Y9988_DICDI
ID Y9988_DICDI Reviewed; 1371 AA.
AC Q54C38;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0293292;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0293292;
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 -!- DOMAIN: The protein kinase domain 2 is predicted to be catalytically
CC inactive.
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; AAFI02000200; EAL60845.1; -; Genomic_DNA.
DR RefSeq; XP_629228.1; XM_629226.1.
DR AlphaFoldDB; Q54C38; -.
DR SMR; Q54C38; -.
DR STRING; 44689.DDB0219988; -.
DR PaxDb; Q54C38; -.
DR EnsemblProtists; EAL60845; EAL60845; DDB_G0293292.
DR GeneID; 8629110; -.
DR KEGG; ddi:DDB_G0293292; -.
DR dictyBase; DDB_G0293292; -.
DR eggNOG; KOG0589; Eukaryota.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_252337_0_0_1; -.
DR InParanoid; Q54C38; -.
DR OMA; YIESSNW; -.
DR PhylomeDB; Q54C38; -.
DR PRO; PR:Q54C38; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005524; F:ATP 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; 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 InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1371
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0293292"
FT /id="PRO_0000362070"
FT DOMAIN 9..269
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1131..1371
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1371 AA; 160550 MW; 7EFC80705E8A0AE0 CRC64;
MMEEYQEINK ILHEIDDGNT KRKVQLVKNK KDGKLYVCKT IDFNNNNETK DSKVKREREY
LFLKQYSSPS FSHLNIAKYI KHFETRDNHG YLQKLTIIIE YYEGGDLTNL KNLNEVLPKD
IIYLFFTMLV ILKEFKNSII HRDIKPENIF FVKNGPDLEF YLGDMGSSSM VITDQKNTLI
GTNQYMAPEI DLGGYTCKVD IYSLGKTMLS LITLVHSPMN SIFESLFQLC TLENFKIRPS
IDQLIEFVCR QYDQSRYTIS LSSYTHPNTR SIIKYFKDKK FNILKEGEKI NFKIDIQSKF
YNCISVYRGF AYNEYIVEEE EKEKEEYQKE ENQQSIPNVL SIVELIQPPL QDLSKDFENV
LINHINYIRD GGINGSIRSL LHPDIIIKTK CDRVKGFEIK AHSNITNTEG LFIENAHLIY
KPVNLSWKKI FLEREDEITP DVQLKAVFLS LLVAFKISND ENDFLTGTLF DKLMEHIYFV
KSPSLPPPSQ ISPIKEPLSS YELKISFPFN HRAHIYGVKV PLNPNYLNLF FGGEIKDTLI
SNLIQTLNIL APNNLQYKSI LIKLISIILK EEKRILKSYS NLGLEIYFKE FNEIIKNEIA
LEGIVSDKLL VSKIDTTKKI EKIRGFRNGH SNSDADIYIS EFKGKYYAID KFEHIPGLFE
ILEPFSNKAI DDFNQHFKFI STFVDVNESF GLVYTIFELP SSLINSYQTT RKSCENKNIL
DKDKTFRNLL NQHLSYYQNI QNNRYKLNGT DLTSKKLSFT EYQYNIIISN DCDIHYYFSF
VGKNGSGLVQ SFFDIGAWVY GDENVKKIKV LSFFYLLQCL FDYQTKNTHN SVDIDFPNIL
YYLKKFYYSS LVDYGLNGMD SSSKIFNYDL NNSYSFIKIG FLIYNILDLY KPNIIPDQTL
YYDSDLIVML LENSSNKFLC FRKQYYSDLD KTKLKLTPEN IVPQNNDNDN SIILLPLLII
KDDITSFHFF DYNLKDSIKT IEDFNNEKEC LLYYLQNIQK NPSNANSLVL INLNLFEENE
STDNESFLFF DIFYLIKQLH GLSTIIDSWD NFISSLSKPI SLVSNYIQTN LKKILDDPLS
IDILYNDESM SHFKPFIYDK IKEIKKNVWL IRDKNNNNYI RKLSGYIKSK FKEVEKYGFE
FIDDVSISNP YLKIAVENGW PISFLSSHFK RDNSNLFDYL FNKELIILEL LKEKGVDGIS
QLESYFVENN IIYILTKYHG DYSNLEEINE LNQEDLFEIL VQMSDKLKIL ESLQIYHRDI
KPENILFKRE IVNGNIQSKV CLIDFSISDF GFILKTNESG SKMYQAPEIY QEEYRSKEND
ITNQHYKLDI YSLGFTLSHL MKKFNCNPPS LVQIVKKMIK HKAFLLKQPT L
