KARG_CHIOP
ID KARG_CHIOP Reviewed; 223 AA.
AC P86699;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Arginine kinase {ECO:0000303|PubMed:21059421};
DE Short=AK {ECO:0000303|PubMed:21059421};
DE EC=2.7.3.3 {ECO:0000250|UniProtKB:P51541};
DE AltName: Allergen=Chi o 3;
DE Flags: Fragments;
OS Chionoecetes opilio (Crab-beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Majoidea; Majidae; Chionoecetes.
OX NCBI_TaxID=41210;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND ALLERGEN.
RC TISSUE=Muscle {ECO:0000269|PubMed:21059421};
RX PubMed=21059421; DOI=10.1016/j.jprot.2010.10.010;
RA Abdel Rahman A.M., Kamath S.D., Lopata A.L., Robinson J.J., Helleur R.J.;
RT "Biomolecular characterization of allergenic proteins in snow crab
RT (Chionoecetes opilio) and de novo sequencing of the second allergen
RT arginine kinase using tandem mass spectrometry.";
RL J. Proteomics 74:231-241(2011).
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 Evidence={ECO:0000250|UniProtKB:P51541};
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:21059421}.
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 Allergome; 9057; Chi o 2.
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 InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PE 1: Evidence at protein level;
KW Allergen; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..223
FT /note="Arginine kinase"
FT /id="PRO_0000410433"
FT DOMAIN 9..?
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 56..222
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 59..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51541"
FT BINDING 150..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 175..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51541"
FT NON_CONS 24..25
FT /evidence="ECO:0000303|PubMed:21059421"
FT NON_CONS 31..32
FT /evidence="ECO:0000303|PubMed:21059421"
FT NON_CONS 63..64
FT /evidence="ECO:0000303|PubMed:21059421"
FT NON_CONS 99..100
FT /evidence="ECO:0000303|PubMed:21059421"
FT NON_CONS 159..160
FT /evidence="ECO:0000303|PubMed:21059421"
SQ SEQUENCE 223 AA; 25316 MW; 8E10F265DF731B93 CRC64;
MADAATISKL EEGFKKLQGA TDCKDVFDQL KQTDKHPNKD FGDVNQFVNV DPDGKFVIST
RVRLIDDHFL FKEGDRFLQA ANACRYWPSG RGIFHNDKKI ISMQMGGDLG QVYRRLVSAV
NEIEKRVPFS HHDRLGFLTF CPTNLGTTVR ASVHIKLPKX EKLEEVAGKY SLQVRGTRGE
HTEAEGGVYD ISNKRRMGLT EFQAVKEMQD GILELIKIEK EMQ
