ID A0A1U8CFA1_MESAU Unreviewed; 1018 AA.
AC A0A1U8CFA1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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|RefSeq:XP_012978092.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012978092.1};
RN [1] {ECO:0000313|RefSeq:XP_012978092.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_012978092.1; XM_013122638.2.
DR AlphaFoldDB; A0A1U8CFA1; -.
DR GeneID; 101844326; -.
DR CTD; 26750; -.
DR OrthoDB; 5308056at2759; -.
DR Proteomes; UP000189706; Unplaced.
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; 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; 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; 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, ECO:0000313|RefSeq:XP_012978092.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1018
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010569176"
FT DOMAIN 1..107
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 722..1008
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 152..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 110322 MW; 7F4F8A0D304E4C40 CRC64;
MLVLAKIPLL LAEEAAPATC MSIIVWKRYS DFKKLHKELW QIHRNLFRHS ELFPPFAKGI
VFGRFDKTVI EERRQCAEDL LQFSANIPAL YNSKQLEDFF KGGIVNDGSA LIGPADEYPD
SLPDTLPECG AEGFSSDSDL TSLTVDADSG AEVDDGMASW QGSPGRTVGL SLSADSSAAG
PGASDSKASR AEDRESRSLF PSSLKPRLGR RDYLERAGQL IKLAVKKEEE DDYEAASDFY
RKGVDLLLEG VQGESSPTRR EAVKRRTAEY LMRAESISSL RASPRLDSGL QPPGSLSSRP
PWNLRSPAEE LKAFRVLGVI DKVLLVMDTR TEQTFILKGL RKSSECSRSR KTIIPRCVPN
MVCLHKYIIS EESVFLVLQH AEGGKLWSYI SKFLNRSSQE SFDVKETKPR VPHRVYLQQP
SASPPDSSSF ESRGSDMGGM LQVLPVKTSL TPSSQEDSNQ EDDGQDSSPR WPDSGSSSEE
ECTAGYLTLC NEYGQEKIDL GSLNEEPIAL PGGGASADTQ AALSPLAGDR PSPSRQLKFS
PGDEDPEAAC FPQTSDSLTM SKNSPMEFFR IDSKDSTSEL LGLDFGEKLH GLKPEPLRAL
LTLADGEGGA EEAQDSISRG SDDSVPVISF KEAAFEGVCG AEEGRPDLLV NLPGEPQPTK
EASAADPAKF AQASTGRLES KLFEAPDVLC LRLSSEQCHG PGKEDPEEPD DPAGSLPCGV
TPKHQVQAGP GVLGTAVDDS SAGGHFLWPR SDPESEGLGR AEAAVTARDA GESPPHASSA
HSGAKGRGAH ADTAAVEEVL LFTEQAKEEP SPLFQRDSET KEQSVLALGG EKEIHQIFED
LDKKLAASSR FLIPEGCVQR WAAEMVVALD ALHREGIVCR DLNPNNILLN DGGHIQLTYF
SRWSEVEDSC DSDAIARMYC APEVGAVTEE TAACDWWSLG AVLFELLTGK TLVECHPAGI
NTHTTLNMPG CVSEEARSLI QQLLQFNPLE RLGAGVAGVE DIKSHPFFTP VDWAELTR
//