PK3_DICDI
ID PK3_DICDI Reviewed; 910 AA.
AC P34102; Q54M90;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein kinase 3;
DE Short=PK3;
DE EC=2.7.11.1;
GN Name=pkgC; ORFNames=DDB_G0286125;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 626-666.
RX PubMed=1996312; DOI=10.1073/pnas.88.4.1115;
RA Haribabu B., Dottin R.P.;
RT "Identification of a protein kinase multigene family of Dictyostelium
RT discoideum: molecular cloning and expression of a cDNA encoding a
RT developmentally regulated protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1115-1119(1991).
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. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000085; EAL64355.1; -; Genomic_DNA.
DR EMBL; M59746; AAA33188.1; -; Genomic_DNA.
DR PIR; C38578; C38578.
DR RefSeq; XP_637858.1; XM_632766.1.
DR AlphaFoldDB; P34102; -.
DR SMR; P34102; -.
DR STRING; 44689.DDB0220130; -.
DR PaxDb; P34102; -.
DR EnsemblProtists; EAL64355; EAL64355; DDB_G0286125.
DR GeneID; 8625455; -.
DR KEGG; ddi:DDB_G0286125; -.
DR dictyBase; DDB_G0286125; pkgC.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_319439_0_0_1; -.
DR InParanoid; P34102; -.
DR OMA; FLFMCMD; -.
DR Reactome; R-DDI-166208; mTORC1-mediated signalling.
DR Reactome; R-DDI-198693; AKT phosphorylates targets in the nucleus.
DR PRO; PR:P34102; -.
DR Proteomes; UP000002195; Chromosome 4.
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; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd05123; STKc_AGC; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..910
FT /note="Protein kinase 3"
FT /id="PRO_0000086548"
FT DOMAIN 498..763
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 764..854
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 119..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 621
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 504..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 664
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 910 AA; 99305 MW; 298EE6422EE86BFD CRC64;
MSFKKQTKTP TSWFPGLKKE RDLSHHKERY CTQYDVIKVN AYGKRQQRTL AVSSLGVSNL
NGQSCQWFVR NSDVYSIEQD PTDSHKFSLT FLHRYHFEAE TPEQAKSIIS EFKRLGVGSP
SGGGGGGSGV SSNGSNSTAT SPNTSPIRLY VSDPSNQPTS SSPPPQPPLS ESVGVHRSSP
MLSSSRMISQ LSQSTSENNI SSPTYHPQGL SGSSTSSSSA SGGGGNNNNA NNSTPPNLIA
SSASNSSLYS SSINSSGIIN SSNNNSSISF NNNNNNNNSN LTTTTTTTST FKTPTLPISQ
ASKFNNESES MGLSPLTPNS NSQTALMQHI NAMPNTPNSN STEGSRVWKI RAEELKKQFL
LKKSSKSTQT VATTTPTPIT KADIKIVLDD NKDDKNKDNN IGSGGSGNSS SKINKEKDNP
YINQPSSLPS NNNSNNNNIT KSNSTTTSQT NDKKDVCSST INFDNLEVSS SSDRDLSSSK
SLNKKNKQSI KKLTIDDFEL LKVLGVGSFG RVYLVRRKDT GKFYAMKVLN KKDMLKKKQI
AHTNTEKMVL STMDHPFIVR LHFAFQNEDF LFMCMDYVPG GELFHHLQKA GKFPEELAKF
YIAEVICSLH YLHSNNIIYR DIKPENILLD EEGHIKLTDF GLSKSGITSV VGSKNGGEGG
FATTFCGTPE YLAPEIITGA GHGKAADWWS VGILLFEMLT GRSPFLASNR NDMYKSMIQG
NLRMPMFLSS DAQDLLEKLL VPDPNKRLGS TQGFEEISSH PFFELIPWRM LESKMITPPF
KPTIKEISLP NSNSNSNNNS QQPTNNNLTL SCDPELNAKI NFQRRKSSAA SVYNLDSPFK
NFSWNKEEED GIMGERESIG SISSNNSISS SPTSSSPINN NNSGGSNTAG GHRILTRKST
IGKNLRKGSV
