ID   KARG_PENJP              Reviewed;         355 AA.
AC   P51545;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Arginine kinase;
DE            Short=AK;
DE            EC=2.7.3.3;
OS   Penaeus japonicus (Kuruma prawn) (Marsupenaeus japonicus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=27405;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Tail muscle;
RX   PubMed=7765044;
RA   Furukohri T., Okamoto S., Suzuki T.;
RT   "Evolution of phosphagen kinase (III). Amino acid sequence of arginine
RT   kinase from the shrimp Penaeus japonicus.";
RL   Zool. Sci. 11:229-234(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   AlphaFoldDB; P51545; -.
DR   SMR; P51545; -.
DR   PRIDE; P51545; -.
DR   BRENDA; 2.7.3.3; 4590.
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   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..355
FT                   /note="Arginine kinase"
FT                   /id="PRO_0000212004"
FT   DOMAIN          8..90
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          118..355
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         63..67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         121..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         279..283
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         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   355 AA;  39991 MW;  84D53D715721C5F4 CRC64;
     VDAAVLEKLQ AGFKKLEAAT DCKSLLKKYL SKDIFDKLKG QKTSLGATLL DVIQSGVENL
     DSGVGIYAPD AEAYTLFAPL FDPIIEDYHV GFKQTDKHPN KDFGDVSSFV NVDPEGQYVI
     STRVRCGRSM EGYPFNPCLT EAQYKEMQQK VSSTLSSLEG ELKGTYFPLT GMSKEVQQKL
     IDDHFLFKEG DRFLQAANAC RYWPAGRGIY HNDNKTFLVW VNEEDHLRII SMQMGGDLGQ
     VFRRLTSAVN EIEKRIPFSH HDRLGFLTFC PTNLGTTVRA SVHIKLPKLA ANRDKLEEVA
     GKYNLQVRGT RGEHTEAEGG IYDISNKRRM GLTEFQAVKE MQDGILQLIK MEKEM