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Conserved domains on  [gi|119389674]
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Chain A, Manganese-dependent inorganic pyrophosphatase

Protein Classification

DHH family phosphoesterase( domain architecture ID 11440779)

DHH family phosphoesterase such as Saccharomyces cerevisiae exopolyphosphatase Ppx1p that catalyzes the degradation of inorganic polyphosphates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-308 0e+00

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


:

Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 525.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674   1 MEKILIFGHQNPDTDTICSAIAYADLKNKLGFNAEPVRLGQVNGETQYALDYFKQESPRLVETAAnEVNGVILVDHNERQ 80
Cdd:COG1227    1 MMKILVFGHKNPDTDSICSAIAYAYLKNQLGEDAEAVRLGEPNPETAFVLDYFGVEAPELIEDVA-AGKKVILVDHNELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674  81 QSIKDIEEVQVLEVIDHHRIANFETAEPLYYRAEPVGCTATILNKMYKENNVKIEKEIAGLMLSAIISDSLLFKSPTCTD 160
Cdd:COG1227   80 QSVDGIDEAEILEIIDHHRIGDFETAAPLYIRIEPVGCTATIIAKLYKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674 161 QDVAAAKELAEIAGVDAEEYGLNMLKAGADLSKKTVEELISLDAKEFTLGSKKVEIAQVNTVDIEDVKKRQAELEAVISK 240
Cdd:COG1227  160 EDREAAEELAEIAGVDIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDELEAAMKK 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119389674 241 VVAEKNLDLFLLVITDILENDSLALAIGNEAAKVEKAFNVTLENNTALLKGVVSRKKQVVPVLTDAMA 308
Cdd:COG1227  240 VKAEKGYDLVLLLVTDILNEGSTLLVVGDDVAVVEKAFGVTLENNTVWLPGVVSRKKQVVPPLTEAFA 307
 
Name Accession Description Interval E-value
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-308 0e+00

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 525.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674   1 MEKILIFGHQNPDTDTICSAIAYADLKNKLGFNAEPVRLGQVNGETQYALDYFKQESPRLVETAAnEVNGVILVDHNERQ 80
Cdd:COG1227    1 MMKILVFGHKNPDTDSICSAIAYAYLKNQLGEDAEAVRLGEPNPETAFVLDYFGVEAPELIEDVA-AGKKVILVDHNELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674  81 QSIKDIEEVQVLEVIDHHRIANFETAEPLYYRAEPVGCTATILNKMYKENNVKIEKEIAGLMLSAIISDSLLFKSPTCTD 160
Cdd:COG1227   80 QSVDGIDEAEILEIIDHHRIGDFETAAPLYIRIEPVGCTATIIAKLYKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674 161 QDVAAAKELAEIAGVDAEEYGLNMLKAGADLSKKTVEELISLDAKEFTLGSKKVEIAQVNTVDIEDVKKRQAELEAVISK 240
Cdd:COG1227  160 EDREAAEELAEIAGVDIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDELEAAMKK 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119389674 241 VVAEKNLDLFLLVITDILENDSLALAIGNEAAKVEKAFNVTLENNTALLKGVVSRKKQVVPVLTDAMA 308
Cdd:COG1227  240 VKAEKGYDLVLLLVTDILNEGSTLLVVGDDVAVVEKAFGVTLENNTVWLPGVVSRKKQVVPPLTEAFA 307
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-308 0e+00

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 509.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674   1 MEKILIFGHQNPDTDTICSAIAYADLKNKLGFNAEPVRLGQVNGETQYALDYFKQESPRLVETAANEVNgVILVDHNERQ 80
Cdd:PRK05427   1 MMKILVFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEVQ-VILVDHNEFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674  81 QSIKDIEEVQVLEVIDHHRIANFETAEPLYYRAEPVGCTATILNKMYKENNVKIEKEIAGLMLSAIISDSLLFKSPTCTD 160
Cdd:PRK05427  80 QSPDDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674 161 QDVAAAKELAEIAGVDAEEYGLNMLKAGADLSKKTVEELISLDAKEFTLGSKKVEIAQVNTVDIEDVKKRQAELEAVISK 240
Cdd:PRK05427 160 QDKAAAEELAEIAGVDIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119389674 241 VVAEKNLDLFLLVITDILENDSLALAIGNEAAKVEKAFNVTLENNTALLKGVVSRKKQVVPVLTDAMA 308
Cdd:PRK05427 240 VKAEEGYDLFLLLITDILNEGSELLVVGDDKDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFA 307
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
184-306 5.50e-46

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: 151.58  E-value: 5.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674  184 MLKAGADLSKKTVEELISLDAKEFTLGSKKVEIAQVNTVDIEDVKKRQAELEAVISKVVAEKNLDLFLLVITDILENDSL 263
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLERKDELLAALEKFAERKGLDLLVLMTTDILREGSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 119389674  264 ALAI-GNEAAKVEKAFNVTLENNTALLKGVVSRKKQVVPVLTDA 306
Cdd:pfam02833  81 LLVAgGEAEELVEKAFGVALEDESLGLEGVVSRKKQVVPLLREA 124
 
Name Accession Description Interval E-value
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
1-308 0e+00

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 525.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674   1 MEKILIFGHQNPDTDTICSAIAYADLKNKLGFNAEPVRLGQVNGETQYALDYFKQESPRLVETAAnEVNGVILVDHNERQ 80
Cdd:COG1227    1 MMKILVFGHKNPDTDSICSAIAYAYLKNQLGEDAEAVRLGEPNPETAFVLDYFGVEAPELIEDVA-AGKKVILVDHNELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674  81 QSIKDIEEVQVLEVIDHHRIANFETAEPLYYRAEPVGCTATILNKMYKENNVKIEKEIAGLMLSAIISDSLLFKSPTCTD 160
Cdd:COG1227   80 QSVDGIDEAEILEIIDHHRIGDFETAAPLYIRIEPVGCTATIIAKLYKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674 161 QDVAAAKELAEIAGVDAEEYGLNMLKAGADLSKKTVEELISLDAKEFTLGSKKVEIAQVNTVDIEDVKKRQAELEAVISK 240
Cdd:COG1227  160 EDREAAEELAEIAGVDIEAYGLEMFKAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVETVDPEEVLDRKDELEAAMKK 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119389674 241 VVAEKNLDLFLLVITDILENDSLALAIGNEAAKVEKAFNVTLENNTALLKGVVSRKKQVVPVLTDAMA 308
Cdd:COG1227  240 VKAEKGYDLVLLLVTDILNEGSTLLVVGDDVAVVEKAFGVTLENNTVWLPGVVSRKKQVVPPLTEAFA 307
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
1-308 0e+00

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 509.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674   1 MEKILIFGHQNPDTDTICSAIAYADLKNKLGFNAEPVRLGQVNGETQYALDYFKQESPRLVETAANEVNgVILVDHNERQ 80
Cdd:PRK05427   1 MMKILVFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEPNPETAFVLDYFGVEAPELITSVAGEVQ-VILVDHNEFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674  81 QSIKDIEEVQVLEVIDHHRIANFETAEPLYYRAEPVGCTATILNKMYKENNVKIEKEIAGLMLSAIISDSLLFKSPTCTD 160
Cdd:PRK05427  80 QSPDDIDEATVVGVVDHHRLGNFETSNPLYYRIEPVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674 161 QDVAAAKELAEIAGVDAEEYGLNMLKAGADLSKKTVEELISLDAKEFTLGSKKVEIAQVNTVDIEDVKKRQAELEAVISK 240
Cdd:PRK05427 160 QDKAAAEELAEIAGVDIEAYGLEMLKAKSDVSGKSAEELIDMDAKEFEMNGKKVGIGQVETVDLSEVLDRKAELEAAMKA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119389674 241 VVAEKNLDLFLLVITDILENDSLALAIGNEAAKVEKAFNVTLENNTALLKGVVSRKKQVVPVLTDAMA 308
Cdd:PRK05427 240 VKAEEGYDLFLLLITDILNEGSELLVVGDDKDVVEKAFNVKLEDNTAFLDGVVSRKKQVVPQLTEAFA 307
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
71-309 3.09e-120

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 355.68  E-value: 3.09e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674  71 VILVDHNERQQSIKDIEEVQVLEVIDHHRIANFETAEPLYYRAEPVGCTATILNKMYKENNVKIEKEIAGLMLSAIISDS 150
Cdd:PRK14869 307 VILVDHNEKSQAVEGIEEAEILEIIDHHRLGDIQTSNPIFFRNEPVGSTSTIVARMYRENGIEPSPEIAGLLLAAILSDT 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674 151 LLFKSPTCTDQDVAAAKELAEIAGVDAEEYGLNMLKAGADLSKKTVEELISLDAKEFTLGSKKVEIAQVNTVDIEDVKKR 230
Cdd:PRK14869 387 LLFKSPTTTELDREAAEWLAEIAGIDPEEFAKEMFKAGSSLEGKTPEEIFNRDFKEFTIGGVKFGVGQVETMDFEEFFEL 466
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119389674 231 QAELEAVISKVVAEKNLDLFLLVITDILENDSLALAIGNEAAKVEKAFNVTLENNTALLKGVVSRKKQVVPVLTDAMAE 309
Cdd:PRK14869 467 KEELLEALEKLREEEGYDLLLLMVTDIIEEGSELLVAGDEKEIVARAFGVPLEDNSFYLPGVVSRKKQVVPPLTKALRT 545
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
184-306 5.50e-46

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: 151.58  E-value: 5.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674  184 MLKAGADLSKKTVEELISLDAKEFTLGSKKVEIAQVNTVDIEDVKKRQAELEAVISKVVAEKNLDLFLLVITDILENDSL 263
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLERKDELLAALEKFAERKGLDLLVLMTTDILREGSL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 119389674  264 ALAI-GNEAAKVEKAFNVTLENNTALLKGVVSRKKQVVPVLTDA 306
Cdd:pfam02833  81 LLVAgGEAEELVEKAFGVALEDESLGLEGVVSRKKQVVPLLREA 124
DHH pfam01368
DHH family; It is predicted that this family of proteins all perform a phosphoesterase ...
3-146 4.27e-27

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: 103.42  E-value: 4.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674    3 KILIFGHQNPDTDTICSAIA-YADLKNKLGFNAEPVRlgqvngETQYALDYFKqeSPRLVETAANEVNGVILVDHNERqq 81
Cdd:pfam01368   1 KIVIYGHYNPDGDGIGSALGlYRYLKELVGPDVEYYI------PDRLEEGYGI--NPEAIEELIDFDTLLITVDCGIK-- 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119389674   82 SIKDIEEVQVLE----VIDHHRIANF--ETAEPLYYRAEPVGCTATILNKM----YKENNVKIEKEIAGLMLSAI 146
Cdd:pfam01368  71 SVEGIELAKELGidviVIDHHLPNDFlpDADAIINPREPPASSTSEVVFKLlqyaYGEEGKEIDKELADLLLLGI 145
NrnA COG0618
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ...
2-256 4.35e-23

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: 96.80  E-value: 4.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674   2 EKILIFGHQNPDTDTICSAIAYADLKNKLGFNAEPVRLGQVNGEtqyaLDYFKQESP-RLVETAANEVNGVILVDHN--E 78
Cdd:COG0618   11 DRILILTHVNPDGDALGSALALALLLRALGKEVTIVYPGEIPHE----LAFLPGADEiVRLEDVDLEYDLVIVVDTSspD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674  79 RQQSIKD-IEEVQVLEVIDHHrIANFETAEPLYYRaEPVGCTATILNKMYKENNVKIEKEIAGLMLSAIISDSLLFKSPT 157
Cdd:COG0618   87 RIGDLAElLEKAKPVIVIDHH-PSNDDFGDFNDVD-PDAGATSEIIYELLKELGIEIDPEIATALYTGIVTDTGSFRYSN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119389674 158 CTDQDVAAAKELaeiagvdaeeyglnmLKAGADLSkkTVEELIS-------LDAKEFTLGSKKVE------IAQVNTVDI 224
Cdd:COG0618  165 TTPRDFRAAAEL---------------LEKGADLD--LIARILYpslsleqLKLLGRALENLEVLedgkvaYSYLTKEDL 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 119389674 225 EDVKKRQAELEAVISKVVAEKNLD-LFLLVITD 256
Cdd:COG0618  228 EEFGATPDDTEGLVDYLLSIEGVEvAVVFGEVE 260
 
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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