GenomeNet

Database: UniProt
Entry: T1J6W9_STRMM
LinkDB: T1J6W9_STRMM
Original site: T1J6W9_STRMM 
ID   T1J6W9_STRMM            Unreviewed;       374 AA.
AC   T1J6W9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230};
DE            EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR009398-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR009398-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) 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; JH431896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1J6W9; -.
DR   STRING; 126957.T1J6W9; -.
DR   EnsemblMetazoa; SMAR009398-RA; SMAR009398-PA; SMAR009398.
DR   eggNOG; KOG3581; Eukaryota.
DR   HOGENOM; CLU_019868_0_0_1; -.
DR   OMA; ACPTNVG; -.
DR   OrthoDB; 35839at2759; -.
DR   PhylomeDB; T1J6W9; -.
DR   Proteomes; UP000014500; 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:UP000014500};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00843}.
FT   DOMAIN          27..109
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51509"
FT   DOMAIN          137..374
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51510"
FT   BINDING         140..144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         298..302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         327..332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ   SEQUENCE   374 AA;  41669 MW;  955CFB93F1B245C5 CRC64;
     MNGVAIVITN FITQKRIMSV DDATKTKLEE GFKKLQGAGD CKSLLKKYLT QPVFDDLKTK
     KTAMGATLQD IIQSGVANLD SGVGVYAPDA ESYTLFAGLF NPIIEDYHGG FKSTDKHPAK
     DFGDVSALGD LDPEGAFVIS TRVRCGRSLQ GYPFNPCLTE AQYKEMEEKV SSTLSGLTGE
     LKGTYYPLTG MSKEVQQKLI DDHFLFKEGD RFLQEANACR YWPAGRGIYH NDAKTFLVWC
     NEEDHLRIIS MQMGGNLKEV FARLTNAVNE IEKRLPFSHD DRLGFLTFCP TNLGTTIRAS
     VHIKLPKLAQ NRDKLEEIAS KFNLQVRGTS GEHTESVGGV YDISNKRRMG LTEYQAVKEM
     NDGILEMIKM EKAA
//
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