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Conserved domains on  [gi|1708321120|gb|QDQ42814|]
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tetrapyrrole methylase family protein/MazG family protein [Methylacidiphilum kamchatkense Kam1]

Protein Classification

YabN family protein( domain architecture ID 11467694)

YabN family protein contains an N-terminal S-AdoMet-dependent tetrapyrrole methylase domain and a MazG family nucleoside triphosphate pyrophosphohydrolase domain, similar to Bacillus subtilis protein YabN

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 8-259 9.71e-127

Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only];


:

Pssm-ID: 443156 [Multi-domain]  Cd Length: 268  Bit Score: 360.19  E-value: 9.71e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120   8 PTDPLLRILSIMTILRSPQGCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNFS 87
Cdd:COG3956     7 PLYAFERLLEIMARLRDPDGCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLLQVVFHAQIAEEEGAFD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  88 FLEVLDDLCTKLIRRHPHVFGTESATTTDEVHKHWEKIKKAEKPH----RESLFDGIPSLLPPLLKAIKLQSRASKMQLD 163
Cdd:COG3956    87 FDDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAEkgegRKSVLDGVPRSLPALMRAYKLQKKAARVGFD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120 164 WTSPEGPLLKMEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKRCRFVEKELKDKANP 243
Cdd:COG3956   167 WPDVEGVLDKVEEELAELKEALASGDQEAIEEELGDLLFALVNLARHLGIDPEEALRRANRKFERRFRYIEAAAAEQGKS 246

                         250
                  ....*....|....*....
gi 1708321120 244 ---VSPEELDRLWERAKEE 259
Cdd:COG3956   247 ledLSLEEMDALWQEAKKA 265
 
Name Accession Description Interval E-value
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 8-259 9.71e-127

Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only];


Pssm-ID: 443156 [Multi-domain]  Cd Length: 268  Bit Score: 360.19  E-value: 9.71e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120   8 PTDPLLRILSIMTILRSPQGCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNFS 87
Cdd:COG3956     7 PLYAFERLLEIMARLRDPDGCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLLQVVFHAQIAEEEGAFD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  88 FLEVLDDLCTKLIRRHPHVFGTESATTTDEVHKHWEKIKKAEKPH----RESLFDGIPSLLPPLLKAIKLQSRASKMQLD 163
Cdd:COG3956    87 FDDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAEkgegRKSVLDGVPRSLPALMRAYKLQKKAARVGFD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120 164 WTSPEGPLLKMEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKRCRFVEKELKDKANP 243
Cdd:COG3956   167 WPDVEGVLDKVEEELAELKEALASGDQEAIEEELGDLLFALVNLARHLGIDPEEALRRANRKFERRFRYIEAAAAEQGKS 246

                         250
                  ....*....|....*....
gi 1708321120 244 ---VSPEELDRLWERAKEE 259
Cdd:COG3956   247 ledLSLEEMDALWQEAKKA 265
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 8-259 1.18e-109

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 316.72  E-value: 1.18e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120   8 PTDPLLRILSIMTILRSPQ-GCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNF 86
Cdd:PRK09562    5 TSEAIDRLLEIMARLRDPEgGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQVVFHAQMAEEQGAF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  87 SFLEVLDDLCTKLIRRHPHVFGTESATTTDEVHKHWEKIKKAEKPHReSLFDGIPSLLPPLLKAIKLQSRASKMQLDWTS 166
Cdd:PRK09562   85 DFADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIKAEERAES-SVLDGIPRGLPALMRAYKIQKKAARVGFDWES 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120 167 PEGPLLKMEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKRCRFVEKELKDKANP--- 243
Cdd:PRK09562  164 LEPVLDKVEEEIDELKEALAQGDQAKIEEEFGDLLFALVNLARHLGIDPEAALRKANAKFERRFRAVEQLAAAQGKTled 243

                         250
                  ....*....|....*.
gi 1708321120 244 VSPEELDRLWERAKEE 259
Cdd:PRK09562  244 ASLEEMDALWQEAKRQ 259
mazG TIGR00444
MazG family protein; This family of prokaryotic proteins has no known function. It includes ...
 18-257 6.33e-79

MazG family protein; This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli. [Unknown function, General]


Pssm-ID: 273082 [Multi-domain]  Cd Length: 248  Bit Score: 238.57  E-value: 6.33e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  18 IMTILRSPQ-GCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNFSFLEVLDDLC 96
Cdd:TIGR00444   1 IIAQLRDPEnGCPWDKKQTFQSLIPYTLEETYEVLEAIAREDFDDLREELGDLLLQVVFYAQMAQEEGYFDFDDVCAGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  97 TKLIRRHPHVFGTESATTTDEVHKHWEKIKKAEKPHRE--SLFDGIPSLLPPLLKAIKLQSRASKMQLDWTSPEGPLLKM 174
Cdd:TIGR00444  81 EKLVRRHPHVFADVKAEDESEVLARWEQIKAEEKAQKAqtSALDDVPRTLPALMRAAKIQKRCAKVGFDWEDVSPVWDKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120 175 EEELQEIKEAYKEKDLE--KIKKEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKRCRFVEKELKDKANP---VSPEEL 249
Cdd:TIGR00444 161 YEELDEVMYEARQAVVEqnKLEEEMGDLLFATVNLARHLKTDAEIALQKANEKFERRFREVERIVAARGLEltgVDLEEM 240


                  ....*...
gi 1708321120 250 DRLWERAK 257
Cdd:TIGR00444 241 EELWQQVK 248
NTP-PPase_MazG_Nterm cd11528
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ...
 14-126 4.05e-62

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage.


Pssm-ID: 212135  Cd Length: 114  Bit Score: 190.80  E-value: 4.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  14 RILSIMTILRSPQGCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNFSFLEVLD 93
Cdd:cd11528     2 RLVEIVARLRGPGGCPWDREQTHESLRPYLLEEAYELVEAIEEGDPDNLREELGDVLLQVLFHAQIAEEEGAFDLDDVID 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1708321120  94 DLCTKLIRRHPHVFGTESATTTDEVHKHWEKIK 126
Cdd:cd11528    82 GLTEKLIRRHPHVFGDEKAETAEEVLRNWEKIK 114
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 34-107 7.19e-32

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 112.31  E-value: 7.19e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708321120  34 QTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNFSFLEVLDDLCTKLIRRHPHVF 107
Cdd:pfam03819   1 QTHETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRRHPHVF 74
 
Name Accession Description Interval E-value
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 8-259 9.71e-127

Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only];


Pssm-ID: 443156 [Multi-domain]  Cd Length: 268  Bit Score: 360.19  E-value: 9.71e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120   8 PTDPLLRILSIMTILRSPQGCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNFS 87
Cdd:COG3956     7 PLYAFERLLEIMARLRDPDGCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLLQVVFHAQIAEEEGAFD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  88 FLEVLDDLCTKLIRRHPHVFGTESATTTDEVHKHWEKIKKAEKPH----RESLFDGIPSLLPPLLKAIKLQSRASKMQLD 163
Cdd:COG3956    87 FDDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAEkgegRKSVLDGVPRSLPALMRAYKLQKKAARVGFD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120 164 WTSPEGPLLKMEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKRCRFVEKELKDKANP 243
Cdd:COG3956   167 WPDVEGVLDKVEEELAELKEALASGDQEAIEEELGDLLFALVNLARHLGIDPEEALRRANRKFERRFRYIEAAAAEQGKS 246

                         250
                  ....*....|....*....
gi 1708321120 244 ---VSPEELDRLWERAKEE 259
Cdd:COG3956   247 ledLSLEEMDALWQEAKKA 265
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 8-259 1.18e-109

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 316.72  E-value: 1.18e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120   8 PTDPLLRILSIMTILRSPQ-GCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNF 86
Cdd:PRK09562    5 TSEAIDRLLEIMARLRDPEgGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQVVFHAQMAEEQGAF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  87 SFLEVLDDLCTKLIRRHPHVFGTESATTTDEVHKHWEKIKKAEKPHReSLFDGIPSLLPPLLKAIKLQSRASKMQLDWTS 166
Cdd:PRK09562   85 DFADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIKAEERAES-SVLDGIPRGLPALMRAYKIQKKAARVGFDWES 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120 167 PEGPLLKMEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKRCRFVEKELKDKANP--- 243
Cdd:PRK09562  164 LEPVLDKVEEEIDELKEALAQGDQAKIEEEFGDLLFALVNLARHLGIDPEAALRKANAKFERRFRAVEQLAAAQGKTled 243

                         250
                  ....*....|....*.
gi 1708321120 244 VSPEELDRLWERAKEE 259
Cdd:PRK09562  244 ASLEEMDALWQEAKRQ 259
mazG TIGR00444
MazG family protein; This family of prokaryotic proteins has no known function. It includes ...
 18-257 6.33e-79

MazG family protein; This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli. [Unknown function, General]


Pssm-ID: 273082 [Multi-domain]  Cd Length: 248  Bit Score: 238.57  E-value: 6.33e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  18 IMTILRSPQ-GCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNFSFLEVLDDLC 96
Cdd:TIGR00444   1 IIAQLRDPEnGCPWDKKQTFQSLIPYTLEETYEVLEAIAREDFDDLREELGDLLLQVVFYAQMAQEEGYFDFDDVCAGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  97 TKLIRRHPHVFGTESATTTDEVHKHWEKIKKAEKPHRE--SLFDGIPSLLPPLLKAIKLQSRASKMQLDWTSPEGPLLKM 174
Cdd:TIGR00444  81 EKLVRRHPHVFADVKAEDESEVLARWEQIKAEEKAQKAqtSALDDVPRTLPALMRAAKIQKRCAKVGFDWEDVSPVWDKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120 175 EEELQEIKEAYKEKDLE--KIKKEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKRCRFVEKELKDKANP---VSPEEL 249
Cdd:TIGR00444 161 YEELDEVMYEARQAVVEqnKLEEEMGDLLFATVNLARHLKTDAEIALQKANEKFERRFREVERIVAARGLEltgVDLEEM 240


                  ....*...
gi 1708321120 250 DRLWERAK 257
Cdd:TIGR00444 241 EELWQQVK 248
PRK12334 PRK12334
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 5-234 9.98e-67

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 237065 [Multi-domain]  Cd Length: 277  Bit Score: 208.37  E-value: 9.98e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120   5 DSLPTDPLLRILSIMTILRSPqgCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEG 84
Cdd:PRK12334   57 DDQPGARLLDAVAVMDRLRSP--GPWESEQTHRSLARYLLEETYELLDAIESGDRDELREELGDVLLQVLFHARIAEEAP 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  85 N--FSFLEVLDDLCTKLIRRHPHVFGTESATTTDEVHKHWEKIKKAEKpHRESLFDGIPSLLPPLLKAIKLQSRASKMQL 162
Cdd:PRK12334  135 EdpFDIDDVAATLVAKLVRRHPHVFADGEAISLEEQLAQWEARKAAEK-ARTSVLDGVPLGQPALALAAKVLSRARKAGL 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708321120 163 DWTSPEGpllkmeeelqEIKEAykekdlekikkEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKRCRFVE 234
Cdd:PRK12334  214 PVPLAPA----------EDSED-----------ELGALLLALVAVAVAAGVDAEAALRAAVRDFRDRIRAAE 264
NTP-PPase_MazG_Nterm cd11528
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ...
 14-126 4.05e-62

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage.


Pssm-ID: 212135  Cd Length: 114  Bit Score: 190.80  E-value: 4.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  14 RILSIMTILRSPQGCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNFSFLEVLD 93
Cdd:cd11528     2 RLVEIVARLRGPGGCPWDREQTHESLRPYLLEEAYELVEAIEEGDPDNLREELGDVLLQVLFHAQIAEEEGAFDLDDVID 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1708321120  94 DLCTKLIRRHPHVFGTESATTTDEVHKHWEKIK 126
Cdd:cd11528    82 GLTEKLIRRHPHVFGDEKAETAEEVLRNWEKIK 114
PRK12333 PRK12333
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 14-231 3.21e-51

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 237064 [Multi-domain]  Cd Length: 204  Bit Score: 166.13  E-value: 3.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  14 RILSIMTILRSPQGCPWDREQTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNFSFLEVLD 93
Cdd:PRK12333    3 RLLEVMRRLRGPDGCPWDREQTHESLRPYLLEEAAEAVDALSEGDPQELAEELGDVLLQVAFHSVIAEEEGRFTYPDVER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  94 DLCTKLIRRHPHVFGTESATTTDEVHKHWEKIKKAEKPHRE-SLFDGIPSLLPPLLKAIKLQsraSKMQLDWTSPEGpll 172
Cdd:PRK12333   83 GIVEKLIRRHPHVFGDVQVSGPEEVVANWQAIKAAERGGGPrSAAERVPASLGALARAAELQ---KKLGREAGSREG--- 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1708321120 173 kMEEELQEikeaykekdlekikKEIGDLIFSAINFARLLGIDPEEAMKASLltfEKRCR 231
Cdd:PRK12333  157 -VIAALEE--------------GGVAEALWAVVAWARAEGIDPEIALRERT---EKACA 197
NTP-PPase_MazG_Cterm cd11529
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG ...
 145-257 7.99e-42

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs'; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the C-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer. Each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active sites and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity, along with structural features such as EEXX(E/D) motifs and key basic catalytic residues. It has been shown that the C-terminus NTPase activity is responsible for regulation of bacterial cell survival under nutritional stress.


Pssm-ID: 212136  Cd Length: 116  Bit Score: 139.14  E-value: 7.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120 145 PPLLKAIKLQSRASKMQLDWTSPEGPLLKMEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKASLL 224
Cdd:cd11529     1 PALMRAQKLQKRAAKVGFDWPDAEGVLDKVEEELAELKEALASGDKEEIEEELGDLLFSLVNLARFLGVDPEEALRRANR 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1708321120 225 TFEKRCRFVEKELKDKANP---VSPEELDRLWERAK 257
Cdd:cd11529    81 KFERRFRYMEELAAEQGKDledLSLEELDALWEEAK 116
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 34-107 7.19e-32

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 112.31  E-value: 7.19e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708321120  34 QTHKSLKAKLIEECYELIEAIDSEDMASMKEELGDILLHVLFHAQIAQEEGNFSFLEVLDDLCTKLIRRHPHVF 107
Cdd:pfam03819   1 QTHETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRRHPHVF 74
NTP-PPase_u3 cd11540
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 167-222 6.49e-07

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria and archaea, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D].


Pssm-ID: 212147  Cd Length: 76  Bit Score: 46.08  E-value: 6.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1708321120 167 PEGPLLKMEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKAS 222
Cdd:cd11540    21 PRKQLLKLVEEVGELSEAIAKNKQEEIKDSIGDVLVVLIILCAQLGLSLEECLEIA 76
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 166-230 1.62e-05

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 41.81  E-value: 1.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708321120 166 SPEGPLLKMEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLL----GIDPEEAMKASLLTFEKRC 230
Cdd:pfam03819   2 THETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAeeegGFDLEDVFQRILEKLIRRH 70
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
163-229 7.53e-05

NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];


Pssm-ID: 441300  Cd Length: 95  Bit Score: 40.56  E-value: 7.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120 163 DWTSPEGP---LLKMEEELQEIKEAY----------KEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKR 229
Cdd:COG1694    15 GWGQYHSPknlAAALTEEVGELAEAFqwltgeqskkDPEKKEELAEELADVLIYLLCLANQLGIDLEEAFEEKMEKNEKR 94
NTP-PPase_BsYpjD cd11531
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative ...
 171-229 1.21e-04

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative pyrophosphatase YpjD from Bacillus subtilis and its bacterial homologs; This family includes a putative pyrophosphatase Ypjd from Bacillus subtilis (BsYpjD) and its homologs. Although its biological role has not been described in detail, BsYpjD shows significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, BsYpjD contains a single MazG-like domain.


Pssm-ID: 212138  Cd Length: 93  Bit Score: 39.98  E-value: 1.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708321120 171 LLKMEEELQEIKEA---------YKEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKR 229
Cdd:cd11531    25 LARLTEEVGELAREinhrygekpKPGEDEGELEEELADILFVLTCLANQLGIDLEEAFKRTMEKKETR 92
NTP-PPase_u4 cd11541
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 189-229 7.67e-04

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D].


Pssm-ID: 212148  Cd Length: 91  Bit Score: 37.59  E-value: 7.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1708321120 189 DLEKIKKEIGDLIFSAINFARLLGIDPEEAMKASLLTFEKR 229
Cdd:cd11541    50 DKEALAEELGDVLWYLAALANVLGISLEEIAEANIAKLRSR 90
NTP-PPase_DR2231_like cd11530
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 174-221 1.07e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Deinococcus radiodurans DR2231 protein and its bacterial homologs; This family includes a MazG-like NTP-PPase from Deinococcus radiodurans (DR2231), a putative NTP-PPase YP_001813558.1 from Exiguobacterium sibiricum and their bacterial homologs. DR2231 shows significant structural resemblance to MazG proteins, but is functionally related to the dimeric dUTPases. It can hydrolyze dUTP into dUMP. DR2231-like proteins contain a well conserved divalent ion binding motif, EXXEX(12-28)EXXD, which is the identity signature for the all-alpha-helical NTP-PPase superfamily. Unlike normal dimeric dUTPase-like proteins with a central four-helix bundle forming the active site, YP_001813558.1 displays a very unusual interlaced segment-swapped dimer. It potentially prefers to hydrolyze dCTPs or its derivatives. YP_001813558.1-like proteins contain a variant divalent ion binding motif, EXXEX(12-28)AXXD.


Pssm-ID: 212137  Cd Length: 88  Bit Score: 37.25  E-value: 1.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1708321120 174 MEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKA 221
Cdd:cd11530    33 LAEELAELAEALKKGDMVELADALADLLYVAYGTAVEHGIDLDAAFAE 80
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
28-77 1.12e-03

NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];


Pssm-ID: 441300  Cd Length: 95  Bit Score: 37.48  E-value: 1.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708321120  28 CPWDREQTHKSLKAKLIEECYELIEAI----------DSEDMASMKEELGDILLHVLFHA 77
Cdd:COG1694    14 RGWGQYHSPKNLAAALTEEVGELAEAFqwltgeqskkDPEKKEELAEELADVLIYLLCLA 73
NTP-PPase_SsMazG cd11535
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Sulfolobus ...
 165-221 1.29e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Sulfolobus solfataricus (Ss) and its homologs from archaea and bacteria; This family includes a MazG-like protein from Sulfolobus solfataricus (SsMazG) and its homologs from archaea and bacteria. Although its biological roles remain still unclear, SsMazG shows significant sequence similarity to the NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, SsMazG contains a single MazG-like domain. It is predicted that SsMazG might participate in house-cleaning by preventing incorporation of the oxidation product 2-oxo-(d)ATP (iso-dGTP), a mutagenic derivative of ATP, into DNA.


Pssm-ID: 212142  Cd Length: 76  Bit Score: 36.80  E-value: 1.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1708321120 165 TSPEGPLLKMEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLLGIDPEEAMKA 221
Cdd:cd11535    17 RGVEKTFLWLVEEVGELAKALRKNDGENIEEELADVFAWLLSLANLLGIDLEEAFKK 73
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 173-217 2.45e-03

Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the histidine biosynthetic pathway.


Pssm-ID: 426294  Cd Length: 83  Bit Score: 36.06  E-value: 2.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1708321120 173 KMEEELQEIKEAYKEKDLEKIKKEIGDLIFSAINFARLLGIDPEE 217
Cdd:pfam01503  30 KIGEEAVELLEAAKAGDLAELADELADLLYHTYGLLVLQGVDLDA 74
NTP-PPase_u3 cd11540
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 42-70 3.14e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria and archaea, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D].


Pssm-ID: 212147  Cd Length: 76  Bit Score: 35.68  E-value: 3.14e-03
                          10        20
                  ....*....|....*....|....*....
gi 1708321120  42 KLIEECYELIEAIDSEDMASMKEELGDIL 70
Cdd:cd11540    27 KLVEEVGELSEAIAKNKQEEIKDSIGDVL 55
NTP-PPase_COG4997 cd11532
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 37-70 6.47e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from archaea and bacteria; The family includes some uncharacterized hypothetical proteins from archaea and bacteria. Although their biological roles remain unclear, the family members show significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, the family contains a single MazG-like domain.


Pssm-ID: 212139  Cd Length: 95  Bit Score: 35.21  E-value: 6.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1708321120  37 KSLKAKLIEECYELIEAIDSEDMasmkEELGDIL 70
Cdd:cd11532    32 EALKKKLVEEAAEYAEAKTEDSL----EELADLL 61
 
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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