Y2417_DICDI
ID Y2417_DICDI Reviewed; 528 AA.
AC Q54SK3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0282417;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0282417;
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; AAFI02000047; EAL66068.1; -; Genomic_DNA.
DR RefSeq; XP_640036.1; XM_634944.1.
DR AlphaFoldDB; Q54SK3; -.
DR STRING; 44689.DDB0231179; -.
DR PaxDb; Q54SK3; -.
DR PRIDE; Q54SK3; -.
DR EnsemblProtists; EAL66068; EAL66068; DDB_G0282417.
DR GeneID; 8623562; -.
DR KEGG; ddi:DDB_G0282417; -.
DR dictyBase; DDB_G0282417; -.
DR HOGENOM; CLU_516249_0_0_1; -.
DR Reactome; R-DDI-156711; Polo-like kinase mediated events.
DR Reactome; R-DDI-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-DDI-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR PRO; PR:Q54SK3; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005524; F:ATP 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..528
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0282417"
FT /id="PRO_0000362046"
FT DOMAIN 136..466
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 49..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 142..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 528 AA; 59477 MW; 62E3CCE3C8A6D3FC CRC64;
MHQPSDFTNL DVNFLIFQSN LPITNNAPTD ISIVNNSINI LPVEINNNNN NNNNNNNNNN
NNNNNNNNNN NNNNKNNNDG DDAAATNSIN VIPVFEKTIQ IGTTTKSGHF ILDATAEVND
IQEIEENKDF IVRDTQQNRV LIGEGHYGKV YRSMYVSSDG RSLVNKMLKG KRECTKEVEA
LIDVFDASKM VTTQYFTTLG FSSIIMENMV DIGYVTLKQL LSMDDKQFSA LASPFTCRSQ
MIKPIINAMV IALYSVNIEK NYTHFDLNHG NIFVNIHTLD TCQSISGSGS GSGSGSGSNT
RNPVVLGDFG CARKMDVPIR LCDTNGHENY KSLERYWDYN QCRIKTTSFI RDNEDIFSLG
VLIFEMLLTF VHPGTTLFEQ NVLFLLKFHG IEIVPTGGPN NNYTTLKVAF SNDIRNFTSN
TQFTTITFDS KFNPIISQII NYIQYYRNRP NSSQVLESLI NNHQYSLNNN LPPIFVENPN
DKYEPVDANS SDDSSVLYHS YDSSDADDTP SFEITITRDN FNQSINHQ
