ID G3XE48_9NEOP Unreviewed; 133 AA.
AC G3XE48;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 22-FEB-2023, entry version 36.
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:BAK95982.1};
OS Inurois viidaleppi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC Geometridae; Alsophilinae; Inurois.
OX NCBI_TaxID=749362 {ECO:0000313|EMBL:BAK95982.1};
RN [1] {ECO:0000313|EMBL:BAK95982.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F1428_viidaleppi {ECO:0000313|EMBL:BAK95982.1},
RC F1429_viidaleppi {ECO:0000313|EMBL:BAK95983.1}, F1430_viidaleppi
RC {ECO:0000313|EMBL:BAK95984.1}, and F1431_viidaleppi
RC {ECO:0000313|EMBL:BAK95985.1};
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; AB553082; BAK95982.1; -; Genomic_DNA.
DR EMBL; AB553083; BAK95983.1; -; Genomic_DNA.
DR EMBL; AB553084; BAK95984.1; -; Genomic_DNA.
DR EMBL; AB553085; BAK95985.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XE48; -.
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:BAK95982.1"
FT NON_TER 133
FT /evidence="ECO:0000313|EMBL:BAK95982.1"
SQ SEQUENCE 133 AA; 15074 MW; 80D59FE47D3EF06A CRC64;
LFDPIIEDYH TGFKSTDKHP AKNWGDVESL GNLDPAGEYV VSTRVRCGRS MEGYPFNPCL
TEAQYKEMEE KVATTLSGLE GELKGTFYPL TGMSKETQQQ LIDDHFLFKE GDRFLQAANA
CRFWPSGRGI YHN
//
