NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|739564097|ref|WP_037422229|]
View 

MULTISPECIES: RelA/SpoT domain-containing protein [Shewanella]

Protein Classification

RelA/SpoT domain-containing protein( domain architecture ID 10143703)

RelA/SpoT domain-containing protein similar to ppGpp synthetase (RelA) and ppGpp synthetase/hydrolase (SpoT)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 78-188 1.24e-15

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: 71.22  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739564097  78 AQNELGNLLQRVTADTQAQVILPDVKSYQRAAEKVASKFK--GDASQITDLARASIVSNSISELMQSYYALSEQAQVV-- 153
Cdd:cd05399    3 ALEEIADLLRDAGIIGRVASVSGRVKSPYSIYEKLRRKGKdlPILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIpg 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 739564097 154 KQKNRFAEPKASGYRDLNLLVRLPE--SGMIAEVQLH 188
Cdd:cd05399   83 RVKDYIAEPKENGYQSLHLVVRGPEdkAGVLIEIQIR 119
 
Name Accession Description Interval E-value
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 78-188 1.24e-15

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: 71.22  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739564097  78 AQNELGNLLQRVTADTQAQVILPDVKSYQRAAEKVASKFK--GDASQITDLARASIVSNSISELMQSYYALSEQAQVV-- 153
Cdd:cd05399    3 ALEEIADLLRDAGIIGRVASVSGRVKSPYSIYEKLRRKGKdlPILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIpg 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 739564097 154 KQKNRFAEPKASGYRDLNLLVRLPE--SGMIAEVQLH 188
Cdd:cd05399   83 RVKDYIAEPKENGYQSLHLVVRGPEdkAGVLIEIQIR 119
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 102-206 1.39e-10

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: 57.19  E-value: 1.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739564097   102 VKSYQRAAEKVASKFKGDASQITDLARASIVSNSISELMQSYYALSEQAQVV--KQKNRFAEPKASGYRDLNLLVRLPEs 179
Cdd:smart00954   3 VKHLYSIYKKMRRKGEISFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIpgRFKDYIANPKPNGYRSLHTTVIGPE- 81

                           90       100
                   ....*....|....*....|....*....
gi 739564097   180 GMIAEVQL--HLKDIADIKSGPEHKVYEQ 206
Cdd:smart00954  82 GRPVEIQIrtILMHAWAELGHAAHYKYKE 110
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 102-186 1.54e-03

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: 37.53  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739564097  102 VKSYQRAAEKVASKfKGDASQITDLARASIVSNS------ISELMQSYYalseQAQVVKQKNRFAEPKASGYRDLNLLVR 175
Cdd:pfam04607   3 VKSPYSIYEKMQRK-GLLFEEIYDLIGIRIIVQFvddcyrVLGIIHSLW----DPIPGRFKDYIAIPKPNGYRSLHTTVI 77

                          90
                  ....*....|.
gi 739564097  176 LPESGMIAEVQ 186
Cdd:pfam04607  78 IGPEGVPVEIQ 88
 
Name Accession Description Interval E-value
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 78-188 1.24e-15

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: 71.22  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739564097  78 AQNELGNLLQRVTADTQAQVILPDVKSYQRAAEKVASKFK--GDASQITDLARASIVSNSISELMQSYYALSEQAQVV-- 153
Cdd:cd05399    3 ALEEIADLLRDAGIIGRVASVSGRVKSPYSIYEKLRRKGKdlPILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIpg 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 739564097 154 KQKNRFAEPKASGYRDLNLLVRLPE--SGMIAEVQLH 188
Cdd:cd05399   83 RVKDYIAEPKENGYQSLHLVVRGPEdkAGVLIEIQIR 119
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 102-206 1.39e-10

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: 57.19  E-value: 1.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739564097   102 VKSYQRAAEKVASKFKGDASQITDLARASIVSNSISELMQSYYALSEQAQVV--KQKNRFAEPKASGYRDLNLLVRLPEs 179
Cdd:smart00954   3 VKHLYSIYKKMRRKGEISFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIpgRFKDYIANPKPNGYRSLHTTVIGPE- 81

                           90       100
                   ....*....|....*....|....*....
gi 739564097   180 GMIAEVQL--HLKDIADIKSGPEHKVYEQ 206
Cdd:smart00954  82 GRPVEIQIrtILMHAWAELGHAAHYKYKE 110
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 102-186 1.54e-03

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: 37.53  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739564097  102 VKSYQRAAEKVASKfKGDASQITDLARASIVSNS------ISELMQSYYalseQAQVVKQKNRFAEPKASGYRDLNLLVR 175
Cdd:pfam04607   3 VKSPYSIYEKMQRK-GLLFEEIYDLIGIRIIVQFvddcyrVLGIIHSLW----DPIPGRFKDYIAIPKPNGYRSLHTTVI 77

                          90
                  ....*....|.
gi 739564097  176 LPESGMIAEVQ 186
Cdd:pfam04607  78 IGPEGVPVEIQ 88
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH