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Conserved domains on  [gi|493632882|ref|WP_006584753|]
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manganese-dependent inorganic pyrophosphatase [Lactobacillus jensenii]

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
1-311 0e+00

putative manganese-dependent inorganic pyrophosphatase; Provisional


:

Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 510.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882   1 MAKELIFGHQNPDTDAIGTAIAYSYFQNHFGFDTEAVALGEPNDETAFALKKFGFEAPRVIKTAANEVDaVMLVDHNEPQ 80
Cdd:PRK05427   1 MMKILVFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEVQ-VILVDHNEFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882  81 QSVSDIDKVTVTHVVDHHRIMNFNTAAPLYFRDEPVGCTSTVLWQMFNEKGLEIPQNIAGIMLSAIISDTLLLKSPTTTD 160
Cdd:PRK05427  80 QSPDDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882 161 KDHEAVEALAKIAGVDYKSYGLEMLKAGTNIADKSEEDLIDLDAKSFELNGHTVRIAQVNTVDLPEAMERKAAFIGAMEA 240
Cdd:PRK05427 160 QDKAAAEELAEIAGVDIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKA 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493632882 241 SSKANSYDMFVLVLTDILESNSEGIVVGSDetKSLFEKAFDKKLVDSAVELPGVVSRKKQVVPPLTEAFEG 311
Cdd:PRK05427 240 VKAEEGYDLFLLLITDILNEGSELLVVGDD--KDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFAA 308
 
Name Accession Description Interval E-value
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-311 0e+00

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 510.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882   1 MAKELIFGHQNPDTDAIGTAIAYSYFQNHFGFDTEAVALGEPNDETAFALKKFGFEAPRVIKTAANEVDaVMLVDHNEPQ 80
Cdd:PRK05427   1 MMKILVFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEVQ-VILVDHNEFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882  81 QSVSDIDKVTVTHVVDHHRIMNFNTAAPLYFRDEPVGCTSTVLWQMFNEKGLEIPQNIAGIMLSAIISDTLLLKSPTTTD 160
Cdd:PRK05427  80 QSPDDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882 161 KDHEAVEALAKIAGVDYKSYGLEMLKAGTNIADKSEEDLIDLDAKSFELNGHTVRIAQVNTVDLPEAMERKAAFIGAMEA 240
Cdd:PRK05427 160 QDKAAAEELAEIAGVDIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKA 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493632882 241 SSKANSYDMFVLVLTDILESNSEGIVVGSDetKSLFEKAFDKKLVDSAVELPGVVSRKKQVVPPLTEAFEG 311
Cdd:PRK05427 240 VKAEEGYDLFLLLITDILNEGSELLVVGDD--KDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFAA 308
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-310 2.62e-176

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 489.67  E-value: 2.62e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882   1 MAKELIFGHQNPDTDAIGTAIAYSYFQNHFGFDTEAVALGEPNDETAFALKKFGFEAPRVIKTAAnEVDAVMLVDHNEPQ 80
Cdd:COG1227    1 MMKILVFGHKNPDTDSICSAIAYAYLKNQLGEDAEAVRLGEPNPETAFVLDYFGVEAPELIEDVA-AGKKVILVDHNELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882  81 QSVSDIDKVTVTHVVDHHRIMNFNTAAPLYFRDEPVGCTSTVLWQMFNEKGLEIPQNIAGIMLSAIISDTLLLKSPTTTD 160
Cdd:COG1227   80 QSVDGIDEAEILEIIDHHRIGDFETAAPLYIRIEPVGCTATIIAKLYKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882 161 KDHEAVEALAKIAGVDYKSYGLEMLKAGTNIADKSEEDLIDLDAKSFELNGHTVRIAQVNTVDLPEAMERKAAFIGAMEA 240
Cdd:COG1227  160 EDREAAEELAEIAGVDIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDELEAAMKK 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882 241 SSKANSYDMFVLVLTDILESNSEGIVVGSDETKslFEKAFDKKLVDSAVELPGVVSRKKQVVPPLTEAFE 310
Cdd:COG1227  240 VKAEKGYDLVLLLVTDILNEGSTLLVVGDDVAV--VEKAFGVTLENNTVWLPGVVSRKKQVVPPLTEAFA 307
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
184-308 3.03e-44

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: 147.34  E-value: 3.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882  184 MLKAGTNIADKSEEDLIDLDAKSFELNGHTVRIAQVNTVDLPEAMERKAAFIGAMEASSKANSYDMFVLVLTDILESNSE 263
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLERKDELLAALEKFAERKGLDLLVLMTTDILREGSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 493632882  264 GIVVGSDEtKSLFEKAFDKKLVDSAVELPGVVSRKKQVVPPLTEA 308
Cdd:pfam02833  81 LLVAGGEA-EELVEKAFGVALEDESLGLEGVVSRKKQVVPLLREA 124
 
Name Accession Description Interval E-value
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-311 0e+00

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 510.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882   1 MAKELIFGHQNPDTDAIGTAIAYSYFQNHFGFDTEAVALGEPNDETAFALKKFGFEAPRVIKTAANEVDaVMLVDHNEPQ 80
Cdd:PRK05427   1 MMKILVFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEVQ-VILVDHNEFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882  81 QSVSDIDKVTVTHVVDHHRIMNFNTAAPLYFRDEPVGCTSTVLWQMFNEKGLEIPQNIAGIMLSAIISDTLLLKSPTTTD 160
Cdd:PRK05427  80 QSPDDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882 161 KDHEAVEALAKIAGVDYKSYGLEMLKAGTNIADKSEEDLIDLDAKSFELNGHTVRIAQVNTVDLPEAMERKAAFIGAMEA 240
Cdd:PRK05427 160 QDKAAAEELAEIAGVDIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKA 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493632882 241 SSKANSYDMFVLVLTDILESNSEGIVVGSDetKSLFEKAFDKKLVDSAVELPGVVSRKKQVVPPLTEAFEG 311
Cdd:PRK05427 240 VKAEEGYDLFLLLITDILNEGSELLVVGDD--KDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFAA 308
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-310 2.62e-176

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 489.67  E-value: 2.62e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882   1 MAKELIFGHQNPDTDAIGTAIAYSYFQNHFGFDTEAVALGEPNDETAFALKKFGFEAPRVIKTAAnEVDAVMLVDHNEPQ 80
Cdd:COG1227    1 MMKILVFGHKNPDTDSICSAIAYAYLKNQLGEDAEAVRLGEPNPETAFVLDYFGVEAPELIEDVA-AGKKVILVDHNELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882  81 QSVSDIDKVTVTHVVDHHRIMNFNTAAPLYFRDEPVGCTSTVLWQMFNEKGLEIPQNIAGIMLSAIISDTLLLKSPTTTD 160
Cdd:COG1227   80 QSVDGIDEAEILEIIDHHRIGDFETAAPLYIRIEPVGCTATIIAKLYKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882 161 KDHEAVEALAKIAGVDYKSYGLEMLKAGTNIADKSEEDLIDLDAKSFELNGHTVRIAQVNTVDLPEAMERKAAFIGAMEA 240
Cdd:COG1227  160 EDREAAEELAEIAGVDIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDELEAAMKK 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882 241 SSKANSYDMFVLVLTDILESNSEGIVVGSDETKslFEKAFDKKLVDSAVELPGVVSRKKQVVPPLTEAFE 310
Cdd:COG1227  240 VKAEKGYDLVLLLVTDILNEGSTLLVVGDDVAV--VEKAFGVTLENNTVWLPGVVSRKKQVVPPLTEAFA 307
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
71-310 2.97e-107

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 322.55  E-value: 2.97e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882  71 VMLVDHNEPQQSVSDIDKVTVTHVVDHHRIMNFNTAAPLYFRDEPVGCTSTVLWQMFNEKGLEIPQNIAGIMLSAIISDT 150
Cdd:PRK14869 307 VILVDHNEKSQAVEGIEEAEILEIIDHHRLGDIQTSNPIFFRNEPVGSTSTIVARMYRENGIEPSPEIAGLLLAAILSDT 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882 151 LLLKSPTTTDKDHEAVEALAKIAGVDYKSYGLEMLKAGTNIADKSEEDLIDLDAKSFELNGHTVRIAQVNTVDLPEAMER 230
Cdd:PRK14869 387 LLFKSPTTTELDREAAEWLAEIAGIDPEEFAKEMFKAGSSLEGKTPEEIFNRDFKEFTIGGVKFGVGQVETMDFEEFFEL 466
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882 231 KAAFIGAMEASSKANSYDMFVLVLTDILESNSEGIVVGSDEtkSLFEKAFDKKLVDSAVELPGVVSRKKQVVPPLTEAFE 310
Cdd:PRK14869 467 KEELLEALEKLREEEGYDLLLLMVTDIIEEGSELLVAGDEK--EIVARAFGVPLEDNSFYLPGVVSRKKQVVPPLTKALR 544
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
184-308 3.03e-44

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: 147.34  E-value: 3.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882  184 MLKAGTNIADKSEEDLIDLDAKSFELNGHTVRIAQVNTVDLPEAMERKAAFIGAMEASSKANSYDMFVLVLTDILESNSE 263
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLERKDELLAALEKFAERKGLDLLVLMTTDILREGSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 493632882  264 GIVVGSDEtKSLFEKAFDKKLVDSAVELPGVVSRKKQVVPPLTEA 308
Cdd:pfam02833  81 LLVAGGEA-EELVEKAFGVALEDESLGLEGVVSRKKQVVPLLREA 124
NrnA COG0618
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ...
5-176 8.44e-24

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: 98.72  E-value: 8.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882   5 LIFGHQNPDTDAIGTAIAYSYFQNHFGFDTEAVALGEPNDETAFaLKkfGFEAPRVIKTAANEVDAVMLVDHNEPQ---Q 81
Cdd:COG0618   14 LILTHVNPDGDALGSALALALLLRALGKEVTIVYPGEIPHELAF-LP--GADEIVRLEDVDLEYDLVIVVDTSSPDrigD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882  82 SVSDIDKVTVTHVVDHHRimnFNTA-APLYFRDEPVGCTSTVLWQMFNEKGLEIPQNIAGIMLSAIISDTLLLKSPTTTD 160
Cdd:COG0618   91 LAELLEKAKPVIVIDHHP---SNDDfGDFNDVDPDAGATSEIIYELLKELGIEIDPEIATALYTGIVTDTGSFRYSNTTP 167
                        170
                 ....*....|....*.
gi 493632882 161 KDHEAVEALAKiAGVD 176
Cdd:COG0618  168 RDFRAAAELLE-KGAD 182
DHH pfam01368
DHH family; It is predicted that this family of proteins all perform a phosphoesterase ...
5-146 9.28e-22

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: 89.17  E-value: 9.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493632882    5 LIFGHQNPDTDAIG-TAIAYSYFQNHFGFDTEAVAlgePNdetafALKKFGFEAPRVIKTAANEVDAVMLVDHNEPqqSV 83
Cdd:pfam01368   3 VIYGHYNPDGDGIGsALGLYRYLKELVGPDVEYYI---PD-----RLEEGYGINPEAIEELIDFDTLLITVDCGIK--SV 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493632882   84 SDIDKVTVTH----VVDHHRIMNF--NTAAPLYFRDEPVGCTSTVLWQM----FNEKGLEIPQNIAGIMLSAI 146
Cdd:pfam01368  73 EGIELAKELGidviVIDHHLPNDFlpDADAIINPREPPASSTSEVVFKLlqyaYGEEGKEIDKELADLLLLGI 145
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
1-63 1.84e-18

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 85.65  E-value: 1.84e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493632882   1 MAKELIFGHQNPDTDAIGTAIAYSYFQNHFGFDT-EAVALGEPNDETAFALKKFGFEAPRVIKT 63
Cdd:PRK14869   2 MKPIYVIGHKNPDTDSICSAIAYAELKNKLGEGNyIPARLGELNPETKFVLDYFGVEAPELIED 65
 
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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