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Database: UniProt
Entry: G3XDW6_9NEOP
LinkDB: G3XDW6_9NEOP
Original site: G3XDW6_9NEOP 
ID   G3XDW6_9NEOP            Unreviewed;       133 AA.
AC   G3XDW6;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   22-FEB-2023, entry version 34.
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:BAK95900.1};
OS   Inurois kyushuensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC   Geometridae; Alsophilinae; Inurois.
OX   NCBI_TaxID=570123 {ECO:0000313|EMBL:BAK95900.1};
RN   [1] {ECO:0000313|EMBL:BAK95900.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F557_kyushuensis {ECO:0000313|EMBL:BAK95900.1},
RC   F558_kyushuensis {ECO:0000313|EMBL:BAK95901.1}, and F559_kyushuensis
RC   {ECO:0000313|EMBL:BAK95902.1};
RA   Yamamoto S., Beljaev E.A., Sota T.;
RT   "Diversification by repeated shift of reproductive timing in the geometrid
RT   moths of the genus Inurois (Lepidoptera: Geometridae).";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; AB553000; BAK95900.1; -; Genomic_DNA.
DR   EMBL; AB553001; BAK95901.1; -; Genomic_DNA.
DR   EMBL; AB553002; BAK95902.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XDW6; -.
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; 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; 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..11
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51509"
FT   DOMAIN          39..133
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51510"
FT   BINDING         42..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         105
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:BAK95900.1"
FT   NON_TER         133
FT                   /evidence="ECO:0000313|EMBL:BAK95900.1"
SQ   SEQUENCE   133 AA;  15102 MW;  9BC7066F7D3EEF65 CRC64;
     LFDPIIEDYH TGFKSTDKHP AKNWGDVESL GNLDPAGEYV VSTRVRCGRS MEGYPFNPCL
     TEVQYKEMEE KVATTLSGLE GELKGTFYPL TGMSKETQQQ LIDDHFLFKE GDRFLQAANA
     CRFWPSGRGI YHN
//
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