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Conserved domains on  [gi|492016809|ref|WP_005718615|]
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MULTISPECIES: GTP pyrophosphokinase family protein [Lactobacillus]

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 ...
 4-208 6.96e-91

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: 268.18  E-value: 6.96e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809   4 DWDNFLWPYNEAVRELKVKFRSLRQGFlTKGEHSPIEFVIGRVKTVDSIKEKMKRRVISPDV--IETDMQDIAGIRIVTQ 81
Cdd:COG2357   14 DYERFLPPYEAALEELKTKLEILLDEF-EKHGGSPIEHVTSRVKSPESIIEKLRRKGLPLTYenILEEITDIAGIRIICY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809  82 FVDDIYKVVDLIHARDDMEVVEERDYIQNAKPSGYRSYHMVINYTVYLPEGPKKLIAEVQIRTMAMNFWATVEHTLNYKY 161
Cdd:COG2357   93 FVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLSDGPKGVPVEIQIRTIAMDFWAELEHKLRYKY 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 492016809 162 QGVYPDDISARLKSTAEAAYRLDEEMSSIKDEVQEAQKIFTKNKGKE 208
Cdd:COG2357  173 DGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEEAQKEFEDKEAIA 219
 
Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 4-208 6.96e-91

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: 268.18  E-value: 6.96e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809   4 DWDNFLWPYNEAVRELKVKFRSLRQGFlTKGEHSPIEFVIGRVKTVDSIKEKMKRRVISPDV--IETDMQDIAGIRIVTQ 81
Cdd:COG2357   14 DYERFLPPYEAALEELKTKLEILLDEF-EKHGGSPIEHVTSRVKSPESIIEKLRRKGLPLTYenILEEITDIAGIRIICY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809  82 FVDDIYKVVDLIHARDDMEVVEERDYIQNAKPSGYRSYHMVINYTVYLPEGPKKLIAEVQIRTMAMNFWATVEHTLNYKY 161
Cdd:COG2357   93 FVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLSDGPKGVPVEIQIRTIAMDFWAELEHKLRYKY 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 492016809 162 QGVYPDDISARLKSTAEAAYRLDEEMSSIKDEVQEAQKIFTKNKGKE 208
Cdd:COG2357  173 DGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEEAQKEFEDKEAIA 219
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 44-163 1.28e-49

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: 156.94  E-value: 1.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809   44 GRVKTVDSIKEKMKRRVISPDvietDMQDIAGIRIVTQFVDDIYKVVDLIHARDDMEVVEERDYIQNAKPSGYRSYHMVI 123
Cdd:pfam04607   1 GRVKSPYSIYEKMQRKGLLFE----EIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRSLHTTV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 492016809  124 NYtvylpeGPKKLIAEVQIRTMAMNFWAT--VEHTLNYKYQG 163
Cdd:pfam04607  77 II------GPEGVPVEIQIRTIAMHFWAEygIAHHWRYKEGG 112
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 44-163 2.69e-46

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: 148.49  E-value: 2.69e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809    44 GRVKTVDSIKEKMKRRvisPDVIETDMQDIAGIRIVTQFVDDIYKVVDLIHARDDMEVVEERDYIQNAKPSGYRSYHMVI 123
Cdd:smart00954   1 GRVKHLYSIYKKMRRK---GEISFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLHTTV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 492016809   124 nytvylpEGPKKLIAEVQIRTMAMNFWATVEHTLNYKYQG 163
Cdd:smart00954  78 -------IGPEGRPVEIQIRTILMHAWAELGHAAHYKYKE 110
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 34-153 1.44e-36

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: 124.38  E-value: 1.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809  34 GEHSPIEFVIGRVKTVDSIKEKMKRRVISPDvIETDMQDIAGIRIVTQFVDDIYKVVDLIHARDDMEVVEERDYIQNAKP 113
Cdd:cd05399   15 GIIGRVASVSGRVKSPYSIYEKLRRKGKDLP-ILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIPGRVKDYIAEPKE 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492016809 114 SGYRSYHmvinYTVYLPEGPKKLIAEVQIRTMAMNFWATV 153
Cdd:cd05399   94 NGYQSLH----LVVRGPEDKAGVLIEIQIRTILMHAWAEL 129
relA PRK10872
(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional
 24-162 1.72e-10

(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional


Pssm-ID: 182797 [Multi-domain]  Cd Length: 743  Bit Score: 59.80  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809  24 RSLRQGFLTKGEHSPIefvIGRVKTVDSIKEKMKRRVISPDvietDMQDIAGIRIVTQFVDDIYKVVDLIHARDDMEVVE 103
Cdd:PRK10872 234 GHLRAEMKAEGVKAEV---YGRPKHIYSIWRKMQKKSLAFD----ELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDE 306

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492016809 104 ERDYIQNAKPSGYRSYHmvinyTVYLpeGPKKLIAEVQIRTMAMNFWATVEHTLNYKYQ 162
Cdd:PRK10872 307 FDDYVANPKPNGYQSIH-----TVVL--GPGGKTVEIQIRTRQMHEDAELGVAAHWKYK 358
 
Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 4-208 6.96e-91

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: 268.18  E-value: 6.96e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809   4 DWDNFLWPYNEAVRELKVKFRSLRQGFlTKGEHSPIEFVIGRVKTVDSIKEKMKRRVISPDV--IETDMQDIAGIRIVTQ 81
Cdd:COG2357   14 DYERFLPPYEAALEELKTKLEILLDEF-EKHGGSPIEHVTSRVKSPESIIEKLRRKGLPLTYenILEEITDIAGIRIICY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809  82 FVDDIYKVVDLIHARDDMEVVEERDYIQNAKPSGYRSYHMVINYTVYLPEGPKKLIAEVQIRTMAMNFWATVEHTLNYKY 161
Cdd:COG2357   93 FVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLSDGPKGVPVEIQIRTIAMDFWAELEHKLRYKY 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 492016809 162 QGVYPDDISARLKSTAEAAYRLDEEMSSIKDEVQEAQKIFTKNKGKE 208
Cdd:COG2357  173 DGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEEAQKEFEDKEAIA 219
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 44-163 1.28e-49

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: 156.94  E-value: 1.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809   44 GRVKTVDSIKEKMKRRVISPDvietDMQDIAGIRIVTQFVDDIYKVVDLIHARDDMEVVEERDYIQNAKPSGYRSYHMVI 123
Cdd:pfam04607   1 GRVKSPYSIYEKMQRKGLLFE----EIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRSLHTTV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 492016809  124 NYtvylpeGPKKLIAEVQIRTMAMNFWAT--VEHTLNYKYQG 163
Cdd:pfam04607  77 II------GPEGVPVEIQIRTIAMHFWAEygIAHHWRYKEGG 112
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 44-163 2.69e-46

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: 148.49  E-value: 2.69e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809    44 GRVKTVDSIKEKMKRRvisPDVIETDMQDIAGIRIVTQFVDDIYKVVDLIHARDDMEVVEERDYIQNAKPSGYRSYHMVI 123
Cdd:smart00954   1 GRVKHLYSIYKKMRRK---GEISFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLHTTV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 492016809   124 nytvylpEGPKKLIAEVQIRTMAMNFWATVEHTLNYKYQG 163
Cdd:smart00954  78 -------IGPEGRPVEIQIRTILMHAWAELGHAAHYKYKE 110
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 34-153 1.44e-36

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: 124.38  E-value: 1.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809  34 GEHSPIEFVIGRVKTVDSIKEKMKRRVISPDvIETDMQDIAGIRIVTQFVDDIYKVVDLIHARDDMEVVEERDYIQNAKP 113
Cdd:cd05399   15 GIIGRVASVSGRVKSPYSIYEKLRRKGKDLP-ILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIPGRVKDYIAEPKE 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492016809 114 SGYRSYHmvinYTVYLPEGPKKLIAEVQIRTMAMNFWATV 153
Cdd:cd05399   94 NGYQSLH----LVVRGPEDKAGVLIEIQIRTILMHAWAEL 129
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
42-148 4.87e-13

(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 67.10  E-value: 4.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809  42 VIGRVKTVDSIKEKMKRRVISPDvietDMQDIAGIRIVTQFVDDIYKVVDLIHARddMEVVEER--DYIQNAKPSGYRSY 119
Cdd:COG0317  242 VSGRPKHIYSIYRKMQRKGLSFE----EIYDLYAFRIIVDTVDDCYAALGIVHSL--WKPIPGRfkDYIAIPKPNGYQSL 315

                         90       100
                 ....*....|....*....|....*....
gi 492016809 120 HMvinyTVYLPEGpkKLIaEVQIRTMAMN 148
Cdd:COG0317  316 HT----TVIGPDG--KPV-EVQIRTEEMH 337
relA PRK10872
(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional
 24-162 1.72e-10

(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional


Pssm-ID: 182797 [Multi-domain]  Cd Length: 743  Bit Score: 59.80  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809  24 RSLRQGFLTKGEHSPIefvIGRVKTVDSIKEKMKRRVISPDvietDMQDIAGIRIVTQFVDDIYKVVDLIHARDDMEVVE 103
Cdd:PRK10872 234 GHLRAEMKAEGVKAEV---YGRPKHIYSIWRKMQKKSLAFD----ELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDE 306

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492016809 104 ERDYIQNAKPSGYRSYHmvinyTVYLpeGPKKLIAEVQIRTMAMNFWATVEHTLNYKYQ 162
Cdd:PRK10872 307 FDDYVANPKPNGYQSIH-----TVVL--GPGGKTVEIQIRTRQMHEDAELGVAAHWKYK 358
PRK11092 PRK11092
bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;
42-148 2.59e-05

bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;


Pssm-ID: 236843 [Multi-domain]  Cd Length: 702  Bit Score: 44.34  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492016809  42 VIGRVKTVDSIKEKMKRRVISPDVIetdmQDIAGIRIVTQFVDDIYKVVDLIHARDDMEVVEERDYIQNAKPSGYRSYH- 120
Cdd:PRK11092 233 VSGREKHLYSIYCKMVLKEQRFHSI----MDIYAFRVIVDDSDTCYRVLGQMHSLYKPRPGRVKDYIAIPKANGYQSLHt 308

                         90       100
                 ....*....|....*....|....*....
gi 492016809 121 -MVinytvylpeGPKKLIAEVQIRTMAMN 148
Cdd:PRK11092 309 sMI---------GPHGVPVEVQIRTEDMD 328
 
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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