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Conserved domains on  [gi|516233922|ref|WP_017637885|]
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MULTISPECIES: manganese-dependent inorganic pyrophosphatase [Staphylococcus]

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
1-309 1.48e-179

putative manganese-dependent inorganic pyrophosphatase; Provisional


:

Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 497.81  E-value: 1.48e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922   1 MANTYIFGHKNPDTDAISSAIIMADFEQQTGNtNAKAYRLGEVGAETQFALDHFNVKAPELLEDNLDGQEVILVDHNEFQ 80
Cdd:PRK05427   1 MMKILVFGHKNPDTDSICSAIAYAYLKKALGL-DAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEVQVILVDHNEFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922  81 QSADSIADSTIKHVVDHHRIANFETASPLYYRAEPVGCTATILYKMYKERGFEIKPEIAGLMISAIISDSLLFKSPTCTE 160
Cdd:PRK05427  80 QSPDDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922 161 EDVNAAQALKDIANVDLDAYGLEMLKAGASTTDKSADELLDMDAKSFTMGDYVTRIAQVNTVDIDEVLNRKEELEKSMLE 240
Cdd:PRK05427 160 QDKAAAEELAEIAGVDIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516233922 241 TSAEEKYDLFVLVVTDIINSDSKILVVGAEKNKVGEAFNVQLEDDMAFLTGVVSRKKQVVPQITEALTK 309
Cdd:PRK05427 240 VKAEEGYDLFLLLITDILNEGSELLVVGDDKDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFAA 308
 
Name Accession Description Interval E-value
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-309 1.48e-179

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 497.81  E-value: 1.48e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922   1 MANTYIFGHKNPDTDAISSAIIMADFEQQTGNtNAKAYRLGEVGAETQFALDHFNVKAPELLEDNLDGQEVILVDHNEFQ 80
Cdd:PRK05427   1 MMKILVFGHKNPDTDSICSAIAYAYLKKALGL-DAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEVQVILVDHNEFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922  81 QSADSIADSTIKHVVDHHRIANFETASPLYYRAEPVGCTATILYKMYKERGFEIKPEIAGLMISAIISDSLLFKSPTCTE 160
Cdd:PRK05427  80 QSPDDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922 161 EDVNAAQALKDIANVDLDAYGLEMLKAGASTTDKSADELLDMDAKSFTMGDYVTRIAQVNTVDIDEVLNRKEELEKSMLE 240
Cdd:PRK05427 160 QDKAAAEELAEIAGVDIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516233922 241 TSAEEKYDLFVLVVTDIINSDSKILVVGAEKNKVGEAFNVQLEDDMAFLTGVVSRKKQVVPQITEALTK 309
Cdd:PRK05427 240 VKAEEGYDLFLLLITDILNEGSELLVVGDDKDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFAA 308
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-307 5.69e-177

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 491.21  E-value: 5.69e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922   1 MANTYIFGHKNPDTDAISSAIIMADFEQQTGnTNAKAYRLGEVGAETQFALDHFNVKAPELLEDNLDGQEVILVDHNEFQ 80
Cdd:COG1227    1 MMKILVFGHKNPDTDSICSAIAYAYLKNQLG-EDAEAVRLGEPNPETAFVLDYFGVEAPELIEDVAAGKKVILVDHNELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922  81 QSADSIADSTIKHVVDHHRIANFETASPLYYRAEPVGCTATILYKMYKERGFEIKPEIAGLMISAIISDSLLFKSPTCTE 160
Cdd:COG1227   80 QSVDGIDEAEILEIIDHHRIGDFETAAPLYIRIEPVGCTATIIAKLYKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922 161 EDVNAAQALKDIANVDLDAYGLEMLKAGASTTDKSADELLDMDAKSFTMGDYVTRIAQVNTVDIDEVLNRKEELEKSMLE 240
Cdd:COG1227  160 EDREAAEELAEIAGVDIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDELEAAMKK 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516233922 241 TSAEEKYDLFVLVVTDIINSDSKILVVGAEKNKVGEAFNVQLEDDMAFLTGVVSRKKQVVPQITEAL 307
Cdd:COG1227  240 VKAEKGYDLVLLLVTDILNEGSTLLVVGDDVAVVEKAFGVTLENNTVWLPGVVSRKKQVVPPLTEAF 306
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
184-306 1.18e-42

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: 143.11  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922  184 MLKAGASTTDKSADELLDMDAKSFTMGDYVTRIAQVNTVDIDEVLNRKEELEKSMLETSAEEKYDLFVLVVTDIINSDSK 263
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLERKDELLAALEKFAERKGLDLLVLMTTDILREGSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 516233922  264 ILVVGAE-KNKVGEAFNVQLEDDMAFLTGVVSRKKQVVPQITEA 306
Cdd:pfam02833  81 LLVAGGEaEELVEKAFGVALEDESLGLEGVVSRKKQVVPLLREA 124
 
Name Accession Description Interval E-value
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-309 1.48e-179

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 497.81  E-value: 1.48e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922   1 MANTYIFGHKNPDTDAISSAIIMADFEQQTGNtNAKAYRLGEVGAETQFALDHFNVKAPELLEDNLDGQEVILVDHNEFQ 80
Cdd:PRK05427   1 MMKILVFGHKNPDTDSICSAIAYAYLKKALGL-DAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEVQVILVDHNEFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922  81 QSADSIADSTIKHVVDHHRIANFETASPLYYRAEPVGCTATILYKMYKERGFEIKPEIAGLMISAIISDSLLFKSPTCTE 160
Cdd:PRK05427  80 QSPDDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922 161 EDVNAAQALKDIANVDLDAYGLEMLKAGASTTDKSADELLDMDAKSFTMGDYVTRIAQVNTVDIDEVLNRKEELEKSMLE 240
Cdd:PRK05427 160 QDKAAAEELAEIAGVDIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516233922 241 TSAEEKYDLFVLVVTDIINSDSKILVVGAEKNKVGEAFNVQLEDDMAFLTGVVSRKKQVVPQITEALTK 309
Cdd:PRK05427 240 VKAEEGYDLFLLLITDILNEGSELLVVGDDKDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFAA 308
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-307 5.69e-177

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 491.21  E-value: 5.69e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922   1 MANTYIFGHKNPDTDAISSAIIMADFEQQTGnTNAKAYRLGEVGAETQFALDHFNVKAPELLEDNLDGQEVILVDHNEFQ 80
Cdd:COG1227    1 MMKILVFGHKNPDTDSICSAIAYAYLKNQLG-EDAEAVRLGEPNPETAFVLDYFGVEAPELIEDVAAGKKVILVDHNELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922  81 QSADSIADSTIKHVVDHHRIANFETASPLYYRAEPVGCTATILYKMYKERGFEIKPEIAGLMISAIISDSLLFKSPTCTE 160
Cdd:COG1227   80 QSVDGIDEAEILEIIDHHRIGDFETAAPLYIRIEPVGCTATIIAKLYKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922 161 EDVNAAQALKDIANVDLDAYGLEMLKAGASTTDKSADELLDMDAKSFTMGDYVTRIAQVNTVDIDEVLNRKEELEKSMLE 240
Cdd:COG1227  160 EDREAAEELAEIAGVDIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDELEAAMKK 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516233922 241 TSAEEKYDLFVLVVTDIINSDSKILVVGAEKNKVGEAFNVQLEDDMAFLTGVVSRKKQVVPQITEAL 307
Cdd:COG1227  240 VKAEKGYDLVLLLVTDILNEGSTLLVVGDDVAVVEKAFGVTLENNTVWLPGVVSRKKQVVPPLTEAF 306
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
71-307 8.04e-108

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 324.09  E-value: 8.04e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922  71 VILVDHNEFQQSADSIADSTIKHVVDHHRIANFETASPLYYRAEPVGCTATILYKMYKERGFEIKPEIAGLMISAIISDS 150
Cdd:PRK14869 307 VILVDHNEKSQAVEGIEEAEILEIIDHHRLGDIQTSNPIFFRNEPVGSTSTIVARMYRENGIEPSPEIAGLLLAAILSDT 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922 151 LLFKSPTCTEEDVNAAQALKDIANVDLDAYGLEMLKAGASTTDKSADELLDMDAKSFTMGDYVTRIAQVNTVDIDEVLNR 230
Cdd:PRK14869 387 LLFKSPTTTELDREAAEWLAEIAGIDPEEFAKEMFKAGSSLEGKTPEEIFNRDFKEFTIGGVKFGVGQVETMDFEEFFEL 466
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516233922 231 KEELEKSMLETSAEEKYDLFVLVVTDIINSDSKILVVGAEKNKVGEAFNVQLEDDMAFLTGVVSRKKQVVPQITEAL 307
Cdd:PRK14869 467 KEELLEALEKLREEEGYDLLLLMVTDIIEEGSELLVAGDEKEIVARAFGVPLEDNSFYLPGVVSRKKQVVPPLTKAL 543
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
184-306 1.18e-42

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: 143.11  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922  184 MLKAGASTTDKSADELLDMDAKSFTMGDYVTRIAQVNTVDIDEVLNRKEELEKSMLETSAEEKYDLFVLVVTDIINSDSK 263
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLERKDELLAALEKFAERKGLDLLVLMTTDILREGSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 516233922  264 ILVVGAE-KNKVGEAFNVQLEDDMAFLTGVVSRKKQVVPQITEA 306
Cdd:pfam02833  81 LLVAGGEaEELVEKAFGVALEDESLGLEGVVSRKKQVVPLLREA 124
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
1-77 1.77e-23

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 100.29  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922   1 MANTYIFGHKNPDTDAISSAIIMADFEQQTGNTNAKAYRLGEVGAETQFALDHFNVKAPELLED------NLDGQEVILV 74
Cdd:PRK14869   2 MKPIYVIGHKNPDTDSICSAIAYAELKNKLGEGNYIPARLGELNPETKFVLDYFGVEAPELIEDvkpqvrDLEIDKPVTV 81

                 ...
gi 516233922  75 DHN 77
Cdd:PRK14869  82 SPD 84
DHH pfam01368
DHH family; It is predicted that this family of proteins all perform a phosphoesterase ...
3-146 3.30e-23

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: 93.02  E-value: 3.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922    3 NTYIFGHKNPDTDAISSAIIMADFEQQTGNTNAKAYrlgevgAETQFALDHFnvKAPELLEDNLDGQE-VILVDHNEFqq 81
Cdd:pfam01368   1 KIVIYGHYNPDGDGIGSALGLYRYLKELVGPDVEYY------IPDRLEEGYG--INPEAIEELIDFDTlLITVDCGIK-- 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516233922   82 SADSIADSTIKH----VVDHHRIANF--ETASPLYYRAEPVGCTATILYKM----YKERGFEIKPEIAGLMISAI 146
Cdd:pfam01368  71 SVEGIELAKELGidviVIDHHLPNDFlpDADAIINPREPPASSTSEVVFKLlqyaYGEEGKEIDKELADLLLLGI 145
NrnA COG0618
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ...
6-179 2.70e-21

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: 91.79  E-value: 2.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922   6 IFGHKNPDTDAISSAIIMADFEQQTGnTNAKAYRLGEVGAETQFALDHFNVKAPEllEDNLDGQEVILVDHNEFQ---QS 82
Cdd:COG0618   15 ILTHVNPDGDALGSALALALLLRALG-KEVTIVYPGEIPHELAFLPGADEIVRLE--DVDLEYDLVIVVDTSSPDrigDL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516233922  83 ADSIADSTIKHVVDHHrIANFETASPLYYRaEPVGCTATILYKMYKERGFEIKPEIAGLMISAIISDSLLFKSPTCTEED 162
Cdd:COG0618   92 AELLEKAKPVIVIDHH-PSNDDFGDFNDVD-PDAGATSEIIYELLKELGIEIDPEIATALYTGIVTDTGSFRYSNTTPRD 169
                        170
                 ....*....|....*..
gi 516233922 163 VNAAQALKDiANVDLDA 179
Cdd:COG0618  170 FRAAAELLE-KGADLDL 185
 
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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