Reviewed, UniProtKB/Swiss-Prot O61122 (SVKA_DICDI)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase svkA
    EC=2.7.11.1
Alternative name(s):
    Severin kinase A

Gene names

Name:	svkA
ORF Names:	DDB_0191176

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in regulation of actin cytoskeleton organization during cell motility; F-actin fragmenting and capping protein allowing dynamic rearrangements of the actin cytoskeleton. Also part of a regulatory pathway from the centrosome to the midzone, thus regulating the completion of cell division.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium. Manganese.
Enzyme regulation	Phosphorylation of severin is reduced with high concentrations of calcium ions.
Subcellular location	Cytoplasm › cytoskeleton › actin patch.
Post-translational modification	Autophosphorylated.
Miscellaneous	Amoeba lacking svkA exhibit drastic defects in cytokinesis (impairs cell division and leads to multinucleated cells, frequently fails to severe the final connecting bridge between the 2 daughter cells), development and directed slug movement.
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Contains 1 protein kinase domain.
Biophysicochemical properties	pH dependence: Optimum pH is 7.5.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Actin-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	positive regulation of cell division Ref.1 Inferred from mutant phenotype. Source: UniProtKB protein amino acid phosphorylation Ref.1 Inferred from mutant phenotype. Source: UniProtKB regulation of actin cytoskeleton organization and biogenesis Ref.1 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	actin cytoskeleton Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	protein serine/threonine kinase activity Ref.1 Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 478	478	Serine/threonine-protein kinase svkA
Regions
	Domain	12 – 262	251	Protein kinase
	Nucleotide binding	18 – 26	9	ATP By similarity
	Compositional bias	323 – 356	34	Gln-rich
	Compositional bias	349 – 406	58	Thr-rich
Sites
	Active site	132	1	Proton acceptor By similarity
	Binding site	41	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O61122-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: B4935BE0812CDC32	FASTA	478	52,616
	10 20 30 40 50 60 MASKKGDPEE LYVRQEKIGK GSFGEVFKGI NKKTNETIAI KTIDLEDAED EIEDIQQEIN 70 80 90 100 110 120 VLSQCESPFV TKYFGSFLKG SKLWIIMEYL AGGSVLDLMK PGPFDEGYIA IILRELLKGL 130 140 150 160 170 180 EYLHSEGKIH RDIKAANVLL SASGDVKLAD FGVSGQLTDQ MTKRNTFVGT PFWMAPEVIK 190 200 210 220 230 240 QTGYDSKADI WSMGITALEM AKGEPPRADL HPMRALFLIP KDPPPTLEGN FSKGFKEFCA 250 260 270 280 290 300 LCLNKDPNQR PTAKDLLKHK FIKAAKKTSS LTDLIERRQK WLQLNGNNAD DENDDLDRDA 310 320 330 340 350 360 KSNEEDFGWE FPTIKQKSPV AVQEQQQTPQ KPTVVSTPIK EQQQQQQPTP VTTPQQPVTT 370 380 390 400 410 420 TTTTPTTETK VRSLSNSSQT TPVKTTVAAT TAPATTPASN APTSTTPNGA AVTQQQAPRA 430 440 450 460 470 SALTSVIYPV LSKLLKNTSD ENVINALAQL KMAFDNAEKA KPGITHSLIA QIIETLKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and cloning of a Dictyostelium Ste20-like protein kinase that phosphorylates the actin-binding protein severin." Eichinger L., Baehler M., Dietz M., Eckerskorn C., Schleicher M. J. Biol. Chem. 273:12952-12959(1998) [PubMed: 9582328] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-26; 319-329; 341-351 AND 386-403, FUNCTION, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION. Strain: AX2.
[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]	"The Ste20-like kinase SvkA of Dictyostelium discoideum is essential for late stages of cytokinesis." Rohlfs M., Arasada R., Batsios P., Janzen J., Schleicher M. J. Cell Sci. 120:4345-4354(2007) [PubMed: 18042625] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF059534 mRNA. Translation: AAC24522.1. AAFI02000085 Genomic DNA. Translation: EAL64204.1.
RefSeq	XP_637749.1.
3D structure databases
HSSP	HSSP built from PDB template 1F3M based on UniProtKB Q13153.
ModBase	Search...
Genome annotation databases
GeneID	3389326.
KEGG	ddi:DDB_0191176.
Organism-specific databases
dictyBase	DDB0191176. svkA.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR002290. Ser_thr_pkinase. IPR001245. Tyr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. [Graphical view]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

SVKA_DICDI

Accession

Primary (citable) accession number: O61122
Secondary accession number(s): Q54LT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	August 1, 1998
Last modified:	July 22, 2008
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)