ID   CDKL2_MACFA             Reviewed;         570 AA.
AC   Q4R7T5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Cyclin-dependent kinase-like 2 {ECO:0000250|UniProtKB:Q92772};
DE            EC=2.7.11.22;
GN   Name=CDKL2 {ECO:0000250|UniProtKB:Q92772}; ORFNames=QtsA-14426;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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=2.7.11.22;
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=2.7.11.22;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR   EMBL; AB168727; BAE00837.1; -; mRNA.
DR   RefSeq; NP_001270008.1; NM_001283079.1.
DR   AlphaFoldDB; Q4R7T5; -.
DR   SMR; Q4R7T5; -.
DR   STRING; 9541.XP_005555098.1; -.
DR   Ensembl; ENSMFAT00000032645; ENSMFAP00000024505; ENSMFAG00000043830.
DR   GeneID; 101926402; -.
DR   CTD; 8999; -.
DR   VEuPathDB; HostDB:ENSMFAG00000043830; -.
DR   eggNOG; KOG0593; Eukaryota.
DR   GeneTree; ENSGT00940000160368; -.
DR   OrthoDB; 398098at2759; -.
DR   Proteomes; UP000233100; Chromosome 5.
DR   Bgee; ENSMFAG00000043830; Expressed in temporal lobe and 11 other tissues.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..570
FT                   /note="Cyclin-dependent kinase-like 2"
FT                   /id="PRO_0000085815"
FT   DOMAIN          4..287
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          311..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           45..51
FT                   /note="[NKR]KIAxRE"
FT   ACT_SITE        126
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   570 AA;  64710 MW;  4F88F8C3F820806B CRC64;
     MEKYENLGLV GEGSYGMVVK CRNKDTGRIV AIKKFLESDD DKMVKKIAMR EIKLLKQLRH
     ENLVNLLEVC KKKKRWYLVF EFVDHTILDD LELFPNGLDY QVVQKYLFQI INGIGFCHSH
     NIIHRDIKPE NILVSQSGVV KLCDFGFART LAAPGEVYTD YVATRWYRAP ELLVGDVKYG
     KAVDVWAIGC LVTEMFMGEP LFPGDSDIDQ LYHIMMCLGN LIPRHQELFY KNPVFAGVRL
     PEIKEREPLE RRYPKLSEVV IDLAKKCLHI DPDKRPFCSE LLHHDFFQMD GFAERFSQEL
     QLKVQKDARN ISLSKKSQNR KKEKEKDDSL GEERKTLVVQ DTNADPKIKD CKLFKIKGSK
     IDGEKAEKGN RASNASCLHD SRTSHIKIVP STSLKDCSNV SVDHTRNPGV AIPPLMHNLS
     AVAPGINSGM GTATLPIQSY RVDEKTKKCS IPFVKPNRHS PSGIYNINVT TLVSSEKSLF
     RASKKRREYS RTDVHLPELN YNHLPELRAL EGTARNSRLT KKESKILSES RIPSLAAIDL
     HTPSITLHQV SGPPLSDDSG ADLPQMEHQH