FHKE_DICDI
ID FHKE_DICDI Reviewed; 712 AA.
AC Q54VI1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable serine/threonine-protein kinase fhkE;
DE EC=2.7.11.1;
DE AltName: Full=Forkhead-associated kinase protein E;
GN Name=fhkE; Synonyms=fhake; ORFNames=DDB_G0280321;
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).
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; AAFI02000035; EAL67387.1; -; Genomic_DNA.
DR RefSeq; XP_641374.1; XM_636282.1.
DR AlphaFoldDB; Q54VI1; -.
DR SMR; Q54VI1; -.
DR STRING; 44689.DDB0216333; -.
DR PaxDb; Q54VI1; -.
DR EnsemblProtists; EAL67387; EAL67387; DDB_G0280321.
DR GeneID; 8622508; -.
DR KEGG; ddi:DDB_G0280321; -.
DR dictyBase; DDB_G0280321; fhkE.
DR eggNOG; KOG0615; Eukaryota.
DR HOGENOM; CLU_388034_0_0_1; -.
DR InParanoid; Q54VI1; -.
DR OMA; NIHIANT; -.
DR PhylomeDB; Q54VI1; -.
DR PRO; PR:Q54VI1; -.
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; IPR019406; APLF_PBZ.
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 Pfam; PF10283; zf-CCHH; 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; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..712
FT /note="Probable serine/threonine-protein kinase fhkE"
FT /id="PRO_0000367488"
FT DOMAIN 46..100
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 145..411
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 431..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 414..442
FT /evidence="ECO:0000255"
FT COMPBIAS 461..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 151..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 712 AA; 79684 MW; 69E64AF84541C538 CRC64;
MDELTQANTL AIDEDLVDSV NSVKGWGILK SLNPSYPDIS LVENVITFGR LKDSTVHYND
KSISGSHCKI TRESNDDDGV VIAFIYDNST NGTFIDNIKV GKGSRCLLAS GQEISLTPQK
QLEKIAYIFQ TVEKEIEDGG PSNKYFIGEM LGQGNFATVK LAVERTTGVK YAVKIVDKKK
YFMNSSARKD SLMDEVNILR GLSHPNIIQI IEVFENEKVL SLILELVECG ELLNDIVSNL
FYTEDKAKTL FRQIVDGVLY LHNKGIAHRD LKPENILLKH KNFNQNDAIK LTDFGLSRTV
SDGSFMKTMC GTPQYLAPEI LTSSGGHNGY GLEVDCWSMG AILYIMLCGY PPFDDSREVS
IFEQIRNAKF EFDPEDWSSV SEEAKDLIKR LLCVDPHKRY TCNNIIQHPW FNPNVKLSTL
LEEDERLRKK AEAEVEANNN NTNKSNSPKM LGKRKSEDGN CSDSNNNNNS GSKSLSSIKS
NTTMLDCDEK SNNNNNNGHK KSKSDPTSNN SLFNNDNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNSND TTDSDTDDET ISLPVITKNS KSMSNLQNHL
NNNKINSDDE SETSTNNNNN NNNNNNNNNN NNNNNNNNNK PSTINNNFPV PFPKSPTKNS
PNASPPIKPQ NSSNNNSGLA GIDKPKCQYD PNCYRKNPQH LRDFYHTVSS NK
