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Database: UniProt
Entry: A0A1S3PN10_SALSA
LinkDB: A0A1S3PN10_SALSA
Original site: A0A1S3PN10_SALSA 
ID   A0A1S3PN10_SALSA        Unreviewed;       536 AA.
AC   A0A1S3PN10;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=LOC106586202 {ECO:0000313|RefSeq:XP_014028684.1};
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_014028684.1};
RN   [1] {ECO:0000313|RefSeq:XP_014028684.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014028684.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   RefSeq; XP_014028684.1; XM_014173209.1.
DR   AlphaFoldDB; A0A1S3PN10; -.
DR   STRING; 8030.ENSSSAP00000120483; -.
DR   PaxDb; 8030-ENSSSAP00000120483; -.
DR   Ensembl; ENSSSAT00000155837; ENSSSAP00000120483; ENSSSAG00000081507.
DR   GeneID; 106586202; -.
DR   KEGG; sasa:106586202; -.
DR   OrthoDB; 152877at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa25.
DR   Bgee; ENSSSAG00000081507; Expressed in brain and 6 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06610; STKc_OSR1_SPAK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR48012:SF14; STE20_SPS1-RELATED PROLINE-ALANINE-RICH PROTEIN KINASE; 1.
DR   PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR   Pfam; PF12202; OSR1_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|PROSITE-
KW   ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_014028684.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          29..303
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          326..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   536 AA;  59832 MW;  3F3C9690E2C32709 CRC64;
     MAEQGGSPAP AQNPQPVLTM SWPITRESYE LQEVIGSGAT AVVQAALCTP RQERVAIKRI
     NLEKCQTSMD ELLKEIQAMS QCNHPNVVTY YTSFVVKDEL WLVMKLLSGG SMLDIIKHTF
     SKGEHKNGVL DELIIATILK EVLEGLDYLH RNGQIHRDVK AGNILLGEDG SVQIADFGVS
     AFLATGGDMT RNKVRKTFVG TPCWMAPEVM EQVRGYDFKA DIWSFGITAI ELATGSAPYH
     RYPPMKVLML TLQNDPPTLD TGVEDKEMLK KYGKSFRKLI TLCLQKEPAK RPTATELLKC
     KFFQKAKNRE YLIEKLLCRA PNITQRAKRE PEQNSRSMGS VSGSEKELDA VRRVRRVPGS
     SGHLHKTEDG DWEWSDDELD EGSEEGKAAV NQGRSRRVRE ENEDENEDDE QNANIVPIEG
     LSIQHPQVQP FEKNTGPYIQ GALNMVLRLR NSRKELNDIR FEFTPGRDTA DGVSQELFSA
     GLVNGHDVVV VAANLQKIVD DPTTYKVLTF KLVSGCDDTE IPDNVKLIGF AQLSVS
//
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