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Conserved domains on  [gi|503764593|ref|WP_013998669|]
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manganese-dependent inorganic pyrophosphatase [Methanococcus maripaludis]

Protein Classification

manganese-dependent inorganic pyrophosphatase( domain architecture ID 11480923)

manganese-dependent inorganic pyrophosphatase catalyzes the hydrolysis of pyrophosphate to phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-307 2.22e-158

putative manganese-dependent inorganic pyrophosphatase; Provisional


:

Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 443.88  E-value: 2.22e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593   1 MMYVVGHKNPDSDSICSAIALAYFL-----DAFPARLGELNPESQFILKRFGLMEPELIKTAEGK-ELFLVDHAEKSQNL 74
Cdd:PRK05427   3 KILVFGHKNPDTDSICSAIAYAYLKkalglDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEvQVILVDHNEFQQSP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593  75 DDFDKGKLIGIIDHHKIG-ISTTEPIIYLSKPVGSTASVISELYfrgildiiGGKNKELKADIAGVLLSAILSDTLLFKS 153
Cdd:PRK05427  83 DDIDEATVVGVVDHHRLGnFETSNPLYYRIEPVGCTATILYKMF--------KENGVEIPKEIAGLMLSAILSDTLLFKS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593 154 PTATPLDKELAEKLADIAGIsDITAYGMEMLTAKSTVGKMTSEEILHIDYKPFDMSGKKVGIGQAEVIDMSEVASKKEAI 233
Cdd:PRK05427 155 PTTTEQDKAAAEELAEIAGV-DIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAEL 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503764593 234 QNLIDEMIEKEGYDMVLFIVTDIMKEGSEVLVAG-NKYAFETAFELKLDGKSVFIDGLMSRKKQVVPPLEKYYSN 307
Cdd:PRK05427 234 EAAMKAVKAEEGYDLFLLLITDILNEGSELLVVGdDKDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFAA 308
 
Name Accession Description Interval E-value
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-307 2.22e-158

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 443.88  E-value: 2.22e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593   1 MMYVVGHKNPDSDSICSAIALAYFL-----DAFPARLGELNPESQFILKRFGLMEPELIKTAEGK-ELFLVDHAEKSQNL 74
Cdd:PRK05427   3 KILVFGHKNPDTDSICSAIAYAYLKkalglDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEvQVILVDHNEFQQSP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593  75 DDFDKGKLIGIIDHHKIG-ISTTEPIIYLSKPVGSTASVISELYfrgildiiGGKNKELKADIAGVLLSAILSDTLLFKS 153
Cdd:PRK05427  83 DDIDEATVVGVVDHHRLGnFETSNPLYYRIEPVGCTATILYKMF--------KENGVEIPKEIAGLMLSAILSDTLLFKS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593 154 PTATPLDKELAEKLADIAGIsDITAYGMEMLTAKSTVGKMTSEEILHIDYKPFDMSGKKVGIGQAEVIDMSEVASKKEAI 233
Cdd:PRK05427 155 PTTTEQDKAAAEELAEIAGV-DIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAEL 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503764593 234 QNLIDEMIEKEGYDMVLFIVTDIMKEGSEVLVAG-NKYAFETAFELKLDGKSVFIDGLMSRKKQVVPPLEKYYSN 307
Cdd:PRK05427 234 EAAMKAVKAEEGYDLFLLLITDILNEGSELLVVGdDKDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFAA 308
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-306 1.20e-146

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 414.17  E-value: 1.20e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593   1 MMYVVGHKNPDSDSICSAIALAYFL-----DAFPARLGELNPESQFILKRFGLMEPELIKT-AEGKELFLVDHAEKSQNL 74
Cdd:COG1227    3 KILVFGHKNPDTDSICSAIAYAYLKnqlgeDAEAVRLGEPNPETAFVLDYFGVEAPELIEDvAAGKKVILVDHNELAQSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593  75 DDFDKGKLIGIIDHHKIG-ISTTEPIIYLSKPVGSTASVISELYFRgildiiggKNKELKADIAGVLLSAILSDTLLFKS 153
Cdd:COG1227   83 DGIDEAEILEIIDHHRIGdFETAAPLYIRIEPVGCTATIIAKLYKE--------NGVEIPKEIAGLMLSAILSDTLLFKS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593 154 PTATPLDKELAEKLADIAGIsDITAYGMEMLTAKSTVGKMTSEEILHIDYKPFDMSGKKVGIGQAEVIDMSEVASKKEAI 233
Cdd:COG1227  155 PTTTDEDREAAEELAEIAGV-DIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDEL 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503764593 234 QNLIDEMIEKEGYDMVLFIVTDIMKEGSEVLVAGNK-YAFETAFELKLDGKSVFIDGLMSRKKQVVPPLEKYYS 306
Cdd:COG1227  234 EAAMKKVKAEKGYDLVLLLVTDILNEGSTLLVVGDDvAVVEKAFGVTLENNTVWLPGVVSRKKQVVPPLTEAFA 307
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
183-304 3.16e-39

DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called DHHA2 for DHH associated domain. This domain is diagnostic of DHH subfamily 2 members. The domain is about 120 residues long and contains a conserved DXK motif at its amino terminus.


Pssm-ID: 460719  Cd Length: 124  Bit Score: 134.25  E-value: 3.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593  183 MLTAKSTVGKMTSEEILHIDYKPFDMSGKKVGIGQAEVIDMSEVASKKEAIQNLIDEMIEKEGYDMVLFIVTDIMKEGSE 262
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLERKDELLAALEKFAERKGLDLLVLMTTDILREGSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 503764593  263 VLVAG--NKYAFETAFELKLDGKSVFIDGLMSRKKQVVPPLEKY 304
Cdd:pfam02833  81 LLVAGgeAEELVEKAFGVALEDESLGLEGVVSRKKQVVPLLREA 124
 
Name Accession Description Interval E-value
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-307 2.22e-158

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 443.88  E-value: 2.22e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593   1 MMYVVGHKNPDSDSICSAIALAYFL-----DAFPARLGELNPESQFILKRFGLMEPELIKTAEGK-ELFLVDHAEKSQNL 74
Cdd:PRK05427   3 KILVFGHKNPDTDSICSAIAYAYLKkalglDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEvQVILVDHNEFQQSP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593  75 DDFDKGKLIGIIDHHKIG-ISTTEPIIYLSKPVGSTASVISELYfrgildiiGGKNKELKADIAGVLLSAILSDTLLFKS 153
Cdd:PRK05427  83 DDIDEATVVGVVDHHRLGnFETSNPLYYRIEPVGCTATILYKMF--------KENGVEIPKEIAGLMLSAILSDTLLFKS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593 154 PTATPLDKELAEKLADIAGIsDITAYGMEMLTAKSTVGKMTSEEILHIDYKPFDMSGKKVGIGQAEVIDMSEVASKKEAI 233
Cdd:PRK05427 155 PTTTEQDKAAAEELAEIAGV-DIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAEL 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503764593 234 QNLIDEMIEKEGYDMVLFIVTDIMKEGSEVLVAG-NKYAFETAFELKLDGKSVFIDGLMSRKKQVVPPLEKYYSN 307
Cdd:PRK05427 234 EAAMKAVKAEEGYDLFLLLITDILNEGSELLVVGdDKDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFAA 308
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-306 1.20e-146

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 414.17  E-value: 1.20e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593   1 MMYVVGHKNPDSDSICSAIALAYFL-----DAFPARLGELNPESQFILKRFGLMEPELIKT-AEGKELFLVDHAEKSQNL 74
Cdd:COG1227    3 KILVFGHKNPDTDSICSAIAYAYLKnqlgeDAEAVRLGEPNPETAFVLDYFGVEAPELIEDvAAGKKVILVDHNELAQSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593  75 DDFDKGKLIGIIDHHKIG-ISTTEPIIYLSKPVGSTASVISELYFRgildiiggKNKELKADIAGVLLSAILSDTLLFKS 153
Cdd:COG1227   83 DGIDEAEILEIIDHHRIGdFETAAPLYIRIEPVGCTATIIAKLYKE--------NGVEIPKEIAGLMLSAILSDTLLFKS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593 154 PTATPLDKELAEKLADIAGIsDITAYGMEMLTAKSTVGKMTSEEILHIDYKPFDMSGKKVGIGQAEVIDMSEVASKKEAI 233
Cdd:COG1227  155 PTTTDEDREAAEELAEIAGV-DIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDEL 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503764593 234 QNLIDEMIEKEGYDMVLFIVTDIMKEGSEVLVAGNK-YAFETAFELKLDGKSVFIDGLMSRKKQVVPPLEKYYS 306
Cdd:COG1227  234 EAAMKKVKAEKGYDLVLLLVTDILNEGSTLLVVGDDvAVVEKAFGVTLENNTVWLPGVVSRKKQVVPPLTEAFA 307
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
42-303 7.51e-91

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 280.18  E-value: 7.51e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593  42 ILKRFGLMEPEliktaeGKELFLVDHAEKSQNLDDFDKGKLIGIIDHHKIG-ISTTEPIIYLSKPVGSTASVISELYFRg 120
Cdd:PRK14869 293 VISRYHLLSPV------RKKVILVDHNEKSQAVEGIEEAEILEIIDHHRLGdIQTSNPIFFRNEPVGSTSTIVARMYRE- 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593 121 ildiiggKNKELKADIAGVLLSAILSDTLLFKSPTATPLDKELAEKLADIAGIsDITAYGMEMLTAKSTVGKMTSEEILH 200
Cdd:PRK14869 366 -------NGIEPSPEIAGLLLAAILSDTLLFKSPTTTELDREAAEWLAEIAGI-DPEEFAKEMFKAGSSLEGKTPEEIFN 437
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593 201 IDYKPFDMSGKKVGIGQAEVIDMSEVASKKEAIQNLIDEMIEKEGYDMVLFIVTDIMKEGSEVLVAGNKYAF-ETAFELK 279
Cdd:PRK14869 438 RDFKEFTIGGVKFGVGQVETMDFEEFFELKEELLEALEKLREEEGYDLLLLMVTDIIEEGSELLVAGDEKEIvARAFGVP 517
                        250       260
                 ....*....|....*....|....
gi 503764593 280 LDGKSVFIDGLMSRKKQVVPPLEK 303
Cdd:PRK14869 518 LEDNSFYLPGVVSRKKQVVPPLTK 541
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
183-304 3.16e-39

DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called DHHA2 for DHH associated domain. This domain is diagnostic of DHH subfamily 2 members. The domain is about 120 residues long and contains a conserved DXK motif at its amino terminus.


Pssm-ID: 460719  Cd Length: 124  Bit Score: 134.25  E-value: 3.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593  183 MLTAKSTVGKMTSEEILHIDYKPFDMSGKKVGIGQAEVIDMSEVASKKEAIQNLIDEMIEKEGYDMVLFIVTDIMKEGSE 262
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLERKDELLAALEKFAERKGLDLLVLMTTDILREGSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 503764593  263 VLVAG--NKYAFETAFELKLDGKSVFIDGLMSRKKQVVPPLEKY 304
Cdd:pfam02833  81 LLVAGgeAEELVEKAFGVALEDESLGLEGVVSRKKQVVPLLREA 124
DHH pfam01368
DHH family; It is predicted that this family of proteins all perform a phosphoesterase ...
3-144 2.03e-18

DHH family; It is predicted that this family of proteins all perform a phosphoesterase function. It included the single stranded DNA exonuclease RecJ.


Pssm-ID: 460177 [Multi-domain]  Cd Length: 145  Bit Score: 79.92  E-value: 2.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593    3 YVVGHKNPDSDSICSAIALAYFLDAF-PARLGELNPESqfILKRFGLMEPELIKTAEGKEL-FLVDHAEKSQNLDD--FD 78
Cdd:pfam01368   3 VIYGHYNPDGDGIGSALGLYRYLKELvGPDVEYYIPDR--LEEGYGINPEAIEELIDFDTLlITVDCGIKSVEGIElaKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503764593   79 KGKLIGIIDHHK---IGISTTEPIIYLSKPVGSTASVISELyfrgILDIIGGKNKELKADIAGVLLSAI 144
Cdd:pfam01368  81 LGIDVIVIDHHLpndFLPDADAIINPREPPASSTSEVVFKL----LQYAYGEEGKEIDKELADLLLLGI 145
NrnA COG0618
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ...
4-176 1.02e-16

nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440383 [Multi-domain]  Cd Length: 312  Bit Score: 79.08  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593   4 VVGHKNPDSDSICSAIALAYFLDAF--PARL---GELNPESQFILKRFGLMEPELIKtAEGKELFLVDHAEKSQNLDD-- 76
Cdd:COG0618   15 ILTHVNPDGDALGSALALALLLRALgkEVTIvypGEIPHELAFLPGADEIVRLEDVD-LEYDLVIVVDTSSPDRIGDLae 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503764593  77 -FDKGKLIGIIDHHkigISTTE--PIIYLSKPVGSTASVISELYFRgildiiggKNKELKADIAGVLLSAILSDTLLFKS 153
Cdd:COG0618   94 lLEKAKPVIVIDHH---PSNDDfgDFNDVDPDAGATSEIIYELLKE--------LGIEIDPEIATALYTGIVTDTGSFRY 162
                        170       180
                 ....*....|....*....|....*..
gi 503764593 154 PTATPLDKELAEKL----ADIAGISDI 176
Cdd:COG0618  163 SNTTPRDFRAAAELlekgADLDLIARI 189
 
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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