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Conserved domains on  [gi|1239365793|ref|WP_095431732|]
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MULTISPECIES: GTP pyrophosphokinase family protein [Bacillus]

Protein Classification

GTP pyrophosphokinase family protein( domain architecture ID 10789386)

GTP pyrophosphokinase family protein similar to Bacillus subtilis GTP pyrophosphokinases, YwaC and YjbM

Gene Ontology:  GO:0015969

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 2-212 5.91e-38

ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport and metabolism, Signal transduction mechanisms];


:

Pssm-ID: 441924 [Multi-domain]  Cd Length: 286  Bit Score: 136.06  E-value: 5.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793   2 EVLLNEKSIKLAVPMHF---RVKEWESVLNKCQR--YSLKPSNI-EEINDLAGIRIVTLFKSDINTIQKIIKSTFTILRE 75
Cdd:COG2357    34 EILLDEFEKHGGSPIEHvtsRVKSPESIIEKLRRkgLPLTYENIlEEITDIAGIRIICYFVDDIYRVAELLRSQFDVKII 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793  76 EDTANRLSEDQFGYGSIHYEATLPNSWFEIPsykifKDKIVEIQLRTASQHAWAAASHILNYKKESHVPQPVRRTINRVS 155
Cdd:COG2357   114 EEKDYIKNPKPNGYRSLHLIVRVPVFLSDGP-----KGVPVEIQIRTIAMDFWAELEHKLRYKYDGEIPEEIKRRLKRAA 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365793 156 ALLETVDLEFERVLQEREEfYQIPVADQNQLNTDTLKKILDELLPAENKSDDEDYST 212
Cdd:COG2357   189 ALLELLDEEMSEIRDEIEE-AQKEFEDKEAIAEESLAALLLLLEDLGVDLDFILAIE 244
 
Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 2-212 5.91e-38

ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 441924 [Multi-domain]  Cd Length: 286  Bit Score: 136.06  E-value: 5.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793   2 EVLLNEKSIKLAVPMHF---RVKEWESVLNKCQR--YSLKPSNI-EEINDLAGIRIVTLFKSDINTIQKIIKSTFTILRE 75
Cdd:COG2357    34 EILLDEFEKHGGSPIEHvtsRVKSPESIIEKLRRkgLPLTYENIlEEITDIAGIRIICYFVDDIYRVAELLRSQFDVKII 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793  76 EDTANRLSEDQFGYGSIHYEATLPNSWFEIPsykifKDKIVEIQLRTASQHAWAAASHILNYKKESHVPQPVRRTINRVS 155
Cdd:COG2357   114 EEKDYIKNPKPNGYRSLHLIVRVPVFLSDGP-----KGVPVEIQIRTIAMDFWAELEHKLRYKYDGEIPEEIKRRLKRAA 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365793 156 ALLETVDLEFERVLQEREEfYQIPVADQNQLNTDTLKKILDELLPAENKSDDEDYST 212
Cdd:COG2357   189 ALLELLDEEMSEIRDEIEE-AQKEFEDKEAIAEESLAALLLLLEDLGVDLDFILAIE 244
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 19-129 2.66e-21

Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; This family includes the catalytic domains of Escherichia coli ppGpp synthetase (RelA), ppGpp synthetase/hydrolase (SpoT), and related proteins. RelA synthesizes (p)ppGpp in response to amino-acid starvation and in association with ribosomes. (p)ppGpp triggers the bacterial stringent response. SpoT catalyzes (p)ppGpp synthesis under carbon limitation in a ribosome-independent manner. It also catalyzes (p)ppGpp degradation. Gram-negative bacteria have two enzymes involved in (p)ppGpp metabolism while most Gram-positive organisms have a single Rel-Spo enzyme (Rel), which both synthesizes and degrades (p)ppGpp. The Arabidopsis thaliana Rel-Spo proteins, At-RSH1,-2, and-3 appear to regulate a rapid (p)ppGpp-mediated response to pathogens and other stresses. This catalytic domain is found in association with an N-terminal HD domain and a C-terminal metal dependent phosphohydrolase domain (TGS). Some Rel-Spo proteins also have a C-terminal regulatory ACT domain. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition.Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism.


Pssm-ID: 143389 [Multi-domain]  Cd Length: 129  Bit Score: 87.40  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793  19 RVKEWESVLNKCQRYSLKPSNIEEINDLAGIRIVTLFKSDINTIQKIIKSTFTIL--REEDTANRLSEdqFGYGSIHYea 96
Cdd:cd05399    26 RVKSPYSIYEKLRRKGKDLPILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIpgRVKDYIAEPKE--NGYQSLHL-- 101

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1239365793  97 tlpnsWFEIPSYKifKDKIVEIQLRTASQHAWA 129
Cdd:cd05399   102 -----VVRGPEDK--AGVLIEIQIRTILMHAWA 127
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 19-142 5.97e-21

Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ somewhat. RelA produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species.


Pssm-ID: 214934 [Multi-domain]  Cd Length: 111  Bit Score: 85.70  E-value: 5.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793   19 RVKEWESVLNKCQRYSLKPsnIEEINDLAGIRIVTLFKSDINTIQKIIKSTFTILREEDTANRLSEDQFGYGSIHYeatl 98
Cdd:smart00954   2 RVKHLYSIYKKMRRKGEIS--FDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLHT---- 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1239365793   99 pnswfeipSYKIFKDKIVEIQLRTASQHAWAAASHILNYKKESH 142
Cdd:smart00954  76 --------TVIGPEGRPVEIQIRTILMHAWAELGHAAHYKYKEG 111
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 19-138 6.26e-21

Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and SpoT of Escherichia coli, and their homologs in plants and in other eubacteria. RelA is a guanosine 3',5'-bis-pyrophosphate (ppGpp) synthetase (EC:2.7.6.5) while SpoT is thought to be a bifunctional enzyme catalysing both ppGpp synthesis and degradation (ppGpp 3'-pyrophosphohydrolase, (EC:3.1.7.2)). This region is often found in association with HD (pfam01966), a metal-dependent phosphohydrolase, TGS (pfam02824) which is a possible nucleotide-binding region, and the ACT regulatory domain (pfam01842).


Pssm-ID: 428031 [Multi-domain]  Cd Length: 113  Bit Score: 85.68  E-value: 6.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793  19 RVKEWESVLNKCQRyslKPSNIEEINDLAGIRIVTLFKSDINTIQKIIKSTFTIL--REEDTANRLseDQFGYGSIHYea 96
Cdd:pfam04607   2 RVKSPYSIYEKMQR---KGLLFEEIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIpgRFKDYIAIP--KPNGYRSLHT-- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1239365793  97 TLPNSwfeipsykiFKDKIVEIQLRTASQHAWAAAS--HILNYK 138
Cdd:pfam04607  75 TVIIG---------PEGVPVEIQIRTIAMHFWAEYGiaHHWRYK 109
 
Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 2-212 5.91e-38

ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 441924 [Multi-domain]  Cd Length: 286  Bit Score: 136.06  E-value: 5.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793   2 EVLLNEKSIKLAVPMHF---RVKEWESVLNKCQR--YSLKPSNI-EEINDLAGIRIVTLFKSDINTIQKIIKSTFTILRE 75
Cdd:COG2357    34 EILLDEFEKHGGSPIEHvtsRVKSPESIIEKLRRkgLPLTYENIlEEITDIAGIRIICYFVDDIYRVAELLRSQFDVKII 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793  76 EDTANRLSEDQFGYGSIHYEATLPNSWFEIPsykifKDKIVEIQLRTASQHAWAAASHILNYKKESHVPQPVRRTINRVS 155
Cdd:COG2357   114 EEKDYIKNPKPNGYRSLHLIVRVPVFLSDGP-----KGVPVEIQIRTIAMDFWAELEHKLRYKYDGEIPEEIKRRLKRAA 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365793 156 ALLETVDLEFERVLQEREEfYQIPVADQNQLNTDTLKKILDELLPAENKSDDEDYST 212
Cdd:COG2357   189 ALLELLDEEMSEIRDEIEE-AQKEFEDKEAIAEESLAALLLLLEDLGVDLDFILAIE 244
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 19-129 2.66e-21

Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; This family includes the catalytic domains of Escherichia coli ppGpp synthetase (RelA), ppGpp synthetase/hydrolase (SpoT), and related proteins. RelA synthesizes (p)ppGpp in response to amino-acid starvation and in association with ribosomes. (p)ppGpp triggers the bacterial stringent response. SpoT catalyzes (p)ppGpp synthesis under carbon limitation in a ribosome-independent manner. It also catalyzes (p)ppGpp degradation. Gram-negative bacteria have two enzymes involved in (p)ppGpp metabolism while most Gram-positive organisms have a single Rel-Spo enzyme (Rel), which both synthesizes and degrades (p)ppGpp. The Arabidopsis thaliana Rel-Spo proteins, At-RSH1,-2, and-3 appear to regulate a rapid (p)ppGpp-mediated response to pathogens and other stresses. This catalytic domain is found in association with an N-terminal HD domain and a C-terminal metal dependent phosphohydrolase domain (TGS). Some Rel-Spo proteins also have a C-terminal regulatory ACT domain. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition.Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism.


Pssm-ID: 143389 [Multi-domain]  Cd Length: 129  Bit Score: 87.40  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793  19 RVKEWESVLNKCQRYSLKPSNIEEINDLAGIRIVTLFKSDINTIQKIIKSTFTIL--REEDTANRLSEdqFGYGSIHYea 96
Cdd:cd05399    26 RVKSPYSIYEKLRRKGKDLPILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIpgRVKDYIAEPKE--NGYQSLHL-- 101

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1239365793  97 tlpnsWFEIPSYKifKDKIVEIQLRTASQHAWA 129
Cdd:cd05399   102 -----VVRGPEDK--AGVLIEIQIRTILMHAWA 127
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 19-142 5.97e-21

Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ somewhat. RelA produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species.


Pssm-ID: 214934 [Multi-domain]  Cd Length: 111  Bit Score: 85.70  E-value: 5.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793   19 RVKEWESVLNKCQRYSLKPsnIEEINDLAGIRIVTLFKSDINTIQKIIKSTFTILREEDTANRLSEDQFGYGSIHYeatl 98
Cdd:smart00954   2 RVKHLYSIYKKMRRKGEIS--FDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLHT---- 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1239365793   99 pnswfeipSYKIFKDKIVEIQLRTASQHAWAAASHILNYKKESH 142
Cdd:smart00954  76 --------TVIGPEGRPVEIQIRTILMHAWAELGHAAHYKYKEG 111
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 19-138 6.26e-21

Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and SpoT of Escherichia coli, and their homologs in plants and in other eubacteria. RelA is a guanosine 3',5'-bis-pyrophosphate (ppGpp) synthetase (EC:2.7.6.5) while SpoT is thought to be a bifunctional enzyme catalysing both ppGpp synthesis and degradation (ppGpp 3'-pyrophosphohydrolase, (EC:3.1.7.2)). This region is often found in association with HD (pfam01966), a metal-dependent phosphohydrolase, TGS (pfam02824) which is a possible nucleotide-binding region, and the ACT regulatory domain (pfam01842).


Pssm-ID: 428031 [Multi-domain]  Cd Length: 113  Bit Score: 85.68  E-value: 6.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365793  19 RVKEWESVLNKCQRyslKPSNIEEINDLAGIRIVTLFKSDINTIQKIIKSTFTIL--REEDTANRLseDQFGYGSIHYea 96
Cdd:pfam04607   2 RVKSPYSIYEKMQR---KGLLFEEIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIpgRFKDYIAIP--KPNGYRSLHT-- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1239365793  97 TLPNSwfeipsykiFKDKIVEIQLRTASQHAWAAAS--HILNYK 138
Cdd:pfam04607  75 TVIIG---------PEGVPVEIQIRTIAMHFWAEYGiaHHWRYK 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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