CDKL3_MACFA
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 03-AUG-2022, entry version 72.
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}; 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}.
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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.XP_005557834.1; -.
DR PRIDE; Q4R8T9; -.
DR GeneID; 101866587; -.
DR CTD; 51265; -.
DR eggNOG; KOG0593; Eukaryota.
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: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; 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
