ID A0A2Y9TFC0_PHYMC Unreviewed; 800 AA.
AC A0A2Y9TFC0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000606};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000606};
GN Name=RPS6KA5 {ECO:0000313|RefSeq:XP_023986844.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023986844.1};
RN [1] {ECO:0000313|RefSeq:XP_023986844.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023986844.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_023986844.1; XM_024131076.3.
DR AlphaFoldDB; A0A2Y9TFC0; -.
DR STRING; 9755.ENSPCTP00005017446; -.
DR Ensembl; ENSPCTT00005019247; ENSPCTP00005017446; ENSPCTG00005012440.
DR KEGG; pcad:102989152; -.
DR InParanoid; A0A2Y9TFC0; -.
DR OrthoDB; 5489497at2759; -.
DR Proteomes; UP000248484; Chromosome 11.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044024; F:histone H2AS1 kinase activity; IEA:Ensembl.
DR GO; GO:0035175; F:histone H3S10 kinase activity; IEA:Ensembl.
DR GO; GO:0044022; F:histone H3S28 kinase activity; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043687; P:post-translational protein modification; IEA:Ensembl.
DR GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR CDD; cd14179; STKc_MSK1_C; 1.
DR CDD; cd05613; STKc_MSK1_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; 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 Reference proteome {ECO:0000313|Proteomes:UP000248484};
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 50..319
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 320..388
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 427..688
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT ACT_SITE 545
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT BINDING 56..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 433..441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 800 AA; 89620 MW; 6A722CF9494A9228 CRC64;
MEEEGGSGGG GATGTSRDGG AGGEQLLTVK HELRTANLTG HAEKVGIENF ELLKVLGTGA
YGKVFLVRKI SGHDAGKLYA MKVLKKATIV QKAKTTEHTR TERQVLEHIR QSPFLVTLHY
AFQTETKLHL ILDYINGGEL FTHLSQRERF TEHGVQIYVG EIVLALEHLH KLGIIYRDIK
LENILLDSNG HVVLTDFGLS KEFVADEAER AYSFCGTIEY MAPDIVRGGD SGHDKAVDWW
SLGVLMYELL TGASPFTVDG EKNSQAEISR RILKSEPPYP QEMSAVAKDL IQRLLMKDPK
KRLGCGPRDA DEIKEHLFFQ KINWDDLAAK KVPAPFKPVI RDELDVSNFA EEFTEMDPTY
SPAALPQSSE RLFQGYSFVA PSILFKRNAA VIDPLQFHMG VDRPGVTNVA RSAMMKDSPF
YQHYDLDLKD KPLGEGSFSI CRKCIHKKSN QAFAVKIISK RLEANTQKEI TALKLCEGHP
NIVKLHEVFH DQLHTFLVME LLNGGELFER IKRKKHFSET EASYIMRKLV SAVSHMHDVG
VVHRDLKPEN LLFTDENDNL EIKVIDFGFA RLKPPDNQPL KTPCFTLHYA APELLNHNGY
DESCDLWSLG VILYTMLSGQ VPFQSHDKSL TCTSAVEIMK KIKKGDFSFE GEAWKNVSQE
AKDLIQGLLT VDPNKRLKMS GLRYNEWLQD GSQLSSNPLM TPDILGSSGA AVHTCVKATF
HAFNKYKREG FCLQNVDKAP LAKRRKMKKT STSTETRSSS SESSHSSSSH SHGKRTPTKT
LQPSNPADSN NPETLFQFSD
//
