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Conserved domains on  [gi|1720403776|ref|XP_030108440|]
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exopolyphosphatase PRUNE1 isoform X2 [Mus musculus]

Protein Classification

DHH family phosphoesterase( domain architecture ID 13383556)

DHH family phosphoesterase such as exopolyphosphatase PRUNE1, a phosphodiesterase (PDE) that has higher activity toward cAMP than cGMP as substrate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
187-327 1.68e-19

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: 83.79  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776 187 LQKAKFDVSGLTTEQMLRKDQKTVYRQGTKVAISAIYMDLKAFLQR--TDLFTDLSSFCHDHSYDALVAMTIFFNTQNEp 264
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLErkDELLAALEKFAERKGLDLLVLMTTDILREGS- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720403776 265 vrqLAIFCPHEAlRMTICGILERSTSP-PLKLtpipstsPNLQAyhqgntqvSRKKLLPVLQEA 327
Cdd:pfam02833  80 ---LLLVAGGEA-EELVEKAFGVALEDeSLGL-------EGVVS--------RKKQVVPLLREA 124
PPX1 super family cl34195
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
2-254 2.40e-14

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


The actual alignment was detected with superfamily member COG1227:

Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 73.27  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776   2 VSALALAFYLTKT-SEAEdifiPVLnikrseL-PLRGDNVFFLQEVKIPEPALIFRDEidllalhqAGQlTLILVDHHIL 79
Cdd:COG1227    18 CSAIAYAYLKNQLgEDAE----AVR------LgEPNPETAFVLDYFGVEAPELIEDVA--------AGK-KVILVDHNEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776  80 PKSDAALEEA-VAEVLDHRPI---EQKycPPCHVSVELVGSCATLVTERILQgAPETLDRQTAALLHGTIILDCVNMdtn 155
Cdd:COG1227    79 AQSVDGIDEAeILEIIDHHRIgdfETA--APLYIRIEPVGCTATIIAKLYKE-NGVEIPKEIAGLMLSAILSDTLLF--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776 156 igKA---TPKDSKYVEELEA-LFPDLPK-RKDIFdslqKAKFDVSGLTTEQMLRKDQKTVYRQGTKVAISAI-YMDLKAF 229
Cdd:COG1227   153 --KSpttTDEDREAAEELAEiAGVDIEAyGLEMF----KAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVeTVDPEEV 226
                         250       260
                  ....*....|....*....|....*.
gi 1720403776 230 LQRTD-LFTDLSSFCHDHSYDALVAM 254
Cdd:COG1227   227 LDRKDeLEAAMKKVKAEKGYDLVLLL 252
 
Name Accession Description Interval E-value
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
187-327 1.68e-19

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: 83.79  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776 187 LQKAKFDVSGLTTEQMLRKDQKTVYRQGTKVAISAIYMDLKAFLQR--TDLFTDLSSFCHDHSYDALVAMTIFFNTQNEp 264
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLErkDELLAALEKFAERKGLDLLVLMTTDILREGS- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720403776 265 vrqLAIFCPHEAlRMTICGILERSTSP-PLKLtpipstsPNLQAyhqgntqvSRKKLLPVLQEA 327
Cdd:pfam02833  80 ---LLLVAGGEA-EELVEKAFGVALEDeSLGL-------EGVVS--------RKKQVVPLLREA 124
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
2-254 2.40e-14

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 73.27  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776   2 VSALALAFYLTKT-SEAEdifiPVLnikrseL-PLRGDNVFFLQEVKIPEPALIFRDEidllalhqAGQlTLILVDHHIL 79
Cdd:COG1227    18 CSAIAYAYLKNQLgEDAE----AVR------LgEPNPETAFVLDYFGVEAPELIEDVA--------AGK-KVILVDHNEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776  80 PKSDAALEEA-VAEVLDHRPI---EQKycPPCHVSVELVGSCATLVTERILQgAPETLDRQTAALLHGTIILDCVNMdtn 155
Cdd:COG1227    79 AQSVDGIDEAeILEIIDHHRIgdfETA--APLYIRIEPVGCTATIIAKLYKE-NGVEIPKEIAGLMLSAILSDTLLF--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776 156 igKA---TPKDSKYVEELEA-LFPDLPK-RKDIFdslqKAKFDVSGLTTEQMLRKDQKTVYRQGTKVAISAI-YMDLKAF 229
Cdd:COG1227   153 --KSpttTDEDREAAEELAEiAGVDIEAyGLEMF----KAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVeTVDPEEV 226
                         250       260
                  ....*....|....*....|....*.
gi 1720403776 230 LQRTD-LFTDLSSFCHDHSYDALVAM 254
Cdd:COG1227   227 LDRKDeLEAAMKKVKAEKGYDLVLLL 252
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
71-254 1.48e-07

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 53.30  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776  71 LILVDHHILPKSDAALEEA-VAEVLDH---------RPIeqkycppcHVSVELVGSCATLVTERIL-QGApeTLDRQTAA 139
Cdd:PRK14869  307 VILVDHNEKSQAVEGIEEAeILEIIDHhrlgdiqtsNPI--------FFRNEPVGSTSTIVARMYReNGI--EPSPEIAG 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776 140 LLHGTIILDCVN--MDTnigkATPKDSKYVEELEAL-FPDLPK-RKDIFdslqKAKFDVSGLTTEQMLRKDQKTVYRQGT 215
Cdd:PRK14869  377 LLLAAILSDTLLfkSPT----TTELDREAAEWLAEIaGIDPEEfAKEMF----KAGSSLEGKTPEEIFNRDFKEFTIGGV 448
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720403776 216 KVAISAIY-MDLKAFLQR-TDLFTDLSSFCHDHSYDALVAM 254
Cdd:PRK14869  449 KFGVGQVEtMDFEEFFELkEELLEALEKLREEEGYDLLLLM 489
 
Name Accession Description Interval E-value
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
187-327 1.68e-19

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: 83.79  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776 187 LQKAKFDVSGLTTEQMLRKDQKTVYRQGTKVAISAIYMDLKAFLQR--TDLFTDLSSFCHDHSYDALVAMTIFFNTQNEp 264
Cdd:pfam02833   1 LFKAKSDLSGLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLErkDELLAALEKFAERKGLDLLVLMTTDILREGS- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720403776 265 vrqLAIFCPHEAlRMTICGILERSTSP-PLKLtpipstsPNLQAyhqgntqvSRKKLLPVLQEA 327
Cdd:pfam02833  80 ---LLLVAGGEA-EELVEKAFGVALEDeSLGL-------EGVVS--------RKKQVVPLLREA 124
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
2-254 2.40e-14

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 73.27  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776   2 VSALALAFYLTKT-SEAEdifiPVLnikrseL-PLRGDNVFFLQEVKIPEPALIFRDEidllalhqAGQlTLILVDHHIL 79
Cdd:COG1227    18 CSAIAYAYLKNQLgEDAE----AVR------LgEPNPETAFVLDYFGVEAPELIEDVA--------AGK-KVILVDHNEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776  80 PKSDAALEEA-VAEVLDHRPI---EQKycPPCHVSVELVGSCATLVTERILQgAPETLDRQTAALLHGTIILDCVNMdtn 155
Cdd:COG1227    79 AQSVDGIDEAeILEIIDHHRIgdfETA--APLYIRIEPVGCTATIIAKLYKE-NGVEIPKEIAGLMLSAILSDTLLF--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776 156 igKA---TPKDSKYVEELEA-LFPDLPK-RKDIFdslqKAKFDVSGLTTEQMLRKDQKTVYRQGTKVAISAI-YMDLKAF 229
Cdd:COG1227   153 --KSpttTDEDREAAEELAEiAGVDIEAyGLEMF----KAKSDLSGKSAEELLRMDAKEFEMGGKKVGIGQVeTVDPEEV 226
                         250       260
                  ....*....|....*....|....*.
gi 1720403776 230 LQRTD-LFTDLSSFCHDHSYDALVAM 254
Cdd:COG1227   227 LDRKDeLEAAMKKVKAEKGYDLVLLL 252
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
71-254 1.48e-07

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 53.30  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776  71 LILVDHHILPKSDAALEEA-VAEVLDH---------RPIeqkycppcHVSVELVGSCATLVTERIL-QGApeTLDRQTAA 139
Cdd:PRK14869  307 VILVDHNEKSQAVEGIEEAeILEIIDHhrlgdiqtsNPI--------FFRNEPVGSTSTIVARMYReNGI--EPSPEIAG 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776 140 LLHGTIILDCVN--MDTnigkATPKDSKYVEELEAL-FPDLPK-RKDIFdslqKAKFDVSGLTTEQMLRKDQKTVYRQGT 215
Cdd:PRK14869  377 LLLAAILSDTLLfkSPT----TTELDREAAEWLAEIaGIDPEEfAKEMF----KAGSSLEGKTPEEIFNRDFKEFTIGGV 448
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720403776 216 KVAISAIY-MDLKAFLQR-TDLFTDLSSFCHDHSYDALVAM 254
Cdd:PRK14869  449 KFGVGQVEtMDFEEFFELkEELLEALEKLREEEGYDLLLLM 489
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
66-254 8.58e-07

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 50.21  E-value: 8.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776  66 AGQLTLILVDHHILPKSDAALEEA-VAEVLDHR---------PIEqkycppchVSVELVGSCATLVTERILQGAPEtLDR 135
Cdd:PRK05427   65 AGEVQVILVDHNEFQQSPDDIDEAtVVGVVDHHrlgnfetsnPLY--------YRIEPVGCTATILYKMFKENGVE-IPK 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403776 136 QTAALLHGTIILDCVNMdtnigK---ATPKDSKYVEELEAL----FPDLPKrkDIFdslqKAKFDVSGLTTEQMLRKDQK 208
Cdd:PRK05427  136 EIAGLMLSAILSDTLLF-----KsptTTEQDKAAAEELAEIagvdIEAYGL--EML----KAKSDVSGKSAEELIDMDAK 204
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720403776 209 TVYRQGTKVAISAI-YMDLKAFLQRTD-LFTDLSSFCHDHSYDALVAM 254
Cdd:PRK05427  205 EFEMNGKKVGIGQVeTVDLSEVLDRKAeLEAAMKAVKAEEGYDLFLLL 252
 
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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