ID CDKL3_MACFA Reviewed; 590 AA. AC Q4R8T9; Q4R954; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 24-JAN-2024, entry version 78. DE RecName: Full=Cyclin-dependent kinase-like 3 {ECO:0000250|UniProtKB:Q8IVW4}; DE EC=2.7.11.22; GN Name=CDKL3 {ECO:0000250|UniProtKB:Q8IVW4}; GN ORFNames=QtsA-10691, QtsA-11477; 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}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB168359; BAE00482.1; -; mRNA. DR EMBL; AB168242; BAE00367.1; -; mRNA. DR RefSeq; NP_001270689.1; NM_001283760.1. DR AlphaFoldDB; Q4R8T9; -. DR SMR; Q4R8T9; -. DR STRING; 9541.ENSMFAP00000015535; -. DR eggNOG; KOG0593; Eukaryota. DR OrthoDB; 5356570at2759; -. DR Proteomes; UP000233100; Unplaced. DR GO; GO:0005737; C:cytoplasm; 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:SF177; CYCLIN-DEPENDENT KINASE-LIKE 3; 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; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..590 FT /note="Cyclin-dependent kinase-like 3" FT /id="PRO_0000085821" FT DOMAIN 4..286 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 459..508 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 547..590 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 45..51 FT /note="[NKR]KIAxRE" FT COMPBIAS 466..484 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 557..582 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 125 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" FT MOD_RES 158 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9JM01" FT MOD_RES 160 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9JM01" FT CONFLICT 117..201 FT /note="Missing (in Ref. 1; BAE00367)" FT /evidence="ECO:0000305" FT CONFLICT 490 FT /note="G -> E (in Ref. 1; BAE00367)" FT /evidence="ECO:0000305" FT CONFLICT 495 FT /note="N -> S (in Ref. 1; BAE00367)" FT /evidence="ECO:0000305" SQ SEQUENCE 590 AA; 67204 MW; C47879E193EE3658 CRC64; MEMYETLGKV GEGSYGTVMK CKHKNTGQIV AIKIFYERPE QSVNKIAMRE IKFLKQFHHE NLVNLIEVFR QKKKIHLVFE FIDHTVLDEL QHYCHGLESK RLRKYLFQIL RAIDYLHSNN IIHRDIKPEN ILVSQSGITK LCDFGFARTL AAPGDIYTDY VATRWYRAPE LVLKDTSYGK PVDIWALGCM IIEMATGNPY LPSSSDLDLL HKIVLKVGNL SPHLQNIFSK SPIFAGVVLP QVQHPKNARK KYPKLNGLLA DIVHACLQID PADRISSSDL LHHEYFTRDG FIEKFMPELK AKLLQEAKVN SLIKPKESSK ENELRKDERK TVYTNTLLSS SVLGKEIEKE KKPKEIKVRV IKVKGGRGDI SEPKKKEYEG GLCQQDANEN VHPMSPDTKL VTIEPPNPIN PSTNCNGLKE NPHCGGSMTM PPINLTNSNL MAANLNSNLF HPSVRLTERA KKRRTSSQSI GQVMPNSRQE DPGPIQSQMG KGIFNERTGH SDQMSNENKR KLNFSRSDRK EFHFPELPVT IQPKDTKGME VKQIKMLKRE SKKTDSSKIP TLLNVDQNQE KQENTGNAQT ERKKNLPDVE //