KARG_PLOIN
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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