ID A0A2K6F1I6_PROCO Unreviewed; 694 AA.
AC A0A2K6F1I6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Ribosomal protein S6 kinase A6 {ECO:0000313|Ensembl:ENSPCOP00000007856.1};
GN Name=RPS6KA6 {ECO:0000313|Ensembl:ENSPCOP00000007856.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000007856.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000007856.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009804}.
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DR AlphaFoldDB; A0A2K6F1I6; -.
DR Ensembl; ENSPCOT00000018404.1; ENSPCOP00000007856.1; ENSPCOG00000015184.1.
DR GeneTree; ENSGT00940000159242; -.
DR Proteomes; UP000233160; Unplaced.
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 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: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; 2.
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; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000606-
KW 51}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000606-51};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 53..279
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 280..349
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 375..632
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT ACT_SITE 492
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT BINDING 59..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 381..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 694 AA; 78543 MW; E95CE68BAD217951 CRC64;
MGLSTSAIWK NTRVEIVNPY EVKRKVKDEG VVKEIPITHH VKEGYEKADP AQFELLKVLG
QGSFGKVMNI FSTFMERDIL VEVNHPFIVK LHYAFQTEGK LYLILDFLRG GDVFTRLSKE
VLFTEEDVKF YLAELALALD HLHQLGIVYR DLKPEKYIFC DTVVDFGLSK ESVDQEKKAY
SFCGTVEYMA PEVVNRRGHS QSADWWSYGV LMFEMLTGTL PFQGKDRNET MNMILKAKLG
MPQFLSGEAQ SLLRMLFKRN PANRLGSEGV EEIKRHLFFA NIDWNKLYKR EVQPPFKPAS
GKPDDTFCFD PEFTAKTPKD SPGLPASANA HQLFKGFSFV ATSIAEEYKI TPITSANVLP
IVQINGNAAQ FSEVYELKED IGVGSYSVCK RCIHVTTNME FAVKIIDKSK RDPSEEIEIL
MRYGQHPNII TLKDVFDDGR YIYLVTDLMK GGELLDRILK QKCFSEREAS DVLYVVTKTV
DYLHCQGVVH RDLKPSNILY MDELANADSI RICDFGFAKQ LRGENGLLLT PCYTANFVAP
EVLMQQGYDA ACDIWSLGVL FYTMLAGYTP FANGPNDTPE EILLRIGNGK FSLSGGNWDN
ISDGAKDLLS HMLHMDPHQR YTTEQVLKHP WITHRDQLPN DQPKRNDAVH VVKGAVVATY
SALTHKAFQP LLEPVAASSL AQRRSMKKRT STGL
//