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Database: UniProt/TrEMBL
Entry: R1DUA5_EMIHU
LinkDB: R1DUA5_EMIHU
Original site: R1DUA5_EMIHU 
ID   R1DUA5_EMIHU            Unreviewed;       415 AA.
AC   R1DUA5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Putative arginine kinase {ECO:0000313|EMBL:EOD18070.1};
GN   ORFNames=EMIHUDRAFT_196115 {ECO:0000313|EMBL:EOD18070.1};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD18070.1};
RN   [1] {ECO:0000313|EMBL:EOD18070.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD18070.1};
RG   DOE Joint Genome Institute;
RA   Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA   Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA   Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA   Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA   Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA   Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA   Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA   Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA   Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA   Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA   Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA   Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA   Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT   "Genome variability drives Emilianias global distribution.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000013827}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX   PubMed=23760476; DOI=10.1038/nature12221;
RA   Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA   Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA   Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA   Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA   Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA   Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA   Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA   Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA   Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA   Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA   Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA   Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA   Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA   van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA   Wurch L.L.;
RT   "Pan genome of the phytoplankton Emiliania underpins its global
RT   distribution.";
RL   Nature 499:209-213(2013).
RN   [3] {ECO:0000313|EnsemblProtists:EOD18070}
RP   IDENTIFICATION.
RG   EnsemblProtists;
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   EMBL; KB866472; EOD18070.1; -; Genomic_DNA.
DR   RefSeq; XP_005770499.1; XM_005770442.1.
DR   STRING; 2903.R1DUA5; -.
DR   PaxDb; 2903-EOD18070; -.
DR   EnsemblProtists; EOD18070; EOD18070; EMIHUDRAFT_196115.
DR   GeneID; 19046071; -.
DR   KEGG; ehx:EMIHUDRAFT_196115; -.
DR   eggNOG; KOG3581; Eukaryota.
DR   HOGENOM; CLU_019868_0_0_1; -.
DR   OMA; YHGQEEN; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
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; 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; ARGININE OR CREATINE KINASE; 1.
DR   PANTHER; PTHR11547:SF64; PHOSPHAGEN KINASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 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:UP000013827};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00843}.
FT   DOMAIN          33..118
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51509"
FT   DOMAIN          151..413
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51510"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         154..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         281
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         334..338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         365..370
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ   SEQUENCE   415 AA;  44016 MW;  CC6951C1A0B8EA09 CRC64;
     MGGGASKAKK QATASEVVPE ASAAAANAGT SSKIEELTAQ AKVAAEANPD NLCAKTLLEA
     EVQTWMATLP AAKLDELALC AKSGLDNHDS GLGCYAVDPA NYDELAPFFD RVCEGYHHGG
     GKVHTTNWSL DGVEGLPEDG QLDLQKLGLG KELSMRVRVG RNLTAFPLPG LMTKADRVNF
     EKTMLKAFDV LKANPDYGGN VFSMTPNDVW SEVTGEAENP NLISADKYQE LVDAHVMFKD
     MAADPYLASA GIASDWPCGR GCYQSADGGF IIWFGEEDQL RIMCMAKGFV LNAVFDRLHT
     ALQAVEAIDG IAFATSTKYG YVTSCPSNLG TGMRASVHVA VPNLTSDGTD AKAKAAAKPL
     GLSVRGMGGE HTPIGKDGTI DLSPSSRLFI TEAEIVTKLY NGIKLLLEKE AEAQE
//
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