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Conserved domains on  [gi|515627702|ref|WP_017060302|]
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MULTISPECIES: manganese-dependent inorganic pyrophosphatase [Vibrio]

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
1-297 3.23e-154

putative manganese-dependent inorganic pyrophosphatase; Provisional


:

Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 433.10  E-value: 3.23e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702   1 MILVVGHKNPDSDSICSALVATELLKARGEEATPIRQGEINRETQHILEVAGAEKPELRTSVAGE-KIWLVDYSDLAQAP 79
Cdd:PRK05427   3 KILVFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEvQVILVDHNEFQQSP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702  80 DDVADAEIVGIVDHHRLGDVMTVNPMEAWIWPVGCTNTVLFNMFKIEGHAISQQIAKLMMSAILSDTVGFASPTCTQKDK 159
Cdd:PRK05427  83 DDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTEQDK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702 160 DAVAELAEIAGVtDVDAFIKALLIAKTNIEGLSAAQLVEKDLKGYPFNGRDVVVGQVELATLEQVDGMIEALEADLEERC 239
Cdd:PRK05427 163 AAAEELAEIAGV-DIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKAVK 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515627702 240 EKDGLAFAAVMLTDITTAQTRLLYKGEWAEKLVK----HEKDGVLMMENTLSRKKQGWPWLQ 297
Cdd:PRK05427 242 AEEGYDLFLLLITDILNEGSELLVVGDDKDVVEKafnvKLEDNTAFLDGVVSRKKQVVPQLT 303
 
Name Accession Description Interval E-value
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-297 3.23e-154

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 433.10  E-value: 3.23e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702   1 MILVVGHKNPDSDSICSALVATELLKARGEEATPIRQGEINRETQHILEVAGAEKPELRTSVAGE-KIWLVDYSDLAQAP 79
Cdd:PRK05427   3 KILVFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEvQVILVDHNEFQQSP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702  80 DDVADAEIVGIVDHHRLGDVMTVNPMEAWIWPVGCTNTVLFNMFKIEGHAISQQIAKLMMSAILSDTVGFASPTCTQKDK 159
Cdd:PRK05427  83 DDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTEQDK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702 160 DAVAELAEIAGVtDVDAFIKALLIAKTNIEGLSAAQLVEKDLKGYPFNGRDVVVGQVELATLEQVDGMIEALEADLEERC 239
Cdd:PRK05427 163 AAAEELAEIAGV-DIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKAVK 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515627702 240 EKDGLAFAAVMLTDITTAQTRLLYKGEWAEKLVK----HEKDGVLMMENTLSRKKQGWPWLQ 297
Cdd:PRK05427 242 AEEGYDLFLLLITDILNEGSELLVVGDDKDVVEKafnvKLEDNTAFLDGVVSRKKQVVPQLT 303
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-291 4.70e-121

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 349.07  E-value: 4.70e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702   1 MILVVGHKNPDSDSICSALVATELLKARGEEATPIRQGEINRETQHILEVAGAEKPELRTSVA-GEKIWLVDYSDLAQAP 79
Cdd:COG1227    3 KILVFGHKNPDTDSICSAIAYAYLKNQLGEDAEAVRLGEPNPETAFVLDYFGVEAPELIEDVAaGKKVILVDHNELAQSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702  80 DDVADAEIVGIVDHHRLGDVMTVNPMEAWIWPVGCTNTVLFNMFKIEGHAISQQIAKLMMSAILSDTVGFASPTCTQKDK 159
Cdd:COG1227   83 DGIDEAEILEIIDHHRIGDFETAAPLYIRIEPVGCTATIIAKLYKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTDEDR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702 160 DAVAELAEIAGVtDVDAFIKALLIAKTNIEGLSAAQLVEKDLKGYPFNGRDVVVGQVELATLEQVDGMIEALEADLEERC 239
Cdd:COG1227  163 EAAEELAEIAGV-DIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDELEAAMKKVK 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515627702 240 EKDGLAFAAVMLTDITTAQTRLLYKGEWAEKLVK----HEKDGVLMMENTLSRKKQ 291
Cdd:COG1227  242 AEKGYDLVLLLVTDILNEGSTLLVVGDDVAVVEKafgvTLENNTVWLPGVVSRKKQ 297
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
181-297 1.91e-28

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: 105.74  E-value: 1.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702  181 LLIAKTNIEGLSAAQLVEKDLKGYPFNGRDVVVGQVELATLEQVDGMIEALEADLEERCEKDGLAFAAVMLTDITTAQTR 260
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLERKDELLAALEKFAERKGLDLLVLMTTDILREGSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 515627702  261 LLYKGEWAEKLV-----KHEKDGVLMMENTLSRKKQGWPWLQ 297
Cdd:pfam02833  81 LLVAGGEAEELVekafgVALEDESLGLEGVVSRKKQVVPLLR 122
 
Name Accession Description Interval E-value
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-297 3.23e-154

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 433.10  E-value: 3.23e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702   1 MILVVGHKNPDSDSICSALVATELLKARGEEATPIRQGEINRETQHILEVAGAEKPELRTSVAGE-KIWLVDYSDLAQAP 79
Cdd:PRK05427   3 KILVFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEvQVILVDHNEFQQSP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702  80 DDVADAEIVGIVDHHRLGDVMTVNPMEAWIWPVGCTNTVLFNMFKIEGHAISQQIAKLMMSAILSDTVGFASPTCTQKDK 159
Cdd:PRK05427  83 DDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTEQDK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702 160 DAVAELAEIAGVtDVDAFIKALLIAKTNIEGLSAAQLVEKDLKGYPFNGRDVVVGQVELATLEQVDGMIEALEADLEERC 239
Cdd:PRK05427 163 AAAEELAEIAGV-DIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKAVK 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515627702 240 EKDGLAFAAVMLTDITTAQTRLLYKGEWAEKLVK----HEKDGVLMMENTLSRKKQGWPWLQ 297
Cdd:PRK05427 242 AEEGYDLFLLLITDILNEGSELLVVGDDKDVVEKafnvKLEDNTAFLDGVVSRKKQVVPQLT 303
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-291 4.70e-121

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 349.07  E-value: 4.70e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702   1 MILVVGHKNPDSDSICSALVATELLKARGEEATPIRQGEINRETQHILEVAGAEKPELRTSVA-GEKIWLVDYSDLAQAP 79
Cdd:COG1227    3 KILVFGHKNPDTDSICSAIAYAYLKNQLGEDAEAVRLGEPNPETAFVLDYFGVEAPELIEDVAaGKKVILVDHNELAQSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702  80 DDVADAEIVGIVDHHRLGDVMTVNPMEAWIWPVGCTNTVLFNMFKIEGHAISQQIAKLMMSAILSDTVGFASPTCTQKDK 159
Cdd:COG1227   83 DGIDEAEILEIIDHHRIGDFETAAPLYIRIEPVGCTATIIAKLYKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTDEDR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702 160 DAVAELAEIAGVtDVDAFIKALLIAKTNIEGLSAAQLVEKDLKGYPFNGRDVVVGQVELATLEQVDGMIEALEADLEERC 239
Cdd:COG1227  163 EAAEELAEIAGV-DIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDELEAAMKKVK 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515627702 240 EKDGLAFAAVMLTDITTAQTRLLYKGEWAEKLVK----HEKDGVLMMENTLSRKKQ 291
Cdd:COG1227  242 AEKGYDLVLLLVTDILNEGSTLLVVGDDVAVVEKafgvTLENNTVWLPGVVSRKKQ 297
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
66-296 1.75e-66

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 217.01  E-value: 1.75e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702  66 KIWLVDYSDLAQAPDDVADAEIVGIVDHHRLGDVMTVNPMEAWIWPVGCTNTVLFNMFKIEGHAISQQIAKLMMSAILSD 145
Cdd:PRK14869 306 KVILVDHNEKSQAVEGIEEAEILEIIDHHRLGDIQTSNPIFFRNEPVGSTSTIVARMYRENGIEPSPEIAGLLLAAILSD 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702 146 TVGFASPTCTQKDKDAVAELAEIAGVtDVDAFIKALLIAKTNIEGLSAAQLVEKDLKGYPFNGRDVVVGQVELATLEQVD 225
Cdd:PRK14869 386 TLLFKSPTTTELDREAAEWLAEIAGI-DPEEFAKEMFKAGSSLEGKTPEEIFNRDFKEFTIGGVKFGVGQVETMDFEEFF 464
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515627702 226 GMIEALEADLEERCEKDGLAFAAVMLTDITTAQTRLLYKGEWAEKLVK----HEKDGVLMMENTLSRKKQGWPWL 296
Cdd:PRK14869 465 ELKEELLEALEKLREEEGYDLLLLMVTDIIEEGSELLVAGDEKEIVARafgvPLEDNSFYLPGVVSRKKQVVPPL 539
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
181-297 1.91e-28

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: 105.74  E-value: 1.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702  181 LLIAKTNIEGLSAAQLVEKDLKGYPFNGRDVVVGQVELATLEQVDGMIEALEADLEERCEKDGLAFAAVMLTDITTAQTR 260
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLERKDELLAALEKFAERKGLDLLVLMTTDILREGSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 515627702  261 LLYKGEWAEKLV-----KHEKDGVLMMENTLSRKKQGWPWLQ 297
Cdd:pfam02833  81 LLVAGGEAEELVekafgVALEDESLGLEGVVSRKKQVVPLLR 122
NrnA COG0618
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ...
2-167 1.36e-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: 92.56  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702   2 ILVVGHKNPDSDSICSALVATELLKARGEEATPIRQGEINRETQHILEVAGAEKPElRTSVAGEKIWLVDYSDLAQAPDD 81
Cdd:COG0618   13 ILILTHVNPDGDALGSALALALLLRALGKEVTIVYPGEIPHELAFLPGADEIVRLE-DVDLEYDLVIVVDTSSPDRIGDL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702  82 ---VADAEIVGIVDHH----RLGDVMTVNPmeawiwPVGCTNTVLFNMFKIEGHAISQQIAKLMMSAILSDTVGFASPTC 154
Cdd:COG0618   92 aelLEKAKPVIVIDHHpsndDFGDFNDVDP------DAGATSEIIYELLKELGIEIDPEIATALYTGIVTDTGSFRYSNT 165
                        170
                 ....*....|...
gi 515627702 155 TQKDKDAVAELAE 167
Cdd:COG0618  166 TPRDFRAAAELLE 178
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
1-62 4.28e-17

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 81.42  E-value: 4.28e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515627702   1 MILVVGHKNPDSDSICSALVATELLKARGE-EATPIRQGEINRETQHILEVAGAEKPELRTSV 62
Cdd:PRK14869   4 PIYVIGHKNPDTDSICSAIAYAELKNKLGEgNYIPARLGELNPETKFVLDYFGVEAPELIEDV 66
DHH pfam01368
DHH family; It is predicted that this family of proteins all perform a phosphoesterase ...
2-142 2.26e-15

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: 71.83  E-value: 2.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702    2 ILVVGHKNPDSDSICSALVATELLKARG----EEATPIRQGE---INRETqhILEVAGAEKpelrtsvageKIWLVDYSD 74
Cdd:pfam01368   2 IVIYGHYNPDGDGIGSALGLYRYLKELVgpdvEYYIPDRLEEgygINPEA--IEELIDFDT----------LLITVDCGI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515627702   75 LaqAPDDVADAEIVGI----VDHHRLGDVM-----TVNPMEAwiwPVGCTNTVLFNM----FKIEGHAISQQIAKLMMSA 141
Cdd:pfam01368  70 K--SVEGIELAKELGIdvivIDHHLPNDFLpdadaIINPREP---PASSTSEVVFKLlqyaYGEEGKEIDKELADLLLLG 144

                  .
gi 515627702  142 I 142
Cdd:pfam01368 145 I 145
 
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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