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Database: UniProt
Entry: A0A087Y4H9_POEFO
LinkDB: A0A087Y4H9_POEFO
Original site: A0A087Y4H9_POEFO 
ID   A0A087Y4H9_POEFO        Unreviewed;       509 AA.
AC   A0A087Y4H9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000605};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000605};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000012932.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000012932.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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         ECO:0000256|PIRNR:PIRNR000605};
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:PIRNR000605};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
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:PIRNR000605}.
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DR   EMBL; AYCK01007213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007558026.1; XM_007557964.2.
DR   AlphaFoldDB; A0A087Y4H9; -.
DR   STRING; 48698.ENSPFOP00000012932; -.
DR   Ensembl; ENSPFOT00000012950.2; ENSPFOP00000012932.2; ENSPFOG00000012827.2.
DR   GeneID; 103142092; -.
DR   KEGG; pfor:103142092; -.
DR   CTD; 562242; -.
DR   eggNOG; KOG0598; Eukaryota.
DR   GeneTree; ENSGT00940000155062; -.
DR   OMA; GTQHGEY; -.
DR   OrthoDB; 5489497at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd05584; STKc_p70S6K; 1.
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; IPR016238; Ribosomal_S6_kinase.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF48; RIBOSOMAL PROTEIN S6 KINASE BETA-1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000605; Ribsml_S6_kin_1; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000605};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000605};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000605};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000605};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000605}.
FT   DOMAIN          66..327
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          328..398
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000605-50"
FT   BINDING         72..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000605-51"
FT   BINDING         98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000605-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   509 AA;  56851 MW;  4980277E8AFFD6B4 CRC64;
     MAGVFDIDLD QPDENVSDDE LEDGNQHGEY MDQCSSFEFN MDGCEQFEIS ENSVNKGTEQ
     IGPECFELLK VLGKGGYGKV FQVRKVTGAA CGKIFAMKVL KKAMIVRNAK DTAHTKAERN
     ILEEVKHPFI VDLIYAFQTG GKLYLILEYL SGGELFMQLE REGIFMEDTA CFYLAEISMA
     LGHLHQKGII YRDLKPENIM LNNNGHVKLT DFGLCKESIH DGTYTHTFCG TIEYMAPEIL
     MRSGHNRAVD WWSLGALMYD MLTGAPPFTG ENRKKTIDKI LKCKLSLPPY LTQEARELLK
     KLLRRSPSSR LGGGSGDSAD VQAHSFFRFI NWDDLLARKV EPPFKPFLQS ADDVSQFDSK
     FTSQTPVDSP DDSTLSESAN QVFLGFTYVA PSVLENLKEK FSFEPKVRSP RKFPGSPRTP
     VSPVKFAGGD CWPRGPPLTD APALLSLSSA MDQPMEVSTP EHMDTSSGFI TETSAPLPIR
     HPSGLHAGSY KKQAYPLNSR RPEHLRMNL
//
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