ID A0A1J5H471_9BACT Unreviewed; 485 AA.
AC A0A1J5H471;
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=AUK20_02280 {ECO:0000313|EMBL:OIP79284.1};
OS Parcubacteria group bacterium CG2_30_45_37.
OC Bacteria.
OX NCBI_TaxID=1805319 {ECO:0000313|EMBL:OIP79284.1, ECO:0000313|Proteomes:UP000183231};
RN [1] {ECO:0000313|EMBL:OIP79284.1, ECO:0000313|Proteomes:UP000183231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_45_37 {ECO:0000313|EMBL:OIP79284.1};
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:OIP79284.1}.
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DR EMBL; MNZH01000060; OIP79284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5H471; -.
DR Proteomes; UP000183231; 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 44..142
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 381..442
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 485 AA; 56422 MW; C10D1053A95A3DF8 CRC64;
MTINQIISQF KENRPKADTT MIQLAFEFAQ KAHADQKRKN GEPYIQHSLH TAFVLTQIKA
DLETVVAGLL HDIPEDTEYT LADIEKNFGE EVADLVEGIT KLSKIKYRGI ERYSESLRKM
FLAMAKDLRV ILIKFADRLH NLRTLESLPL EKRLRIAKET LEIYAPIAGL LGVFRLKWQL
EDICFKHLYP EEYKKLEYKY EVEKKYEHNQ YIQKTKNILG AKLKEAKIPF QITSRFKHLY
GIYLKMQKKD RKFAEIYDVF AMRVVVPSIA DCYKTLGIIH SLWRPNPSRF KDYIAVPKPN
GYRALHTTVY GLESKSCEFQ IRTKEMDEQA KFGIAAHWYY KAKGSVSINQ PGWVKEVLKI
QKDTEDTLDF IKQIKFDVFH DRIFVFTPKG DVFDLPKGST PIDFAYYVHS DIGNQAVGAM
VNDKIATLDQ GLKNGDLVEI IREKKRKGPS RDWLKIVKTA TARNKIKQNL RNSMLDNIKK
FIPKI
//
