ID A0A3B3Y4F7_9TELE Unreviewed; 736 AA.
AC A0A3B3Y4F7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000606};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000606};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000022216.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000022216.1}
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|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 AlphaFoldDB; A0A3B3Y4F7; -.
DR Ensembl; ENSPMET00000013299.1; ENSPMEP00000022216.1; ENSPMEG00000003174.1.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF115; RIBOSOMAL PROTEIN S6 KINASE ALPHA-5; 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 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 1..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 267..335
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 365..627
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 676..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT ACT_SITE 483
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT BINDING 5..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 371..379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 736 AA; 83235 MW; 3AF6746DAD55E5A4 CRC64;
LLKVLGTGAY GKVFLVRKVS GHDAGKLYAM KVLKKATIVQ KAKTAEHTRT ERQVLEHIRQ
SPYLITLHYA FQTDTKLHLI LDYVNGGELF THLVQRVRFK EQEVALYSGE IVLALEHLHK
LGIVYRDLKL ENILLDSNGH IVLTDFGLSK EFDQVERAFS VCGTVEYMAP EIVEGGDSGH
DKAVDWWSLG VLMYELLTGG SPFTVDGDEN SHSDIAKRIC KKDPPFPKDM GPLAKDLIQR
LLVKDPKKRL GSGPNGAENV KKHPFYQKIN WEDLAGKKVP APFKPVIRDE LDVSNFAEEF
TEMDPTYSPA ALPQNCDRIF QGYSFMAPSI LFKRNVVMDD PIQLCGGSER PGSAAVARSA
MMKMDLQDSA LGEGSFSICR RCTHKNTGQQ YAVKIVSKRM EAQTQREIAA LKLCDGHPNI
VKLHEIYHDQ LHTFLVLELL GGGELLERIR RKQHFSETEA SRIMRKLVSA VSHMHDVGVV
HRDLKPENLL FTDESENSEI KIIDFGFARL KPPDNQLLKT PCFTLQYAAP EILKYNGYDE
SCDLWSLGVI LYTMLSGQVP FQCQEKSLIH TSAEEIMHKI KQGDFSFGGE AWRNVSQQAK
DLIQGELLTV DPDKRIKMCG LRYNAWLQDD SQLSSNPLMT PDILGSSTAS VHTCVKATFN
AFNKCKREGF RLQTVDKAPL AKRRKMKKTS TSTETRTRSN PPGRQRLARR LAQRWVFLGS
RCVQKKKKKK RKSEKF
//
