NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2070836160|ref|WP_218818888|]
View 

3',5'-cyclic-AMP phosphodiesterase, partial [Pseudomonas aeruginosa]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 3-183 3.24e-118

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 PRK11148:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 275  Bit Score: 335.75  E-value: 3.24e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160   3 LESLLTLPLAGEARVRILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEG 82
Cdd:PRK11148    1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  83 IASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERHTL 162
Cdd:PRK11148   81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                         170       180
                  ....*....|....*....|.
gi 2070836160 163 LLLHHHPLPAGCSWLDQHSLR 183
Cdd:PRK11148  161 VLLHHHPLPAGCAWLDQHSLR 181
 
Name Accession Description Interval E-value
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 3-183 3.24e-118

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 335.75  E-value: 3.24e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160   3 LESLLTLPLAGEARVRILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEG 82
Cdd:PRK11148    1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  83 IASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERHTL 162
Cdd:PRK11148   81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                         170       180
                  ....*....|....*....|.
gi 2070836160 163 LLLHHHPLPAGCSWLDQHSLR 183
Cdd:PRK11148  161 VLLHHHPLPAGCAWLDQHSLR 181
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 19-183 4.23e-60

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 187.10  E-value: 4.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  19 ILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGNHD 98
Cdd:cd07402     1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  99 FQPAMYSALQDAG---ISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERHTLLLLHHHPLPAGCS 175
Cdd:cd07402    81 DRAAMREALPEPPyddNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160


                  ....*...
gi 2070836160 176 WLDQHSLR 183
Cdd:cd07402   161 WMDAIRLR 168
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
17-161 5.24e-37

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 127.89  E-value: 5.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  17 VRILQITDTHLFAQKheallGVNTWESYQAVLEAIRphQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGN 96
Cdd:COG1409     1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADIN--APRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070836160  97 HDFQPAM----YSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERHT 161
Cdd:COG1409    74 HDIRAAMaeayREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPV 142
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 18-135 4.51e-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: 51.83  E-value: 4.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  18 RILQITDTHLFAQkheallgvntWESYQAVLEAIRPHqHEFDLIVATGDLAQ--DQSSAAYQHFAEGIAsfRAPCVWLPG 95
Cdd:pfam00149   2 RILVIGDLHLPGQ----------LDDLLELLKKLLEE-GKPDLVLHAGDLVDrgPPSEEVLELLERLIK--YVPVYLVRG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2070836160  96 NHDFQPAMYSALQDA-GISPAKRVFIGEQWQILLLDSQVFG 135
Cdd:pfam00149  69 NHDFDYGECLRLYPYlGLLARPWKRFLEVFNFLPLAGILSG 109
 
Name Accession Description Interval E-value
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 3-183 3.24e-118

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 335.75  E-value: 3.24e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160   3 LESLLTLPLAGEARVRILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEG 82
Cdd:PRK11148    1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  83 IASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERHTL 162
Cdd:PRK11148   81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                         170       180
                  ....*....|....*....|.
gi 2070836160 163 LLLHHHPLPAGCSWLDQHSLR 183
Cdd:PRK11148  161 VLLHHHPLPAGCAWLDQHSLR 181
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 19-183 4.23e-60

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 187.10  E-value: 4.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  19 ILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGNHD 98
Cdd:cd07402     1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  99 FQPAMYSALQDAG---ISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERHTLLLLHHHPLPAGCS 175
Cdd:cd07402    81 DRAAMREALPEPPyddNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160


                  ....*...
gi 2070836160 176 WLDQHSLR 183
Cdd:cd07402   161 WMDAIRLR 168
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
17-161 5.24e-37

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 127.89  E-value: 5.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  17 VRILQITDTHLFAQKheallGVNTWESYQAVLEAIRphQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGN 96
Cdd:COG1409     1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADIN--APRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070836160  97 HDFQPAM----YSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERHT 161
Cdd:COG1409    74 HDIRAAMaeayREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPV 142
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
9-112 6.85e-10

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 56.34  E-value: 6.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160   9 LPlAGEARVRILQITDTHlfaqkhealLGVNTWESY-QAVLEAIRphQHEFDLIVATGDLAqDQSSAAYQHFAEGIASFR 87
Cdd:COG1408    36 LP-PAFDGLRIVQLSDLH---------LGPFIGGERlERLVEKIN--ALKPDLVVLTGDLV-DGSVAELEALLELLKKLK 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2070836160  88 APC----VWlpGNHDF---QPAMYSALQDAGI 112
Cdd:COG1408   103 APLgvyaVL--GNHDYyagLEELRAALEEAGV 132
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 18-135 4.51e-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: 51.83  E-value: 4.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  18 RILQITDTHLFAQkheallgvntWESYQAVLEAIRPHqHEFDLIVATGDLAQ--DQSSAAYQHFAEGIAsfRAPCVWLPG 95
Cdd:pfam00149   2 RILVIGDLHLPGQ----------LDDLLELLKKLLEE-GKPDLVLHAGDLVDrgPPSEEVLELLERLIK--YVPVYLVRG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2070836160  96 NHDFQPAMYSALQDA-GISPAKRVFIGEQWQILLLDSQVFG 135
Cdd:pfam00149  69 NHDFDYGECLRLYPYlGLLARPWKRFLEVFNFLPLAGILSG 109
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
18-112 4.74e-09

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 53.48  E-value: 4.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  18 RILQITDTHLfaqkheallgvnTWESYQAVLEAIRphQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGNH 97
Cdd:COG2129     1 KILAVSDLHG------------NFDLLEKLLELAR--AEDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNH 66

                          90
                  ....*....|....*
gi 2070836160  98 DFqPAMYSALQDAGI 112
Cdd:COG2129    67 DD-PEVLDALEESGV 80
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 20-99 3.58e-06

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: 44.57  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  20 LQITDTHLfaqkheallgvnTWESYQAVLEAIRPHQHEFDLIVATGDLAQD-QSSAAYQHFAEGIASFRAPCVWLPGNHD 98
Cdd:cd00838     1 LVISDIHG------------NLEALEAVLEAALAKAEKPDLVICLGDLVDYgPDPEEVELKALRLLLAGIPVYVVPGNHD 68


                  .
gi 2070836160  99 F 99
Cdd:cd00838    69 I 69
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 18-114 2.79e-05

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE 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: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 43.04  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  18 RILQITDTHLFAQKHEALLgvntwesyQAVLEAIRphQHEFDLIVATGDLAQDQSSaAYQHFAEGIASFRAP----CVWl 93
Cdd:cd07385     3 RIVQLSDIHLGPFVGRTRL--------QKVVRKVN--ELNPDLIVITGDLVDGDVS-VLRLLASPLSKLKAPlgvyFVL- 70

                          90       100
                  ....*....|....*....|....*
gi 2070836160  94 pGNHDF----QPAMYSALQDAGISP 114
Cdd:cd07385    71 -GNHDYysgdVEVWIAALEKAGITV 94
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 19-121 3.95e-05

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: 42.30  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  19 ILQITDTHlfaqkheallgvntwESYQAvLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGNHD 98
Cdd:cd07392     1 ILAISDVH---------------GDVPK-LKKIKLKAEEADAVIVAGDITHFGPGEEAIEALNLLLAIGAPVLAVPGNCD 64

                          90       100
                  ....*....|....*....|....
gi 2070836160  99 fQPAMYSALQDAGIS-PAKRVFIG 121
Cdd:cd07392    65 -TPEVLGELNSAGLNiHGKVVEVG 87
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
17-161 1.59e-04

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 41.05  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  17 VRILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRphQHEFDLIVATGDL--AQDQSSAAYQHFAEGIASFRA---PCV 91
Cdd:COG0420     1 MRFLHTADWHLGKPLHGASRREDQLAALDRLVDLAI--EEKVDAVLIAGDLfdSANPSPEAVRLLAEALRRLSEagiPVV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070836160  92 WLPGNHDFQP---AMYSALQDAGIspakRVFIGEQWQILLLDS----QVFGVPHgeLSEFQLEWLERKLADAPERHT 161
Cdd:COG0420    79 LIAGNHDSPSrlsAGSPLLENLGV----HVFGSVEPEPVELEDglgvAVYGLPY--LRPSDEEALRDLLERLPRALD 149
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 18-99 1.93e-04

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 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: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 40.33  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  18 RILQITDTHL-FAQKHEALLGVNTWESYQAVLEAIRphQHEFDLIVATGDLAQDQS-SAAYQHFAegIASFRA------P 89
Cdd:cd00840     1 RFLHTADWHLgYPLYGLSRREEDFFKAFEEIVDLAI--EEKVDFVLIAGDLFDSNNpSPEALKLA--IEGLRRlceagiP 76

                          90
                  ....*....|
gi 2070836160  90 CVWLPGNHDF 99
Cdd:cd00840    77 VFVIAGNHDS 86
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 36-154 2.34e-04

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 40.36  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  36 LGVNTWESYQAvLEAIRPHQHEFDLIVATGDLAQD--QSSA----AYQHFAEGIASfRAPCVWLPGNHD----FQPAMYS 105
Cdd:cd00839    13 MGQNTNNSTNT-LDHLEKELGNYDAIIHVGDIAYAdgYNNGsrwdTFMRQIEPLAS-YVPYMVAPGNHEadynGSTSKIK 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2070836160 106 ALQDAGISPAKRVFIGEQW---------QILLLDSQVFGVPHGELSEfQLEWLERKLA 154
Cdd:cd00839    91 FFMPGRGMPPSPSGSTENLwysfdvgpvHFISLSTETDFLKGDNISP-QYDWLEADLA 147
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 59-159 7.58e-04

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 38.85  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  59 DLIVATGDL-----AQDQSSAAYQHFAEGIASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVF-----IGEQWQILL 128
Cdd:cd07396    48 AFVVQLGDIidgynAKDRSKEALDAVLSILDRLKGPVHHVLGNHEFYNFPREYLNHLKTLNGEDAYyysfsPGPGFRFLV 127

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2070836160 129 LDSQVFgvpHGELSEFQLEWLERKLADAPER 159
Cdd:cd07396   128 LDFVKF---NGGIGEEQLAWLRNELTSADAN 155
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 19-98 3.01e-03

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the 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: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 36.12  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070836160  19 ILQITDTHLFAQKHEALLGVNTWEsyqaVLEAIRPhqhefDLIVATGDLAQDQSSAAYQHFAEGIASFRA-PCVWLPGNH 97
Cdd:cd07400     1 IAHISDLHFGEERKPEVLELNLLD----EINALKP-----DLVVVTGDLTQRARPAEFEEAREFLDALEPePVVVVPGNH 71


                  .
gi 2070836160  98 D 98
Cdd:cd07400    72 D 72
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH