Y9452_DICDI
ID Y9452_DICDI Reviewed; 516 AA.
AC Q54C18;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0293276;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0293276;
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. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the AGC Ser/Thr protein kinase
CC family, lacks the AGC-kinase C-terminal domain at the C-terminus.
CC {ECO:0000305}.
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DR EMBL; AAFI02000200; EAL60837.1; -; Genomic_DNA.
DR RefSeq; XP_629248.1; XM_629246.1.
DR AlphaFoldDB; Q54C18; -.
DR SMR; Q54C18; -.
DR STRING; 44689.DDB0229452; -.
DR PaxDb; Q54C18; -.
DR PRIDE; Q54C18; -.
DR EnsemblProtists; EAL60837; EAL60837; DDB_G0293276.
DR GeneID; 8629130; -.
DR KEGG; ddi:DDB_G0293276; -.
DR dictyBase; DDB_G0293276; -.
DR eggNOG; KOG0606; Eukaryota.
DR HOGENOM; CLU_528334_0_0_1; -.
DR InParanoid; Q54C18; -.
DR OMA; CKLINSF; -.
DR PhylomeDB; Q54C18; -.
DR PRO; PR:Q54C18; -.
DR Proteomes; UP000002195; Chromosome 6.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine 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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..516
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0293276"
FT /id="PRO_0000355016"
FT DOMAIN 232..479
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 69..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 238..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 516 AA; 58102 MW; 7AC935A4C46FBCDF CRC64;
MYIYINNEIE ELIECAKKIP ILNNNENGND HNKSISKLIT IFKSKQRSRS SSFSLDTLNF
NLSSSSSNSI EIDDENPYNT NNNNNSNNNN NNNNNNCNNS NNSNNNKNIN SLDNIDINNN
NKNNFNDCSS YSSFSSSECL SDIGNSCIDS LELFRLSDDI EEESEMIFNQ VGPDRYNDLA
NIFSKSHKNL TILLKDINRD TLDCSECIDG SLSDNEWEKC LCCGDIHSLG DYKHVECIGK
GGYGVVCKFI NKKTNEIRAI KTIRKDYSAL KEINTLKELG GQFTVNIFHT FLSPCKEKVL
IEMEYLSGGD CAFHLNDVGV GFPEELAKQY TAETVLCLDF IHEKSIIHCD IKPNNMVIDS
DGHIKLLDFG NAKKFNQKKP TSNDGILGSP RYISPEVLLF EPQSPAVDYW SLGIVMFELI
TGTTPFIGET PEEIFESILS RNTECIEIQK DAKDLIIKLL DPNPSTRIGS KDIKNHPYFN
GINWDTIKTS QPIWKPNSSN NFITSINGCC KLINSF
