ID   KARG_LIOJA              Reviewed;         349 AA.
AC   O15990;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Arginine kinase;
DE            Short=AK;
DE            EC=2.7.3.3;
OS   Liolophura japonica (Chiton) (Acanthopleura japonica).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Polyplacophora;
OC   Neoloricata; Chitonida; Chitonina; Chitonidae; Acanthopleurinae;
OC   Liolophura.
OX   NCBI_TaxID=13599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9217008; DOI=10.1016/s0167-4838(97)00066-6;
RA   Suzuki T., Ban T., Furukohri T.;
RT   "Evolution of phosphagen kinase V. cDNA-derived amino acid sequences of two
RT   molluscan arginine kinases from the chiton Liolophura japonica and the
RT   turbanshell Battilus cornutus.";
RL   Biochim. Biophys. Acta 1340:1-6(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine;
CC         Xref=Rhea:RHEA:22940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:32682, ChEBI:CHEBI:58477, ChEBI:CHEBI:456216; EC=2.7.3.3;
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; AB008012; BAA22871.1; -; mRNA.
DR   AlphaFoldDB; O15990; -.
DR   SMR; O15990; -.
DR   GO; GO:0004054; F:arginine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR   GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.135.10; -; 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; PTHR11547; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF48034; SSF48034; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..349
FT                   /note="Arginine kinase"
FT                   /id="PRO_0000212001"
FT   DOMAIN          3..85
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          113..349
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         58..62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
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         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         302..307
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   349 AA;  39102 MW;  2D39B32035621CFE CRC64;
     MADLAELWEK VSSNKDSKSL LKKHLTKEVY EKLKDKKTKF GGTLADCIRS GAKNLDSGVG
     VYASDPEAYT VFQDLLGPVI LDYHKITELK HPACDFGDLS NLGFGDFDPS GDWIVSTRVR
     VGRSHASFGF PPTLNKEQRV EMQRVTQGAL EGLTGELKGK YYPLEGMTPD VQKQLTEDHF
     LFNDSDRFLK AASGYDDWPT GRGIFFNDNK TFLVWVNEED HIRIISMQKG GDLAAVYKRL
     VGGIKELEKK LEFARLPNLG YLTFCPSNLG TTLRASVHIK IPKVAKKPEF KEICDKLNLQ
     ARGIHGEHTE SVGGVYDISN KRRMGLSEIE AIQEMRKGVE EIIKLEKAA