ID A0A2K6SH41_SAIBB Unreviewed; 745 AA.
AC A0A2K6SH41;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000606};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000606};
GN Name=RPS6KA6 {ECO:0000313|Ensembl:ENSSBOP00000006716.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000006716.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000006716.1}
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 RefSeq; XP_010345639.1; XM_010347337.1.
DR AlphaFoldDB; A0A2K6SH41; -.
DR Ensembl; ENSSBOT00000023466.1; ENSSBOP00000006716.1; ENSSBOG00000020333.1.
DR GeneID; 101035085; -.
DR CTD; 27330; -.
DR GeneTree; ENSGT00940000159242; -.
DR OrthoDB; 5489497at2759; -.
DR Proteomes; UP000233220; 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 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:UP000233220};
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 73..330
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 331..400
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 426..683
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT ACT_SITE 543
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT BINDING 79..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 432..440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 745 AA; 84198 MW; 9B7CC3EB98866F05 CRC64;
MGLSTSAIWK NTRVEIVNPY EVKRKVKVNG LKMVDEPMEE GEADSCHDEG VVKEIPITHH
VKEGYEKADP AQFELLKVLG QGSFGKVFLV RKKTGPDAGQ LYAMKVLKKA SLKVRDRVRT
KMERDILVEV NHPFIVKLHY AFQTEGKLYL ILDFLRGGDV FTRLSKEVLF TEEDVKFYLA
ELALALDHLH QLGIVYRDLK PENILLDEIG HIKLTDFGLS KESVDQEKKA YSFCGTVEYM
APEVVNRRGH SQSADWWSYG VLMFEMLTGT LPFQGKDRNE TMNMILKAKL GMPQFLSAEA
QSLLRMLFKR NPANRLGSEG VEEIKRHLFF TNIDWDKLYK REVQPPFKPA SGKPDDTFCF
DPEFTAKTPK DSPGLPASAN AHQLFKGFSF VATSIAEEYK INPITSANVL PIVQINGNAA
QFGEVYELKE DIGVGSYSVC KRCIHATTNM EFAVKIIDKS KRDPSEEIEI LMRYGQHPNI
ITLKDVFDDG RYVYLVTDLM KGGELLDRIL KQKCFSEREA SDILYVISKT VDYLHCQGVV
HRDLKPSNIL YMDESASADS IRICDFGFAK QLRGENGLLL TPCYTANFVA PEVLMQQGYD
AACDIWSLGV LFYTMLAGYT PFANGPNDTP EEILLRIGNG KFSLSGGNWD NISDGAKDLL
SHMLHMDPHQ RYTTEQILKH SWITHRDQLP NDQPKRNDMS HVVKGAMVAT YSALTHKTFQ
PVLEPVAASS LAQRRSMKKR TSTGL
//
