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Conserved domains on  [gi|447000427|ref|WP_001077683|]
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MULTISPECIES: GTP pyrophosphokinase family protein [Staphylococcus]

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 ...
 1-211 8.16e-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: 267.80  E-value: 8.16e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427   1 MNQWDQFLTPYKQAVDELKVKLKGMRKQYEVGEqASPIEFVTGRVKPIASIIDKANKRQIP--FDRLREEMYDIAGLRMM 78
Cdd:COG2357   12 LADYERFLPPYEAALEELKTKLEILLDEFEKHG-GSPIEHVTSRVKSPESIIEKLRRKGLPltYENILEEITDIAGIRII 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427  79 CQFVEDIDVVVNILRQRKDFKVIEERDYIRNTKESGYRSYHVIIEYPIETLQGQKFILAEIQIRTLAMNFWATIEHTLRY 158
Cdd:COG2357   91 CYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLSDGPKGVPVEIQIRTIAMDFWAELEHKLRY 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447000427 159 KYDGAYPDEIQHRLERAAEAAYLLDEEMSEIKDEIQEAQKYYTQKRSKKHEND 211
Cdd:COG2357  171 KYDGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEEAQKEFEDKEAIAEESL 223
 
Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 1-211 8.16e-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: 267.80  E-value: 8.16e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427   1 MNQWDQFLTPYKQAVDELKVKLKGMRKQYEVGEqASPIEFVTGRVKPIASIIDKANKRQIP--FDRLREEMYDIAGLRMM 78
Cdd:COG2357   12 LADYERFLPPYEAALEELKTKLEILLDEFEKHG-GSPIEHVTSRVKSPESIIEKLRRKGLPltYENILEEITDIAGIRII 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427  79 CQFVEDIDVVVNILRQRKDFKVIEERDYIRNTKESGYRSYHVIIEYPIETLQGQKFILAEIQIRTLAMNFWATIEHTLRY 158
Cdd:COG2357   91 CYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLSDGPKGVPVEIQIRTIAMDFWAELEHKLRY 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447000427 159 KYDGAYPDEIQHRLERAAEAAYLLDEEMSEIKDEIQEAQKYYTQKRSKKHEND 211
Cdd:COG2357  171 KYDGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEEAQKEFEDKEAIAEESL 223
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 43-162 1.59e-46

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: 149.24  E-value: 1.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427   43 GRVKPIASIIDKANKRQIPFdrlrEEMYDIAGLRMMCQFVEDIDVVVNILRQRKDFKVIEERDYIRNTKESGYRSYHVII 122
Cdd:pfam04607   1 GRVKSPYSIYEKMQRKGLLF----EEIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRSLHTTV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 447000427  123 EYpietlqGQKFILAEIQIRTLAMNFWAT--IEHTLRYKYDG 162
Cdd:pfam04607  77 II------GPEGVPVEIQIRTIAMHFWAEygIAHHWRYKEGG 112
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 43-163 1.59e-40

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: 133.85  E-value: 1.59e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427    43 GRVKPIASIIDKANKRQipfDRLREEMYDIAGLRMMCQFVEDIDVVVNILRQRKDFKVIEERDYIRNTKESGYRSYHVII 122
Cdd:smart00954   1 GRVKHLYSIYKKMRRKG---EISFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLHTTV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 447000427   123 EYPIETlqgqkfiLAEIQIRTLAMNFWATIEHTLRYKYDGA 163
Cdd:smart00954  78 IGPEGR-------PVEIQIRTILMHAWAELGHAAHYKYKEG 111
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 36-152 1.19e-28

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: 103.97  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427  36 SPIEFVTGRVKPIASIIDKANKRQIPFdRLREEMYDIAGLRMMCQFVEDIDVVVNILRqrKDFKVI--EERDYIRNTKES 113
Cdd:cd05399   18 GRVASVSGRVKSPYSIYEKLRRKGKDL-PILDEITDLVGVRVVLLFVDDCYRVLDLLH--SLFKVIpgRVKDYIAEPKEN 94

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 447000427 114 GYRSYHVIIEYPIETLQgqkfILAEIQIRTLAMNFWATI 152
Cdd:cd05399   95 GYQSLHLVVRGPEDKAG----VLIEIQIRTILMHAWAEL 129
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
 12-146 1.93e-08

(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: 53.55  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427   12 KQAVDELKVKLKGMRKQYEVGEQASPIEF-VTGRVKPIASIIDKANKRQIPFDrlreEMYDIAGLRMMCQFVEDIDVVVN 90
Cdd:TIGR00691 178 NEQKVNRENKLEKFKSELEKRLEDSGIEAeLEGRSKHLYSIYQKMTRKGQNFD----EIHDLLAIRIIVKSELDCYRVLG 253

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 447000427   91 ILRqrKDFKVIEER--DYIRNTKESGYRSYHViieypieTLQGQKFILAEIQIRTLAM 146
Cdd:TIGR00691 254 IIH--LLFKPIPGRfkDYIASPKENGYQSLHT-------TVRGPKGLPVEIQIRTEDM 302
relA PRK10872
(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional
 41-192 8.08e-06

(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional


Pssm-ID: 182797 [Multi-domain]  Cd Length: 743  Bit Score: 45.94  E-value: 8.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427  41 VTGRVKPIASIIDKANKRQIPFDrlreEMYDIAGLRMMCQFVED----IDVVVNILRQRKDfkviEERDYIRNTKESGYR 116
Cdd:PRK10872 249 VYGRPKHIYSIWRKMQKKSLAFD----ELFDVRAVRIVAERLQDcyaaLGIVHTHYRHLPD----EFDDYVANPKPNGYQ 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427 117 SYHVIIEYPietlqGQKFIlaEIQIRTLAMNFWATIEHTLRYKY-DGA--------YPDEIQ--HRL----ERAAEAAYL 181
Cdd:PRK10872 321 SIHTVVLGP-----GGKTV--EIQIRTRQMHEDAELGVAAHWKYkEGAaagggrsgHEDRIAwlRKLiawqEEMADSGEM 393

                        170
                 ....*....|.
gi 447000427 182 LDEEMSEIKDE 192
Cdd:PRK10872 394 LDEVRSQVFDD 404
 
Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 1-211 8.16e-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: 267.80  E-value: 8.16e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427   1 MNQWDQFLTPYKQAVDELKVKLKGMRKQYEVGEqASPIEFVTGRVKPIASIIDKANKRQIP--FDRLREEMYDIAGLRMM 78
Cdd:COG2357   12 LADYERFLPPYEAALEELKTKLEILLDEFEKHG-GSPIEHVTSRVKSPESIIEKLRRKGLPltYENILEEITDIAGIRII 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427  79 CQFVEDIDVVVNILRQRKDFKVIEERDYIRNTKESGYRSYHVIIEYPIETLQGQKFILAEIQIRTLAMNFWATIEHTLRY 158
Cdd:COG2357   91 CYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLSDGPKGVPVEIQIRTIAMDFWAELEHKLRY 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447000427 159 KYDGAYPDEIQHRLERAAEAAYLLDEEMSEIKDEIQEAQKYYTQKRSKKHEND 211
Cdd:COG2357  171 KYDGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEEAQKEFEDKEAIAEESL 223
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 43-162 1.59e-46

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: 149.24  E-value: 1.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427   43 GRVKPIASIIDKANKRQIPFdrlrEEMYDIAGLRMMCQFVEDIDVVVNILRQRKDFKVIEERDYIRNTKESGYRSYHVII 122
Cdd:pfam04607   1 GRVKSPYSIYEKMQRKGLLF----EEIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRSLHTTV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 447000427  123 EYpietlqGQKFILAEIQIRTLAMNFWAT--IEHTLRYKYDG 162
Cdd:pfam04607  77 II------GPEGVPVEIQIRTIAMHFWAEygIAHHWRYKEGG 112
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 43-163 1.59e-40

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: 133.85  E-value: 1.59e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427    43 GRVKPIASIIDKANKRQipfDRLREEMYDIAGLRMMCQFVEDIDVVVNILRQRKDFKVIEERDYIRNTKESGYRSYHVII 122
Cdd:smart00954   1 GRVKHLYSIYKKMRRKG---EISFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLHTTV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 447000427   123 EYPIETlqgqkfiLAEIQIRTLAMNFWATIEHTLRYKYDGA 163
Cdd:smart00954  78 IGPEGR-------PVEIQIRTILMHAWAELGHAAHYKYKEG 111
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 36-152 1.19e-28

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: 103.97  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427  36 SPIEFVTGRVKPIASIIDKANKRQIPFdRLREEMYDIAGLRMMCQFVEDIDVVVNILRqrKDFKVI--EERDYIRNTKES 113
Cdd:cd05399   18 GRVASVSGRVKSPYSIYEKLRRKGKDL-PILDEITDLVGVRVVLLFVDDCYRVLDLLH--SLFKVIpgRVKDYIAEPKEN 94

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 447000427 114 GYRSYHVIIEYPIETLQgqkfILAEIQIRTLAMNFWATI 152
Cdd:cd05399   95 GYQSLHLVVRGPEDKAG----VLIEIQIRTILMHAWAEL 129
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
12-147 1.27e-09

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 57.09  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427  12 KQAVDELKVKLKGMRKQYEVgeqaspiefvTGRVKPIASIIDKANKRQIPFdrlrEEMYDIAGLRMMCQFVEDIDVVVNI 91
Cdd:COG0317  223 EEIIEELKEELAEAGIKAEV----------SGRPKHIYSIYRKMQRKGLSF----EEIYDLYAFRIIVDTVDDCYAALGI 288

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 447000427  92 LRQRkdFKVIEER--DYIRNTKESGYRSYHVIIEYPietlQGQKFilaEIQIRTLAMN 147
Cdd:COG0317  289 VHSL--WKPIPGRfkDYIAIPKPNGYQSLHTTVIGP----DGKPV---EVQIRTEEMH 337
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
 12-146 1.93e-08

(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: 53.55  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427   12 KQAVDELKVKLKGMRKQYEVGEQASPIEF-VTGRVKPIASIIDKANKRQIPFDrlreEMYDIAGLRMMCQFVEDIDVVVN 90
Cdd:TIGR00691 178 NEQKVNRENKLEKFKSELEKRLEDSGIEAeLEGRSKHLYSIYQKMTRKGQNFD----EIHDLLAIRIIVKSELDCYRVLG 253

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 447000427   91 ILRqrKDFKVIEER--DYIRNTKESGYRSYHViieypieTLQGQKFILAEIQIRTLAM 146
Cdd:TIGR00691 254 IIH--LLFKPIPGRfkDYIASPKENGYQSLHT-------TVRGPKGLPVEIQIRTEDM 302
relA PRK10872
(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional
 41-192 8.08e-06

(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional


Pssm-ID: 182797 [Multi-domain]  Cd Length: 743  Bit Score: 45.94  E-value: 8.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427  41 VTGRVKPIASIIDKANKRQIPFDrlreEMYDIAGLRMMCQFVED----IDVVVNILRQRKDfkviEERDYIRNTKESGYR 116
Cdd:PRK10872 249 VYGRPKHIYSIWRKMQKKSLAFD----ELFDVRAVRIVAERLQDcyaaLGIVHTHYRHLPD----EFDDYVANPKPNGYQ 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447000427 117 SYHVIIEYPietlqGQKFIlaEIQIRTLAMNFWATIEHTLRYKY-DGA--------YPDEIQ--HRL----ERAAEAAYL 181
Cdd:PRK10872 321 SIHTVVLGP-----GGKTV--EIQIRTRQMHEDAELGVAAHWKYkEGAaagggrsgHEDRIAwlRKLiawqEEMADSGEM 393

                        170
                 ....*....|.
gi 447000427 182 LDEEMSEIKDE 192
Cdd:PRK10872 394 LDEVRSQVFDD 404
 
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.
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