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Conserved domains on  [gi|695307531|gb|AIT16286|]
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3'-phosphoadenosine 5'-phosphatase, partial [Wallemia canadensis]

Protein Classification

FIG domain-containing protein( domain architecture ID 299)

FIG (FBPase/IMPase/glpX-like) domain-containing protein belongs to a superfamily of metal-dependent phosphatases with various substrates; such as fructose-1,6-bisphosphatase (both the major and the glpX-encoded variant), inositol-monophosphatases and inositol polyphosphatases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FIG super family cl00289
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 1-117 2.99e-38

FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with various substrates. Fructose-1,6-bisphospatase (both the major and the glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate to fructose-6-phosphate in gluconeogenesis. Inositol-monophosphatases and inositol polyphosphatases play vital roles in eukaryotic signalling, as they participate in metabolizing the messenger molecule Inositol-1,4,5-triphosphate. Many of these enzymes are inhibited by Li+.


The actual alignment was detected with superfamily member TIGR01330:

Pssm-ID: 469707 [Multi-domain]  Cd Length: 353  Bit Score: 131.53  E-value: 2.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695307531    1 CLALLIEGKVELGVIACPNLPVD-----PSKPDGPRGVVFGAIKGQGAFQRPISetNGPLS--KISMNSItkESIAQASF 73
Cdd:TIGR01330 153 CLALIENGKVVLGVIGCPNLPLSsygaqNLKGSESKGCIFRAVRGSGAFMYSLS--SDAESptKVHVSSV--KDTKDAIF 228

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 695307531   74 CESVESGHSSQGDSANIAKELNITKEPVRMDSQAKYCSISRGDG 117
Cdd:TIGR01330 229 CEGVEKGHSSHDEQTAIANKLGISKSPLRLDSQAKYAALARGDA 272
 
Name Accession Description Interval E-value
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 1-117 2.99e-38

3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase.


Pssm-ID: 273558 [Multi-domain]  Cd Length: 353  Bit Score: 131.53  E-value: 2.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695307531    1 CLALLIEGKVELGVIACPNLPVD-----PSKPDGPRGVVFGAIKGQGAFQRPISetNGPLS--KISMNSItkESIAQASF 73
Cdd:TIGR01330 153 CLALIENGKVVLGVIGCPNLPLSsygaqNLKGSESKGCIFRAVRGSGAFMYSLS--SDAESptKVHVSSV--KDTKDAIF 228

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 695307531   74 CESVESGHSSQGDSANIAKELNITKEPVRMDSQAKYCSISRGDG 117
Cdd:TIGR01330 229 CEGVEKGHSSHDEQTAIANKLGISKSPLRLDSQAKYAALARGDA 272
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 1-117 5.48e-34

PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase family, and catalyses the hydrolysis of 3'-phosphoadenosine-5'-phosphate (PAP) to AMP. In Saccharomyces cerevisiae, HAL2 (MET22) is involved in methionine biosynthesis and provides increased salt tolerance when over-expressed. Bacterial members of this domain family may differ in their substrate specificity and dephosphorylate different targets, as the substrate binding site does not appear to be conserved in that sub-set.


Pssm-ID: 238775 [Multi-domain]  Cd Length: 274  Bit Score: 118.57  E-value: 5.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695307531   1 CLALLIEGKVELGVIACPNLPVDpskpDGPRGVVFGAIKGQGAFQRPisETNGPLSKISMNSITKESIaqASFCESVESG 80
Cdd:cd01517   95 ALALIEDGEVVLGVIGCPNLPLD----DGGGGDLFSAVRGQGAWLRP--LDGSSLQPLSVRQLTNAAR--ASFCESVESA 166

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 695307531  81 HSSQGDSANIAKeLNITKEPVRMDSQAKYCSISRGDG 117
Cdd:cd01517  167 HSSHRLQAAIKA-LGGTPQPVRLDSQAKYAAVARGAA 202
Inositol_P pfam00459
Inositol monophosphatase family;
1-117 4.26e-09

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 52.35  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695307531    1 CLALLIEGKVELGVIACPnlpvdpskpdgPRGVVFGAIKGQGAFQrpisetNGPLSKISMNSITKESIAQASFCESVESG 80
Cdd:pfam00459 108 SIGLAVNGEPVLGVIYQP-----------FAGQLYSAAKGKGAFL------NGQPLPVSRAPPLSEALLVTLFGVSSRKD 170

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 695307531   81 HSSQGDSANIAKELNITKEPVRMDSQAKYCSISRGDG 117
Cdd:pfam00459 171 TSEASFLAKLLKLVRAPGVRRVGSAALKLAMVAAGKA 207
 
Name Accession Description Interval E-value
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 1-117 2.99e-38

3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase.


Pssm-ID: 273558 [Multi-domain]  Cd Length: 353  Bit Score: 131.53  E-value: 2.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695307531    1 CLALLIEGKVELGVIACPNLPVD-----PSKPDGPRGVVFGAIKGQGAFQRPISetNGPLS--KISMNSItkESIAQASF 73
Cdd:TIGR01330 153 CLALIENGKVVLGVIGCPNLPLSsygaqNLKGSESKGCIFRAVRGSGAFMYSLS--SDAESptKVHVSSV--KDTKDAIF 228

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 695307531   74 CESVESGHSSQGDSANIAKELNITKEPVRMDSQAKYCSISRGDG 117
Cdd:TIGR01330 229 CEGVEKGHSSHDEQTAIANKLGISKSPLRLDSQAKYAALARGDA 272
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 1-117 5.48e-34

PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase family, and catalyses the hydrolysis of 3'-phosphoadenosine-5'-phosphate (PAP) to AMP. In Saccharomyces cerevisiae, HAL2 (MET22) is involved in methionine biosynthesis and provides increased salt tolerance when over-expressed. Bacterial members of this domain family may differ in their substrate specificity and dephosphorylate different targets, as the substrate binding site does not appear to be conserved in that sub-set.


Pssm-ID: 238775 [Multi-domain]  Cd Length: 274  Bit Score: 118.57  E-value: 5.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695307531   1 CLALLIEGKVELGVIACPNLPVDpskpDGPRGVVFGAIKGQGAFQRPisETNGPLSKISMNSITKESIaqASFCESVESG 80
Cdd:cd01517   95 ALALIEDGEVVLGVIGCPNLPLD----DGGGGDLFSAVRGQGAWLRP--LDGSSLQPLSVRQLTNAAR--ASFCESVESA 166

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 695307531  81 HSSQGDSANIAKeLNITKEPVRMDSQAKYCSISRGDG 117
Cdd:cd01517  167 HSSHRLQAAIKA-LGGTPQPVRLDSQAKYAAVARGAA 202
Inositol_P pfam00459
Inositol monophosphatase family;
1-117 4.26e-09

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 52.35  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695307531    1 CLALLIEGKVELGVIACPnlpvdpskpdgPRGVVFGAIKGQGAFQrpisetNGPLSKISMNSITKESIAQASFCESVESG 80
Cdd:pfam00459 108 SIGLAVNGEPVLGVIYQP-----------FAGQLYSAAKGKGAFL------NGQPLPVSRAPPLSEALLVTLFGVSSRKD 170

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 695307531   81 HSSQGDSANIAKELNITKEPVRMDSQAKYCSISRGDG 117
Cdd:pfam00459 171 TSEASFLAKLLKLVRAPGVRRVGSAALKLAMVAAGKA 207
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 1-112 1.19e-03

Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent metal ions such as Mg++, and many members are inhibited by Li+ (which is thought to displace a bivalent ion in the active site). Substrates include fructose-1,6-bisphosphate, inositol poly- and monophosphates, PAP and PAPS, sedoheptulose-1,7-bisphosphate and probably others.


Pssm-ID: 238815 [Multi-domain]  Cd Length: 238  Bit Score: 36.91  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695307531   1 CLALLIEGKVELGVIACPnlpvdpskpdgPRGVVFGAIKGQGAFqrpiseTNGPLSKISMNSitkeSIAQASFceSVESG 80
Cdd:cd01637   98 SIALYEDGKPVLGVIYDP-----------MLDELYYAGRGKGAF------LNGKKLPLSKDT----PLNDALL--STNAS 154

                         90       100       110
                 ....*....|....*....|....*....|...
gi 695307531  81 HSSQGDSANIAKELNITKEPVRMDSQA-KYCSI 112
Cdd:cd01637  155 MLRSNRAAVLASLVNRALGIRIYGSAGlDLAYV 187
 
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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