ID A0A2K5KS05_CERAT Unreviewed; 1043 AA.
AC A0A2K5KS05;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=RPS6KC1 {ECO:0000313|Ensembl:ENSCATP00000003487.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000003487.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000003487.1}
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|ARBA:ARBA00001433};
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};
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DR AlphaFoldDB; A0A2K5KS05; -.
DR Ensembl; ENSCATT00000015159.1; ENSCATP00000003487.1; ENSCATG00000013042.1.
DR GeneTree; ENSGT00940000155656; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000013042; Expressed in spleen and 12 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02677; MIT_SNX15; 1.
DR CDD; cd07287; PX_RPK118_like; 1.
DR CDD; cd05576; STKc_RPK118_like; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042132; PX_S6K-delta-1.
DR InterPro; IPR035053; STK_RPK118-like.
DR PANTHER; PTHR15508; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR15508:SF2; RIBOSOMAL PROTEIN S6 KINASE DELTA-1; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF116846; MIT domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50195; PX; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..132
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 771..1033
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 204..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 116010 MW; 55B326A82A1D9E9E CRC64;
MTSYRERSAD LARFYTVTEP QRHPRGYTVY KVTARVVSRR NPEDVQEIIV WKRYSDFKKL
HKELWQIHKN LFRHSELFPP FAKGIVFGRF DETVIEERRQ CAEDLLQFSA NIPALYNSKQ
LEDFFKGGII NDSSELIGPA EAHSDSLIDT FPECSTEGFS SDSDLISLTV DVDSLAELDD
GMASNQNSPI RTFGLNLSSD SSALGAVASD SEQSKTEEER ESRSLFPGSL KPRLGKRDYL
EKAGELIKLA LKKEEEDDYE AASDFYRKGV DLLLEGVQGE SSPTRREAVK RRTAEYLMRA
ESISGLYGKF QLDDVSQPPG TGGHRAPKAT EDTTDLFVLC QGLRKSSEYS RNRKTIIPRC
VPNMVCLHKY IISEESVFLV LQHAEGGKLW SYISKFLNRS PEESFDIKEV KKSTLAKVHL
QQPTSSPQDS SSFESRGSDG GSVLRALPLK SSLTPSSQDD SNQEDDGQDS SPKWPDSGSS
SEEECTTSYL TLCNEYGQEK IEPGSLNEEP FMKTEGNGVD TKAIQSFPTH LAADSDSPST
QLRAHELKFF PNDDPEAVSS PRTSDSLSRS KNSPMEFFRI DSKDSASELL GLDFGEKLYS
LKSEPLKPFF TLPDGDSASR SFNTSESKIE FKAQDTISRG SDDSVPVISF KDAAFDDVSG
TDEGRPDLLV NLPGELEPTR EAAAMGPTKF TQTNIGIIEN KLLEAPDVLC LRLSTEQCQA
HEEKGMEELS DPSGPKSRRI TEKHYAQDDP RMLFVAAVDP SSSGDMSLLP SSDPRFQGLG
VVESAVTANN TEESLFHICS PLSGANEYIA STDTLKTEEV LLFTDQTDDL AKEEPTSLFQ
RDSETKGESG LALEGDKEIH QIFEDLDKKL ALTSRFYIPE GCIQRWAAEM VVALDALHRE
GIVCRDLNPN NILLNDRGHI QLTYFSRWSE VEDSCDSDAI ERMYCAPEVG AITEETEACD
WWSLGAVLFE LLTGKTLVEC HPAGINTHTT LNMPECVSEE ARSLIQQLLQ FNPLERLGAG
VAGVEDIKSH PFFTPVDWAE LMR
//
