ID A0A1J4VXA6_9BACT Unreviewed; 484 AA.
AC A0A1J4VXA6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=TGS domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUJ71_01115 {ECO:0000313|EMBL:OIO39269.1};
OS Candidatus Omnitrophica bacterium CG1_02_49_16.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1805290 {ECO:0000313|EMBL:OIO39269.1, ECO:0000313|Proteomes:UP000182296};
RN [1] {ECO:0000313|EMBL:OIO39269.1, ECO:0000313|Proteomes:UP000182296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_49_16 {ECO:0000313|EMBL:OIO39269.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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:OIO39269.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNVU01000019; OIO39269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4VXA6; -.
DR STRING; 1805290.AUJ71_01115; -.
DR Proteomes; UP000182296; 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 46..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 383..444
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 484 AA; 56074 MW; 5817D943F04FB6BF CRC64;
MPLNLAQLLA QIKQNNPKAD TTLVELAYEY AAQAHAGQTR RSGEPYIQHP LRTALTLAQI
RAENDVVIAG LLHDVPEDTG RPLAEIEKQF GKKIAALVEG ITKLSKVKYR GIERHTESLK
KMFIAMAADI RVILIRFADR LHNLETLDAL PENKRLRIAQ ETMEIYVPIA GLLGIWHFKN
KMEDICFRYL HPEEYKKLQY RYEVEQRMEN QAFIKKTEEI LVPKLKEADL RFEIQGRFKS
LYSIFQKMQK KERKFSEIYD VFALRVIVET VADCYKTIGV IHSLWKPKPN RFKDYIAVPK
SNGYQALHTA VFGPNGKVTE FQVATRKMYE KSLYGIAAHW YYKSNKKYLS KQPKWVRDIL
ELMRQAKNSE EFVNVAKIDV FQNRIFVFTP KGDVIDLPER STPIDFAYAV HSDIGHHCVG
AMINEKIGKL DTPLKSGDTV EIITEKNKKP SRDWLKIAKT ARAREKIRQS LKTNGGFMKF
IKWK
//
