Y2350_DICDI
ID Y2350_DICDI Reviewed; 1224 AA.
AC Q54DC8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0292350 {ECO:0000312|dictyBase:DDB_G0292350};
DE EC=2.7.11.1;
GN ORFNames=DDB_G0292350;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL61299.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL61299.1};
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 Evidence={ECO:0000250|UniProtKB:Q869N2};
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; Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000250|UniProtKB:Q869N2, ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AAFI02000189; EAL61299.1; -; Genomic_DNA.
DR RefSeq; XP_629713.1; XM_629711.1.
DR AlphaFoldDB; Q54DC8; -.
DR SMR; Q54DC8; -.
DR STRING; 44689.DDB0230010; -.
DR PaxDb; Q54DC8; -.
DR EnsemblProtists; EAL61299; EAL61299; DDB_G0292350.
DR GeneID; 8628627; -.
DR KEGG; ddi:DDB_G0292350; -.
DR dictyBase; DDB_G0292350; -.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_268380_0_0_1; -.
DR InParanoid; Q54DC8; -.
DR OMA; QFLMSEW; -.
DR Reactome; R-DDI-75153; Apoptotic execution phase.
DR PRO; PR:Q54DC8; -.
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:0046872; F:metal ion 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; 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; Coiled coil; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1224
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0292350"
FT /id="PRO_0000374049"
FT DOMAIN 935..1193
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 57..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..381
FT /evidence="ECO:0000255"
FT COILED 540..569
FT /evidence="ECO:0000255"
FT COMPBIAS 708..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1063
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 941..949
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 964
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1224 AA; 138962 MW; 1A4EFE0AC3F74815 CRC64;
MKSFLNKNKN SKKIIILDDN DFSKYQQRYD LQNQNIEIVS SPLQNIRSQQ INDGVQMSGS
IQSDLSSSDN FTSSGGFGGG GNSSSNTSNR NSDNSTQRPL MVDIGLEYKY RLALEQNPND
FKALVKWGSL IYKNIKNQMG GKHVDVCLMD WNEELIPIPQ NNNNHHNHNH HNNHTSGNFT
GNINSNTTLS NSFFETLNSF NLREPLFDVC GKYQSSLQLS GGSNLLNIPF STLLNYNLNE
QLNILVNNLN NSSPSSSSSS IKTKNTTSTT TTTTTTKNLN DISNNINNSR VLRSVSLPPA
PPPPPTEDPN SPWSDPILWM KWGDCLFLLC TYLELPMYRA TCEKYFKCIQ ILFKQQEKQH
QQQQQQQQNQ QDKEKFEKQN NYNIKLLAIV LRKWGITLSR YSRRMKSQFL MSEWTSDENI
QVEELWKVLH SQSIQSLLIS NKISPSLVTQ YHLATAYHRH AITLNQFGCQ SKEEIYGLIT
NSCKIYYETL LESLSDTFLQ QLQLQQQQQP WHDIEYYNNN EIFNDQFKSK SLENWGRALD
VQLSTKLNDE EETIEKEEED LNSVDEYLTT FSKSVLKGVT PSLEGVVSLC LNSKQALQYK
AINSVSVLCR SSEIVKSPIY NELMDQMTKV ESFVSKRDDA ESLLSQQKTL KSMPPKLQAY
VRMSGLGEEE IMRNFEIAWN SIYFLTKDTI PNQPIPPNYY RSNKKNKLKQ RQLNDSNNQD
EKEEPEEIKP PLLPSIHRTN QLNNNNNNNN NINNNNINNN NINNNKNGNS GGETPSPSSS
FVITPFTSNS QSKFNTQRQF LSNSTLFNLS SSGIFTNNNN NNNGGSTITT TTTNNISPTK
TNGWTLTLPS KAPTRRATVS LININDLINQ QQQNQINSVS TLSQNNIILN NNNNLDNKPI
SKYIPNSIIR TTVNPPLLSR CDETIFSSGT PLPLFRDKIK LGTGAFGNVF YAIRKSDSSP
VAIKVLMERT KKDSPIIPEL YIHSACNHSN IVTYIESYLC KGHVWIILEY CDGGTVRDLL
QATCTPGNPN NLQLFEETLI AYIITELLEG LVYLRSKGII HRDLKSRNIL LTRKGKVKIA
DFGLATTCSL GRGRTRMCGT MGRIAPEVIR REPYDTQSDI YSLGCLIIEM AEGTVPYGKD
SSLKALFYTA IHQYKLPNPK KYTKEFVDFL YLCLNPDPFK RPTPEMLLHH TFLSGADRGK
SILLGRFKNQ DTRKNLLLDN FVAF
