P34099 (KAPC_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-dependent protein kinase catalytic subunit
EC=2.7.11.11

Alternative name(s):
Dd GPK2
DdPK3

Gene names

Name:	pkaC
Synonyms:	PK2, PK3
ORF Names:	DDB_G0283907

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	648 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for differentiation and fruit morphogenesis.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	In Dictyostelium the holoenzyme is a dimer composed of a regulatory (R) and a catalytic (C) subunit. In the presence of cAMP it dissociates into the active C subunit and an R monomer.
Developmental stage	CAPK activity is low in vegetatively growing amoebae, increases during development of aggregation and reaches a maximum at culmination.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding cAMP
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of sorocarp stalk cell differentiation Inferred from genetic interaction. Source: dictyBase regulation of sporulation resulting in formation of a cellular spore Inferred from mutant phenotype. Source: dictyBase sporulation resulting in formation of a cellular spore Inferred from mutant phenotype. Source: dictyBase
Cellular component	centrosome Traceable author statement. Source: dictyBase cytosol Traceable author statement. Source: dictyBase
Molecular function	ATP binding Inferred by curator. Source: dictyBase cAMP-dependent protein kinase activity Traceable author statement. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 648	648	cAMP-dependent protein kinase catalytic subunit		PRO_0000086068
Regions
	Domain	336 – 590	255	Protein kinase
	Domain	591 – 648	58	AGC-kinase C-terminal
	Nucleotide binding	342 – 350	9	ATP By similarity
	Compositional bias	58 – 64	7	Asn-rich
	Compositional bias	136 – 223	88	Gln-rich
	Compositional bias	233 – 250	18	Thr-rich
Sites
	Active site	459	1	Proton acceptor By similarity
	Binding site	365	1	ATP By similarity
Amino acid modifications
	Modified residue	490	1	Phosphothreonine By similarity
Experimental info
	Sequence conflict	342	1	I → L in M38703. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P34099 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: 20FBC07E4A82142C	FASTA	648	74,458
	10 20 30 40 50 60 MSNSNNNSSS GNHNSTTINN PKVNVYSNIP NSTTYTYGSG GGGTLSGNNT NNNNTNNNNN 70 80 90 100 110 120 NNNNSSGDNK NHSPVTSATD RLTKMDIEEK WDNKNYEKDE REKSPLFHIL ASNLNSFGNF 130 140 150 160 170 180 KVPSTFSLTP PEPNKQQQPQ QQPQQQQPQQ QQPQQQQPQQ QQQQQPQQQQ QPQQQLQQNN 190 200 210 220 230 240 QQQQQQLQQQ QLQQQLQQQQ QQQQQQQQQQ QQKQQKQQQQ QQQHLHQDGI VNTPSTTQTS 250 260 270 280 290 300 TTTTTTTTTT NPHTSGLSLQ HAHSSYTPSN VLHSPTHFQS SLPTRLDTNP ITTPIRQQQQ 310 320 330 340 350 360 SQQQLQQQQL QQIPPPTVNS FFLPPPVNAR ERLKEFKQIR VIGTGTFGKV YLIQNTKDGC 370 380 390 400 410 420 YYAMKCLNKA YVVQLKQVEH LNSEKSILSS IHHPFIVNLY QAFQDEKKLY LLFEYVAGGE 430 440 450 460 470 480 VFTHLRKSMK FSNSTAKFYA AEIVLALEFL HKQNIVYRDL KPENLLIDNQ GHIKITDFGF 490 500 510 520 530 540 AKRVEDRTFT LCGTPEYLAP EIIQSKGHGK AVDWWALGIL IFEMLAGYPP FYDDDTFAIY 550 560 570 580 590 600 NKILAGRITF PLGFDVDAKD LIKRLLTADR TRRLGALKDG ALDVKNHRWF SDINWERLYQ 610 620 630 640 RRDNGPFIPK IQHQGDSSNF EMYDEEEMVE EPPSSNYVDP YAHLFKDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of two genes encoding putative protein kinases regulated during Dictyostelium discoideum development." Buerki E., Anjard C., Scholder J.-C., Reymond C.D. Gene 102:57-65(1991) [PubMed: 1864510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AX3.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"An unusual catalytic subunit for the cAMP-dependent protein kinase of Dictyostelium discoideum." Anjard C., Etchebehere L., Pinaud S., Veron M., Reymond C.D. Biochemistry 32:9532-9538(1993) [PubMed: 8373760] [Abstract] Cited for: CHARACTERIZATION.
[4]	"DdPK3, which plays essential roles during Dictyostelium development, encodes the catalytic subunit of cAMP-dependent protein kinase." Mann S.K.O., Yonemoto W.M., Taylor S.S., Firtel R.A. Proc. Natl. Acad. Sci. U.S.A. 89:10701-10705(1992) [PubMed: 1332055] [Abstract] Cited for: CHARACTERIZATION. Strain: AX3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M38703 Genomic DNA. No translation available. AAFI02000058 Genomic DNA. Translation: EAL65441.1.
PIR	JQ1150.
RefSeq	XP_638835.1. XM_633743.1.
3D structure databases
ProteinModelPortal	P34099.
SMR	P34099. Positions 330-630.
ModBase	Search...
Protein-protein interaction databases
STRING	P34099.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0215408; DDB0215408; DDB_G0283907.
GeneID	8624359.
GenomeReviews	Gene locus pkaC in contig CM000153_GR.
KEGG	ddi:DDB_G0283907.
Organism-specific databases
dictyBase	DDB_G0283907. pkaC.
Phylogenomic databases
eggNOG	KOG0616.
GeneTree	EPrGT00050000001059.
HOGENOM	HBG755340.
OMA	GAYISHI.
PhylomeDB	P34099.
Enzyme and pathway databases
BRENDA	2.7.11.11. 1939.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K04345.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KAPC_DICDI

Accession

Primary (citable) accession number: P34099
Secondary accession number(s): Q54QA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	December 4, 2007
Last modified:	November 16, 2011
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)