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Database: UniProt
Entry: W8BCX7_CERCA
LinkDB: W8BCX7_CERCA
Original site: W8BCX7_CERCA 
ID   W8BCX7_CERCA            Unreviewed;       415 AA.
AC   W8BCX7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   22-FEB-2023, entry version 35.
DE   RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230};
DE            EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230};
GN   Name=KARG {ECO:0000313|EMBL:JAB99130.1};
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB99130.1};
RN   [1] {ECO:0000313|EMBL:JAB99130.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Geib S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB99130.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA   Calla B., Hall B., Hou S., Geib S.M.;
RT   "A genomic perspective to assessing quality of mass-reared SIT flies used
RT   in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT   California.";
RL   BMC Genomics 15:98-98(2014).
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; GAMC01007425; JAB99130.1; -; mRNA.
DR   RefSeq; XP_004526798.1; XM_004526741.2.
DR   AlphaFoldDB; W8BCX7; -.
DR   EnsemblMetazoa; XM_004526741.3; XP_004526798.1; LOC101448504.
DR   GeneID; 101448504; -.
DR   OrthoDB; 35839at2759; -.
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   2: Evidence at transcript level;
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          65..150
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51509"
FT   DOMAIN          178..415
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51510"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         181..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         288
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         339..343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         368..373
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ   SEQUENCE   415 AA;  45659 MW;  2BC8006C6385F2CB CRC64;
     MGGCASKDKK DTVVDGDAAA AATDKAAENG EEAAANTTAE PSATTANGDA INNEGKLNIM
     VDAAVLAKLE DGFAKLAASD SKSLLKKYLT KEVFDNLKNK KTPTFGSTLL DVIQSGLANH
     DSGVGIYAPD AEAYTVFADL FDPIIEDYHG GFKKTDKHPA KDFGDVNSFG NLDPNNEFVI
     STRVRCGRSM EGYPFNPCLS EAQYKEMEEK VSSTLSGLEG ELKGKFYPLT GMEKSVQQQL
     IDDHFLFKEG DRFLQAANAC RYWPSGRGIY HNDNKTFLVW CNEEDHLRII SMQMGGDLGE
     VFRRLTNAVN EIEKRVPFSH DDRLGFLTFC PTNLGTTIRA SVHIKLPKLA ANLAKLEEVA
     GKYNLQVRGT RGEHTEAEGG IYDISNKRRM GLTEYQAVKE MYDGITELIK IEKSM
//
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