NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489737772|ref|WP_003641867|]
View 

MULTISPECIES: GTP pyrophosphokinase family protein [Lactiplantibacillus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 20-222 8.33e-72

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: 220.42  E-value: 8.33e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  20 PELLQAVDQLKAYSLRYEVAMKLVLDKLDYISREYElRYGYALIDSKQSRIKSPESIVGKMQRKHLPLTLNAVFNNLHDI 99
Cdd:COG2357    6 EEIREFLADYERFLPPYEAALEELKTKLEILLDEFE-KHGGSPIEHVTSRVKSPESIIEKLRRKGLPLTYENILEEITDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772 100 AGIRLIVRFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLHLILGVPVYTVDGPSIIEVELQVRTIAMNFWASL 179
Cdd:COG2357   85 AGIRIICYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLSDGPKGVPVEIQIRTIAMDFWAEL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489737772 180 EHELNYKKNVPHQDALRASLTKKAQLITELDQEMDDIKQRMYE 222
Cdd:COG2357  165 EHKLRYKYDGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEE 207
 
Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 20-222 8.33e-72

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: 220.42  E-value: 8.33e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  20 PELLQAVDQLKAYSLRYEVAMKLVLDKLDYISREYElRYGYALIDSKQSRIKSPESIVGKMQRKHLPLTLNAVFNNLHDI 99
Cdd:COG2357    6 EEIREFLADYERFLPPYEAALEELKTKLEILLDEFE-KHGGSPIEHVTSRVKSPESIIEKLRRKGLPLTYENILEEITDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772 100 AGIRLIVRFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLHLILGVPVYTVDGPSIIEVELQVRTIAMNFWASL 179
Cdd:COG2357   85 AGIRIICYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLSDGPKGVPVEIQIRTIAMDFWAEL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489737772 180 EHELNYKKNVPHQDALRASLTKKAQLITELDQEMDDIKQRMYE 222
Cdd:COG2357  165 EHKLRYKYDGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEE 207
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 68-188 2.26e-44

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: 144.61  E-value: 2.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772   68 SRIKSPESIVGKMQRKHLPltlnavFNNLHDIAGIRLIVRFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLHL 147
Cdd:pfam04607   1 GRVKSPYSIYEKMQRKGLL------FEEIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRSLHT 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489737772  148 ILGVpvytvdGPSIIEVELQVRTIAMNFWAS--LEHELNYKKN 188
Cdd:pfam04607  75 TVII------GPEGVPVEIQIRTIAMHFWAEygIAHHWRYKEG 111
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 68-188 2.21e-41

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: 136.93  E-value: 2.21e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772    68 SRIKSPESIVGKMQRKHlpltlNAVFNNLHDIAGIRLIVRFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLHl 147
Cdd:smart00954   1 GRVKHLYSIYKKMRRKG-----EISFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLH- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 489737772   148 ilgvpvYTVDGPSIIEVELQVRTIAMNFWASLEHELNYKKN 188
Cdd:smart00954  75 ------TTVIGPEGRPVEIQIRTILMHAWAELGHAAHYKYK 109
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 67-179 5.78e-31

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: 110.51  E-value: 5.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  67 QSRIKSPESIVGKMQRKHLPLTlnaVFNNLHDIAGIRLIVRFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLH 146
Cdd:cd05399   24 SGRVKSPYSIYEKLRRKGKDLP---ILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIPGRVKDYIAEPKENGYQSLH 100

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489737772 147 LILGVPVYTVDGPsiieVELQVRTIAMNFWASL 179
Cdd:cd05399  101 LVVRGPEDKAGVL----IEIQIRTILMHAWAEL 129
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
 35-220 9.92e-16

(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. RelA (EC 2.7.6.5) produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT (EC 3.1.7.2) 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. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 213552 [Multi-domain]  Cd Length: 683  Bit Score: 75.51  E-value: 9.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772   35 RYEVAMKLV-------LDKLDYISREYELRYGYALIDSK-QSRIKSPESIVGKMQRKhlpltlNAVFNNLHDIAGIRLIV 106
Cdd:TIGR00691 169 EYENIKSLVneqkvnrENKLEKFKSELEKRLEDSGIEAElEGRSKHLYSIYQKMTRK------GQNFDEIHDLLAIRIIV 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  107 RFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLHLilgvpvyTVDGPSIIEVELQVRTIAMN---------FWA 177
Cdd:TIGR00691 243 KSELDCYRVLGIIHLLFKPIPGRFKDYIASPKENGYQSLHT-------TVRGPKGLPVEIQIRTEDMDrvaeygiaaHWI 315

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 489737772  178 slehelnYKKNVPHQDALRASLTKKAQLItELDQEMDDIKQRM 220
Cdd:TIGR00691 316 -------YKEGNPQKEALIDDMRWLNYLV-EWQQESANFFEFI 350
PRK11092 PRK11092
bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;
50-174 7.24e-09

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


Pssm-ID: 236843 [Multi-domain]  Cd Length: 702  Bit Score: 55.51  E-value: 7.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  50 ISREYELRYGYALIDSKQS-RIKSPESIVGKMQRKHLPltlnavFNNLHDIAGIRLIVRflsDVKTVENLLATQADI--- 125
Cdd:PRK11092 216 ILSEIEGRLQEAGIPCRVSgREKHLYSIYCKMVLKEQR------FHSIMDIYAFRVIVD---DSDTCYRVLGQMHSLykp 286

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489737772 126 KVLRVKDYIHHPKANGYQSLHLILgvpvytvDGPSIIEVELQVRTIAMN 174
Cdd:PRK11092 287 RPGRVKDYIAIPKANGYQSLHTSM-------IGPHGVPVEVQIRTEDMD 328
 
Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 20-222 8.33e-72

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: 220.42  E-value: 8.33e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  20 PELLQAVDQLKAYSLRYEVAMKLVLDKLDYISREYElRYGYALIDSKQSRIKSPESIVGKMQRKHLPLTLNAVFNNLHDI 99
Cdd:COG2357    6 EEIREFLADYERFLPPYEAALEELKTKLEILLDEFE-KHGGSPIEHVTSRVKSPESIIEKLRRKGLPLTYENILEEITDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772 100 AGIRLIVRFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLHLILGVPVYTVDGPSIIEVELQVRTIAMNFWASL 179
Cdd:COG2357   85 AGIRIICYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLSDGPKGVPVEIQIRTIAMDFWAEL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489737772 180 EHELNYKKNVPHQDALRASLTKKAQLITELDQEMDDIKQRMYE 222
Cdd:COG2357  165 EHKLRYKYDGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEE 207
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 68-188 2.26e-44

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: 144.61  E-value: 2.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772   68 SRIKSPESIVGKMQRKHLPltlnavFNNLHDIAGIRLIVRFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLHL 147
Cdd:pfam04607   1 GRVKSPYSIYEKMQRKGLL------FEEIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRSLHT 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489737772  148 ILGVpvytvdGPSIIEVELQVRTIAMNFWAS--LEHELNYKKN 188
Cdd:pfam04607  75 TVII------GPEGVPVEIQIRTIAMHFWAEygIAHHWRYKEG 111
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 68-188 2.21e-41

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: 136.93  E-value: 2.21e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772    68 SRIKSPESIVGKMQRKHlpltlNAVFNNLHDIAGIRLIVRFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLHl 147
Cdd:smart00954   1 GRVKHLYSIYKKMRRKG-----EISFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLH- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 489737772   148 ilgvpvYTVDGPSIIEVELQVRTIAMNFWASLEHELNYKKN 188
Cdd:smart00954  75 ------TTVIGPEGRPVEIQIRTILMHAWAELGHAAHYKYK 109
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 67-179 5.78e-31

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: 110.51  E-value: 5.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  67 QSRIKSPESIVGKMQRKHLPLTlnaVFNNLHDIAGIRLIVRFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLH 146
Cdd:cd05399   24 SGRVKSPYSIYEKLRRKGKDLP---ILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIPGRVKDYIAEPKENGYQSLH 100

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489737772 147 LILGVPVYTVDGPsiieVELQVRTIAMNFWASL 179
Cdd:cd05399  101 LVVRGPEDKAGVL----IEIQIRTILMHAWAEL 129
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
 35-220 9.92e-16

(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. RelA (EC 2.7.6.5) produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT (EC 3.1.7.2) 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. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 213552 [Multi-domain]  Cd Length: 683  Bit Score: 75.51  E-value: 9.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772   35 RYEVAMKLV-------LDKLDYISREYELRYGYALIDSK-QSRIKSPESIVGKMQRKhlpltlNAVFNNLHDIAGIRLIV 106
Cdd:TIGR00691 169 EYENIKSLVneqkvnrENKLEKFKSELEKRLEDSGIEAElEGRSKHLYSIYQKMTRK------GQNFDEIHDLLAIRIIV 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  107 RFLSDVKTVENLLATQADIKVLRVKDYIHHPKANGYQSLHLilgvpvyTVDGPSIIEVELQVRTIAMN---------FWA 177
Cdd:TIGR00691 243 KSELDCYRVLGIIHLLFKPIPGRFKDYIASPKENGYQSLHT-------TVRGPKGLPVEIQIRTEDMDrvaeygiaaHWI 315

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 489737772  178 slehelnYKKNVPHQDALRASLTKKAQLItELDQEMDDIKQRM 220
Cdd:TIGR00691 316 -------YKEGNPQKEALIDDMRWLNYLV-EWQQESANFFEFI 350
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
69-174 1.74e-15

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 74.81  E-value: 1.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  69 RIKSPESIVGKMQRKHLPltlnavFNNLHDIAGIRLIVrflsdvKTVENLLAtqadikVL------------RVKDYIHH 136
Cdd:COG0317  245 RPKHIYSIYRKMQRKGLS------FEEIYDLYAFRIIV------DTVDDCYA------ALgivhslwkpipgRFKDYIAI 306

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489737772 137 PKANGYQSLHLilgvpvyTVDGPSIIEVELQVRTIAMN 174
Cdd:COG0317  307 PKPNGYQSLHT-------TVIGPDGKPVEVQIRTEEMH 337
PRK11092 PRK11092
bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;
50-174 7.24e-09

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


Pssm-ID: 236843 [Multi-domain]  Cd Length: 702  Bit Score: 55.51  E-value: 7.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  50 ISREYELRYGYALIDSKQS-RIKSPESIVGKMQRKHLPltlnavFNNLHDIAGIRLIVRflsDVKTVENLLATQADI--- 125
Cdd:PRK11092 216 ILSEIEGRLQEAGIPCRVSgREKHLYSIYCKMVLKEQR------FHSIMDIYAFRVIVD---DSDTCYRVLGQMHSLykp 286

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489737772 126 KVLRVKDYIHHPKANGYQSLHLILgvpvytvDGPSIIEVELQVRTIAMN 174
Cdd:PRK11092 287 RPGRVKDYIAIPKANGYQSLHTSM-------IGPHGVPVEVQIRTEDMD 328
relA PRK10872
(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional
 69-179 3.39e-08

(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional


Pssm-ID: 182797 [Multi-domain]  Cd Length: 743  Bit Score: 53.25  E-value: 3.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737772  69 RIKSPESIVGKMQRKHLpltlnaVFNNLHDIAGIRLIVRFLSD-------VKTVENLLATQADikvlrvkDYIHHPKANG 141
Cdd:PRK10872 252 RPKHIYSIWRKMQKKSL------AFDELFDVRAVRIVAERLQDcyaalgiVHTHYRHLPDEFD-------DYVANPKPNG 318

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489737772 142 YQSLHLIlgvpvytVDGPSIIEVELQVRTIAMNFWASL 179
Cdd:PRK10872 319 YQSIHTV-------VLGPGGKTVEIQIRTRQMHEDAEL 349
 
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