ID A0A1F8BML3_9BACT Unreviewed; 501 AA.
AC A0A1F8BML3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=TGS domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2893_01140 {ECO:0000313|EMBL:OGM65314.1};
OS Candidatus Woesebacteria bacterium RIFCSPLOWO2_01_FULL_39_25.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802521 {ECO:0000313|EMBL:OGM65314.1, ECO:0000313|Proteomes:UP000176725};
RN [1] {ECO:0000313|EMBL:OGM65314.1, ECO:0000313|Proteomes:UP000176725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGM65314.1}.
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DR EMBL; MGHH01000005; OGM65314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8BML3; -.
DR STRING; 1802521.A2893_01140; -.
DR Proteomes; UP000176725; 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; IPR004811; RelA/Spo_fam.
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; 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 47..148
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 402..465
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 501 AA; 57538 MW; B99E517F46D3D1F9 CRC64;
MENDFREVLK IVKSYNDNKL ALDLIKKAWK FAKLAHTGQK RYSGEPYVIH ELETAKILTS
WKLDTDTIVA GFLHDVVEDG AADLSDIKKE FGEEVARLVD GVTKVSHIKL KKQEIEEEYI
ENLRKMFLAM AKDLRVVLVK LADRLHNMRT LSYVPKDRQE KIALETLEIY APLSERLGMG
QVSSELEDLA FPYVFPSEYV RVKKGATIYY KKAEENIRKM KRSLLKALSS EGIEAKIDGR
KKSFYSLWKK LERLGIEWNF GKIYDIVALR ILVKTVTECY TALGVVHRSF KLVPHFGISD
FIAQPKPNGY QSIHTRVFGP RGKITEVQIR TFDMHEQAEH GVAAHWAYSD AKRKAVINDQ
ELDKRGVTAS EEKLSWIKQL AEWQKEISDS KEFLQAVKFD ALRERIFVFS PRGDVFDLPV
GSTPIDFAYA LHSDLGDYLK AAKADGKIIP LNYKLKSGQV VEILKSKEKR SPNHDWLEFV
VTTQARREIG KALRKTDVDR K
//
