Home | Contact

Phosphagen (guanidino) kinases, including creatine kinase (CK), arginine kinase (AK), taurocyamine kinase (TK), lombricine kinase (LK), glycocyamine kinase (GK), and hypotaurocyamine kinase (HTK), are enzymes that catalyze the reversible transfer of the γ-phosphoryl group of adenosine triphosphate (ATP) to naturally occuring guanidino compounds such as creatine, arginine, yelding adenosine diphosphate (ADP) and a phosphorylated guanidine typically referred to as phosphagen (phosphocreatine, phosphoarginine and etc). Members of this enzyme family play a key role in animals as ATP-buffering systems in cells that display high and variable rates of ATP turnover. Phosphagen kinases have been found in all animal species and in some protozoa, such as trypanosomes, choanoflagellates, and the ciliates, Paramecium tetraurelia, Paramecium caudatum, and Tetrahymena. Eukaryotic phosphagen kinases consist of a small, ~100-residue, α-helical N-terminal domain and a larger, 250+-residue, C-terminal α/β saddle domain in which many key residues involved in catalysis are found (see <PDB:3L2E>). The N-terminal domain undergoes significant conformational movements during catalysis, closing down on the catalytic pocket. It is involved in dimer formation. Bacterial phosphagen kinases have the large C-terminal domain seen in eukaryotic phosphagen kinases but lack the N-terminal domain [1,2,3,4].

A cysteine residue is implicated in the catalytic activity of these enzymes. The region around this active site residue is highly conserved and can be used as a signature pattern. We also developed two profiles, which cover respectively the entire phosphagen kinase N- and C-terminal domains.

December 2010 / Text revised; profiles added.

PROSITE methods (with tools and information) covered by this documentation:

PHOSPHAGEN_KINASE_C, PS51510; Phosphagen kinase C-terminal domain profile  (MATRIX)

Sequences known to belong to this class detected by the profile: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Domain architecture view of Swiss-Prot proteins matching PS51510 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS51510 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS51510 • Scan Swiss-Prot/TrEMBL entries against PS51510 • view ligand binding statistics

Matching PDB structures: 1BG0 1CRK 1G0W 1I0E ... [ALL]

PHOSPHAGEN_KINASE_N, PS51509; Phosphagen kinase N-terminal domain profile  (MATRIX)

Sequences known to belong to this class detected by the profile: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Domain architecture view of Swiss-Prot proteins matching PS51509 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS51509 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS51509 • Scan Swiss-Prot/TrEMBL entries against PS51509 • view ligand binding statistics

Matching PDB structures: 1BG0 1CRK 1G0W 1I0E ... [ALL]

PHOSPHAGEN_KINASE, PS00112; Phosphagen kinase active site signature  (PATTERN)

Consensus pattern: C-P-x(0,1)-[ST]-N-[ILV]-G-T C is the active site residue Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00112 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00112 • Scan Swiss-Prot/TrEMBL entries against PS00112 • view ligand binding statistics

Matching PDB structures: 1BG0 1CRK 1G0W 1I0E ... [ALL]

1	Authors	Tanaka K., Uda K., Shimada M., Takahashi K., Gamou S., Ellington W.R., Suzuki T.
	Title	Evolution of the cytoplasmic and mitochondrial phosphagen kinases unique to annelid groups.
	Source	J. Mol. Evol. 65:616-625(2007).
	PubMed ID	17932618
	DOI	10.1007/s00239-007-9046-4

2	Authors	Conejo M., Bertin M., Pomponi S.A., Ellington W.R.
	Title	The early evolution of the phosphagen kinases--insights from choanoflagellate and poriferan arginine kinases.
	Source	J. Mol. Evol. 66:11-20(2008).
	PubMed ID	18064398
	DOI	10.1007/s00239-007-9058-0

3	Authors	Andrews L.D., Graham J., Snider M.J., Fraga D.
	Title	Characterization of a novel bacterial arginine kinase from Desulfotalea psychrophila.
	Source	Comp. Biochem. Physiol. 150:312-319(2008).
	PubMed ID	18499493
	DOI	10.1016/j.cbpb.2008.03.017

4	Authors	Lim K., Pullalarevu S., Surabian K.T., Howard A., Suzuki T., Moult J., Herzberg O.
	Title	Structural basis for the mechanism and substrate specificity of glycocyamine kinase, a phosphagen kinase family member.
	Source	Biochemistry 49:2031-2041(2010).
	PubMed ID	20121101
	DOI	10.1021/bi9020988

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to

Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)

SIB Swiss Institute of Bioinformatics | Disclaimer