ID   CDK15_DANRE             Reviewed;         418 AA.
AC   Q1RLU9;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Cyclin-dependent kinase 15;
DE            EC=2.7.11.22;
DE   AltName: Full=Cell division protein kinase 15;
GN   Name=cdk15; Synonyms=pftk2; ORFNames=zgc:136819;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in the control of
CC       the eukaryotic cell cycle, whose activity is controlled by an
CC       associated cyclin. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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; BC115279; AAI15280.1; -; mRNA.
DR   RefSeq; NP_001035398.1; NM_001040308.1.
DR   RefSeq; XP_005165793.1; XM_005165736.3.
DR   AlphaFoldDB; Q1RLU9; -.
DR   SMR; Q1RLU9; -.
DR   STRING; 7955.ENSDARP00000075572; -.
DR   PaxDb; Q1RLU9; -.
DR   Ensembl; ENSDART00000081129; ENSDARP00000075572; ENSDARG00000006093.
DR   GeneID; 791619; -.
DR   KEGG; dre:791619; -.
DR   CTD; 65061; -.
DR   ZFIN; ZDB-GENE-060421-7193; cdk15.
DR   eggNOG; KOG0594; Eukaryota.
DR   GeneTree; ENSGT00940000159606; -.
DR   HOGENOM; CLU_000288_181_6_1; -.
DR   InParanoid; Q1RLU9; -.
DR   OMA; PYWFHTL; -.
DR   OrthoDB; 1010560at2759; -.
DR   PhylomeDB; Q1RLU9; -.
DR   TreeFam; TF106508; -.
DR   PRO; PR:Q1RLU9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 6.
DR   Bgee; ENSDARG00000006093; Expressed in brain and 7 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   CDD; cd07870; STKc_PFTAIRE2; 1.
DR   InterPro; IPR042761; CDK15_STKc.
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; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..418
FT                   /note="Cyclin-dependent kinase 15"
FT                   /id="PRO_0000391902"
FT   DOMAIN          84..369
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         90..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   418 AA;  47907 MW;  2C0E4D7011739325 CRC64;
     MQNLRHAASE AFQRLGLKQR HLGYEELGEL DGVEKPQPHW FHTLQVRRLR VQRGRSNSDP
     MGGKSFQQEF QWKTGLQFGN ATSYLNLEKL GEGTYATVYK GISRINGHLV ALKVIHMKTE
     EGIPFTAIRE ASLLKGLKHA NIVLLHDIIH TRESLTFVFE YVQTDLAQYM IQHPGGLHSY
     NIRLFMFQLL RGLSYIHGRR ILHRDLKPQN LLISYLGELK LADFGLARSK SIPCQTYSAE
     VVTLWYRPPD VLMGSTDYST ALDIWGAGCI FIEMLQGSPA FPGVADVFEQ LLKIWTVIGV
     PTEEIWPGVS DLPNYKPEWF LPCKPQQFRD VWKRLSQLPY KTEDLAQQML MMNPKDRISA
     QDALLHPYFN TLPPPLMHLR DTVSIFKVPG VRLESEARDI FSPSRRTKTP LAPLAKCW