ID   E0W485_PEDHC            Unreviewed;       356 AA.
AC   E0W485;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230};
DE            EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230};
GN   Name=8239840 {ECO:0000313|EnsemblMetazoa:PHUM616180-PA};
GN   ORFNames=Phum_PHUM616180 {ECO:0000313|EMBL:EEB20441.1};
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC   Pediculus.
OX   NCBI_TaxID=121224;
RN   [1] {ECO:0000313|EMBL:EEB20441.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB20441.1};
RA   Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA   Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA   Amedeo P., Strausberg R.;
RT   "Annotation of Pediculus humanus corporis strain USDA.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB20441.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB20441.1};
RG   The Human Body Louse Genome Consortium;
RA   Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT   "The genome of the human body louse.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:PHUM616180-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM616180-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   EMBL; AAZO01007533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS235886; EEB20441.1; -; Genomic_DNA.
DR   RefSeq; XP_002433179.1; XM_002433134.1.
DR   AlphaFoldDB; E0W485; -.
DR   STRING; 121224.E0W485; -.
DR   EnsemblMetazoa; PHUM616180-RA; PHUM616180-PA; PHUM616180.
DR   GeneID; 8239840; -.
DR   KEGG; phu:Phum_PHUM616180; -.
DR   CTD; 8239840; -.
DR   VEuPathDB; VectorBase:PHUM616180; -.
DR   eggNOG; KOG3581; Eukaryota.
DR   HOGENOM; CLU_019868_0_0_1; -.
DR   InParanoid; E0W485; -.
DR   OMA; ACPTNVG; -.
DR   OrthoDB; 35839at2759; -.
DR   Proteomes; UP000009046; Unassembled WGS sequence.
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:UP000009046};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00843}.
FT   DOMAIN          8..90
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51509"
FT   DOMAIN          118..355
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51510"
FT   BINDING         121..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         279..283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         308..313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ   SEQUENCE   356 AA;  40093 MW;  7F36B1F1EE0BBEA0 CRC64;
     MVEPAVLEKL EAAWKKLCAT ESKSLLKKYL TQEIFDKLKT KKTSFNSSLL DVIQSGVENP
     DSGVGIYAPD AESYSVFADL FDPIIEDYHG GFKKTDKHPP KDWGDVNSLG NLDPTSEFVI
     STRVRCGRSM EGYPFNPCLT EAQYKEMEEK VSSTLSALTG ELKGSFYPLT GMSKEVQQKL
     IDDHFLFKEG DRFLQAANAC RFWPTGRGIY HNDDKTFLVW CNEEDHLRLI SMQPGGDLGA
     VYRRLVSAVN DVEKRIPFSH HDRLGFLTFC PTNLGTTVRA SVHIKLPKLA ANRAKLEEVA
     GKFNLQVRGT RGEHTEAEGG VYDISNKRRM GLTEYEAVKE MHDGIAELIK IERELK
//