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Database: UniProt
Entry: A0A3B3C6B6_ORYME
LinkDB: A0A3B3C6B6_ORYME
Original site: A0A3B3C6B6_ORYME 
ID   A0A3B3C6B6_ORYME        Unreviewed;       727 AA.
AC   A0A3B3C6B6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000606};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000606};
GN   ORFNames=FQA47_007209 {ECO:0000313|EMBL:KAF6717302.1}, FQA47_025313
GN   {ECO:0000313|EMBL:KAF6717830.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000013134.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000013134.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:KAF6717302.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bigg-433 {ECO:0000313|EMBL:KAF6717302.1};
RX   PubMed=32938378;
RA   Liang P., Saqib H.S.A., Ni X., Shen Y.;
RT   "Long-read sequencing and de novo genome assembly of marine medaka (Oryzias
RT   melastigma).";
RL   BMC Genomics 21:0-0(0).
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|PIRNR:PIRNR000606};
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|PIRNR:PIRNR000606};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR000606};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009804, ECO:0000256|PIRNR:PIRNR000606}.
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DR   EMBL; WKFB01000854; KAF6717302.1; -; Genomic_DNA.
DR   EMBL; WKFB01000800; KAF6717830.1; -; Genomic_DNA.
DR   STRING; 30732.ENSOMEP00000013134; -.
DR   PaxDb; 30732-ENSOMEP00000013134; -.
DR   Ensembl; ENSOMET00000033012.1; ENSOMEP00000013134.1; ENSOMEG00000014596.1.
DR   GeneTree; ENSGT00940000159242; -.
DR   OMA; HSWITCK; -.
DR   OrthoDB; 5489497at2759; -.
DR   Proteomes; UP000261560; Unplaced.
DR   Proteomes; UP000646548; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05582; STKc_RSK_N; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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; IPR016239; Ribosomal_S6_kinase_II.
DR   InterPro; IPR041906; RSK_N.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF246; RIBOSOMAL PROTEIN S6 KINASE ALPHA-6; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000606};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000606};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000606};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000646548};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000606};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000606}.
FT   DOMAIN          55..314
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          315..384
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          408..665
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   ACT_SITE        525
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   BINDING         61..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         414..422
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         437
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   727 AA;  81768 MW;  7B26E982CDC25DA1 CRC64;
     MEVNSVSGEV NGHQIMDEPM EEGESFSHCD EGTYKEIPIT HHVKEGCEKA DPSQFELLKV
     LGQGSFGKVF LVRKLVGPDA SQLYAMKVLK KASLKVRDRV RTKMERDILV EVNHPFIVKL
     HYAFQTEGKL YLILDFLRGG DVFTRLSKEV MFTEEDVKFY LAELALALDH LHNLGIVYRD
     LKPENILLDE AGHIKLTDFG LSKESVDADK KAYSFCGTVE YMAPEVVNRR GHTQSADWWS
     LGVLMFEMLT GTLPFQGKDR NETMNMILKA KLGMPQFLSL EAQSLLRMLF KRNPANRLGA
     GPDGVEEIKR HAFFSTIDWN KLYRRELQPP FKPAAGKPDD TFCFDPEFTA KTPKDSPGIP
     PSANAHQLFK GFSFVAPTPM DESKSSPMLS ILPIVQMHGG SAKFSDLYEL QEDIGVGSYS
     ICKRCVHQVS AMEYAVKIID KSKRDPSEEI EILMRYGQHP NIITLKDVYD EGRYVYLVTE
     LMKGGELLDR ILRQKFFSER EASAVLYTIT KTVDYLHCQG VVHRDLKPSN ILYMDDSGNP
     DSIRICDFGF AKQLRGGNGL LLTPCYTANF VAPEVLMRQG YDAACDIWSL GVLLYTMLAG
     YTPFANGPND TPEEILLRIG SGKFSLTGGN WDTVSDSSKD LLSHMLHVDP HQRYSAEQVL
     KHSWITCRDT LPHFQLTRHD APHLVKGAMA ATYSALSQKT SQPVLEPVAA SSLAQRRSMK
     KLTSTDM
//
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