ID   KLOM_LUMTE              Reviewed;          15 AA.
AC   P11918;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Lombricine kinase;
DE            Short=LK;
DE            EC=2.7.3.5;
DE   Flags: Fragment;
OS   Lumbricus terrestris (Common earthworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Oligochaeta; Crassiclitellata; Lumbricina; Lumbricidae; Lumbricinae;
OC   Lumbricus.
OX   NCBI_TaxID=6398;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=5128744; DOI=10.1111/j.1432-1033.1971.tb01581.x;
RA   der Terrossian E., Desvages G., Pradel L.A., Kassab R., van Thoai N.;
RT   "Comparative structural studies of the active site of ATP: guanidine
RT   phosphotransferases. The essential cysteine tryptic peptide of lombricine
RT   kinase from Lumbricus terrestris muscle.";
RL   Eur. J. Biochem. 22:585-592(1971).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-lombricine = ADP + H(+) + N-phospho-L-lombricine;
CC         Xref=Rhea:RHEA:23292, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57825, ChEBI:CHEBI:58356, ChEBI:CHEBI:456216; EC=2.7.3.5;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000305}.
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DR   PIR; A08416; A08416.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050059; F:lombricine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           <1..>15
FT                   /note="Lombricine kinase"
FT                   /id="PRO_0000211986"
FT   NON_TER         1
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1565 MW;  2A45FEF6140E90C4 CRC64;
     LGYITCPGSN LGTLR
//