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Database: UniProt
Entry: C0H9M9_SALSA
LinkDB: C0H9M9_SALSA
Original site: C0H9M9_SALSA 
ID   C0H9M9_SALSA            Unreviewed;       474 AA.
AC   C0H9M9;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Serine/threonine-protein kinase 38 {ECO:0000313|EMBL:ACN10748.1, ECO:0000313|RefSeq:NP_001167076.1};
GN   Name=STK38 {ECO:0000313|EMBL:ACN10748.1};
GN   Synonyms=stk38 {ECO:0000313|RefSeq:NP_001167076.1};
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|EMBL:ACN10748.1};
RN   [1] {ECO:0000313|EMBL:ACN10748.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACN10748.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RA   Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA   Koop B.F.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACN10748.1, ECO:0000313|RefSeq:NP_001167076.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACN10748.1};
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
RN   [3] {ECO:0000313|EMBL:ACN10748.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACN10748.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|RefSeq:NP_001167076.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   EMBL; BT059035; ACN10748.1; -; mRNA.
DR   RefSeq; NP_001167076.1; NM_001173605.1.
DR   STRING; 8030.ENSSSAP00000119323; -.
DR   PaxDb; 8030-ENSSSAP00000119323; -.
DR   GeneID; 100380320; -.
DR   KEGG; sasa:100380320; -.
DR   CTD; 100332206; -.
DR   OrthoDB; 988261at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa12.
DR   Bgee; ENSSSAG00000081088; Expressed in head kidney and 16 other cell types or tissues.
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   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24356:SF221; SERINE_THREONINE-PROTEIN KINASE 38; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACN10748.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          89..382
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          383..463
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   474 AA;  54758 MW;  59C5E90A458B01EB CRC64;
     MATRGHSSCS SMSNHTKERV TMAKVTLENF YSNLISQHEE REMRQQKLER VMDEEGLPDE
     EKCMRRSQHA RKETEFLRLK RTRLGLEDFE SLKVIGRGAF GEVRLVQKKD TGHVYAMKIL
     RKADMLEKEQ VGHIRAERDI LVQADSLWVV KMFYSFQDKM NLYLLMEFLP GGDMMTLLMK
     KDTLSEEETQ FYVAETVLAI DSIHQMGFIH RDIKPDNVLL DSKGHVKLSD FGLCTGLKKA
     HRTEFYRNLN HSVSNDFTSQ YMNSKRKAET WKRNRRQLAF STVGTPDYIA PEVFMQTGYN
     KLCDWWSLGV IMYEMLIGYP PFCSETPQET YKKVMNWKET LVFPPEVPIS ERAKELILRF
     CCEGDHRIGA TGVEEIKRNP FFEGVDYDHI RERPAAIPVE IKSIDDTSNF DEFPESDILS
     PTAAAAPTKS PAAAAAAEAD YKNKDWVFIN YTYKRFEGLT ARGAIPSYMK GSKR
//
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