FHKC_DICDI
ID FHKC_DICDI Reviewed; 595 AA.
AC P34101; Q54TJ0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable serine/threonine-protein kinase fhkC;
DE EC=2.7.11.1;
DE AltName: Full=Forkhead-associated protein kinase C;
DE AltName: Full=Protein kinase 1;
GN Name=fhkC; Synonyms=fhakC, pk1, pkgA; ORFNames=DDB_G0281567;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 347-379.
RX PubMed=1996312; DOI=10.1073/pnas.88.4.1115;
RA Haribabu B., Dottin R.P.;
RT "Identification of a protein kinase multigene family of Dictyostelium
RT discoideum: molecular cloning and expression of a cDNA encoding a
RT developmentally regulated protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1115-1119(1991).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHK2 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000042; EAL66545.1; -; Genomic_DNA.
DR EMBL; M59745; AAA33187.1; -; Genomic_DNA.
DR PIR; B38578; B38578.
DR RefSeq; XP_640601.1; XM_635509.1.
DR AlphaFoldDB; P34101; -.
DR SMR; P34101; -.
DR STRING; 44689.DDB0220031; -.
DR PaxDb; P34101; -.
DR PRIDE; P34101; -.
DR EnsemblProtists; EAL66545; EAL66545; DDB_G0281567.
DR GeneID; 8623211; -.
DR KEGG; ddi:DDB_G0281567; -.
DR dictyBase; DDB_G0281567; fhkC.
DR eggNOG; KOG0615; Eukaryota.
DR HOGENOM; CLU_000288_63_47_1; -.
DR InParanoid; P34101; -.
DR OMA; DKKKMSM; -.
DR PhylomeDB; P34101; -.
DR PRO; PR:P34101; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:dictyBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:dictyBase.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:dictyBase.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
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 InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..595
FT /note="Probable serine/threonine-protein kinase fhkC"
FT /id="PRO_0000086541"
FT DOMAIN 116..170
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 218..479
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 224..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 377
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 595 AA; 67100 MW; B0DCD82C0DA65F99 CRC64;
MNSNKEETTA DGSVSTTEEQ QQQQQPQQQE QINTTTASTT SNGENTASDN NNNSNNNNNN
NTNNTNTNNN CDISMTEDNS KEEDTGIKVI GEGELWGKLI SLNPTYPTIE IRQDSIILGR
SKGVCNYTFT SPTVSGKHCK IYRDPTVKSR NVAFVDDTST NGTFINNEVI GKGSKILIEN
GCEISVIPKK GSEKISFIYQ DCFEEQKEME QGGPQQKYDL REVLGTGNFA SVRLGVEKET
GNKYAIKIID KKKMSMTSKR KDSLMDEVNV LTKVKHQNII SIKEVFETQK NLYLVLELVT
GGELFDKIVS ERKFQEDTCR YILKQLCDSV RYLHSNGIAH RDLKPENILL ATPNSFLLKI
SDFGLSRAMD EGTYMKTMCG TPQYVAPEIL TKGEREGYGK SVDLWSIGVI TYILLCGFPP
FGDPQTKDFF EKIKNGGFSF PSPYWDEISD EAKSLIKNLI KVDVEKRFTI DQALNHPWFT
NHEEKTKEFY EKDKLEFPPP STNDDHQPTP NTTSSNSQLV PESKCDQIQD NTTDNNNNNN
NNNNNNNNNN NNNTTNNSNN IDNNNGNDES KSSKKRQLSE DSNINDEHEQ KKVKN
