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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
 
 
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