DST3_DICDI
ID DST3_DICDI Reviewed; 562 AA.
AC Q54EY4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Serine/threonine-protein kinase dst3 {ECO:0000250|UniProtKB:O61125};
DE EC=2.7.11.1;
GN Name=dst3 {ECO:0000312|EMBL:EAL61617.1}; Synonyms=dstC;
GN ORFNames=DDB_G0291267;
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).
RN [2]
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000177; EAL61617.1; -; Genomic_DNA.
DR RefSeq; XP_635106.1; XM_630014.1.
DR AlphaFoldDB; Q54EY4; -.
DR SMR; Q54EY4; -.
DR STRING; 44689.DDB0216379; -.
DR PaxDb; Q54EY4; -.
DR EnsemblProtists; EAL61617; EAL61617; DDB_G0291267.
DR GeneID; 8628053; -.
DR KEGG; ddi:DDB_G0291267; -.
DR dictyBase; DDB_G0291267; dst3.
DR eggNOG; KOG0574; Eukaryota.
DR HOGENOM; CLU_485238_0_0_1; -.
DR InParanoid; Q54EY4; -.
DR OMA; CKFVEVN; -.
DR PhylomeDB; Q54EY4; -.
DR PRO; PR:Q54EY4; -.
DR Proteomes; UP000002195; Chromosome 6.
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..562
FT /note="Serine/threonine-protein kinase dst3"
FT /id="PRO_0000352755"
FT DOMAIN 23..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 316..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 562 AA; 61799 MW; F531BA5CF7F20C1A CRC64;
MNSDSVENLF ISRISKDDPE AIFQIVEVVG SGSFGTVCAC RWMKKKDRES NGNRLIACKF
VEVNADDVET NLNLVKEIDI LKESMDCPYI VEYKGCYLKS SMLLIVMEYC KGGSLLDIIE
LCGKRLIEEE IAAVCAGVVK GLVYLHSKRT THRDIKAGNV LLDEEGLPKL ADFGVSTIAE
QGQKMNTVIG SPYWMAPEII MGQGYDQKAD IWSLGITAIE IAELVPPRFD VPPSRVIFTI
PHQPPPSLKI PSDWSPEFND FVKQCLSMNP ALRPSAQQLL SHPFILKGSS QQILQKLVNE
SIPLLKEKRA EKIRQLEEQE QQRNSSGSKM VSSVPTRASQ ALTNVRNAES LKGSVVILNS
NTKTASIMRN KNPQPPPPSH SSGAGGAAGS TRRVPGNKSV LNRYPPANNV SNGTIAPSPI
NNNNNNNNTT TKVGKVSSPF LQQQQQQQQQ NNNKNPPPKP TTPSPNKKIG DNISKTTPTT
PTTTQPNTST TTKTGSSLNI KPTNNVNRST ISIGQQKSPL QSSEREASYD EESVSVIYHG
SEDEEDEEEF NHEDYEEINV NI
