DST2_DICDI
ID DST2_DICDI Reviewed; 1142 AA.
AC Q55GC2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Serine/threonine-protein kinase dst2 {ECO:0000250|UniProtKB:O61125};
DE EC=2.7.11.1;
GN Name=dst2 {ECO:0000312|EMBL:EAL73318.1};
GN Synonyms=dstB {ECO:0000303|PubMed:16842885}; ORFNames=DDB_G0267730;
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] {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; AAFI02000003; EAL73318.1; -; Genomic_DNA.
DR RefSeq; XP_647262.1; XM_642170.1.
DR AlphaFoldDB; Q55GC2; -.
DR SMR; Q55GC2; -.
DR STRING; 44689.DDB0216378; -.
DR PaxDb; Q55GC2; -.
DR PRIDE; Q55GC2; -.
DR EnsemblProtists; EAL73318; EAL73318; DDB_G0267730.
DR GeneID; 8616067; -.
DR KEGG; ddi:DDB_G0267730; -.
DR dictyBase; DDB_G0267730; dst2.
DR eggNOG; KOG0576; Eukaryota.
DR HOGENOM; CLU_277632_0_0_1; -.
DR InParanoid; Q55GC2; -.
DR OMA; WTFENLR; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q55GC2; -.
DR Proteomes; UP000002195; Chromosome 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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..1142
FT /note="Serine/threonine-protein kinase dst2"
FT /id="PRO_0000355580"
FT DOMAIN 20..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 300..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 716..1050
FT /evidence="ECO:0000255"
FT COMPBIAS 302..318
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1142 AA; 130779 MW; FF73CFD79066A65F CRC64;
MANIAALEPF VGKEDPVELF ELIEEIAEGS FGTVYKGKHL PTGNIMAVKI IALDEDETFE
DLVVEIDILN RCNHNNIVKY YGSWVKGDEL FIAMECCGGG SITEIYQELN IPLNESQIAY
VCRETLKGLE YLHHTNVIHR DLKGANILLT ESGDVKLADF GVSGLLDKSS KRNTFIGTPY
WMAPEVIENR SNPVPYDTKA DIWSLGITLI ELAEAEPPLS EIHPMKVLFQ IPYRDPPKLK
NQENYSKDFI NFIQSCLQKD PNQRKTATEL LKHPFVTNTK EKAVLTDLIT KYRKFRAAEL
EEGGDEDEDS SEQEGMDSDD KDSDLKKSVG TSDRKSTLIA NGSTSSLSPP ASPSQRKSTG
QNLQLPQIIE QQSSSSSSSS SSSLSSQSLQ PQAVNKSTDR LSANINGSNT KSNTIDKKTT
AAASASASSL NLSTGNLQQS LSGSGSITTN SGVGNGTSGK PTTNGKSSDD RSPDIRTNRK
AGRPVTIRKT LEKRNDAVKK IVNAKLMKQQ LKDIKKQQQK QQEEEEQLLK QQQKEKDDLL
KQNAAKATQQ QKQSAAKEEK IQKQHKVEKE TLSRQQKADR EQLLKKNQSD CSKQRTKVTD
QQKQQQREFK DQQKQQQKQK EHEFKDQNKV LDKSTPKKLS KHIAIHQKVI REQEICVQDL
VFQQKQDFQK LVDDHQNATQ NLFLENKQQS EQLFAWHTQQ NQQFQFQQQC QLENYQEYHT
VLRENMNAEH QLAKSQLEHS HLSETNHLKE RQVTETEQHI KQMTTEQRNS LKEFKLKQTQ
DFKEFLNKLK KELKDEKGNK KQLQQQHKEQ KKQFELTLST QEVDFQKKQA RQKEEEDDIL
LTHQKESFKR LQDKQQNIIR DIEEHCKLQR QQFETEYTFN EEEMLIEHYR QKKALLKQQH
SEQKQIYQEQ TQLQYRLLQE QHKESPALLT DQHLKQKESI EEQQKERLTL QQEEHRIQQE
SLKKQEQKKK GSVTDLPASL ASMQLEQSKQ LQLLSEQLQA ELATMFERHT KETQSLQAEL
AKAQEKLQSD QQKLLHDLTE EQKKSKLKLK SESPSCKENP LHMKKKSTGT TPPSTSSNQK
TLNNSNGASS NGHHHHHHQS AGVGGSGGTI SSSHNTPVLP HNMKHQRSFS TSLPSFKFDN
QD
