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Database: UniProt
Entry: F7L0G6_9FUSO
LinkDB: F7L0G6_9FUSO
Original site: F7L0G6_9FUSO 
ID   F7L0G6_9FUSO            Unreviewed;       724 AA.
AC   F7L0G6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=GTP diphosphokinase {ECO:0000313|EMBL:EGN66969.1};
GN   ORFNames=HMPREF0401_01337 {ECO:0000313|EMBL:EGN66969.1};
OS   Fusobacterium animalis 11_3_2.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=457403 {ECO:0000313|EMBL:EGN66969.1, ECO:0000313|Proteomes:UP000004160};
RN   [1] {ECO:0000313|EMBL:EGN66969.1, ECO:0000313|Proteomes:UP000004160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11_3_2 {ECO:0000313|EMBL:EGN66969.1,
RC   ECO:0000313|Proteomes:UP000004160};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., White A.P.,
RA   Crowley S., Surette M., Strauss J.C., Ambrose C.E., Allen-Vercoe E.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA   Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z.,
RA   Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA   Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusobacterium sp. 11_3_2.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC       is a mediator of the stringent response that coordinates a variety of
CC       cellular activities in response to changes in nutritional abundance.
CC       {ECO:0000256|RuleBase:RU003847}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGN66969.1}.
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DR   EMBL; ACUO01000019; EGN66969.1; -; Genomic_DNA.
DR   RefSeq; WP_005910680.1; NZ_GL945392.1.
DR   AlphaFoldDB; F7L0G6; -.
DR   PATRIC; fig|457403.8.peg.1351; -.
DR   HOGENOM; CLU_012300_3_0_0; -.
DR   Proteomes; UP000004160; Unassembled WGS sequence.
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; cd04876; ACT_RelA-SpoT; 1.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   CDD; cd01668; TGS_RSH; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR004811; RelA/Spo_fam.
DR   InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA/SpoT.
DR   NCBIfam; TIGR00691; spoT_relA; 1.
DR   PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR   PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF19296; RelA_AH_RIS; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:EGN66969.1};
KW   Transferase {ECO:0000313|EMBL:EGN66969.1}.
FT   DOMAIN          45..142
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          380..443
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          650..724
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   724 AA;  82787 MW;  965911F69FE4A4FA CRC64;
     MNYWEQLLDK AKANHLNLDF DKIKLALGFA EESHQGQYRK SGDDYIVHPV EVAKILMDMK
     MDTDTIVAGL LHDVVEDTLI PIADIKYNFG DTVATLVDGV TKLKALPNGT KNQAENIRKM
     ILAMAENIRV ILIKLADRLH NMRTLKFMKP EKQQSISKET LDIYAPLAHR LGMAKVKSEL
     EDIAFSYLHH DEFLEIKRLV DNTKEERKDY IENFIRTMIR TLSELGIKAE VKGRFKHFYS
     IYRKMYQKGK DFDDIYDLMG VRVIVEDKAT CYHVLGIVHS QYTPVPGRFK DYIAVPKSNN
     YQSIHTTIVG PLGKFIEIQI RTKDMDDIAE EGIAAHWNYK ENKKSSKDDN IYGWLRHIIE
     FQNESDSTED FIEGVTGDID RGTVFTFSPK GDIIELPVGA TALDFAFMVH TQVGCKCVGA
     KVNGRMVTID HKLKSGDKVE IITSKNSKGP SIDWLDIVVT HGAKGKIRKF LKDENKENVT
     KLGKDNLEKE ASKLGMTLKE IENDPTLKKH MEKNNISSLD EFYFYIGEKR SRLDILINKI
     KINLEKERAA STLTIEEVLK KKEEKKKEGK NDFGIVIDGV NNTLIRFAKC CTPLPGDEIG
     GFVTKLTGIT VHRKDCPNFH AMIEKDPSRE ILVKWDENLI ETKMNKYNFT FTVVLNDRPN
     ILMEIVNLIA NHKINITSVN SYEVKKDGDR VIKVKISIEI KGKAEYDYLI SNILKLKDVI
     SVER
//
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