ID FHKA_DICDI Reviewed; 593 AA.
AC Q54BF0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Probable serine/threonine-protein kinase fhkA;
DE EC=2.7.11.1;
DE AltName: Full=Forkhead-associated kinase protein A;
GN Name=fhkA; Synonyms=fhakA; ORFNames=DDB_G0293656;
OS Dictyostelium discoideum (Social amoeba).
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; AAFI02000218; EAL60640.1; -; Genomic_DNA.
DR RefSeq; XP_629079.1; XM_629077.1.
DR AlphaFoldDB; Q54BF0; -.
DR SMR; Q54BF0; -.
DR STRING; 44689.Q54BF0; -.
DR TCDB; 1.I.1.1.5; the nuclear pore complex (npc) family.
DR PaxDb; 44689-DDB0216370; -.
DR EnsemblProtists; EAL60640; EAL60640; DDB_G0293656.
DR GeneID; 8629371; -.
DR KEGG; ddi:DDB_G0293656; -.
DR dictyBase; DDB_G0293656; fhkA.
DR eggNOG; KOG0615; Eukaryota.
DR HOGENOM; CLU_000288_63_47_1; -.
DR InParanoid; Q54BF0; -.
DR OMA; FVHDNSF; -.
DR PhylomeDB; Q54BF0; -.
DR PRO; PR:Q54BF0; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:dictyBase.
DR GO; GO:0005730; C:nucleolus; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
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:DNA damage response; ISS:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05117; STKc_CAMK; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR24349:SF243; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE IV; 1.
DR PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..593
FT /note="Probable serine/threonine-protein kinase fhkA"
FT /id="PRO_0000367466"
FT DOMAIN 54..111
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 180..472
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 307
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 186..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 593 AA; 66318 MW; 1A2428DF9E2351EE CRC64;
MSQTNYIPST PNKSTPPSEL SSTPIDENDI GLLVSLNQEI SSNIHVKIKI EENITIGRSK
TCNIVVPELI VSGKHCIITR ADAIENGNTN YGLLMIQDQS TNGTFINGKL IGKGKSRLLK
NGDKLCLGKS TKEIDISFLY KSNYSNQLLL SSSTNNLNNS GTAQYIWERK DIKDDILKDY
DFIKELGSGN FSVVYEGVNK NTGKRVAIKH LNLSKINTHT PKFKSQLNRE IEILKFINHE
NVVEIYDIFY TKDQQLFFIL ELANGGELYN KIGFNEPLLN ENQSKFIFKQ ILNAVSYLHS
KGIAHRDLKP ENILFDSYGD DYLKIKITDF GLARFIHEGE LAKTLCGSPL YVAPEVILSL
HHKNKYGTNS SSSSQSPTKD INSVGYGKSC DAWSLGAILY IVLCGTPPFD DDDDEEMSTP
QLFEKIVSGN YRVEKLEKSL ISSSAADLVK GLLTVDPDKR LTVEQALNHP WITEINNNSN
NNNNNINNNS SNINIIKKSP LKTVNTNNNN NNCKLSSPIK NSSKLKRNLS NEPLNNNISN
NNNTQTSFTG SLLNQLQLNE GELLKKRKTF LSNNDQKENI NPVINNPFLK SSQ
//
