Y0010_DICDI
ID Y0010_DICDI Reviewed; 695 AA.
AC Q54WW7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0279405;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0279405;
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; AAFI02000030; EAL67851.1; -; Genomic_DNA.
DR RefSeq; XP_641810.1; XM_636718.1.
DR AlphaFoldDB; Q54WW7; -.
DR SMR; Q54WW7; -.
DR STRING; 44689.DDB0220010; -.
DR PaxDb; Q54WW7; -.
DR EnsemblProtists; EAL67851; EAL67851; DDB_G0279405.
DR GeneID; 8622006; -.
DR KEGG; ddi:DDB_G0279405; -.
DR dictyBase; DDB_G0279405; -.
DR eggNOG; KOG0585; Eukaryota.
DR HOGENOM; CLU_396614_0_0_1; -.
DR InParanoid; Q54WW7; -.
DR OMA; DYECENK; -.
DR PRO; PR:Q54WW7; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0099139; P:cheating during chimeric sorocarp development; IMP:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein 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..695
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0279405"
FT /id="PRO_0000362037"
FT DOMAIN 201..462
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 119..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 329
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 207..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 695 AA; 79583 MW; 69C189B3D04152A6 CRC64;
MGCIFTKPSP EQQKFDGEDY ECENKKNLNL ISYIRNLLFG NNSHQQLYNE IIPTTTSTTS
TTTNSVYQNI GLDGYNNNNN NNNNNNNNNN IMNNYGYDDY GYSYEEDEDY YDEMPIPTIV
AQPQPQPQPQ PQPQPQPQQP IRIVSQNQQI PTTPPQQISQ FNITGNKSPS SIGSRHRSKP
KETLRAHKKR HKDGHKMVNE YVFVRKLGKG TFGKVKLAYH HDTHHLYAIK IFNKIRLKKQ
TMGIGRPNAF DDVLKEIAIM KKMNHINVVK LYEVINDPQE EYIYIVMEYI EGGSIMSANE
TSEDLARKYF RDIVFGLEYL HEQKVIHKDL KPENLLVNSE GVVKITDFGV SHIFDDDDVV
RCSRGSPAFL APELCRNESQ PISGKGVDVW ALGVSLYCLI FARTPFISKT NSLLDIYDQI
VNHEPTYPRE ISNDLMDLFK RLLDKNPLTR IQIAEIKSHK WTTISGTWPM NELDHLILSV
TDQEMIDAIS TDHTIKPSDN TTTDEDDSDL SSSSGGESSG IIGSSNESKS MYNNVNSKQK
IQNQNQNQNQ NQNQNQNQNQ NQNHNQNQNQ NQNQNNNNNS LIEKSNISIP ASSSSISNND
SCYENRNVYI KDEEMNMICN DSVIMDPIKE LNKIDGLNYG CDFQIGKEYS DFQYNSGHFI
YDLVDENESQ ISRESANDYY LPFKTNKYLN NKSIV
