DST1_DICDI
ID DST1_DICDI Reviewed; 737 AA.
AC Q86IX1; Q556A2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Serine/threonine-protein kinase dst1 {ECO:0000250|UniProtKB:O61125};
DE EC=2.7.11.1;
GN Name=dst1 {ECO:0000312|EMBL:EAL70189.1};
GN Synonyms=dstA {ECO:0000303|PubMed:16842885}; ORFNames=DDB_G0274593;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2] {ECO:0000312|EMBL:EAL70189.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL70189.1};
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).
RN [3] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=16842885; DOI=10.1016/j.ejcb.2006.05.013;
RA Arasada R., Son H., Ramalingam N., Eichinger L., Schleicher M., Rohlfs M.;
RT "Characterization of the Ste20-like kinase Krs1 of Dictyostelium
RT discoideum.";
RL Eur. J. Cell Biol. 85:1059-1068(2006).
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:O61125};
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:O61125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000250|UniProtKB:O61125}.
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DR EMBL; AAFI02000012; EAL70189.1; -; Genomic_DNA.
DR RefSeq; XP_643908.1; XM_638816.1.
DR AlphaFoldDB; Q86IX1; -.
DR SMR; Q86IX1; -.
DR STRING; 44689.DDB0216377; -.
DR PaxDb; Q86IX1; -.
DR PRIDE; Q86IX1; -.
DR EnsemblProtists; EAL70189; EAL70189; DDB_G0274593.
DR GeneID; 8619335; -.
DR KEGG; ddi:DDB_G0274593; -.
DR dictyBase; DDB_G0274593; dst1.
DR eggNOG; KOG0576; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q86IX1; -.
DR OMA; IFMIPRE; -.
DR PhylomeDB; Q86IX1; -.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q86IX1; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0012501; P:programmed cell death; ISS:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; ISS:dictyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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.
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..737
FT /note="Serine/threonine-protein kinase dst1"
FT /id="PRO_0000355579"
FT DOMAIN 29..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 305..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 35..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 737 AA; 81572 MW; 6578C7ECF3E274EC CRC64;
MAIKKPINVK QLSDKLGVPI LPDDPQTIYH IQERLGKGSF GQVFKAVHFA NGKVVAIKII
SLDDQEAIKD VRKEISILAE CNYPNIVQYF GSYFKDHQLW IVMEYCGGGS VSDLLQVIDT
ISEDEIALIC REALKGLNYL HEFKKIHRDI KGGNILLNDR GEVKLADFGV SAQLFNTFSK
RNTFVGTPYW MAPEVIQENK YDGKADVWSL GITAIEMAEG LPPNSNVHPM RVIFMIPREE
SPALTDKSIW SDKFQDFISK CLTKDPAERP TAKELLNHEF IQTKKPLSIL SDLVENCKTL
INNSSMFEDE DEEEGNYSTF VEKKTPSDDE KENNNNTVTN YSTVITKDDD DGSNNYSTVI
TKDEMYSTVI TKDDAQTDDD NNNFSTVITK EDPPTDEESD SSCSSSSSSS RNITSPISKR
KPRQPITNSP KISPISSNNI NKIPADNVVS SNQATTTTTT TTTTTTTAAS TTTDQDEGDV
KNIVNKFQLN KPITSSNSTS VTPQKPPFPS NNTTTTSNIN TPIKPSNGLK KSNSNTPVQL
KTSGDKTPTT TPLKNISNNN SVIYNNSNNI NNNNNNNIIA PKSPSPTTGQ KIIKTNSGGV
LKSSGGLSSK RSPSSKPKHS SSSKEPKESL SENLQNIYRN DCTIQLPFLT LNNISSDYLL
SIDYRYNDFK SSLDDLCADP NLISSKLSFS PYIGNLIKSL SYHKDIQENE LMTPKESVQN
TKIVNDLSST VKTIFRL
