ID   KTRC_AREMA              Reviewed;          16 AA.
AC   P11917;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Taurocyamine kinase;
DE            EC=2.7.3.4;
DE   Flags: Fragment;
OS   Arenicola marina (Lugworm) (Lumbricus marinus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Arenicolidae; Arenicola.
OX   NCBI_TaxID=6344;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=166684; DOI=10.1016/0005-2795(75)90209-3;
RA   Brevet A., Zeitoun Y., Pradel L.A.;
RT   "Comparative structural studies of the active site of ATP: guanidine
RT   phosphotransferases. The essential cysteine tryptic peptide of taurocyamine
RT   kinase from Arenicola marina.";
RL   Biochim. Biophys. Acta 393:1-9(1975).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + taurocyamine = ADP + H(+) + N-phosphotaurocyamine;
CC         Xref=Rhea:RHEA:22516, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57838, ChEBI:CHEBI:58064, ChEBI:CHEBI:456216; EC=2.7.3.4;
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00843}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A11488; A11488.
DR   AlphaFoldDB; P11917; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050324; F:taurocyamine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           <1..>16
FT                   /note="Taurocyamine kinase"
FT                   /id="PRO_0000211987"
FT   DOMAIN          <1..>16
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   NON_TER         1
FT   NON_TER         16
SQ   SEQUENCE   16 AA;  1636 MW;  CF05E7326D427E94 CRC64;
     LGYLGTCPTN IGTGLR