ID J7K3Q2_9HYME Unreviewed; 224 AA.
AC J7K3Q2;
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:AFQ91836.1};
OS Leptanilla sp. GR03.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Leptanillinae; Leptanillini; Leptanilla.
OX NCBI_TaxID=1227759 {ECO:0000313|EMBL:AFQ91836.1};
RN [1] {ECO:0000313|EMBL:AFQ91836.1}
RP NUCLEOTIDE SEQUENCE.
RA Ward P.S., Sumnicht T.P.;
RT "Molecular and morphological evidence for three sympatric species of
RT Leptanilla (Hymenoptera: Formicidae) on the Greek island of Rhodes.";
RL Myrmecol News 17:5-11(2012).
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006798, ECO:0000256|PROSITE-ProRule:PRU00842}.
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; JN967885; AFQ91836.1; -; Genomic_DNA.
DR EMBL; JN967886; AFQ91837.1; -; Genomic_DNA.
DR EMBL; JN967887; AFQ91838.1; -; Genomic_DNA.
DR AlphaFoldDB; J7K3Q2; -.
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; 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 Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF48034; Guanido kinase N-terminal domain; 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..81
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51509"
FT DOMAIN 109..224
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51510"
FT BINDING 112..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 219
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:AFQ91836.1"
FT NON_TER 224
FT /evidence="ECO:0000313|EMBL:AFQ91836.1"
SQ SEQUENCE 224 AA; 25178 MW; C76ED8AA26845C6B CRC64;
LEAGFAKLAA SDSKSLLKKH LSKEVFDQLK TRKTSFGSTL LDVIQSGLEN HDSGVGIYAP
DAEAYTVFAE LFDPIIDDYH GGFKKSDKHP PKDFGDVDSF GNLDPNSEYI VSTRVRCGRS
LEGYPFNPCL TEAQYKEMEE KVSSTLSGLA GELKGTFYPL TGMSKDVQQK LIDDHFLFKE
GDRFLQTANA CRFWPTGRGI FHNDDKTFLV WCNEEDHLRI ISMQ
//
