ID   KARG_HALMK              Reviewed;         358 AA.
AC   P51544;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Arginine kinase;
DE            Short=AK;
DE            EC=2.7.3.3;
OS   Haliotis madaka (Giant abalone) (Nordotis madaka).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX   NCBI_TaxID=81897;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=8145248; DOI=10.1006/jmbi.1994.1237;
RA   Suzuki T., Furukohri T.;
RT   "Evolution of phosphagen kinase. Primary structure of glycocyamine kinase
RT   and arginine kinase from invertebrates.";
RL   J. Mol. Biol. 237:353-357(1994).
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   -!- SUBUNIT: Monomer.
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; D26104; BAA05100.1; -; mRNA.
DR   PIR; S46407; S46407.
DR   AlphaFoldDB; P51544; -.
DR   SMR; P51544; -.
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..358
FT                   /note="Arginine kinase"
FT                   /id="PRO_0000212002"
FT   DOMAIN          6..88
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          116..353
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         61..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         119..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         278..282
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         306..311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   358 AA;  39814 MW;  35ABACE7EC8A2D1E CRC64;
     MLAMASVEEL WAKLDGAADC KSLLKNNLTK ERYEALKDKK TKFGGTLADC IRSGCLNLDS
     GVGIYACDPD AYTVFADVLD AVIKEYHKVP ELKHPEPEMG DLDKLNFGDL DPSGEYIVST
     RVRVGRSHDS YGFPPVLTKQ ERLKMEEDTK AAFEKFSGEL AGKYFPLEGM SKEDQKQMTE
     DHFLFKDDDR FLRDAGGYND WCSGRGIFFN TAKNFLVWVN EEDHLRLISM QKGGDLAAVY
     KRLVVAINTM TASGLSFAKR DGLGYLTFCP SNLGTALRAS VHMKIPNLAA SPEFKSFCDN
     LNIQARGIHG EHTESVGGVY DLSNKRRLGL TEYQAVEEMR VGVEACLAKE KELAAAKK