Y1918_DICDI
ID Y1918_DICDI Reviewed; 669 AA.
AC Q54DY0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0291918;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0291918;
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. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000186; EAL61489.1; -; Genomic_DNA.
DR RefSeq; XP_629916.1; XM_629914.1.
DR AlphaFoldDB; Q54DY0; -.
DR SMR; Q54DY0; -.
DR STRING; 44689.DDB0229381; -.
DR PaxDb; Q54DY0; -.
DR EnsemblProtists; EAL61489; EAL61489; DDB_G0291918.
DR GeneID; 8628417; -.
DR KEGG; ddi:DDB_G0291918; -.
DR dictyBase; DDB_G0291918; -.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_410748_0_0_1; -.
DR InParanoid; Q54DY0; -.
DR OMA; CSHRDIK; -.
DR PhylomeDB; Q54DY0; -.
DR PRO; PR:Q54DY0; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; 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; IEA:InterPro.
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..669
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0291918"
FT /id="PRO_0000362045"
FT DOMAIN 13..360
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 396..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 669 AA; 74583 MW; DC8EB4040D2BFC90 CRC64;
MSNQRVLYWP ETYNNIKELG RGVSGVVYKA SHKKTGQIVA IKLVDMKQSK ISTEQIQGEI
RALLTLNPEN ERTHINIIKL IQCFIHKTTA IFILEYVDGG TLEDFMYSFE RGMPLSLISH
CLYQSVNAIE YMNSKKCSHR DIKPANILML RNRKPKLKQQ SEQQQQEDGG YIRYSGQFQL
EPSSQENNNY QFDPDELPIL KVTDYGYASI SGNDSAEIHS TLAGSPLYMA PEIIHIILSP
FLEPGTGKLS ADSSEGYNPL LVDVWAIGAV AFRLITGDDL ISVIFPNLNQ TTVLAALVNL
AKMIDNGDFQ KGLDSIPNEI RKYGLVDPDI ELGISFITSL LQLDPKKRLP LKETLNHPFL
AKGKLSFTQT LNQHYKDNKD VLGSIVPSDI SNFLNQNQQQ QQQQQKSFST SSLPQVNHNN
DTNNNNNNNN NNNNNNNNNN NNNNNNNNNN EKDKDNQSNN SSSSSSSSSP PSPTISKSSP
SSLSSSLSPS SSTDDLPKAM KWSSSVKPPK KSNFAPTFLS HQRSDKITLF PKLLPPPTKD
APPLETMNWR SPPVEVGDSI TWTTLTQDAI FQVQFSVLTS FLKVISASNS YQFRIITSLT
KVPLEIAVSN HKDTILYMYN IVKSVIAPQL ISLSNAFDEN SIRSVLAAIL YQIGTETEQA
EIANCWTLV
