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Conserved domains on  [gi|15598283|ref|NP_251777|]
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hypothetical protein PA3087 [Pseudomonas aeruginosa PAO1]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10164800)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)| bifunctional metallophosphatase/5'-nucleotidase contains an N-terminal metallophosphoesterase family domain that contains an active site consisting of two metal ions (usually manganese, iron, or zinc), and a 5'-nucleotidase C-terminal domain; similar to Escherichia coli UshA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 9-309 1.80e-129

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 368.42  E-value: 1.80e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283   9 YDLIGDVHGCAHTLDRLLDLLGYRLQGGVWRHPRRQALFLGDIVDRGPRIREALHRVHAMVDAGEALCIMGNHEFNALGW 88
Cdd:cd07413   1 YDLIGDVHGCAHTLDRLLDLLGYRLQGGVWRHPRRQALFVGDLIDRGPRIREVLHRVHAMVDAGEALCVMGNHEFNALAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283  89 STPAAPGSGRQYVREHTPRHARLIKETLEQFEGHdaDWRDFLGWFQQLPLFLDAGRFRMVHACWDgeliatlrrqfpdgr 168
Cdd:cd07413  81 HTPAPPGSGRQYVREHSPKNARQHKATLDQFEGH--DWRDFLGWFQTLPLFLDLGRFRVVHACWD--------------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283 169 iseaflqesaepgsfadlacNRLLRGTDMRLPHGATLTSSDGYTRAFFRTKFWvedeaprtygdivfqpdalpeaiarep 248
Cdd:cd07413 144 --------------------ERLLKGPEMRLPHGAELTDKDGYTRDFFRVKWW--------------------------- 176

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598283 249 lseeqksslltygadEPLLFVGHYWRRGTPAPIRPNLACLDYSAVMYGKLAAYRLDEETRL 309
Cdd:cd07413 177 ---------------VPPVFVGHYWRRGTPAPIRPNLACLDYSAVKYGKLAAYRWDGETRL 222
 
Name Accession Description Interval E-value
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 9-309 1.80e-129

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 368.42  E-value: 1.80e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283   9 YDLIGDVHGCAHTLDRLLDLLGYRLQGGVWRHPRRQALFLGDIVDRGPRIREALHRVHAMVDAGEALCIMGNHEFNALGW 88
Cdd:cd07413   1 YDLIGDVHGCAHTLDRLLDLLGYRLQGGVWRHPRRQALFVGDLIDRGPRIREVLHRVHAMVDAGEALCVMGNHEFNALAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283  89 STPAAPGSGRQYVREHTPRHARLIKETLEQFEGHdaDWRDFLGWFQQLPLFLDAGRFRMVHACWDgeliatlrrqfpdgr 168
Cdd:cd07413  81 HTPAPPGSGRQYVREHSPKNARQHKATLDQFEGH--DWRDFLGWFQTLPLFLDLGRFRVVHACWD--------------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283 169 iseaflqesaepgsfadlacNRLLRGTDMRLPHGATLTSSDGYTRAFFRTKFWvedeaprtygdivfqpdalpeaiarep 248
Cdd:cd07413 144 --------------------ERLLKGPEMRLPHGAELTDKDGYTRDFFRVKWW--------------------------- 176

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598283 249 lseeqksslltygadEPLLFVGHYWRRGTPAPIRPNLACLDYSAVMYGKLAAYRLDEETRL 309
Cdd:cd07413 177 ---------------VPPVFVGHYWRRGTPAPIRPNLACLDYSAVKYGKLAAYRWDGETRL 222
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 9-81 4.77e-13

bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 67.81  E-value: 4.77e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598283    9 YDLIGDVHGCAHTLDRLLDLLGYRLQGGVWRHP-RRQALFLGDIVDRGPRIREALHRVHAMVDAGEALCIMGNH 81
Cdd:PRK13625   3 YDIIGDIHGCYQEFQALTEKLGYNWSSGLPVHPdQRKLAFVGDLTDRGPHSLRMIEIVWELVEKKAAYYVPGNH 76
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 11-139 3.78e-07

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 47.98  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283    11 LIGDVH--GCAHTLDRLLDLLGYRLQGGVWrhprrqaLFLGDIVDRGPRIREALHRVHAMVDAGEALCIMGNHEFNALGW 88
Cdd:pfam00149   5 VIGDLHlpGQLDDLLELLKKLLEEGKPDLV-------LHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHDFDYGEC 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15598283    89 STPaapgsgrqyvrehtprharliketLEQFEGHDADWRDFLGWFQQLPLF 139
Cdd:pfam00149  78 LRL------------------------YPYLGLLARPWKRFLEVFNFLPLA 104
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
11-88 6.37e-05

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 42.98  E-value: 6.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283  11 LIGDVHGCAHTLDRLLDLLgyrlqggvwrhPRRQA---LFLGDIVDRGPRIREALHRVHAMvdagEALCIMGNHEFNALG 87
Cdd:COG0622   4 VISDTHGNLPALEAVLEDL-----------EREGVdliVHLGDLVGYGPDPPEVLDLLREL----PIVAVRGNHDGAVLR 68


                .
gi 15598283  88 W 88
Cdd:COG0622  69 G 69
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 12-57 8.75e-04

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 40.27  E-value: 8.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 15598283     12 IGDVHGCAHTLDRLLDLLGyrlqggvwRHPRRQALFLGDIVDRGPR 57
Cdd:smart00156  33 CGDIHGQFDDLLRLFDKNG--------QPPETNYVFLGDYVDRGPF 70
 
Name Accession Description Interval E-value
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 9-309 1.80e-129

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 368.42  E-value: 1.80e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283   9 YDLIGDVHGCAHTLDRLLDLLGYRLQGGVWRHPRRQALFLGDIVDRGPRIREALHRVHAMVDAGEALCIMGNHEFNALGW 88
Cdd:cd07413   1 YDLIGDVHGCAHTLDRLLDLLGYRLQGGVWRHPRRQALFVGDLIDRGPRIREVLHRVHAMVDAGEALCVMGNHEFNALAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283  89 STPAAPGSGRQYVREHTPRHARLIKETLEQFEGHdaDWRDFLGWFQQLPLFLDAGRFRMVHACWDgeliatlrrqfpdgr 168
Cdd:cd07413  81 HTPAPPGSGRQYVREHSPKNARQHKATLDQFEGH--DWRDFLGWFQTLPLFLDLGRFRVVHACWD--------------- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283 169 iseaflqesaepgsfadlacNRLLRGTDMRLPHGATLTSSDGYTRAFFRTKFWvedeaprtygdivfqpdalpeaiarep 248
Cdd:cd07413 144 --------------------ERLLKGPEMRLPHGAELTDKDGYTRDFFRVKWW--------------------------- 176

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598283 249 lseeqksslltygadEPLLFVGHYWRRGTPAPIRPNLACLDYSAVMYGKLAAYRLDEETRL 309
Cdd:cd07413 177 ---------------VPPVFVGHYWRRGTPAPIRPNLACLDYSAVKYGKLAAYRWDGETRL 222
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 10-172 5.21e-28

Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein phosphatase E) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases and a key signal transduction pathway component controlling the expression of spore germination receptors GerA and GerK in Bacillus subtilis. PrpE is closely related to ApaH (also known symmetrical Ap(4)A hydrolase and bis(5'nucleosyl)-tetraphosphatase). PrpE has specificity for phosphotyrosine only, unlike the serine/threonine phosphatases to which it is related. The Bacilli members of this family are single domain proteins while the other members have N- and C-terminal domains in addition to this phosphatase domain. Pnkp is the end-healing and end-sealing component of an RNA repair system present in bacteria. It is composed of three catalytic modules: an N-terminal polynucleotide 5' kinase, a central 2',3' phosphatase, and a C-terminal ligase. Pnkp is a Mn(2+)-dependent phosphodiesterase-monoesterase that dephosphorylates 2',3'-cyclic phosphate RNA ends. An RNA binding site is suggested by a continuous tract of positive surface potential flanking the active site. The PPP (phosphoprotein phosphatase) family, to which PrpE belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 108.76  E-value: 5.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283  10 DLIGDVHGCAHTLDRLLDLLGYRL-QGGVWRHPR-RQALFLGDIVDRGPRIREALHRVHAMVDAGEALCIMGNHEFNALG 87
Cdd:cd07423   1 DIIGDVHGCYDELVELLEKLGYQKkEEGLYVHPEgRKLVFLGDLVDRGPDSIDVLRLVMNMVKAGKALYVPGNHCNKLYR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283  88 WStpaapgSGRQYVREHTprharlIKETLEQFEGHDADWRD-----FLGWFQQLPLF--LDAGRFRMVHACWDGELIatl 160
Cdd:cd07423  81 YL------KGRNVQLAHG------LETTVEELEALSKEERPefrerFAEFLESLPSHlvLDGGRLVVAHAGIKEEMI--- 145

                       170
                ....*....|..
gi 15598283 161 rrqfpdGRISEA 172
Cdd:cd07423 146 ------GRGSKR 151
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 12-163 7.26e-26

phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 102.83  E-value: 7.26e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283  12 IGDVHGCAHTLDRLLDLLGYrlqggvwrHPRRQALFLGDIVDRGPRIREALHRVHAMV--DAGEALCIMGNHEFNALGWs 89
Cdd:cd00144   3 VGDIHGCFDDLLRLLEKLGF--------PPEDKYLFLGDYVDRGPDSVEVIDLLLALKilYPDNVFLLRGNHEFMLLNF- 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598283  90 tpaapgsgrqYVREHTPRHARLIKETLEQFeghdadWRDFLGWFQQLPLFLD-AGRFRMVHACWDGELIATLRRQ 163
Cdd:cd00144  74 ----------LYGFYDERTLRCLRKGGEEL------WREFNEVFNYLPLAALvDGKILCVHGGLSPDLTLLDQIR 132
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 9-81 4.77e-13

bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 67.81  E-value: 4.77e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598283    9 YDLIGDVHGCAHTLDRLLDLLGYRLQGGVWRHP-RRQALFLGDIVDRGPRIREALHRVHAMVDAGEALCIMGNH 81
Cdd:PRK13625   3 YDIIGDIHGCYQEFQALTEKLGYNWSSGLPVHPdQRKLAFVGDLTDRGPHSLRMIEIVWELVEKKAAYYVPGNH 76
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
11-163 1.07e-11

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 64.03  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283   11 LIGDVHGCAHTLDRLLDLLGYrlqggvwrHPRRQAL-FLGDIVDRGPRIREALHRVHAMVDAgeALCIMGNHEFNALGws 89
Cdd:PRK00166   5 AIGDIQGCYDELQRLLEKIDF--------DPAKDTLwLVGDLVNRGPDSLEVLRFVKSLGDS--AVTVLGNHDLHLLA-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283   90 tpAAPGSGRqyvrehtPRHarliKETLEQ-FEGHDADwrDFLGWFQQLPL--FLDAGRFRMVHA----CWDgelIATLRR 162
Cdd:PRK00166  73 --VAAGIKR-------NKK----KDTLDPiLEAPDRD--ELLDWLRHQPLlhVDEELGLVMVHAgippQWD---LATALA 134


                 .
gi 15598283  163 Q 163
Cdd:PRK00166 135 L 135
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 11-153 8.11e-11

Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as symmetrically cleaving Ap4A hydrolase and bis(5'nucleosyl)-tetraphosphatase) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases that hydrolyzes the nucleotide-signaling molecule diadenosine tetraphosphate (Ap(4)A) into two ADP and also hydrolyzes Ap(5)A, Gp(4)G, and other extending compounds. Null mutations in apaH result in high intracellular levels of Ap(4)A which correlate with multiple phenotypes, including a decreased expression of catabolite-repressible genes, a reduction in the expression of flagellar operons, and an increased sensitivity to UV and heat. Ap4A hydrolase is important in responding to heat shock and oxidative stress via regulating the concentration of Ap4A in bacteria. Ap4A hydrolase is also thought to play a role in siderophore production, but the mechanism by which ApaH interacts with siderophore pathways in unknown. The PPP (phosphoprotein phosphatase) family, to which ApaH belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and PrpA/PrpB. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277365 [Multi-domain]  Cd Length: 257  Bit Score: 61.41  E-value: 8.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283  11 LIGDVHGCAHTLDRLLDLLGYrlqggvwrHPRRQAL-FLGDIVDRGPRIREALHRVHAMVDAgeALCIMGNHEFNALGws 89
Cdd:cd07422   3 AIGDIQGCYDELQRLLEKINF--------DPAKDRLwLVGDLVNRGPDSLETLRFVKSLGDS--AVVVLGNHDLHLLA-- 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598283  90 tpAAPGSGRqyvrehtPRHarliKETLEQ-FEGHDADwrDFLGWFQQLPLFL--DAGRFRMVHA----CWD 153
Cdd:cd07422  71 --VAAGIKK-------LKK----KDTLDEiLEAPDRD--ELLDWLRHQPLLHrdDELGIVMVHAgippQWD 126
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 11-139 3.78e-07

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 47.98  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283    11 LIGDVH--GCAHTLDRLLDLLGYRLQGGVWrhprrqaLFLGDIVDRGPRIREALHRVHAMVDAGEALCIMGNHEFNALGW 88
Cdd:pfam00149   5 VIGDLHlpGQLDDLLELLKKLLEEGKPDLV-------LHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHDFDYGEC 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15598283    89 STPaapgsgrqyvrehtprharliketLEQFEGHDADWRDFLGWFQQLPLF 139
Cdd:pfam00149  78 LRL------------------------YPYLGLLARPWKRFLEVFNFLPLA 104
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
11-88 6.37e-05

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 42.98  E-value: 6.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598283  11 LIGDVHGCAHTLDRLLDLLgyrlqggvwrhPRRQA---LFLGDIVDRGPRIREALHRVHAMvdagEALCIMGNHEFNALG 87
Cdd:COG0622   4 VISDTHGNLPALEAVLEDL-----------EREGVdliVHLGDLVGYGPDPPEVLDLLREL----PIVAVRGNHDGAVLR 68


                .
gi 15598283  88 W 88
Cdd:COG0622  69 G 69
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 11-82 1.23e-04

PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine and tyrosine phosphatases thought to modulate the expression of proteins that protect the cell upon accumulation of misfolded proteins in the periplasm. The PPP (phosphoprotein phosphatase) family, to which PrpA and PrpB belong, is one of two known protein phosphatase families specific for serine and threonine. This family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 42.30  E-value: 1.23e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598283  11 LIGDVHGCAHTLDRLLDLLGYrlqggvwrHPRRQALF-LGDIVDRGPRIREAL-----HRVHAmvdagealcIMGNHE 82
Cdd:cd07424   5 VVGDIHGHFQRLQRALDAVGF--------DPARDRLIsVGDLVDRGPESLEVLellkqPWFHA---------VQGNHE 65
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 11-83 2.28e-04

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing 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. This superfamily includes: the phosphoprotein phosphatases (PPPs), 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: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 40.33  E-value: 2.28e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598283  11 LIGDVHGCAHTLDRLLDLLGYRlqggvwRHPRRQALFLGDIVDRGPRIREALHRVHAMVDAGE-ALCIMGNHEF 83
Cdd:cd00838   2 VISDIHGNLEALEAVLEAALAK------AEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIpVYVVPGNHDI 69
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 12-57 8.75e-04

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 40.27  E-value: 8.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 15598283     12 IGDVHGCAHTLDRLLDLLGyrlqggvwRHPRRQALFLGDIVDRGPR 57
Cdd:smart00156  33 CGDIHGQFDDLLRLFDKNG--------QPPETNYVFLGDYVDRGPF 70
 
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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