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Database: UniProt
Entry: E1U3T9_9CYAN
LinkDB: E1U3T9_9CYAN
Original site: E1U3T9_9CYAN 
ID   E1U3T9_9CYAN            Unreviewed;       758 AA.
AC   E1U3T9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=(P)ppGpp synthetase I {ECO:0000313|EMBL:ACN96096.1};
OS   Fischerella sp. MV11.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC   Fischerella.
OX   NCBI_TaxID=397321 {ECO:0000313|EMBL:ACN96096.1};
RN   [1] {ECO:0000313|EMBL:ACN96096.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MV11 {ECO:0000313|EMBL:ACN96096.1};
RA   Hess W.R., Scholz I.D.;
RT   "High diversity of cyanobacterial nonribosomal peptide synthetase genes in
RT   isolates from geothermal sites and hot springs of Costa Rica.";
RL   Submitted (SEP-2008) 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}.
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DR   EMBL; FJ211389; ACN96096.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1U3T9; -.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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;
FT   DOMAIN          66..165
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          408..471
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          681..755
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   758 AA;  86478 MW;  E4825C871CED8365 CRC64;
     MSSTIVNHPI DITLPEWLES CLHTPPVDGA ATEEDRKYYD TSLICRAFEF AYQLHQGQYR
     KSGEPYICHP IAVAGMLRDL GGSAAMIAAG FLHDVVEDTD VTIEEIEQRF GSEVRCLVEG
     VTKLSKINFK SKTESQAENF RRMFLAMAQD IRVIVVKLAD RLHNMRTLEY MPDEKRRRTA
     TETREIFAPL ANRLGIWRFK WELEDLAFKY LEPEAFRQIQ QLVSEKRTDR EERLKKISET
     LRTRLAEAGI RCLDISGRPK HLYSIYQKMQ RQNKEFHEIY DLAALRIIVQ TNEECYRALA
     VVHDVFRPIP GRFKDYIGLP KPNRYQSLHT GVIGPWGRPL EVQIRTMEMH HVAEYGIAAH
     WKYKETGGSH TGLTASDEKF TWLRQLLEWQ SDLKDAQEYL ESIKDNLFEE DIYVFTPKGD
     LVALKPGSTT VDFAYRIHTE VGNRCTGVRV NGRMVPLSTR LQNGDIVEII TQKNGHPSLD
     WLNFVRTSAA KNRIKQWYKR SRREENIARG RELLEKELGK TGFDNVLKSE AMQAVAERCN
     YHSTEDLLAG LGYGEVTLNL VLNRWREIVK AQQPATNEPD ITTHLPTTAK AAAFLREATP
     ITSRTSDSPI VGVEGLLYHL AGCCTPIPGE AIIGVVTRGK GISIHRQGCH NLEKVECDRL
     VPVSWNQAVE HSGRPVTYAV NLQIEALDRV GVLKDILSRL SDQGINVRHA NVKTSFGQPA
     LIDLGIEIRD RPQLEQLFTQ IKKMSDILNI RRIGQIDE
//
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