ID A0A0R3P2N6_DROPS Unreviewed; 375 AA.
AC A0A0R3P2N6; A0A6I8VJX1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230};
DE EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230};
GN Name=LOC4814030 {ECO:0000313|RefSeq:XP_015042520.1};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_015042520.1};
RN [1] {ECO:0000313|RefSeq:XP_015042520.1}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_015042520.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_015042520.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_015042520.1; XM_015187034.2.
DR AlphaFoldDB; A0A0R3P2N6; -.
DR SMR; A0A0R3P2N6; -.
DR EnsemblMetazoa; FBtr0380310; FBpp0340761; FBgn0076639.
DR GeneID; 4814030; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0076639; Expressed in insect adult head and 2 other cell types or tissues.
DR ExpressionAtlas; A0A0R3P2N6; baseline.
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 CDD; cd07932; arginine_kinase_like; 1.
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 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001819};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00843}.
FT BINDING 141..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 299..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT BINDING 328..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 375 AA; 42170 MW; EAF31ACF4C944ADD CRC64;
MFALWYLTFA VDEIRKQDTM VDAAVLAKLE EGFAKLAASD SKSLLKKYLT KEVFDNLKNK
VTPTFKSTLL DVIQSGLENH DSGVGIYAPD AESYTVFADL FDPIIEDYHG GFKKTDKHPA
SNFGDVKSFG NVDPTNEYVI STRVRCGRSM QGYPFNPCLT EAQYKEMEGK VSTTLSGLDG
ELKGKFYPLT GMEKGVQQQL IDDHFLFKEG DRFLQAANAC RYWPSGRGIY HNDAKTFLVW
CNEEDHLRII SMQQGGDLGQ IYTRLVTAVN EIEKRVPFSH DDRLGFLTFC PTNLGTTIRA
SVHIKVPKLA SNKAKLEEVA AKYNLQVRGT RGEHTEAEGG VYDISNKRRM GLTEYDAVKE
MYDGITELIK LEKSL
//
