ID   CDK5_GLOMM              Reviewed;         292 AA.
AC   Q2PQN9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Cyclin-dependent kinase 5 homolog;
DE            EC=2.7.11.22;
DE   AltName: Full=Cell division protein kinase 5;
GN   Name=Cdk5;
OS   Glossina morsitans morsitans (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fat body;
RX   PubMed=16907828; DOI=10.1111/j.1365-2583.2006.00649.x;
RA   Attardo G.M., Strickler-Dinglasan P., Perkin S.A.H., Caler E.,
RA   Bonaldo M.F., Soares M.B., El-Sayeed N.M.A., Aksoy S.;
RT   "Analysis of fat body transcriptome from the adult tsetse fly, Glossina
RT   morsitans morsitans.";
RL   Insect Mol. Biol. 15:411-424(2006).
CC   -!- FUNCTION: Probably involved in the control of the cell cycle. Interacts
CC       with D1 and D3-type G1 cyclins. Possible regulator of neuronal
CC       differentiation and/or development (By similarity). {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   -!- 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; DQ307184; ABC25084.1; -; mRNA.
DR   AlphaFoldDB; Q2PQN9; -.
DR   SMR; Q2PQN9; -.
DR   STRING; 37546.Q2PQN9; -.
DR   EnsemblMetazoa; GMOY000139-RA; GMOY000139-PA; GMOY000139.
DR   VEuPathDB; VectorBase:GMOY000139; -.
DR   Proteomes; UP000092444; Unassembled WGS sequence.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07839; STKc_CDK5; 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:SF46; CYCLIN-DEPENDENT KINASE 5; 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; Cell cycle; Cell division; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..292
FT                   /note="Cyclin-dependent kinase 5 homolog"
FT                   /id="PRO_0000291621"
FT   DOMAIN          4..286
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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"
FT   MOD_RES         14
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  33206 MW;  8BE6A37641CF9ED8 CRC64;
     MQKYEKLEKI GEGTYGTVFK GRNRETLEIV ALKRVRLDED DEGVPSSALR EICLLKELKH
     KNIVRLYDVL HSEKKLTLVF EHCDQDLKKY FDSLNGDIDM AVCRSFMLQL LRGLAFCHSH
     NVLHRDLKPQ NLLINKNGEL KLADFGLARA FGIPVKCYSA EVVTLWYRPP DVLFGAKLYT
     TSIDMWSAGC IFAELADAGR PLFPGSDVLD QLMKIFRVLG TPTEESWPGV THLSDYVALP
     HFPAITSWSQ IVPRLSSKGR DLLQKLLVCR PNQRVSAEQA MQHPYFTDSS NH
//