ID A0A0G0I2M3_9BACT Unreviewed; 480 AA.
AC A0A0G0I2M3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=(P)ppGpp synthetase I, SpoT/RelA {ECO:0000313|EMBL:KKQ49573.1};
GN ORFNames=US68_C0013G0013 {ECO:0000313|EMBL:KKQ49573.1};
OS Candidatus Shapirobacteria bacterium GW2011_GWE1_38_10.
OC Bacteria; Candidatus Shapirobacteria.
OX NCBI_TaxID=1618488 {ECO:0000313|EMBL:KKQ49573.1, ECO:0000313|Proteomes:UP000034231};
RN [1] {ECO:0000313|EMBL:KKQ49573.1, ECO:0000313|Proteomes:UP000034231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the RelA/SpoT family.
CC {ECO:0000256|ARBA:ARBA00007476}.
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:KKQ49573.1}.
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DR EMBL; LBTX01000013; KKQ49573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0I2M3; -.
DR PATRIC; fig|1618488.3.peg.763; -.
DR Proteomes; UP000034231; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
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; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 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 Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
FT DOMAIN 54..154
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 388..449
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 480 AA; 55041 MW; 34BA1A684D4C2DAF CRC64;
MTLDLSLDQR VHDYWEELNG ILVKNNFDTT RIKEGYDFAF EAHKEQFRVS GEPYISHPVW
VAKLIAQIGI GEEAVIAALL HDCVEDTPVT TDDIAVKFGD EIALLVSGLT EVKKKTSGIE
VHHTNVEVFR RFLFSSVDDV RVLIIRLADK LHNGMTIESL PIDSQIKYAK RVLGIYSPIA
EYVGLHYFKK RLDDIAFKIL YPKETEKLEL MMEEQEKDEI KALNLVKSDI EQVLKINNIN
KIEIQGRIKS LYSTYIKLKK KGEGSVKDRV GIRILTDSVA NCYNILGLLH ARYEYIPDEF
DDYISSPKPN GYRSIQTTLN WKNKTTVEVQ IRTFEMHEFN EFGPASHIAY KMSTDNKSGT
GYEWVRDLIN WQKGSGNVNN YRINVLSKFI YVFTPKGDTI QLPEGSSALD FAYRIHTDIG
DHCAGAKVNN KMVKIGQKLK TGDIVEILIN KKYNINKNWL DIVITSWAKE HIRNKTLLRS
//
