ID J7GS30_9CUCU Unreviewed; 261 AA.
AC J7GS30;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230};
DE EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230};
DE Flags: Fragment;
GN Name=ArgK {ECO:0000313|EMBL:AFP75368.1};
OS Cactopinus rhois.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Cactopinus.
OX NCBI_TaxID=461689 {ECO:0000313|EMBL:AFP75368.1};
RN [1] {ECO:0000313|EMBL:AFP75368.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22852794; DOI=10.1186/1471-2148-12-133;
RA Jordal B.H., Cognato A.I.;
RT "Molecular phylogeny of bark and ambrosia beetles reveals multiple origins
RT of fungus farming during periods of global warming.";
RL BMC Evol. Biol. 12:133-133(2012).
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006798, ECO:0000256|PROSITE-ProRule:PRU00842,
CC ECO:0000256|RuleBase:RU000505}.
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DR EMBL; JX263878; AFP75368.1; -; Genomic_DNA.
DR AlphaFoldDB; J7GS30; -.
DR GO; GO:0004054; F:arginine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; ATP:guanido phosphotransferase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 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:SF38; ARGININE KINASE; 1.
DR PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF48034; Guanido kinase N-terminal domain; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00843};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00843};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00843};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}.
FT DOMAIN 1..21
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 49..261
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 52..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 210..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 239..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFP75368.1"
FT NON_TER 261
FT /evidence="ECO:0000313|EMBL:AFP75368.1"
SQ SEQUENCE 261 AA; 29746 MW; D3D610A7AD5B4C7C CRC64;
DAEAYTVFSD LFDPIIEDYH KGFTKKDKHP PKNWGDVSVF GNLDPAGEYV VSTRVRCGRS
LEGYPFNPCL TEEQYKEMEQ KVSSTLSGLE GELKGTFYPL TGMSKEVQQK LIDDHFLFKE
GDRFLQAANA CRFWPTGRGI YHNENKTFLV WCNEEDHLRI ISMQMGGDLG EVYRRLVTAV
NDIEKRIPFS HHDRLGFLTF CPTNLGTTVR ASVHIKVPKL AANKAKLEEV ASKYNLQVRG
TRGEHTEAEG GIYDISNKRR M
//
