAQ ITMTIAKRKS FIGTPYWMAP
EVAAVERKGG YNHLCDIWAV GITAIELAEL QPPMFDLHPM RALFLMTKSN FQPPKLKDKV
TWTSNFHNFV KISLMKNPKK RPSSDKLLQH PFVSQPLSRT LAIELLDKAS NPDHSSYDDH
LDDEPEEPEE LKYKRVLWLI LGCVSTHCPL SLRLPRFSVG REPPISVPHR IRSGNTREGK
TLSEINFDQV KFDPLLRKET EPHHEPAPDS DGFLDCVEEQ YYTARSNMDL RMDYEAGSPK
SSFLGGHKSL LKSVEEELNQ RGHETHLDDN DDDGGDDDDC GDNDGGDHDD EMQHAKGSTM
RPKEPPPLPP NVKPIPIPQD VANSPAHHGS PAHHGSPGDH DDHGGTIMCC PAAESPARSA
THVPPRPPPP RLPPHKQLSL GNGFSLSEVS GDAGGAEKQS TMPPCVTTRK DRKEIPKPIS
NGLPPTPKVH MGACFSKVFN GCPLKIHCAA SWINPDTRDQ YLLFGAEEGI YTLNLNELHD
SSMEQLFPRR CTWLYVMSNS LLSISGKASQ LYCHNLAGLY EHARQMQKLP MAIPTHRLPD
KIIPRKFSIS NKIPDTKGCQ KCCVVRNPYT GHKYLCGAFQ SSVVMLEWVE PMQKFMLIKN
IDFPLPCPME VFEMLVVPEH QYPLICMGVS KGTELNQVVR FETLDPNTAC PWLKESDTPQ
TCVIHVTQLE RDTILVCLDR SIKIVNMQGR LKSSRKLSAE LTFNFQIESI VCLQDSVLAF
WRHGMQGRSF KSNEITQEIS DNTRIFRLLG SDRVVVLESR PTDNPTAHSN LYILAGHENS
Y
//
