CDKL2_PONAB
ID CDKL2_PONAB Reviewed; 493 AA.
AC Q5R754;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR860264; CAH92406.1; -; mRNA.
DR RefSeq; NP_001126419.1; NM_001132947.1.
DR AlphaFoldDB; Q5R754; -.
DR SMR; Q5R754; -.
DR GeneID; 100173402; -.
DR KEGG; pon:100173402; -.
DR CTD; 8999; -.
DR InParanoid; Q5R754; -.
DR Proteomes; UP000001595; 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: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..493
FT /note="Cyclin-dependent kinase-like 2"
FT /id="PRO_0000085817"
FT DOMAIN 4..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 311..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..384
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 493 AA; 55824 MW; 1A3BA874E873E66A CRC64;
MEKYENLGLV GEGSYGMVMK CRNKDTGRIV AIKKFLESDD DKMVKKIAMR EIKLLKQLRH
ENLVNLLEVC KKKKRWYLVF EFVDHTILDD LELFPNGLDY QVVQKYLFQI INGIGFCHSH
NIIHRDIKPE NILVSKSGVV KLCDFGFART LAAPGEVYTD YVATRWYRAP ELLVGDVKYG
KAVDVWAIGC LVTEMFMGEP LFPGDSDIDQ LYHIMMCLGN LIPRHQELFY KNPVFAGVRL
PEIKEREPLE RRYPKLSEVV IDLAKKCLHI DPDKRPFCAE LLHHDFFQMD GFAERFSQEL
QLKVQKDARN VSLSKKSQNR KKEKEKDDSL GEERKTLVVQ DTNADPKIKD CKLFKIKGSK
IDGEKAEKGS RASNASCLHD SRTSHNKIVP STSLKDCSNV SVDHTRNPSV AIPPLTHNLS
AVAPGINSGM GTATIPIQGH RVDEKTKKCS IPFVKPNRHS PSGIYNINVT TLVSGPPLSD
DSGADLPQME HQH