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P11917 (KTRC_AREMA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Taurocyamine kinase

EC=2.7.3.4
OrganismArenicola marina (Lugworm) (Lumbricus marinus)
Taxonomic identifier6344 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaAnnelidaPolychaetaScolecidaCapitellidaArenicolidaeArenicola

Protein attributes

Sequence length16 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + taurocyamine = ADP + N-phosphotaurocyamine.

Sequence similarities

Belongs to the ATP:guanido phosphotransferase family.

Contains 1 phosphagen kinase C-terminal domain.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

taurocyamine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›16›16Taurocyamine kinase
PRO_0000211987

Regions

Domain‹1 – ›16›16Phosphagen kinase C-terminal

Experimental info

Non-terminal residue11
Non-terminal residue161

Sequences

Sequence LengthMass (Da)Tools
P11917 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: CF05E7326D427E94

FASTA161,636
        10 
LGYLGTCPTN IGTGLR 

« Hide

References

[1]"Comparative structural studies of the active site of ATP: guanidine phosphotransferases. The essential cysteine tryptic peptide of taurocyamine kinase from Arenicola marina."
Brevet A., Zeitoun Y., Pradel L.A.
Biochim. Biophys. Acta 393:1-9(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRA11488.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.590.10. 1 hit.
InterProIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamPF00217. ATP-gua_Ptrans. 1 hit.
[Graphical view]
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKTRC_AREMA
AccessionPrimary (citable) accession number: P11917
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 16, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families