ID D9D6G3_9NEOP Unreviewed; 186 AA.
AC D9D6G3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 22-FEB-2023, entry version 30.
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:ADJ53642.1};
OS Gracillariidae gen. sp. 7 ex Elaeocarpus sylvestris.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tineoidea;
OC Gracillariidae.
OX NCBI_TaxID=796983 {ECO:0000313|EMBL:ADJ53642.1};
RN [1] {ECO:0000313|EMBL:ADJ53642.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G42AK {ECO:0000313|EMBL:ADJ53642.1};
RX PubMed=20427340; DOI=10.1098/rspb.2010.0355;
RA Kawakita A., Okamoto T., Goto R., Kato M.;
RT "Mutualism favours higher host specificity than does antagonism in plant-
RT herbivore interaction.";
RL Proc. R. Soc. B 277:2765-2774(2010).
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU00843, ECO:0000256|RuleBase:RU000505}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00843}.
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DR EMBL; GU816533; ADJ53642.1; -; Genomic_DNA.
DR AlphaFoldDB; D9D6G3; -.
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; 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; 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 PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 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..186
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 4..8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 162..166
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:ADJ53642.1"
FT NON_TER 186
FT /evidence="ECO:0000313|EMBL:ADJ53642.1"
SQ SEQUENCE 186 AA; 21298 MW; CFCB617754537F12 CRC64;
FIVSTRVRCG RSMEGYPFNP CLTEAQYKEM EEKVSTTLSG LEGELKGTFY PLTGMSKETQ
QQLIDDHFLF KEGDRFLQAA NACRFWPSGR GIYHNENKTF LVWCNEEDHL RLISMQMGGD
LKQVYKRLVN AVNDIEKRVP FSHHDRLGFL TFCPTNLGTT VRASVHIKLP KLAADKAKLE
EVASKY
//
