ID A0A2K5MLP8_CERAT Unreviewed; 1018 AA.
AC A0A2K5MLP8;
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=CDC42BPA {ECO:0000313|Ensembl:ENSCATP00000026152.1};
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:ENSCATP00000026152.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000026152.1}
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR AlphaFoldDB; A0A2K5MLP8; -.
DR Ensembl; ENSCATT00000050387.1; ENSCATP00000026152.1; ENSCATG00000036374.1.
DR GeneTree; ENSGT01030000234517; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000036374; Expressed in cerebellum and 12 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd20864; C1_MRCKalpha; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF31; SERINE_THREONINE-PROTEIN KINASE MRCK ALPHA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 298..348
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 368..487
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 513..785
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 857..870
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 252..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..84
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 150..205
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 252..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 114414 MW; 8CBCB3F1759C940A CRC64;
LILKDKLEKT RRESQSEREE FESEFKQQYE REKVLLTEEN KKLTSELDKL TTLYENLSIH
NQQLEEEVKD LADKKESVAH WEAQITEIIQ WVSDEKDARG YLQALASKMT EELEALRNSS
LGTRATDMPW KMRRFAKLDM SARLELQSAL DAEIRAKQAI QEELNKVKAS NIITECKLKD
SEKKNLELLS EIEQLIKDTE ELRSEKGIEH QDSQHSFLAF LNTPSDALDQ FETDPVENTY
VWNPSVKFHI QSRSTSPSTS SEAEPVKTVD STPLPVHTPT LRKKGCPGST GFPLKRKTHQ
FFVKSFTTPT KCHQCTSLMV GLIRQGCSCE VCGFSCHITC VNKAPTTCPV PPEQTKGPLG
IDPQKGIGTA YEGHVRIPKP AGVKKGWQRA LAIVCDFKLF LYDIAEGKAS QPSVVISQVI
DMRDEEFSVS SVLASDVIHA SRKDIPCIFR VTASQLSASN NKCSILMLAD SENEKSKWVG
VLSELHKILK KNKFRDRSVY VPKEAYDSTL PLIKTTQAAA IIDHERIALG NEEGLFVVHV
TKDEIIRVGD NKKIHQIELI PNDQLVAVIS GRNRHVRLFP LSALDGRETD FYKLAETKGC
QTITSGKVRH GALTCLCVAM KRQVLCYELF QSKTRHRKFK EIQVPYNVQW MAIFSEQLCV
GFQSGFLRYP LNGEGSPYSM LHSNDHTLSF IAHQPMDAIC AVEISSKEYL LCFNSIGIYT
DCQGRRSRQQ ELMWPANPSS CCYNAPYLSV YSENAVDIFD VNSMEWIQTL PLKKVRPLNN
EGSLNLLGLE TIRLIYFKNK MAEGDELVVP ETSDNSRKQM VRNINNKRRY SFRVPEEERM
QQRREMLRDP EMRNKLISNP TNFNHIAHMG PGDGIQILKD LPMNPRPQES RTVFSGSVSI
PSITKSRPEP GRSMSASSGL SARSSAQNGS ALKREFSGGS YNAKRQPMPS PSEGSLSSGG
MDQGSDAPAR DFDGEDSDSP RHSTASNSSN LSSPPSPVSP RKTKSLSLES TDRGSWDP
//
