ID   KARG_SCHAM              Reviewed;         356 AA.
AC   P91798;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Arginine kinase;
DE            Short=AK;
DE            EC=2.7.3.3;
GN   Name=ARGK;
OS   Schistocerca americana (American grasshopper).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX   NCBI_TaxID=7009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang Y.M.E., Esbensen P., Bentley D.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
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; U77580; AAC47830.1; -; mRNA.
DR   AlphaFoldDB; P91798; -.
DR   SMR; P91798; -.
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..356
FT                   /note="Arginine kinase"
FT                   /id="PRO_0000211994"
FT   DOMAIN          8..91
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          119..356
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         64..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         280..284
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         309..314
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  40016 MW;  CDB7FA1417D25F44 CRC64;
     MVDAAVLEKL EAGFKKLEAS DSKSLLKKYL TREVFDKLKT KKTPSFGSTL LDCIQSGLEN
     HDSGVGIYAP DAEAYTVFAD LFDPIIEDYH GGFKKTDKHP PKNFGDVDTL ANLDPNGEYV
     ISTRVRCGRS MQGYPFNPCL TEAQYKEMEQ KVSTTLSSLE GELKGQFYPL TGMSKEVQQK
     LIDDHFLFKE GDRFLQAANA CRFWPSGRGI YHNDNKTFLV WCNEEDHLRI ISMQPGGDLG
     QVYRRLVHAV NEIEKRIPFS HDDRLGFLTF CPTNLGTTLR ASVHIKLPKL AADRTKLEEV
     AGKFNLQVRG STGEHTEAEG GVYDISNKRR MGLTEYDAVK EMNDGILELI KIEGSL