ID   KARG_ERISI              Reviewed;         357 AA.
AC   Q9NH48;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, 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   Eriocheir sinensis (Chinese mitten crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Grapsoidea; Varunidae; Eriocheir.
OX   NCBI_TaxID=95602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gill;
RA   Weihrauch D., Towle D.W.;
RT   "Arginine kinase mRNA expression analysis in different haline species of
RT   crustaceans.";
RL   Submitted (FEB-2000) 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; AF233356; AAF43437.1; -; mRNA.
DR   AlphaFoldDB; Q9NH48; -.
DR   SMR; Q9NH48; -.
DR   BRENDA; 2.7.3.3; 10211.
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   Acetylation; ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..357
FT                   /note="Arginine kinase"
FT                   /id="PRO_0000211998"
FT   DOMAIN          9..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"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  40339 MW;  5ECCCE685D562BF1 CRC64;
     MADAATIAKL DEGFKKLEAA TDCKSLLKKY LTKDVFEQLK AKKTKLGATL LDVIQSGVEN
     LDSGVGVYAP DAEAYTLFSP LFDPIIEDYH KGFKQTDKHP NKDFGDVTQF VNVDPDGKFV
     ISTRVRCGRS MEGYPFNPCL TEAQYKEMES KVSSTLSNLE GELKGTYFPL TGMTKEVQQK
     LIDDHFLFKE GDRFLQAANA CRYWPAGRGI YHNDNKTFLV WCNEEDHLRI ISMQMGGDLG
     QVYRRLVSAV NEIEKRVPFS HHDRLGFLTF CPTNLGTTVR ASVHIKLPKL AANREKLEEV
     AGRYSLQVRG TRGEHTEAEG GIYDISNKRR MGLTEFQAVK EMQDGILELI KIEKEMQ