ID A0A1J4WUV4_9BACT Unreviewed; 491 AA.
AC A0A1J4WUV4;
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=AUJ11_00050 {ECO:0000313|EMBL:OIO52970.1};
OS Parcubacteria group bacterium CG1_02_44_65.
OC Bacteria.
OX NCBI_TaxID=1805311 {ECO:0000313|EMBL:OIO52970.1, ECO:0000313|Proteomes:UP000182601};
RN [1] {ECO:0000313|EMBL:OIO52970.1, ECO:0000313|Proteomes:UP000182601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_44_65 {ECO:0000313|EMBL:OIO52970.1};
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:OIO52970.1}.
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; MNWL01000001; OIO52970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4WUV4; -.
DR Proteomes; UP000182601; 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 400..461
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 491 AA; 57319 MW; 8D0C3803BDF29089 CRC64;
MPSTIKDILD EFKKHHSFDS AKVIERAYQF AEKAHRGQKR KSGEDYIYHC LETAMTLAKL
KMDAETIAAG LLHDVLDDTK TSSGQLRKKF GENILNLVKG ICKVGKIKYH GKERMVENLR
KLFLAMAKDI RVILIKLSDR LHNMETLDAL PEEKQKRIAL ETLEIYAPIA NRLGIREIGG
DLEDLAFKYV YPKEYQEVVK RVKDRYIKGK EYLKKITPIV KKNLTRKNVR VIEIHARTKH
YYSLYRKLLR YDMDWHKIYD IVALRIIVPD IESCYAALGV IHKKWKPLIG RIKDYIAISK
PNGYQSLHTT VFCQGGKITE FQIRTPQMHQ ESEYGIAAHW YYSEEKGLKS YIKRKILHQK
PEREFKKELS WVKQLQEWQN EKFSSPEEFI DSLKIDFLKD RIFVFTPKGD IIDLPEGAIP
IDFAYEIHTD VGNQCAGAKV DEKLVPLSRP LQNGEVVEII TQKNKKPNRD WLQIVKTNAA
KSKIKAWFKK N
//