Y1133_DICDI
ID Y1133_DICDI Reviewed; 778 AA.
AC Q54F40;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable protein kinase DDB_G0291133;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0291133;
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. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000175; EAL61850.1; -; Genomic_DNA.
DR RefSeq; XP_635350.1; XM_630258.1.
DR AlphaFoldDB; Q54F40; -.
DR SMR; Q54F40; -.
DR STRING; 44689.DDB0229384; -.
DR PaxDb; Q54F40; -.
DR EnsemblProtists; EAL61850; EAL61850; DDB_G0291133.
DR GeneID; 8627998; -.
DR KEGG; ddi:DDB_G0291133; -.
DR dictyBase; DDB_G0291133; -.
DR eggNOG; KOG0601; Eukaryota.
DR HOGENOM; CLU_359991_0_0_1; -.
DR InParanoid; Q54F40; -.
DR OMA; QARHQFR; -.
DR PRO; PR:Q54F40; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IEA:InterPro.
DR CDD; cd13997; PKc_Wee1_like; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR045067; PKc_Wee1-like.
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; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..778
FT /note="Probable protein kinase DDB_G0291133"
FT /id="PRO_0000362042"
FT DOMAIN 177..462
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 129..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 303
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 183..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 778 AA; 87049 MW; 97114466DEA8E892 CRC64;
MEPTYSIPST PLKTPIRITV NNGHNSGQHS LSLSTCKPTP EQNAFNLNMF SEKKKNQYQT
PKCPSPPLKS TPASRVNSNL PLIHHISSLS MFSPTTSLSD FMNCENGGSN NIDFSSSFGS
SSLNSNNTLS INNNNNNNNN NGGYKIPSSV NKNSNNYNSN SNSNSSNNVI SLFDKNFDVV
CKLGSGSFSD VFKVKSKFDG NSYAIKQARH QFRGFQERER AVREVKAAVS LPPHTNVLQY
YSSWEQNNTL FIQTELCENG SLQDFLDSLS PDQILSEELI WNFLLDVCLG IQHIHSYNML
HLDIKPENLF ISSQGNIKIG DFGMAVKLET TNNNNNGNGG CQSNNTSMDS DCNNLSLDED
DIFFDFLEGD SRYLAYEFLL DKKQISKPSD IFSIGVTFFE MVTGNEMPTN GPLWEQLRSD
KAIDFLEPGK YSDSLYQVIL DMMKSNITER ISLDQILLNE NIQLVQQKRL NQFQNIDNIE
NDNNNNNNTD NNNNNNTDNI NNDNNDDNNN NINNYNLKLI TPYFQYQKER KDEELKEIIE
FGEIREIKEK FEHHQFAIPT PHFVRSNAGR SSSSSLFSDE EEDDDDDDDS GRDSPIHFSL
NNLNNSSSNI GISESNSNNS FSSILEENNE SSSSSPLPSL SFSRRLSTSS LVTTISPKPN
FNTSGNKLFS NENNNSNNNN NNNNNNQNNN NNNGFYGFTN NGSCNNLNNL NNLNSSGEFS
NSSKKKLGKR GLPLLDVVNG GGNSGSKVCA IKRSFDSHPQ ESDKMSPRNL LSLFQETN
