ID   CDKL2_RABIT             Reviewed;         566 AA.
AC   Q9TTK0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-NOV-2023, entry version 111.
DE   RecName: Full=Cyclin-dependent kinase-like 2 {ECO:0000250|UniProtKB:Q92772};
DE            EC=2.7.11.22;
DE   AltName: Full=Serine/threonine-protein kinase KKIAMRE;
GN   Name=CDKL2 {ECO:0000250|UniProtKB:Q92772};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=10531455; DOI=10.1523/jneurosci.19-21-09530.1999;
RA   Gomi H., Sun W., Finch C.E., Itohara S., Yoshimi K., Thompson R.F.;
RT   "Learning induces a CDC2-related protein kinase, KKIAMRE.";
RL   J. Neurosci. 19:9530-9537(1999).
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. Nucleus.
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; AB029045; BAA88508.1; -; mRNA.
DR   RefSeq; NP_001075468.1; NM_001081999.1.
DR   AlphaFoldDB; Q9TTK0; -.
DR   SMR; Q9TTK0; -.
DR   STRING; 9986.ENSOCUP00000002825; -.
DR   PaxDb; 9986-ENSOCUP00000002825; -.
DR   GeneID; 100008614; -.
DR   KEGG; ocu:100008614; -.
DR   CTD; 8999; -.
DR   eggNOG; KOG0593; Eukaryota.
DR   InParanoid; Q9TTK0; -.
DR   OrthoDB; 244018at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07846; STKc_CDKL2_3; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF241; CYCLIN-DEPENDENT KINASE-LIKE 2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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..566
FT                   /note="Cyclin-dependent kinase-like 2"
FT                   /id="PRO_0000085818"
FT   DOMAIN          4..287
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          307..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           45..51
FT                   /note="[NKR]KIAxRE"
FT   COMPBIAS        309..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   566 AA;  64053 MW;  5D57595550902EA9 CRC64;
     MEKYENLGLV GEGSYGMVMK CRNKDSGRIV AIKKFLESDD DKMVKKIAMR EIKLLKQLRH
     ENLVNLLEVC KKKKRWYLVF EFVDHTILDD LELFPNGLDD QVVQKYLFQI INGIGFCHSH
     NIIHRDIKPE NILVSQSGVV KLCDFGFART LAAPGEVYTD YVATRWYRAP ELLVGDVKYG
     KAVDVWAIGC LVTEMLMGEP LFPGDSDIDQ LYLIMRCLGN LIPRHQELFY KNPVFAGVRL
     PEIKESEPLE RRYPKLSEVV IDLAKKCLHV DPDKRPFCAE LLHHDFFQMD GFAERFSQEL
     QMKVQKDARN ISLSKKSQNR KKEKEKDDSL GEERKTLVVQ DTNVDSKFKD SKVFKIKGSK
     IDGEKVDKGN RAAVSMTVGP SHIKAVPSTS LRDCSNVSVD HTRNPGMAIP PLTHNLSAVA
     PGINSGMGTI PGVQSYRVDE KTKKYCIPFV KPNKHSPSGI YNMNVTTSVS SEKNLLQANK
     KRGEYSKTDV RLPELNYNHL PELRALEGIA RNSRLIRKEN KILSESRIPS LAAIDLHTPN
     IAVHQVSGSP LSDGSEADSP WMEHQH
//