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Conserved domains on  [gi|446366897|ref|WP_000444752|]
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MULTISPECIES: 3',5'-cyclic-AMP phosphodiesterase [Enterobacteriaceae]

Protein Classification

3',5'-cyclic-AMP phosphodiesterase( domain architecture ID 10793542)

3',5'-cyclic-AMP phosphodiesterase catalyzes the hydrolysis of adenosine 3',5'-cyclic phosphate (cAMP) to form adenosine 5'-phosphate (5'-AMP); belongs to metallophosphatase (MPP) superfamily, whose members 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
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 1-275 0e+00

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


:

Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 532.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897   1 MESLLTLPLAGEARVRILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEG 80
Cdd:PRK11148   1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  81 IASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPGRHTL 160
Cdd:PRK11148  81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897 161 LLLHHHPLPAGCSWLDQHSLRNAGELDTVLAKFPHVKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTIA 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446366897 241 PGWRTLELHADGTLTTEVHRLADTRFQPDTASEGY 275
Cdd:PRK11148 241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
 
Name Accession Description Interval E-value
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 1-275 0e+00

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


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 532.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897   1 MESLLTLPLAGEARVRILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEG 80
Cdd:PRK11148   1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  81 IASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPGRHTL 160
Cdd:PRK11148  81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897 161 LLLHHHPLPAGCSWLDQHSLRNAGELDTVLAKFPHVKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTIA 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446366897 241 PGWRTLELHADGTLTTEVHRLADTRFQPDTASEGY 275
Cdd:PRK11148 241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 17-253 1.54e-95

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: 280.70  E-value: 1.54e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  17 ILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGNHD 96
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  97 FQPAMYSALQDAG---ISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPGRHTLLLLHHHPLPAGCS 173
Cdd:cd07402   81 DRAAMREALPEPPyddNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897 174 WLDQHSLRNAGELDTVLAKFPHVKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTIAPGWRTLELHADGT 253
Cdd:cd07402  161 WMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHADGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
15-263 1.13e-56

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 181.81  E-value: 1.13e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  15 VRILQITDTHLFAQKheallGVNTWESYQAVLEAIRphQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGN 94
Cdd:COG1409    1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADIN--APRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  95 HDFQPAM----YSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPGRHT--------LLL 162
Cdd:COG1409   74 HDIRAAMaeayREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVivflhhppYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897 163 LhhhplpagcSWLDQHSLRNAGELDTVLAKFpHVKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPhcsnftldtiAPG 242
Cdd:COG1409  154 G---------SGSDRIGLRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL----------PPG 213

                        250       260
                 ....*....|....*....|.
gi 446366897 243 WRTLELHADGtLTTEVHRLAD 263
Cdd:COG1409  214 YRVIEVDGDG-LTVEVRRVDG 233
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-133 5.53e-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: 52.99  E-value: 5.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897   16 RILQITDTHLFAQkheallgvntWESYQAVLEAIRPHqHEFDLIVATGDLAQ--DQSSAAYQHFAEGIAsfRAPCVWLPG 93
Cdd:pfam00149   2 RILVIGDLHLPGQ----------LDDLLELLKKLLEE-GKPDLVLHAGDLVDrgPPSEEVLELLERLIK--YVPVYLVRG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446366897   94 NHDFQPAMYSALQDA-GISPAKRVFIGEQWQILLLDSQVFG 133
Cdd:pfam00149  69 NHDFDYGECLRLYPYlGLLARPWKRFLEVFNFLPLAGILSG 109
 
Name Accession Description Interval E-value
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 1-275 0e+00

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


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 532.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897   1 MESLLTLPLAGEARVRILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEG 80
Cdd:PRK11148   1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  81 IASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPGRHTL 160
Cdd:PRK11148  81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897 161 LLLHHHPLPAGCSWLDQHSLRNAGELDTVLAKFPHVKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTIA 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446366897 241 PGWRTLELHADGTLTTEVHRLADTRFQPDTASEGY 275
Cdd:PRK11148 241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 17-253 1.54e-95

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: 280.70  E-value: 1.54e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  17 ILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGNHD 96
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  97 FQPAMYSALQDAG---ISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPGRHTLLLLHHHPLPAGCS 173
Cdd:cd07402   81 DRAAMREALPEPPyddNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897 174 WLDQHSLRNAGELDTVLAKFPHVKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTIAPGWRTLELHADGT 253
Cdd:cd07402  161 WMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHADGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
15-263 1.13e-56

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 181.81  E-value: 1.13e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  15 VRILQITDTHLFAQKheallGVNTWESYQAVLEAIRphQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGN 94
Cdd:COG1409    1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADIN--APRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  95 HDFQPAM----YSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPGRHT--------LLL 162
Cdd:COG1409   74 HDIRAAMaeayREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVivflhhppYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897 163 LhhhplpagcSWLDQHSLRNAGELDTVLAKFpHVKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPhcsnftldtiAPG 242
Cdd:COG1409  154 G---------SGSDRIGLRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL----------PPG 213

                        250       260
                 ....*....|....*....|.
gi 446366897 243 WRTLELHADGtLTTEVHRLAD 263
Cdd:COG1409  214 YRVIEVDGDG-LTVEVRRVDG 233
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
16-215 1.39e-12

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 65.04  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  16 RILQITDTHLfaqkheallgvnTWESYQAVLEAIRphQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGNH 95
Cdd:COG2129    1 KILAVSDLHG------------NFDLLEKLLELAR--AEDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  96 DFqPAMYSALQDAGispakrvfigeqwqILLLDSQVF---GV-----------PHGELSEFQLEWLERKLAD-------- 153
Cdd:COG2129   67 DD-PEVLDALEESG--------------VHNLHGRVVeigGLriaglggsrptPFGTPYEYTEEEIEERLAKlrekdvdi 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446366897 154 ----APGRHTLLLLHHHPLPAGCSwldqhslrnagELDTVLAKFpHVKYLLCGHIHQELDLDWNGR 215
Cdd:COG2129  132 llthAPPYGTTLDRVEDGPHVGSK-----------ALRELIEEF-QPKLVLHGHIHESRGVDKIGG 185
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
7-110 1.54e-09

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 57.11  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897   7 LPlAGEARVRILQITDTHlfaqkhealLGVNTWESY-QAVLEAIRphQHEFDLIVATGDLAqDQSSAAYQHFAEGIASFR 85
Cdd:COG1408   36 LP-PAFDGLRIVQLSDLH---------LGPFIGGERlERLVEKIN--ALKPDLVVLTGDLV-DGSVAELEALLELLKKLK 102

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446366897  86 APC----VWlpGNHDF---QPAMYSALQDAGI 110
Cdd:COG1408  103 APLgvyaVL--GNHDYyagLEELRAALEEAGV 132
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-133 5.53e-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: 52.99  E-value: 5.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897   16 RILQITDTHLFAQkheallgvntWESYQAVLEAIRPHqHEFDLIVATGDLAQ--DQSSAAYQHFAEGIAsfRAPCVWLPG 93
Cdd:pfam00149   2 RILVIGDLHLPGQ----------LDDLLELLKKLLEE-GKPDLVLHAGDLVDrgPPSEEVLELLERLIK--YVPVYLVRG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446366897   94 NHDFQPAMYSALQDA-GISPAKRVFIGEQWQILLLDSQVFG 133
Cdd:pfam00149  69 NHDFDYGECLRLYPYlGLLARPWKRFLEVFNFLPLAGILSG 109
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 18-97 4.19e-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: 45.34  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  18 LQITDTHLfaqkheallgvnTWESYQAVLEAIRPHQHEFDLIVATGDLAQD-QSSAAYQHFAEGIASFRAPCVWLPGNHD 96
Cdd:cd00838    1 LVISDIHG------------NLEALEAVLEAALAKAEKPDLVICLGDLVDYgPDPEEVELKALRLLLAGIPVYVVPGNHD 68


                 .
gi 446366897  97 F 97
Cdd:cd00838   69 I 69
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 57-205 6.31e-06

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: 46.17  E-value: 6.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  57 DLIVATGDL-----AQDQSSAAYQHFAEGIASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVF-----IGEQWQILL 126
Cdd:cd07396   48 AFVVQLGDIidgynAKDRSKEALDAVLSILDRLKGPVHHVLGNHEFYNFPREYLNHLKTLNGEDAYyysfsPGPGFRFLV 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446366897 127 LDSQVFgvpHGELSEFQLEWLERKLADAPGRHTLLLLHHHPLPAGCSWLDQHSLRNAGELDTVLAKFPHVKYLLCGHIH 205
Cdd:cd07396  128 LDFVKF---NGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWNYEEVLAILESYPCVKACFSGHNH 203
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
15-206 2.95e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 44.13  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  15 VRILQITDTHLFAQKHEALLGVNTWESYQAVLEAIRphQHEFDLIVATGDL--AQDQSSAAYQHFAEGIASFRA---PCV 89
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASRREDQLAALDRLVDLAI--EEKVDAVLIAGDLfdSANPSPEAVRLLAEALRRLSEagiPVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  90 WLPGNHDFQP---AMYSALQDAGIspakRVFIGEQWQILLLDS----QVFGVPHGELSEFQ-----LEWLERKLADAPGR 157
Cdd:COG0420   79 LIAGNHDSPSrlsAGSPLLENLGV----HVFGSVEPEPVELEDglgvAVYGLPYLRPSDEEalrdlLERLPRALDPGGPN 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446366897 158 ----HTllllhhhplpaGCSWLDQHSLRNAGELDTVLAKFPHVKYLLCGHIHQ 206
Cdd:COG0420  155 illlHG-----------FVAGASGSRDIYVAPVPLSALPAAGFDYVALGHIHR 196
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 16-112 5.76e-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: 43.42  E-value: 5.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  16 RILQITDTHLFAQKHEALLgvntwesyQAVLEAIRphQHEFDLIVATGDLAQDQSSaAYQHFAEGIASFRAP----CVWl 91
Cdd:cd07385    3 RIVQLSDIHLGPFVGRTRL--------QKVVRKVN--ELNPDLIVITGDLVDGDVS-VLRLLASPLSKLKAPlgvyFVL- 70

                         90       100
                 ....*....|....*....|....*
gi 446366897  92 pGNHDF----QPAMYSALQDAGISP 112
Cdd:cd07385   71 -GNHDYysgdVEVWIAALEKAGITV 94
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 17-119 8.90e-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: 8.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  17 ILQITDTHlfaqkheallgvntwESYQAvLEAIRPHQHEFDLIVATGDLAQDQSSAAYQHFAEGIASFRAPCVWLPGNHD 96
Cdd:cd07392    1 ILAISDVH---------------GDVPK-LKKIKLKAEEADAVIVAGDITHFGPGEEAIEALNLLLAIGAPVLAVPGNCD 64

                         90       100
                 ....*....|....*....|....
gi 446366897  97 fQPAMYSALQDAGIS-PAKRVFIG 119
Cdd:cd07392   65 -TPEVLGELNSAGLNiHGKVVEVG 87
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 16-97 1.43e-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: 41.49  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  16 RILQITDTHL-FAQKHEALLGVNTWESYQAVLEAIRphQHEFDLIVATGDLAQDQS-SAAYQHFAegIASFRA------P 87
Cdd:cd00840    1 RFLHTADWHLgYPLYGLSRREEDFFKAFEEIVDLAI--EEKVDFVLIAGDLFDSNNpSPEALKLA--IEGLRRlceagiP 76

                         90
                 ....*....|
gi 446366897  88 CVWLPGNHDF 97
Cdd:cd00840   77 VFVIAGNHDS 86
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 34-152 4.31e-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: 41.13  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  34 LGVNTWESYQAvLEAIRPHQHEFDLIVATGDLAQD--QSSA----AYQHFAEGIASfRAPCVWLPGNHD----FQPAMYS 103
Cdd:cd00839   13 MGQNTNNSTNT-LDHLEKELGNYDAIIHVGDIAYAdgYNNGsrwdTFMRQIEPLAS-YVPYMVAPGNHEadynGSTSKIK 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446366897 104 ALQDAGISPAKRVFIGEQW---------QILLLDSQVFGVPHGELSEfQLEWLERKLA 152
Cdd:cd00839   91 FFMPGRGMPPSPSGSTENLwysfdvgpvHFISLSTETDFLKGDNISP-QYDWLEADLA 147
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 17-96 3.07e-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: 36.89  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446366897  17 ILQITDTHLFAQKHEALLGVNTWEsyqaVLEAIRPhqhefDLIVATGDLAQDQSSAAYQHFAEGIASFRA-PCVWLPGNH 95
Cdd:cd07400    1 IAHISDLHFGEERKPEVLELNLLD----EINALKP-----DLVVVTGDLTQRARPAEFEEAREFLDALEPePVVVVPGNH 71


                 .
gi 446366897  96 D 96
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.
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