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Conserved domains on  [gi|1005573348|ref|WP_061665824|]
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MULTISPECIES: GTP pyrophosphokinase family protein [unclassified Bacillus (in: firmicutes)]

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 ...
 1-283 1.15e-51

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: 172.27  E-value: 1.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348   1 MEPSIKEDVSLVNMYENMIPKYNKLGINLTQAIELLLEEHSIQ----YLKVYYRIKESDSFMGKTDRK----RYIDPFNE 72
Cdd:COG2357     1 MSLLEEEIREFLADYERFLPPYEAALEELKTKLEILLDEFEKHggspIEHVTSRVKSPESIIEKLRRKglplTYENILEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348  73 VEDICGIRIICYYKSDIDKICNVINEEFDVLESQDKEELLKPDQFGYRSHHFIVKIKEEWLctpnyKGLADLKAEIQIRT 152
Cdd:COG2357    81 ITDIAGIRIICYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLS-----DGPKGVPVEIQIRT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348 153 NLMHTWAEIEHELGYKKEEDIPSEFRRKFSRISAKLEEADEQFEDLKSDISVYRDSRANSPVILDEDLNADNLQAFLDKY 232
Cdd:COG2357   156 IAMDFWAELEHKLRYKYDGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEEAQKEFEDKEAIAEESLAALLLLLEDLGV 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1005573348 233 FSDRKIYKDGASDLVSELKRLDINLPKLLDLHEKCKDLLLDLEEAERELFD 283
Cdd:COG2357   236 DLDFILAIELSELFLLDLELELAKLLRIAEEIAILRLLDLLESLGRDRLLD 286
 
Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 1-283 1.15e-51

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: 172.27  E-value: 1.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348   1 MEPSIKEDVSLVNMYENMIPKYNKLGINLTQAIELLLEEHSIQ----YLKVYYRIKESDSFMGKTDRK----RYIDPFNE 72
Cdd:COG2357     1 MSLLEEEIREFLADYERFLPPYEAALEELKTKLEILLDEFEKHggspIEHVTSRVKSPESIIEKLRRKglplTYENILEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348  73 VEDICGIRIICYYKSDIDKICNVINEEFDVLESQDKEELLKPDQFGYRSHHFIVKIKEEWLctpnyKGLADLKAEIQIRT 152
Cdd:COG2357    81 ITDIAGIRIICYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLS-----DGPKGVPVEIQIRT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348 153 NLMHTWAEIEHELGYKKEEDIPSEFRRKFSRISAKLEEADEQFEDLKSDISVYRDSRANSPVILDEDLNADNLQAFLDKY 232
Cdd:COG2357   156 IAMDFWAELEHKLRYKYDGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEEAQKEFEDKEAIAEESLAALLLLLEDLGV 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1005573348 233 FSDRKIYKDGASDLVSELKRLDINLPKLLDLHEKCKDLLLDLEEAERELFD 283
Cdd:COG2357   236 DLDFILAIELSELFLLDLELELAKLLRIAEEIAILRLLDLLESLGRDRLLD 286
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 49-172 3.25e-29

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: 108.04  E-value: 3.25e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348   49 YRIKESDSFMGKTDRKRYIdPFNEVEDICGIRIICYYKSDIDKICNVINEEFDVLESQDKEELLKPDQFGYRSHHFIVKI 128
Cdd:smart00954   1 GRVKHLYSIYKKMRRKGEI-SFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLHTTVIG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1005573348  129 KEewlctpnykglaDLKAEIQIRTNLMHTWAEIEHELGYKKEED 172
Cdd:smart00954  80 PE------------GRPVEIQIRTILMHAWAELGHAAHYKYKEG 111
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 28-161 1.69e-26

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: 101.66  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348  28 NLTQAIELLLEEHSIQYLK--VYYRIKESDSFMGKTDRK-RYIDPFNEVEDICGIRIICYYKSDIDKICNVINEEFDVLE 104
Cdd:cd05399     2 AALEEIADLLRDAGIIGRVasVSGRVKSPYSIYEKLRRKgKDLPILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1005573348 105 SQDKEELLKPDQFGYRSHHFIVKIKEEWlctpnykglADLKAEIQIRTNLMHTWAEI 161
Cdd:cd05399    82 GRVKDYIAEPKENGYQSLHLVVRGPEDK---------AGVLIEIQIRTILMHAWAEL 129
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 50-172 2.66e-22

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: 89.92  E-value: 2.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348  50 RIKESDSFMGKTDRKRyiDPFNEVEDICGIRIICYYKSDIDKICNVINEEFDVLESQDKEELLKPDQFGYRSHHFIVKIK 129
Cdd:pfam04607   2 RVKSPYSIYEKMQRKG--LLFEEIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRSLHTTVIIG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1005573348 130 EEwlctpnykglaDLKAEIQIRTNLMHTWAE--IEHELGYKKEED 172
Cdd:pfam04607  80 PE-----------GVPVEIQIRTIAMHFWAEygIAHHWRYKEGGD 113
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
 6-201 2.23e-05

(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: 46.23  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348   6 KEDVSLVNmyENMIPKYNKLGiNLTQAIELLLEEHSIQYlKVYYRIKESDSFMGKTDRKRyiDPFNEVEDICGIRIICYY 85
Cdd:TIGR00691 171 ENIKSLVN--EQKVNRENKLE-KFKSELEKRLEDSGIEA-ELEGRSKHLYSIYQKMTRKG--QNFDEIHDLLAIRIIVKS 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348  86 KSDIDKICNVINEEFDVLESQDKEELLKPDQFGYRSHHFIVKIKEewlctpnykglaDLKAEIQIRTNLMHTWAE----- 160
Cdd:TIGR00691 245 ELDCYRVLGIIHLLFKPIPGRFKDYIASPKENGYQSLHTTVRGPK------------GLPVEIQIRTEDMDRVAEygiaa 312

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1005573348 161 --IEHELGYKKEEDI-PSEFRRKFSRISAKLEEADEQFEDLKSD 201
Cdd:TIGR00691 313 hwIYKEGNPQKEALIdDMRWLNYLVEWQQESANFFEFIENLKSD 356
 
Name Accession Description Interval E-value
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
 1-283 1.15e-51

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: 172.27  E-value: 1.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348   1 MEPSIKEDVSLVNMYENMIPKYNKLGINLTQAIELLLEEHSIQ----YLKVYYRIKESDSFMGKTDRK----RYIDPFNE 72
Cdd:COG2357     1 MSLLEEEIREFLADYERFLPPYEAALEELKTKLEILLDEFEKHggspIEHVTSRVKSPESIIEKLRRKglplTYENILEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348  73 VEDICGIRIICYYKSDIDKICNVINEEFDVLESQDKEELLKPDQFGYRSHHFIVKIKEEWLctpnyKGLADLKAEIQIRT 152
Cdd:COG2357    81 ITDIAGIRIICYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVRVPVFLS-----DGPKGVPVEIQIRT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348 153 NLMHTWAEIEHELGYKKEEDIPSEFRRKFSRISAKLEEADEQFEDLKSDISVYRDSRANSPVILDEDLNADNLQAFLDKY 232
Cdd:COG2357   156 IAMDFWAELEHKLRYKYDGEIPEEIKRRLKRAAALLELLDEEMSEIRDEIEEAQKEFEDKEAIAEESLAALLLLLEDLGV 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1005573348 233 FSDRKIYKDGASDLVSELKRLDINLPKLLDLHEKCKDLLLDLEEAERELFD 283
Cdd:COG2357   236 DLDFILAIELSELFLLDLELELAKLLRIAEEIAILRLLDLLESLGRDRLLD 286
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
 49-172 3.25e-29

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: 108.04  E-value: 3.25e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348   49 YRIKESDSFMGKTDRKRYIdPFNEVEDICGIRIICYYKSDIDKICNVINEEFDVLESQDKEELLKPDQFGYRSHHFIVKI 128
Cdd:smart00954   1 GRVKHLYSIYKKMRRKGEI-SFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLHTTVIG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1005573348  129 KEewlctpnykglaDLKAEIQIRTNLMHTWAEIEHELGYKKEED 172
Cdd:smart00954  80 PE------------GRPVEIQIRTILMHAWAELGHAAHYKYKEG 111
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
 28-161 1.69e-26

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: 101.66  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348  28 NLTQAIELLLEEHSIQYLK--VYYRIKESDSFMGKTDRK-RYIDPFNEVEDICGIRIICYYKSDIDKICNVINEEFDVLE 104
Cdd:cd05399     2 AALEEIADLLRDAGIIGRVasVSGRVKSPYSIYEKLRRKgKDLPILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVIP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1005573348 105 SQDKEELLKPDQFGYRSHHFIVKIKEEWlctpnykglADLKAEIQIRTNLMHTWAEI 161
Cdd:cd05399    82 GRVKDYIAEPKENGYQSLHLVVRGPEDK---------AGVLIEIQIRTILMHAWAEL 129
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
 50-172 2.66e-22

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: 89.92  E-value: 2.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348  50 RIKESDSFMGKTDRKRyiDPFNEVEDICGIRIICYYKSDIDKICNVINEEFDVLESQDKEELLKPDQFGYRSHHFIVKIK 129
Cdd:pfam04607   2 RVKSPYSIYEKMQRKG--LLFEEIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRSLHTTVIIG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1005573348 130 EEwlctpnykglaDLKAEIQIRTNLMHTWAE--IEHELGYKKEED 172
Cdd:pfam04607  80 PE-----------GVPVEIQIRTIAMHFWAEygIAHHWRYKEGGD 113
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
 6-201 2.23e-05

(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: 46.23  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348   6 KEDVSLVNmyENMIPKYNKLGiNLTQAIELLLEEHSIQYlKVYYRIKESDSFMGKTDRKRyiDPFNEVEDICGIRIICYY 85
Cdd:TIGR00691 171 ENIKSLVN--EQKVNRENKLE-KFKSELEKRLEDSGIEA-ELEGRSKHLYSIYQKMTRKG--QNFDEIHDLLAIRIIVKS 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005573348  86 KSDIDKICNVINEEFDVLESQDKEELLKPDQFGYRSHHFIVKIKEewlctpnykglaDLKAEIQIRTNLMHTWAE----- 160
Cdd:TIGR00691 245 ELDCYRVLGIIHLLFKPIPGRFKDYIASPKENGYQSLHTTVRGPK------------GLPVEIQIRTEDMDRVAEygiaa 312

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1005573348 161 --IEHELGYKKEEDI-PSEFRRKFSRISAKLEEADEQFEDLKSD 201
Cdd:TIGR00691 313 hwIYKEGNPQKEALIdDMRWLNYLVEWQQESANFFEFIENLKSD 356
 
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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