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Conserved domains on  [gi|554753004|ref|NP_250739|]
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hypothetical protein PA2049 [Pseudomonas aeruginosa PAO1]

Protein Classification

alkaline phosphatase D family protein( domain architecture ID 10164623)

alkaline phosphatase D family protein similar to Bacillus subtilis alkaline phosphatase D (PhoD), which catalyzes the hydrolysis of a phosphate monoester to produce the corresponding alcohol and phosphate

CATH:  3.60.21.70
EC:  3.1.3.1
Gene Ontology:  GO:0004035|GO:0046872|GO:0016311
PubMed:  25837850|8003970
SCOP:  4004162

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PhoD cd07389
Bacillus subtilis PhoD and related proteins, metallophosphatase domain; PhoD (also known as ...
 250-562 1.38e-25

Bacillus subtilis PhoD and related proteins, metallophosphatase domain; PhoD (also known as alkaline phosphatase D/APaseD in Bacillus subtilis) is a secreted phosphodiesterase encoded by phoD of the Pho regulon in Bacillus subtilis. PhoD homologs are found in prokaryotes, eukaryotes, and archaea. PhoD contains a twin arginine (RR) motif and is transported by the Tat (Twin-arginine translocation) translocation pathway machinery (TatAyCy). This family also includes the Fusarium oxysporum Fso1 protein. PhoD belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


:

Pssm-ID: 277335 [Multi-domain]  Cd Length: 242  Bit Score: 105.94  E-value: 1.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 250 KPIFTSANAHNHLVGLAEVLAMY------LLVW------SPAPWRLVRLEPPPGLDARHAQRFagERRHIEAFRDglPRV 317
Cdd:cd07389    1 RFAFGSCNGYSPGQFLAYRVIALskrkpdVFLWlgdqiyEDGPKGLGPLPPHPGHEALTLEEY--RERYRQYKSD--PDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 318 ARALAHISSLMIFDDHDITDDWNLSarwelTAYGHPFSRRIIGNAllAYLLCQGWGNDPqhcgewlapvaalmegaaadg 397
Cdd:cd07389   77 QKLLASVPIVGIWDDHDIGDNDGDY-----PESPKFYARKAAARQ--AYLEFLPHPNPS--------------------- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 398 rlpcaeqDRLLDALLDFQHWHYrlPGSPTLIVLDTRTRRwrsernlgrpsglmdwealsefqqdllgekaaIIVSPAPMF 477
Cdd:cd07389  129 -------PRRIKRGGIYRSFIF--GDLVKLILLDTRTYR--------------------------------VIASGIQIL 167

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 478 GVKLIEGvqklfswigQPLLVDAENWMAHRGAASVMMNIFRHSRtPGNYLILSGDVHYSFVYDIRIRHRERGPRLWQITS 557
Cdd:cd07389  168 PNDLLEG---------ESDDDLLDSWDGFPHERERLLDLIRLEK-PKNVVFLSGDVHLGEIGRLPSSPPGDGYVLVEVTS 237


                 ....*
gi 554753004 558 SGIKN 562
Cdd:cd07389  238 SGLTN 242
 
Name Accession Description Interval E-value
MPP_PhoD cd07389
Bacillus subtilis PhoD and related proteins, metallophosphatase domain; PhoD (also known as ...
 250-562 1.38e-25

Bacillus subtilis PhoD and related proteins, metallophosphatase domain; PhoD (also known as alkaline phosphatase D/APaseD in Bacillus subtilis) is a secreted phosphodiesterase encoded by phoD of the Pho regulon in Bacillus subtilis. PhoD homologs are found in prokaryotes, eukaryotes, and archaea. PhoD contains a twin arginine (RR) motif and is transported by the Tat (Twin-arginine translocation) translocation pathway machinery (TatAyCy). This family also includes the Fusarium oxysporum Fso1 protein. PhoD belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277335 [Multi-domain]  Cd Length: 242  Bit Score: 105.94  E-value: 1.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 250 KPIFTSANAHNHLVGLAEVLAMY------LLVW------SPAPWRLVRLEPPPGLDARHAQRFagERRHIEAFRDglPRV 317
Cdd:cd07389    1 RFAFGSCNGYSPGQFLAYRVIALskrkpdVFLWlgdqiyEDGPKGLGPLPPHPGHEALTLEEY--RERYRQYKSD--PDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 318 ARALAHISSLMIFDDHDITDDWNLSarwelTAYGHPFSRRIIGNAllAYLLCQGWGNDPqhcgewlapvaalmegaaadg 397
Cdd:cd07389   77 QKLLASVPIVGIWDDHDIGDNDGDY-----PESPKFYARKAAARQ--AYLEFLPHPNPS--------------------- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 398 rlpcaeqDRLLDALLDFQHWHYrlPGSPTLIVLDTRTRRwrsernlgrpsglmdwealsefqqdllgekaaIIVSPAPMF 477
Cdd:cd07389  129 -------PRRIKRGGIYRSFIF--GDLVKLILLDTRTYR--------------------------------VIASGIQIL 167

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 478 GVKLIEGvqklfswigQPLLVDAENWMAHRGAASVMMNIFRHSRtPGNYLILSGDVHYSFVYDIRIRHRERGPRLWQITS 557
Cdd:cd07389  168 PNDLLEG---------ESDDDLLDSWDGFPHERERLLDLIRLEK-PKNVVFLSGDVHLGEIGRLPSSPPGDGYVLVEVTS 237


                 ....*
gi 554753004 558 SGIKN 562
Cdd:cd07389  238 SGLTN 242
 
Name Accession Description Interval E-value
MPP_PhoD cd07389
Bacillus subtilis PhoD and related proteins, metallophosphatase domain; PhoD (also known as ...
 250-562 1.38e-25

Bacillus subtilis PhoD and related proteins, metallophosphatase domain; PhoD (also known as alkaline phosphatase D/APaseD in Bacillus subtilis) is a secreted phosphodiesterase encoded by phoD of the Pho regulon in Bacillus subtilis. PhoD homologs are found in prokaryotes, eukaryotes, and archaea. PhoD contains a twin arginine (RR) motif and is transported by the Tat (Twin-arginine translocation) translocation pathway machinery (TatAyCy). This family also includes the Fusarium oxysporum Fso1 protein. PhoD belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277335 [Multi-domain]  Cd Length: 242  Bit Score: 105.94  E-value: 1.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 250 KPIFTSANAHNHLVGLAEVLAMY------LLVW------SPAPWRLVRLEPPPGLDARHAQRFagERRHIEAFRDglPRV 317
Cdd:cd07389    1 RFAFGSCNGYSPGQFLAYRVIALskrkpdVFLWlgdqiyEDGPKGLGPLPPHPGHEALTLEEY--RERYRQYKSD--PDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 318 ARALAHISSLMIFDDHDITDDWNLSarwelTAYGHPFSRRIIGNAllAYLLCQGWGNDPqhcgewlapvaalmegaaadg 397
Cdd:cd07389   77 QKLLASVPIVGIWDDHDIGDNDGDY-----PESPKFYARKAAARQ--AYLEFLPHPNPS--------------------- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 398 rlpcaeqDRLLDALLDFQHWHYrlPGSPTLIVLDTRTRRwrsernlgrpsglmdwealsefqqdllgekaaIIVSPAPMF 477
Cdd:cd07389  129 -------PRRIKRGGIYRSFIF--GDLVKLILLDTRTYR--------------------------------VIASGIQIL 167

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554753004 478 GVKLIEGvqklfswigQPLLVDAENWMAHRGAASVMMNIFRHSRtPGNYLILSGDVHYSFVYDIRIRHRERGPRLWQITS 557
Cdd:cd07389  168 PNDLLEG---------ESDDDLLDSWDGFPHERERLLDLIRLEK-PKNVVFLSGDVHLGEIGRLPSSPPGDGYVLVEVTS 237


                 ....*
gi 554753004 558 SGIKN 562
Cdd:cd07389  238 SGLTN 242
 
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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