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Database: UniProt
Entry: B5X1L0_SALSA
LinkDB: B5X1L0_SALSA
Original site: B5X1L0_SALSA 
ID   B5X1L0_SALSA            Unreviewed;       361 AA.
AC   B5X1L0;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Serine/threonine-protein kinase Sgk2 {ECO:0000313|EMBL:ACI33191.1, ECO:0000313|RefSeq:NP_001133415.1};
DE            EC=2.7.11.1 {ECO:0000313|RefSeq:NP_001133415.1};
GN   Name=SGK2 {ECO:0000313|EMBL:ACI33191.1};
GN   Synonyms=sgk2 {ECO:0000313|RefSeq:NP_001133415.1};
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:ACI33191.1};
RN   [1] {ECO:0000313|EMBL:ACI33191.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33191.1};
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 (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI33191.1, ECO:0000313|RefSeq:NP_001133415.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33191.1};
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:ACI33191.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33191.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|RefSeq:NP_001133415.1}
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; BT044929; ACI33191.1; -; mRNA.
DR   RefSeq; NP_001133415.1; NM_001139943.1.
DR   STRING; 8030.ENSSSAP00000010010; -.
DR   PaxDb; 8030-ENSSSAP00000010010; -.
DR   GeneID; 100194914; -.
DR   KEGG; sasa:100194914; -.
DR   CTD; 10110; -.
DR   OrthoDB; 3028764at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa13.
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; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF222; SERUM_GLUCOCORTICOID REGULATED KINASE 2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 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:ACI33191.1};
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          32..289
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          290..361
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   361 AA;  40608 MW;  2584FE5DB2CB9881 CRC64;
     MANSNPLRSP SSTLSEVNLG PSANPHAKPT DFDFLAVIGK GTFGKVLLAK LKADNKFYAV
     KVLQKKVILK KKEQKNIMAE RNVLLKSLKH PFLVGLHYSF QTPEKLYFVL DYVNGGELFF
     HLQRERCFLE PRARFYAAEV ASAIGYLHSL NIVYRDLKPE NILLDSQGHV VLTDFGLCKE
     GVEPETTTST FCGTPEYLAP EVLRKEPYDR TVDWWCLGAV LYEMIYSLPP FYSRDVSEMY
     DGILHKPLPL PPGKSGAVCS LLQGLLQKDQ HCRLGAIADF LQIKNHVFFS PINWDDLYHK
     RITPPYNPNV KGPADTQHID PEFTREMVPN SVGRTPELNA GTSSSNAFNG FSYVSGEDSF
     L
//
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