CLKA_DICDI
ID CLKA_DICDI Reviewed; 932 AA.
AC Q54UA9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable serine/threonine-protein kinase clkA;
DE EC=2.7.11.1;
DE AltName: Full=CDC2-like kinase A;
GN Name=clkA; ORFNames=DDB_G0281179;
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. CMGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000040; EAL66886.1; -; Genomic_DNA.
DR RefSeq; XP_640867.1; XM_635775.1.
DR AlphaFoldDB; Q54UA9; -.
DR SMR; Q54UA9; -.
DR STRING; 44689.DDB0230105; -.
DR PaxDb; Q54UA9; -.
DR EnsemblProtists; EAL66886; EAL66886; DDB_G0281179.
DR GeneID; 8622923; -.
DR KEGG; ddi:DDB_G0281179; -.
DR dictyBase; DDB_G0281179; clkA.
DR eggNOG; KOG0671; Eukaryota.
DR HOGENOM; CLU_314091_0_0_1; -.
DR InParanoid; Q54UA9; -.
DR OMA; NEYYLFN; -.
DR PRO; PR:Q54UA9; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0006468; P:protein phosphorylation; ISS:dictyBase.
DR GO; GO:0043484; P:regulation of RNA splicing; 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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..932
FT /note="Probable serine/threonine-protein kinase clkA"
FT /id="PRO_0000355206"
FT DOMAIN 590..920
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 719
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 596..604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 932 AA; 107060 MW; 321536CC3D268982 CRC64;
MDRFQTKRKT YSYNGYSNND YGYYNNNCSN VNYNNDIHYK NNNYNNNNNN NNSNSGNNFN
NNNNNNNNNN NNNNNNNNNN NNNNNYTYGN NNNNNSNNNN NNINNNGNSN NNNNNSNGSE
NNYFQSENQS NKDQNSYFNS SYLRNPVDNY NHNNNNHNNN AFDNNNYNTQ NLGDYSYKND
GYNNDNNNND NNNSYGDTDR EKYSIEKICN ENDYDSVNNN NNNRNYSNSY NNNNYNDGNN
NYNSNNYNYN NNNNNNNNIN NNNNSNSNSN SNSNSNSNSN SNSNSNNNNY NNYGYNNHKS
NNGGNRYSDD DDNVFNNNNN NNNNNNNNYN NYNSNNNYNN DYDYNDGKRA NIYSRNNSNN
NNNSKSGNNN SNNYNHNNSN NNGGYNNYNN GYNNYNNNNS NNSNHNSSYN NNNNNNYNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNIS NNSNNNNFNY
NNDNDRNNSN GNYNNNSSNI NNNNNNNNNS NSYHNSCISY SNGGSNSKNS NKNNYNNQQS
NANGNHVGNS KNNESCNNTN TNIEKSNKSM WDDENDYYKV QVGEYLNNRY KVLCTVGSGT
FSTVVECWDT NSSGQVAIKI VRSAKKYTED ALVEIDILRN LEKTGNSNGK YLSHCIRLLD
SFLFKDHICL VFKRYGLSLY EFLKKNRYRP LPLSQIQNIS KQLLTAIYSM HKLSLVHTDL
KPENILLESS RFTYFDNSIP LQFKNSIDTT SNNSVDHYCH LVDTDIVVID FGGATFENTH
HTAIVCSRPY RPPEIILGMG WSYPCDIWGV GCILVELYLG YTLFDTHNNV QHLAMMEKVM
GPFPNSMSNV SKKYFNDYGT LNRPQNSDEI KSMERVEGLK QLKEYFHPCH DSFFDLASRL
LEYQPSKRIS ASDALSHPFL FETIENDCFG PI
