KARG_SCYSE
ID KARG_SCYSE Reviewed; 356 AA.
AC C9EIP1;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Arginine kinase Scy s 2 {ECO:0000303|PubMed:21432856};
DE Short=AK {ECO:0000303|PubMed:21432856};
DE EC=2.7.3.3 {ECO:0000269|PubMed:21432856};
DE AltName: Allergen=Scy s 2 {ECO:0000305};
OS Scylla serrata (Mud crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Portunoidea; Portunidae; Scylla.
OX NCBI_TaxID=6761;
RN [1] {ECO:0000312|EMBL:ACV96855.1}
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND ALLERGEN.
RC TISSUE=Muscle {ECO:0000303|PubMed:21432856};
RX PubMed=21432856; DOI=10.1002/jsfa.4322;
RA Shen Y., Cao M.J., Cai Q.F., Su W.J., Yu H.L., Ruan W.W., Liu G.M.;
RT "Purification, cloning, expression and immunological analysis of Scylla
RT serrata arginine kinase, the crab allergen.";
RL J. Sci. Food Agric. 91:1326-1335(2011).
CC -!- FUNCTION: Catalyzes the reversible transfer of high energy ATP gamma-
CC phosphate group to L-arginine. {ECO:0000269|PubMed:21432856}.
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:0000269|PubMed:21432856};
CC -!- TISSUE SPECIFICITY: Muscle (at protein level).
CC {ECO:0000269|PubMed:21432856}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in all 4
CC patients tested allergic to crustaceans. {ECO:0000269|PubMed:21432856}.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00843, ECO:0000255|RuleBase:RU000505,
CC ECO:0000305}.
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DR EMBL; GQ851626; ACV96855.1; -; mRNA.
DR AlphaFoldDB; C9EIP1; -.
DR SMR; C9EIP1; -.
DR Allergome; 795; Scy s 2.
DR GO; GO:0004054; F:arginine kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
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; IDA:UniProtKB.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT CHAIN 2..356
FT /note="Arginine kinase Scy s 2"
FT /id="PRO_0000447432"
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|UniProtKB:Q004B5"
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|UniProtKB:Q004B5"
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|UniProtKB:Q004B5"
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|UniProtKB:Q004B5"
SQ SEQUENCE 356 AA; 40189 MW; A1554A4AB830FAAC CRC64;
MADAAVIEKL EEGFKKLEAA TDCKSLLKKY LTKSVFDQLK GKKTSLGATL LDVIQSGVEN
LDSGVGVYAP DAEAYTLFAP LFDPIIEDYH KGFKQTDKHP NKDFGDVNQF VNVDPDGKFV
ISTRVRCGRS MEGYPFNPCL TEAQYKEMES KVSSTLSNLE GELKGTYYPL TGMTKDVQQK
LIDDHFLFKE GDRFLQAANA CRYWPTGRGI YHNDNKTFLV WCNEEDHLRI ISMQMGGDLG
QVYRRLVSAV NEIEKRVPFS HHDRLGFLTF CPTNLGTTVR ASVHIKLPKL AANREKLEEV
AGKYSLQVRG TRGEHTEAEG GVYDISNKRR MGLTEFQAVK EMQDGILELI KMEKEM
