ID D7G573_ECTSI Unreviewed; 931 AA.
AC D7G573;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 28-JUN-2023, entry version 48.
DE SubName: Full=GTP diphosphokinase {ECO:0000313|EMBL:CBJ27227.1};
GN ORFNames=Esi_0063_0026 {ECO:0000313|EMBL:CBJ27227.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ27227.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ27227.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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DR EMBL; FN648852; CBJ27227.1; -; Genomic_DNA.
DR AlphaFoldDB; D7G573; -.
DR STRING; 2880.D7G573; -.
DR EnsemblProtists; CBJ27227; CBJ27227; Esi_0063_0026.
DR eggNOG; KOG1157; Eukaryota.
DR InParanoid; D7G573; -.
DR OrthoDB; 69734at2759; -.
DR Proteomes; UP000002630; Chromosome LG17.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR007685; RelA_SpoT.
DR PANTHER; PTHR21262:SF12; GTP DIPHOSPHOKINASE CRSH, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Kinase {ECO:0000313|EMBL:CBJ27227.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Transferase {ECO:0000313|EMBL:CBJ27227.1}.
FT DOMAIN 176..211
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 20..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 100000 MW; C09EA9D9D55682A8 CRC64;
MQCTAVTLAV CRSAAFDKAD NFEDEVGTAA PPLAETPPRR GVSPAEGGGS SSRGGGAGVE
GPTDDVEDSV VVLSDWLDES QASLGLPGLP GLGNREEHLN QGLVEVVGSQ ANGDDEDGVG
DGSAPFRFQQ LIQQMWATLS RGNQLEYLGK EGKAKVKQAL SVLAAYSALR EHPLQTGVEN
PQQAFSEMDF NSDGEVSFDE FVRWYSMSTA LDEKPQQLPE QANVGPASAR SGNGGVTAPE
VALTRSKTLL STGSRLLVDV EQSLALTSRQ LTNMPAADKS PRSAAAPPTD GGPNHNVGAA
APSPGKAWLG LSAAPTATAG AGLGVTEEEK EAARERWLSG AAAEPGAVGS GTDPVDDSAA
KDLEKALEML RVLVRAHADV DTLVAALASC IIRNPMGRYN LEVIEEQFGP IIRGIVEDRL
LLERLPQPTS AASYLSIQQV TCDCKGAGFL WRLVENCRVP LSSLIRWRVG AHHPMMAWRI
YLHVVNPLFC CSTAVDMYLY VRVSHRMHGR RARAGSAFTC SPPQSFGVKP VLDLDDHHAK
LMRDYLVHSS RDARAVVVHM ADLTCRLRDP SKTPAHTRHT LALEALQLYV PVSNALGLGS
SFRELEELGY KTIFPQTYSN MALWHHDVMG KSHDIVREVK TRMLDALHAR EDIAIRVHSY
RLEGRTKALV FRQNKRADDV HDIIGFRIIV APKRPGTRAS SATGGAGRTR SATGGNTAEE
AENAGARKRP GDDRRRGGPR PARSVFTVKT FPPPYRDADS RLLHDVYEVL VGLFEEVPGR
FKNYVDFPKK NGYRSVHTTV VHPTGIKMEF QVRTALMHVA AEGGSASHSL YKGDLDNPEE
ASLFRSKMTP NILSPAHRQL QSKSKSGEAA TALQPTADGG SPAANVSEKG PAAAAVPLLE
SKRCGKLGVK SDGGGATPVS DLDTSDRCPE P
//
