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Conserved domains on  [gi|1956236906|ref|WP_200203939|]
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metallophosphoesterase [Bacillus toyonensis]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 16-160 7.09e-16

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.


The actual alignment was detected with superfamily member cd00144:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 229  Bit Score: 75.87  E-value: 7.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  16 IIISDIHGELNLLKELLHKVNFKNEDYLIINGDLCEKGSDSIGVVDYVMDLVESNL-NVHVVEGNCEvlvDALLNENPGL 94
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPdNVFLLRGNHE---FMLLNFLYGF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956236906  95 INYLCTRKHSIFNEWLeqlhfsiqedtsiqevkevllshFSKEINWLNKLPTAIE-TEDYIFVHAGL 160
Cdd:cd00144    78 YDERTLRCLRKGGEEL-----------------------WREFNEVFNYLPLAALvDGKILCVHGGL 121
 
Name Accession Description Interval E-value
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 16-160 7.09e-16

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: 75.87  E-value: 7.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  16 IIISDIHGELNLLKELLHKVNFKNEDYLIINGDLCEKGSDSIGVVDYVMDLVESNL-NVHVVEGNCEvlvDALLNENPGL 94
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPdNVFLLRGNHE---FMLLNFLYGF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956236906  95 INYLCTRKHSIFNEWLeqlhfsiqedtsiqevkevllshFSKEINWLNKLPTAIE-TEDYIFVHAGL 160
Cdd:cd00144    78 YDERTLRCLRKGGEEL-----------------------WREFNEVFNYLPLAALvDGKILCVHGGL 121
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 14-113 2.17e-09

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: 54.53  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  14 RVIIISDIH--GELNLLKELLHKVNFKNE-DYLIINGDLCEKGSDSIGVVDYVMDLVEsNLNVHVVEGNCEVLVDALLNE 90
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKpDLVLHAGDLVDRGPPSEEVLELLERLIK-YVPVYLVRGNHDFDYGECLRL 80

                          90       100
                  ....*....|....*....|...
gi 1956236906  91 NPGLINYlcTRKHSIFNEWLEQL 113
Cdd:pfam00149  81 YPYLGLL--ARPWKRFLEVFNFL 101
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
14-92 2.64e-08

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 53.00  E-value: 2.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956236906  14 RVIIISDIHGELNLLKELLHKVNFKNEDYLIINGDLCEKGSDSIGVVDYVMDlvesnLNVHVVEGNCEVLVDALLNENP 92
Cdd:COG0622     1 KIAVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEVLDLLRE-----LPIVAVRGNHDGAVLRGLRSLP 74
PHA02239 PHA02239
putative protein phosphatase
 15-167 6.29e-07

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 49.99  E-value: 6.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  15 VIIISDIHGELNLLKELLHKVN--FKNEDYLIINGDLCEKGSDSIGVVDYVMDLVESNLNVHVVEGNCEvlvDALLN--E 90
Cdd:PHA02239    3 IYVVPDIHGEYQKLLTIMDKINneRKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLLGNHD---DEFYNimE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  91 NpglINYLctrkhSIFN-EWLEQLHFSIQEDTSI-------QEVKEVLLSHFSKEINWLNKLPtaiETED---------- 152
Cdd:PHA02239   80 N---VDRL-----SIYDiEWLSRYCIETLNSYGVstvtlkySSVEENLRNNYDFIKSELKKLK---ESDDyrkfkilmvn 148

                         170       180
                  ....*....|....*....|....
gi 1956236906 153 ---------YIFVHAGledRVDWK 167
Cdd:PHA02239  149 crkyykedkYIFSHSG---GVSWK 169
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 15-82 4.92e-03

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: 38.35  E-value: 4.92e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906   15 VIIISDIHGELNLLKELLHKVNFKNEDYLIINGDLCEKGSDSIGVVD--YVMDLVESNlNVHVVEGNCEV 82
Cdd:smart00156  30 VTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILllFALKILYPN-RIVLLRGNHES 98
 
Name Accession Description Interval E-value
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 16-160 7.09e-16

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: 75.87  E-value: 7.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  16 IIISDIHGELNLLKELLHKVNFKNEDYLIINGDLCEKGSDSIGVVDYVMDLVESNL-NVHVVEGNCEvlvDALLNENPGL 94
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPdNVFLLRGNHE---FMLLNFLYGF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956236906  95 INYLCTRKHSIFNEWLeqlhfsiqedtsiqevkevllshFSKEINWLNKLPTAIE-TEDYIFVHAGL 160
Cdd:cd00144    78 YDERTLRCLRKGGEEL-----------------------WREFNEVFNYLPLAALvDGKILCVHGGL 121
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 15-160 1.89e-10

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: 60.64  E-value: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  15 VIIISDIHGELNLLKELLHKVNFK-NEDYLIINGDLCEKGSDSIGVVDYVMDLVESnlnVHVVEGNCEVLVdallnenpg 93
Cdd:cd07422     1 TYAIGDIQGCYDELQRLLEKINFDpAKDRLWLVGDLVNRGPDSLETLRFVKSLGDS---AVVVLGNHDLHL--------- 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  94 LINYLCTRKHSifnewleqlhfsiQEDTsiqeVKEVLLSHFSKE-INWLNKLPTAIE--TEDYIFVHAGL 160
Cdd:cd07422    69 LAVAAGIKKLK-------------KKDT----LDEILEAPDRDElLDWLRHQPLLHRddELGIVMVHAGI 121
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 14-113 2.17e-09

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: 54.53  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  14 RVIIISDIH--GELNLLKELLHKVNFKNE-DYLIINGDLCEKGSDSIGVVDYVMDLVEsNLNVHVVEGNCEVLVDALLNE 90
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKpDLVLHAGDLVDRGPPSEEVLELLERLIK-YVPVYLVRGNHDFDYGECLRL 80

                          90       100
                  ....*....|....*....|...
gi 1956236906  91 NPGLINYlcTRKHSIFNEWLEQL 113
Cdd:pfam00149  81 YPYLGLL--ARPWKRFLEVFNFL 101
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 16-84 2.34e-09

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: 54.97  E-value: 2.34e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956236906  16 IIISDIHGELNLLKELLHKVNFKNE--DYLIINGDLCEKGSDSIGVVDYVMDLVESNLNVHVVEGNCEVLV 84
Cdd:cd00838     1 LVISDIHGNLEALEAVLEAALAKAEkpDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHDILV 71
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
14-92 2.64e-08

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 53.00  E-value: 2.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956236906  14 RVIIISDIHGELNLLKELLHKVNFKNEDYLIINGDLCEKGSDSIGVVDYVMDlvesnLNVHVVEGNCEVLVDALLNENP 92
Cdd:COG0622     1 KIAVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEVLDLLRE-----LPIVAVRGNHDGAVLRGLRSLP 74
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
14-81 1.86e-07

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 51.17  E-value: 1.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956236906  14 RVIIISDIHGELNLLKELLHKVNFKNEDYLIINGDLCEKGSDSIgVVDYVMDLVESNLNVHVVEGNCE 81
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEE-AREVLEELAALGVPVLAVPGNHD 67
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 17-91 6.22e-07

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: 49.82  E-value: 6.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  17 IISDIHGELNLLKELLHKVNFKNEDY----------LIINGDLCEKGSDSIGVVDYVMDLVESNlNVHVVEGN-CEVLVD 85
Cdd:cd07423     2 IIGDVHGCYDELVELLEKLGYQKKEEglyvhpegrkLVFLGDLVDRGPDSIDVLRLVMNMVKAG-KALYVPGNhCNKLYR 80


                  ....*.
gi 1956236906  86 ALLNEN 91
Cdd:cd07423    81 YLKGRN 86
PHA02239 PHA02239
putative protein phosphatase
 15-167 6.29e-07

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 49.99  E-value: 6.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  15 VIIISDIHGELNLLKELLHKVN--FKNEDYLIINGDLCEKGSDSIGVVDYVMDLVESNLNVHVVEGNCEvlvDALLN--E 90
Cdd:PHA02239    3 IYVVPDIHGEYQKLLTIMDKINneRKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLLGNHD---DEFYNimE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  91 NpglINYLctrkhSIFN-EWLEQLHFSIQEDTSI-------QEVKEVLLSHFSKEINWLNKLPtaiETED---------- 152
Cdd:PHA02239   80 N---VDRL-----SIYDiEWLSRYCIETLNSYGVstvtlkySSVEENLRNNYDFIKSELKKLK---ESDDyrkfkilmvn 148

                         170       180
                  ....*....|....*....|....
gi 1956236906 153 ---------YIFVHAGledRVDWK 167
Cdd:PHA02239  149 crkyykedkYIFSHSG---GVSWK 169
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 14-200 1.64e-06

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: 48.08  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  14 RVIIISDIHGELNLLKELLHKVNFKNE-DYLIINGDLCEKGSDSIGVVDYvmdlvesnLN---VHVVEGNCE-VLVDALL 88
Cdd:cd07424     2 RDFVVGDIHGHFQRLQRALDAVGFDPArDRLISVGDLVDRGPESLEVLEL--------LKqpwFHAVQGNHEqMAIDALR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  89 NENPGLinylcTRKHSifNEWLEQLHFSIQEDtsiqevkeVLLShfskeinwLNKLPTAIETED----YIFVHAGLEDRV 164
Cdd:cd07424    74 GGDDVM-----WRANG--GGWFFDLPDEEAKV--------LLEK--------LHHLPIAIEVESrngkVGIVHADYPFDE 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1956236906 165 DWKETARKNAIAMPEFFNKSHRAN---------KYVVVGHWPVVN 200
Cdd:cd07424   131 YSFGFVEKPEDEEEALWSRDRLQKsqtqpvagaDAFIFGHTPVPE 175
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
17-160 2.21e-06

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 48.62  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  17 IISDIHGELNLLKELLHKVNF-KNEDYLIINGDLCEKGSDSIGVVDYVMDLVESnlnVHVVEGNcevlvdallnenpgli 95
Cdd:PRK00166    5 AIGDIQGCYDELQRLLEKIDFdPAKDTLWLVGDLVNRGPDSLEVLRFVKSLGDS---AVTVLGN---------------- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956236906  96 nylctrkHSIFnewLEQLHFSIQE----DTsiqeVKEVLLSHFSKE-INWLNKLPTAIETED--YIFVHAGL 160
Cdd:PRK00166   66 -------HDLH---LLAVAAGIKRnkkkDT----LDPILEAPDRDElLDWLRHQPLLHVDEElgLVMVHAGI 123
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 14-88 2.22e-04

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain family 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: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 41.10  E-value: 2.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956236906  14 RVIIISDIHGELNLLKELLHKVNfKNEDYLIINGDLcekGSDSIgvvdyVMDLVESNLNVHVVEGNCEVLVDALL 88
Cdd:cd00841     1 KIGVISDTHGNLEAIEKALELFE-DGVDAVIHAGDF---VSPFV-----LNALLELKAPLIAVRGNNDGEVDQLL 66
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 16-224 2.79e-04

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, 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: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 41.52  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  16 IIISDIHGELNLLKELLHKVNF--------KNEDYLIINGDLCEKGSDSIGVVDYVMDL----VESNLNVHVVEGNCEVL 83
Cdd:cd07425     1 VAIGDLHGDLDRLRTILKLAGVidsndrwiGGDTVVVQTGDILDRGDDEIEILKLLEKLkrqaRKAGGKVILLLGNHELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  84 V--DALLNENPGLINYLCTRKHSIFNEWLeqlhfsiqedtsiqevKEVLLShfskeiNWLNKLPTAIETEDYIFVHAGLE 161
Cdd:cd07425    81 NlcGDFRYVHPRGLNEFGGVAKRRYALLS----------------DGGYIG------RYLRTHPVVLVVNDILFVHGGLG 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956236906 162 ---DRVDWKETARKNAIAMPEFFNKSHRANKYVVVGHWPVVNYSEEAPSNNpvidkekKIIAIDGG 224
Cdd:cd07425   139 plwSRGYSLETKNGACERSALDKALAKLGVKRMVVGHTPQEGGVVNTLCGG-------KLIRIDVG 197
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 17-91 7.07e-04

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 40.84  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  17 IISDIHGELNLLKELLHKVNFKNEDYLIIN---------GDLCEKGSDSIGVVDYVMDLVESNLnVHVVEGN-CEVLVDA 86
Cdd:PRK13625    5 IIGDIHGCYQEFQALTEKLGYNWSSGLPVHpdqrklafvGDLTDRGPHSLRMIEIVWELVEKKA-AYYVPGNhCNKLYRF 83


                  ....*
gi 1956236906  87 LLNEN 91
Cdd:PRK13625   84 FLGRN 88
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 15-89 1.05e-03

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. The domain present in members of this family 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: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 39.60  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906  15 VIIISDIHGELNLLKELLHKVNFKneDYLIINGDLCEKGSDSIGVVDyVMDLVESNLNVHVVEGNC------EVLVDALL 88
Cdd:cd07392     1 ILAISDVHGDVPKLKKIKLKAEEA--DAVIVAGDITHFGPGEEAIEA-LNLLLAIGAPVLAVPGNCdtpevlGELNSAGL 77


                  .
gi 1956236906  89 N 89
Cdd:cd07392    78 N 78
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 14-81 3.19e-03

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 37.68  E-value: 3.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956236906  14 RVIIISDIHGELNLLKELLHKvnFKNEDYLIIN-GDLCEKgsdsiGVVDYVMDLVEsnlnVHVVEGNCE 81
Cdd:pfam12850   2 RIGIISDTHDNLALPEAALER--LKGVVDLIIHaGDIVAP-----EVLEELLELAP----VLAVRGNND 59
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 15-82 4.92e-03

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: 38.35  E-value: 4.92e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956236906   15 VIIISDIHGELNLLKELLHKVNFKNEDYLIINGDLCEKGSDSIGVVD--YVMDLVESNlNVHVVEGNCEV 82
Cdd:smart00156  30 VTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILllFALKILYPN-RIVLLRGNHES 98
 
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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