PK4_DICDI
ID PK4_DICDI Reviewed; 992 AA.
AC P34103; Q54Q86;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein kinase 4;
DE EC=2.7.11.1;
DE Flags: Fragment;
GN Name=pkgD; ORFNames=DDB_G0284029;
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 807-835.
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; AAFI02000060; EAL65426.1; -; Genomic_DNA.
DR EMBL; M59747; AAA33189.1; -; Genomic_DNA.
DR PIR; D38578; D38578.
DR RefSeq; XP_638782.1; XM_633690.1.
DR AlphaFoldDB; P34103; -.
DR SMR; P34103; -.
DR STRING; 44689.DDB0218566; -.
DR PaxDb; P34103; -.
DR EnsemblProtists; EAL65426; EAL65426; DDB_G0284029.
DR GeneID; 8624381; -.
DR KEGG; ddi:DDB_G0284029; -.
DR dictyBase; DDB_G0284029; pkgD.
DR eggNOG; KOG0616; Eukaryota.
DR HOGENOM; CLU_301413_0_0_1; -.
DR InParanoid; P34103; -.
DR OMA; MGHIRLT; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR000961; AGC-kinase_C.
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; PS51285; AGC_KINASE_CTER; 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..992
FT /note="Protein kinase 4"
FT /id="PRO_0000086549"
FT DOMAIN 679..934
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 935..992
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 802
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 685..693
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 708
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 833
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 992 AA; 115041 MW; FF7BCFD629677215 CRC64;
QQQQQQQQQQ QQQQQQQHQK TSPSTSFVDY NNINNSNGNN INGTTSTCNS TSSSKSNSKE
IYNENNNNNN NNNNNSFTNV HNNNNNNNNN RKRRNSHISY DTPDSNNIDN NIESNDTESG
FRKNSKKSTD NNNNNNNNNN NNNNNNNNNN NNNNNNNSCN INGNINNGNS NNINNNNCSN
IDSTLADVSK HQYTNQHQQQ QNIQQQQQQQ QQKNQQQQQQ QQQQQQQNNQ QQQQNNQQQQ
QNNQQQQQHQ QQNSQQQQNN QHQQQLQQQQ YQQKHYNNNN NNNNNNQPQT SNQNIQHSQG
LNYNQNQNQN QNQEAPIVVN SLILRSIGMM TSKISKDFEE LTTFMKSSCP MLLRFSGVEN
SYHILEKLNN IITQSLEGLP KTPQCSQPPF NQLIPLSNTT TLTPNNYNNN NNNSNNNNNS
NNNNNNNSNN NNSNNNNSNN SNNNNNNSNN NNSNNNNSNN NNSNNNNNNS NNNNSNNNNS
SNNNNNYSGF NDQQQQQQQQ QQQQQQQQQQ QQQQQQQQHQ QQKHQQTQHS QQHQQQYQQH
IQQNNQYQQN QNITQSSQIP QFKSNNIQSL IHNNQQHYTQ NNLVNNNNNT NNNNNNNNYN
NKTYYQPSVH ENQYMASAIA PIHNHQSSPN PFYQQKLTIP QQTNNQSTRI SAQFIIQNIN
NQQIQGTYIN FNSCKLSDFK LFDLLGSGSF AKVRLCQHIP SERLFCMKIL NQNKIIRLRQ
EVHVCNEKQV LMLTDNPFIV KLYSTFKDDR YLYFLQEFIP GGELFDYIRA NGSLSLYVTQ
IYAAEIVLAL EYLHNQDIIY RDLKPENLLI DQYGHIKLTD FGFAKRITEN TKSMCGTPEY
IAPEILSGHG HGKSADWWSL GILIYEMLVG VPPFVSEGSQ NDIFRLIREA RIQVPPEVDQ
VARDLIEKLV VTDVEKRLGS LEGGIEDIKN HPFFGAINWN SIQNRESAPL KPRIRPLKHH
LMDERDEEDR ISANFIKPDL LERRKNEFFS NF
