CHK1_CAEBR
ID CHK1_CAEBR Reviewed; 493 AA.
AC Q61RA2; A8X2T7;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Serine/threonine-protein kinase chk-1;
DE EC=2.7.11.1;
GN Name=chk-1; ORFNames=CBG06670;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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. Required for checkpoint mediated cell cycle arrest in response
CC to DNA damage in germline cells. Essential for embryogenesis (By
CC 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: Cytoplasm {ECO:0000250}. 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; HE601320; CAP26947.1; -; Genomic_DNA.
DR RefSeq; XP_002647583.1; XM_002647537.1.
DR AlphaFoldDB; Q61RA2; -.
DR SMR; Q61RA2; -.
DR STRING; 6238.CBG06670; -.
DR EnsemblMetazoa; CBG06670.1; CBG06670.1; WBGene00028914.
DR GeneID; 8589581; -.
DR KEGG; cbr:CBG_06670; -.
DR CTD; 8589581; -.
DR WormBase; CBG06670; CBP15640; WBGene00028914; Cbr-chk-1.
DR eggNOG; KOG0590; Eukaryota.
DR HOGENOM; CLU_000288_59_8_1; -.
DR InParanoid; Q61RA2; -.
DR OMA; KRSQGHV; -.
DR OrthoDB; 698464at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cytoplasm; Developmental protein; DNA damage;
KW Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..493
FT /note="Serine/threonine-protein kinase chk-1"
FT /id="PRO_0000085853"
FT DOMAIN 26..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 308..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 493 AA; 56402 MW; 26AE569F0D592B87 CRC64;
MSADVSTKPR GSLPIPTAPG ESNECYRVIR TLGEGAFGEV LLIVNNKNPD MAVAMKKMQI
TTQANTNNIR KEFLIQQKLS KVGHDNFIRA IGMRTENGFH FLFLEYADGG ELFDKIEPDH
GMPTAIAQFY FRQLIEGLKY IHDCDIVHRD IKPENLLLTT SHVLKISDFG MATLYRNEGK
ERLLDLSCGT IPYAAPEVCA GGKYRGPPID VWSSGIVLIA MLTGELPWDR ASDSSYAYLQ
WLGNNNLDEN PWRKMDVRAL CMLRRILTDN VHRRATIEQI KTDPWFTHNY GKLEMTYGRP
LKRARYADEN SPDCNISSTQ QADAVSTAKR RHLETPDKVA HVERQNASFS QPTRTEDLLL
TQNIDMSQNN TNLLERMVCR MTRFCTKFDV PTSYRQLIHA SEHAGYEVRQ TADNRLLVTF
REVSMMVTLY SLKTESRVMV DFRRSRGDGI QFKKMFLEVR NRMNDSICVD GQNFLEDCGY
VPRKPQFVRE ANA
