ID   CHK1_ENCCU              Reviewed;         414 AA.
AC   Q8SSA8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable serine/threonine-protein kinase CHK1 homolog;
DE            EC=2.7.11.1;
GN   Name=CHK1; OrderedLocusNames=ECU03_0620;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   PREDICTION OF FUNCTION.
RX   PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA   Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA   Barton G.J.;
RT   "The complement of protein kinases of the microsporidium Encephalitozoon
RT   cuniculi in relation to those of Saccharomyces cerevisiae and
RT   Schizosaccharomyces pombe.";
RL   BMC Genomics 8:309-309(2007).
CC   -!- FUNCTION: Serine/threonine-protein kinase which is required for
CC       checkpoint-mediated cell cycle arrest and activation of DNA repair in
CC       response to the presence of DNA damage or unreplicated DNA. May also
CC       negatively regulate cell cycle progression during unperturbed cell
CC       cycles (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=2.7.11.1;
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=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. NIM1 subfamily. {ECO:0000305}.
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DR   EMBL; AL590443; CAD26208.1; -; Genomic_DNA.
DR   RefSeq; NP_597573.1; NM_001040937.1.
DR   AlphaFoldDB; Q8SSA8; -.
DR   SMR; Q8SSA8; -.
DR   STRING; 284813.Q8SSA8; -.
DR   PRIDE; Q8SSA8; -.
DR   GeneID; 858735; -.
DR   KEGG; ecu:ECU03_0620; -.
DR   VEuPathDB; MicrosporidiaDB:ECU03_0620; -.
DR   HOGENOM; CLU_000288_59_8_1; -.
DR   InParanoid; Q8SSA8; -.
DR   OMA; ACIKKAC; -.
DR   OrthoDB; 698464at2759; -.
DR   Proteomes; UP000000819; Chromosome III.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..414
FT                   /note="Probable serine/threonine-protein kinase CHK1
FT                   homolog"
FT                   /id="PRO_0000384421"
FT   DOMAIN          4..255
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          291..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        121
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         32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   414 AA;  46023 MW;  D44BD5F2D28DCB8E CRC64;
     MPKYELQETL ASGSTSKVKR AAAPGNAKCV VKVIRKKDVP LRVFLREVKI HRSLRHPNIV
     GFVDSYEDCH GYCIVMKLGC GEVGSMIRAG GGLDPLLAHF YFRQLVSAVE YLHGKCICHR
     DIKPENMLID SAGNLLLSDF GFSTVFFHKG RRRRLRSPAG SLEYMAPEVF EGAYDGELAD
     VWSCGVSLVV FLTGALPWDR AVESDERFSA FVSSRGGCQV PLSSIGDQAM GLVMRMTAKE
     DRRPSVSTVM KDPWVMQPNE LLDESGLCRD SCRLFSLVPR QTGSALHFTQ PGEVHKTPRT
     RPVSSQPRRA GSGDICRVYI GEESLRLALR RVCEALDGMV VSHRIAKEHV MFSTVDSRRS
     VLSGEVGVIR LDEGCCMTIR RAKGDPQEFK RFTRVLAESL GCNGRKCTIL YNEI