ID   A0A8B8WEG2_BALMU        Unreviewed;       421 AA.
AC   A0A8B8WEG2;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   10-JUN-2026, entry version 19.
DE   RecName: Full=cyclin-dependent kinase {ECO:0000256|ARBA:ARBA00012425};
DE            EC=2.7.11.22 {ECO:0000256|ARBA:ARBA00012425};
GN   Name=CDK16 {ECO:0000313|RefSeq:XP_036695538.1};
OS   Balaenoptera musculus (Blue whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=9771 {ECO:0000313|Proteomes:UP000694857, ECO:0000313|RefSeq:XP_036695538.1};
RN   [1] {ECO:0000313|RefSeq:XP_036695538.1}
RP   IDENTIFICATION.
RC   TISSUE=Epidermis and Blubber {ECO:0000313|RefSeq:XP_036695538.1};
RG   RefSeq;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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         Evidence={ECO:0000256|ARBA:ARBA00048367};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00047811};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily.
CC       {ECO:0000256|ARBA:ARBA00006485}.
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DR   RefSeq; XP_036695538.1; XM_036839643.1.
DR   AlphaFoldDB; A0A8B8WEG2; -.
DR   GeneID; 118888515; -.
DR   CTD; 5127; -.
DR   Proteomes; UP000694857; Chromosome X.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006887; P:exocytosis; IEA:TreeGrafter.
DR   GO; GO:0031175; P:neuron projection development; IEA:TreeGrafter.
DR   CDD; cd07873; STKc_PCTAIRE1; 1.
DR   FunFam; 3.30.200.20:FF:000007; Cyclin-dependent kinase 14, putative; 1.
DR   FunFam; 1.10.510.10:FF:000061; Putative cyclin-dependent kinase 17; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR050108; CDK.
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:SF174; CYCLIN-DEPENDENT KINASE 16; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_036695538.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694857};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          90..371
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   421 AA;  47909 MW;  ADCFD5F1C41E53B0 CRC64;
     MGSDGESDQA SATSSDEVQS PVRVRMRNHP PRKISTEDIN KRLSLPADIR LPEGYLEKLT
     LNSPIFDKPL SRRLRRVSLS EIGFGKLETY IKLDKLGEGT YATVYKGKSK LTDNLVALKE
     IRLEHEEGAP CTAIREVSLL KDLKHANIVT LHDIIHTEKS LTLVFEYLDK DLKQYLDDCG
     NVINMHNVKL FLFQLLRGLA YCHRQKVLHR DLKPQNLLIN ERGELKLADF GLARAKSIPT
     KTYSNEVVTL WYRPPDILLG STDYSTQIDM WGVGCIFYEM ATGRPLFPGS TVEEQLHFIF
     RILGTPTEET WPGILSNEEF KTYNYPKYRA EALLSHAPRL DSDGADLLTK LLQFEGRNRI
     SAEDAMKHPF FLSLGERIHK LPDTTSIFAL KEIQLQKEAS IRSSSMPDSG RPAFRVVDTE
     F
//