ID   KLOM_EISFE              Reviewed;         371 AA.
AC   O15991;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   13-SEP-2023, entry version 73.
DE   RecName: Full=Lombricine kinase;
DE            Short=LK;
DE            EC=2.7.3.5;
OS   Eisenia fetida (Red wiggler worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Oligochaeta; Crassiclitellata; Lumbricina; Lumbricidae; Lumbricinae;
OC   Eisenia.
OX   NCBI_TaxID=6396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=9434106; DOI=10.1016/s0167-4838(97)00128-3;
RA   Suzuki T., Kawasaki Y., Furukohri T., Ellington W.R.;
RT   "Evolution of phosphagen kinase. VI. Isolation, characterization and cDNA-
RT   derived amino acid sequence of lombricine kinase from the earthworm Eisenia
RT   foetida, and identification of a possible candidate for the guanidine
RT   substrate recognition site.";
RL   Biochim. Biophys. Acta 1343:152-159(1997).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC       ProRule:PRU00843}.
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DR   EMBL; AB008013; BAA22872.1; -; mRNA.
DR   AlphaFoldDB; O15991; -.
DR   SMR; O15991; -.
DR   KEGG; ag:BAA22872; -.
DR   BioCyc; MetaCyc:MONOMER-18469; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR   GO; GO:0050059; F:lombricine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00716; creatine_kinase_like; 1.
DR   Gene3D; 1.10.135.10; ATP:guanido phosphotransferase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR   InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1.
DR   PANTHER; PTHR11547:SF57; MITOCHONDRIAL CREATINE KINASE; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   SUPFAM; SSF48034; Guanido kinase N-terminal domain; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..371
FT                   /note="Lombricine kinase"
FT                   /id="PRO_0000211985"
FT   DOMAIN          1..86
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          113..355
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         116..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         308..313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         323
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
SQ   SEQUENCE   371 AA;  41781 MW;  8F8409D72F92ACB9 CRC64;
     MPKFTARQNF PDYKSNGHKC MVGRHLTEDM YERLYELRTP NGVSIDKCIQ PSVDNTGRII
     GLVAGDPESY EVFKELFDAV INEKHGGFGP TDKHPPPDLN ANALVGGQFD PKYVKSARIR
     TGRSVKGFCL PPSISRAERR EVERIIVDAL AGLEGDLAGV YYPLKKMTPE QEKQLIADHF
     LFQKPTGHLM VNSGAVRDWP DARGIWHNKD KTFLIWINEE DQVRIIAMQH GGDVKAVFER
     FSRGLTQIEG LMKKHGHEFA WSERLGYICT CPSNLGTGLR ASVHLQLHKL SKHPKFEEII
     LAFHLQKRGT GGEHTEAVDD VYDISNRARL KKSEREFVQL LIDGVGKLIE YEKLLEAGKS
     IDDVLPASLK G
//