ID   KARG_PLOIN              Reviewed;         355 AA.
AC   Q95PM9;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Arginine kinase;
DE            Short=AK;
DE            EC=2.7.3.3;
DE   AltName: Allergen=Plo i 1;
GN   Name=ARGK;
OS   Plodia interpunctella (Indianmeal moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC   Pyralidae; Phycitinae; Plodia.
OX   NCBI_TaxID=58824;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11673567; DOI=10.4049/jimmunol.167.9.5470;
RA   Binder M., Mahler V., Hayek B., Sperr W.R., Scholler M., Prozell S.,
RA   Wiedermann G., Valent P., Valenta R., Duchene M.;
RT   "Molecular and immunological characterization of arginine kinase from the
RT   Indianmeal moth, Plodia interpunctella, a novel cross-reactive invertebrate
RT   pan-allergen.";
RL   J. Immunol. 167:5470-5477(2001).
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   -!- ALLERGEN: Causes an allergic reaction in human.
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; AJ315030; CAC85911.1; -; mRNA.
DR   AlphaFoldDB; Q95PM9; -.
DR   SMR; Q95PM9; -.
DR   Allergome; 575; Plo i 1.
DR   Allergome; 8301; Plo i 1.0101.
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   Allergen; ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..355
FT                   /note="Arginine kinase"
FT                   /id="PRO_0000211993"
FT   DOMAIN          6..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;  39879 MW;  6C497931E9A854F7 CRC64;
     MVDAATLEKL EAGFSKLAAS DSKSLLKKYL TREVFDALKN KKTSFGSTLL DSIQSGVENL
     HSGVGIYAPD AEAYVVFADL FDPIIEDYHN GFKKTDKHPP KNWGDVETLG NLDPAGEFVV
     STRVRCGRSM EGYPFNPCLT EAQYKEMEEK VSSTLSGLEG ELKGTFFPLT GMSKETQQQL
     IDDHFLFKEG DRFLQAANAC RFWPSGRGIY HNENKTFLVW CNEEDHLRLI SMQMGGDLKQ
     VYKRLVRGVN DIAKRIPFSH NERLGFLTFC PTNLGTTVRA SVHIKLPKLA ADKAKLEEVA
     SKYHLQVRGT RGEHTEAEGG VYDISNKRRM GLTEYEAVKE MYDGIAELIK IEKSL