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Conserved domains on  [gi|1541543846|gb|RTM87674|]
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3',5'-cyclic-AMP phosphodiesterase [Enterobacter roggenkampii]

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: 536.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846   1 MESLLNLTVAGGAPVRILQITDTHLFAEKHETLLGVNTWESYQAVLSAIHAENRACDLIVATGDLAQDQSSAAYQHFAEG 80
Cdd:PRK11148    1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  81 IASFSAPCVWLPGNHDFQPAMYSSLQDAGISPAKCVFAGEQWQILLLDSQVFGVPHGELSEFQLDWLETKLAAEPERHTL 160
Cdd:PRK11148   81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846 161 LLLHHHPLPAGCSWLDQHSLRNSAALDRVLAKFPRVKNLLCGHIHQEQDLDWNGRRMLATPSTCVQFKPHCANFTLDTIA 240
Cdd:PRK11148  161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1541543846 241 PGWRWLELHPNGTLTTEVCRLTGAQFRPDTASEGY 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: 536.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846   1 MESLLNLTVAGGAPVRILQITDTHLFAEKHETLLGVNTWESYQAVLSAIHAENRACDLIVATGDLAQDQSSAAYQHFAEG 80
Cdd:PRK11148    1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  81 IASFSAPCVWLPGNHDFQPAMYSSLQDAGISPAKCVFAGEQWQILLLDSQVFGVPHGELSEFQLDWLETKLAAEPERHTL 160
Cdd:PRK11148   81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846 161 LLLHHHPLPAGCSWLDQHSLRNSAALDRVLAKFPRVKNLLCGHIHQEQDLDWNGRRMLATPSTCVQFKPHCANFTLDTIA 240
Cdd:PRK11148  161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1541543846 241 PGWRWLELHPNGTLTTEVCRLTGAQFRPDTASEGY 275
Cdd:PRK11148  241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 17-253 9.69e-93

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: 273.77  E-value: 9.69e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  17 ILQITDTHLFAEKHETLLGVNTWESYQAVLSAIHAENRACDLIVATGDLAQDQSSAAYQHFAEGIASFSAPCVWLPGNHD 96
Cdd:cd07402     1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  97 FQPAMYSSLQDAG---ISPAKCVFAGEQWQILLLDSQVFGVPHGELSEFQLDWLETKLAAEPERHTLLLLHHHPLPAGCS 173
Cdd:cd07402    81 DRAAMREALPEPPyddNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846 174 WLDQHSLRNSAALDRVLAKFPRVKNLLCGHIHQEQDLDWNGRRMLATPSTCVQFKPHCANFTLDTIAPGWRWLELHPNGT 253
Cdd:cd07402   161 WMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHADGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
15-264 1.98e-56

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 181.04  E-value: 1.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  15 VRILQITDTHLFAEKhetllGVNTWESYQAVLSAIHAENraCDLIVATGDLAQDQSSAAYQHFAEGIASFSAPCVWLPGN 94
Cdd:COG1409     1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADINAPR--PDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  95 HDFQPAMYSSLQDA----GISPAKCVFAGEQWQILLLDSQVFGVPHGELSEFQLDWLETKLAAEPERHTLLLLHHHPLPA 170
Cdd:COG1409    74 HDIRAAMAEAYREYfgdlPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVIVFLHHPPYST 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846 171 GcSWLDQHSLRNSAALDRVLAKFpRVKNLLCGHIHQEQDLDWNGRRMLATPSTCVQFKPhcanftldtiAPGWRWLELHP 250
Cdd:COG1409   154 G-SGSDRIGLRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL----------PPGYRVIEVDG 221

                         250
                  ....*....|....
gi 1541543846 251 NGtLTTEVCRLTGA 264
Cdd:COG1409   222 DG-LTVEVRRVDGG 234
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-133 6.48e-08

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: 49.90  E-value: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  16 RILQITDTHLFAEkhetllgvntWESYQAVLSAIHAENRAcDLIVATGDLAQDQS-SAAYQHFAEGIASFsAPCVWLPGN 94
Cdd:pfam00149   2 RILVIGDLHLPGQ----------LDDLLELLKKLLEEGKP-DLVLHAGDLVDRGPpSEEVLELLERLIKY-VPVYLVRGN 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1541543846  95 HDFQPAMYSSLQDA-GISPAKCVFAGEQWQILLLDSQVFG 133
Cdd:pfam00149  70 HDFDYGECLRLYPYlGLLARPWKRFLEVFNFLPLAGILSG 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: 536.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846   1 MESLLNLTVAGGAPVRILQITDTHLFAEKHETLLGVNTWESYQAVLSAIHAENRACDLIVATGDLAQDQSSAAYQHFAEG 80
Cdd:PRK11148    1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  81 IASFSAPCVWLPGNHDFQPAMYSSLQDAGISPAKCVFAGEQWQILLLDSQVFGVPHGELSEFQLDWLETKLAAEPERHTL 160
Cdd:PRK11148   81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846 161 LLLHHHPLPAGCSWLDQHSLRNSAALDRVLAKFPRVKNLLCGHIHQEQDLDWNGRRMLATPSTCVQFKPHCANFTLDTIA 240
Cdd:PRK11148  161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1541543846 241 PGWRWLELHPNGTLTTEVCRLTGAQFRPDTASEGY 275
Cdd:PRK11148  241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 17-253 9.69e-93

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: 273.77  E-value: 9.69e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  17 ILQITDTHLFAEKHETLLGVNTWESYQAVLSAIHAENRACDLIVATGDLAQDQSSAAYQHFAEGIASFSAPCVWLPGNHD 96
Cdd:cd07402     1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  97 FQPAMYSSLQDAG---ISPAKCVFAGEQWQILLLDSQVFGVPHGELSEFQLDWLETKLAAEPERHTLLLLHHHPLPAGCS 173
Cdd:cd07402    81 DRAAMREALPEPPyddNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846 174 WLDQHSLRNSAALDRVLAKFPRVKNLLCGHIHQEQDLDWNGRRMLATPSTCVQFKPHCANFTLDTIAPGWRWLELHPNGT 253
Cdd:cd07402   161 WMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHADGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
15-264 1.98e-56

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 181.04  E-value: 1.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  15 VRILQITDTHLFAEKhetllGVNTWESYQAVLSAIHAENraCDLIVATGDLAQDQSSAAYQHFAEGIASFSAPCVWLPGN 94
Cdd:COG1409     1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADINAPR--PDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  95 HDFQPAMYSSLQDA----GISPAKCVFAGEQWQILLLDSQVFGVPHGELSEFQLDWLETKLAAEPERHTLLLLHHHPLPA 170
Cdd:COG1409    74 HDIRAAMAEAYREYfgdlPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVIVFLHHPPYST 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846 171 GcSWLDQHSLRNSAALDRVLAKFpRVKNLLCGHIHQEQDLDWNGRRMLATPSTCVQFKPhcanftldtiAPGWRWLELHP 250
Cdd:COG1409   154 G-SGSDRIGLRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL----------PPGYRVIEVDG 221

                         250
                  ....*....|....
gi 1541543846 251 NGtLTTEVCRLTGA 264
Cdd:COG1409   222 DG-LTVEVRRVDGG 234
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
16-215 1.50e-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: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  16 RILQITDTHLFAEKHETLLGvntwesyqavlsaiHAENRACDLIVATGDLAQDQSSAAYQHFAEGIASFSAPCVWLPGNH 95
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLE--------------LARAEDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNH 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  96 DFqPAMYSSLQDAGispakcvfageqwqILLLDSQVF---GV-----------PHGELSEFQLDWLETKLAA-------- 153
Cdd:COG2129    67 DD-PEVLDALEESG--------------VHNLHGRVVeigGLriaglggsrptPFGTPYEYTEEEIEERLAKlrekdvdi 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541543846 154 ----EPERHTLLLLHHHPLPAGCSwldqhslrnsaALDRVLAKF-PRVknLLCGHIHQEQDLDWNGR 215
Cdd:COG2129   132 llthAPPYGTTLDRVEDGPHVGSK-----------ALRELIEEFqPKL--VLHGHIHESRGVDKIGG 185
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
10-110 1.43e-09

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 57.11  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  10 AGGAPVRILQITDTHlfaekhetlLGVNTWESY-QAVLSAIHAENraCDLIVATGDLAqDQSSAAYQHFAEGIASFSAPC 88
Cdd:COG1408    38 PAFDGLRIVQLSDLH---------LGPFIGGERlERLVEKINALK--PDLVVLTGDLV-DGSVAELEALLELLKKLKAPL 105

                          90       100
                  ....*....|....*....|....*....
gi 1541543846  89 ----VWlpGNHDF---QPAMYSSLQDAGI 110
Cdd:COG1408   106 gvyaVL--GNHDYyagLEELRAALEEAGV 132
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-133 6.48e-08

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: 49.90  E-value: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  16 RILQITDTHLFAEkhetllgvntWESYQAVLSAIHAENRAcDLIVATGDLAQDQS-SAAYQHFAEGIASFsAPCVWLPGN 94
Cdd:pfam00149   2 RILVIGDLHLPGQ----------LDDLLELLKKLLEEGKP-DLVLHAGDLVDRGPpSEEVLELLERLIKY-VPVYLVRGN 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1541543846  95 HDFQPAMYSSLQDA-GISPAKCVFAGEQWQILLLDSQVFG 133
Cdd:pfam00149  70 HDFDYGECLRLYPYlGLLARPWKRFLEVFNFLPLAGILSG 109
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 51-205 2.38e-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: 47.71  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  51 AENRACDLIVATGDL-----AQDQSSAAYQHFAEGIASFSAPCVWLPGNHDFQPAMYSSLQDAGISPAKCVFA-----GE 120
Cdd:cd07396    42 NRESNLAFVVQLGDIidgynAKDRSKEALDAVLSILDRLKGPVHHVLGNHEFYNFPREYLNHLKTLNGEDAYYysfspGP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846 121 QWQILLLDSQVFgvpHGELSEFQLDWLETKLAAEPERHTLLLLHHHPLPAGCSWLDQHSLRNSAALDRVLAKFPRVKNLL 200
Cdd:cd07396   122 GFRFLVLDFVKF---NGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWNYEEVLAILESYPCVKACF 198


                  ....*
gi 1541543846 201 CGHIH 205
Cdd:cd07396   199 SGHNH 203
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
15-136 9.69e-06

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 45.67  E-value: 9.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  15 VRILQITDTHLfaekHETLLGVNTWESYQAVLSAI--HAENRACDLIVATGDL--AQDQSSAAYQHFAEGIASFSA---P 87
Cdd:COG0420     1 MRFLHTADWHL----GKPLHGASRREDQLAALDRLvdLAIEEKVDAVLIAGDLfdSANPSPEAVRLLAEALRRLSEagiP 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1541543846  88 CVWLPGNHDFQPAM--YSSL-QDAGISpakcVFAGEQWQILLLDS----QVFGVPH 136
Cdd:COG0420    77 VVLIAGNHDSPSRLsaGSPLlENLGVH----VFGSVEPEPVELEDglgvAVYGLPY 128
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 18-97 1.08e-05

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: 44.18  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  18 LQITDTHLfaekhetllgvnTWESYQAVLSAIHAENRACDLIVATGDLAQD-QSSAAYQHFAEGIASFSAPCVWLPGNHD 96
Cdd:cd00838     1 LVISDIHG------------NLEALEAVLEAALAKAEKPDLVICLGDLVDYgPDPEEVELKALRLLLAGIPVYVVPGNHD 68


                  .
gi 1541543846  97 F 97
Cdd:cd00838    69 I 69
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 14-112 7.81e-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: 42.65  E-value: 7.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  14 PVRILQITDTHLFAEKHETLLgvntwesyQAVLSAIHAENRacDLIVATGDLAQDQSSaAYQHFAEGIASFSAP----CV 89
Cdd:cd07385     1 GLRIVQLSDIHLGPFVGRTRL--------QKVVRKVNELNP--DLIVITGDLVDGDVS-VLRLLASPLSKLKAPlgvyFV 69

                          90       100
                  ....*....|....*....|....*..
gi 1541543846  90 WlpGNHDF----QPAMYSSLQDAGISP 112
Cdd:cd07385    70 L--GNHDYysgdVEVWIAALEKAGITV 94
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 17-137 1.49e-04

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: 40.74  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  17 ILQITDTHLFAEKHETLLGVNtwesyqaVLSAIHAENRacDLIVATGDLAQDQSSAAYQ---HFAEGIASFsaPCVWLPG 93
Cdd:cd07400     1 IAHISDLHFGEERKPEVLELN-------LLDEINALKP--DLVVVTGDLTQRARPAEFEearEFLDALEPE--PVVVVPG 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1541543846  94 NHDFQPAM---YSSLQDAGISPAKCVFAGEQWQiLLLDSQVFGVPHG 137
Cdd:cd07400    70 NHDAIVALhhpLLPPPDTGRERNVLLDAGDALK-LLKELGVDLVLHG 115
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 17-111 9.15e-04

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: 39.22  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  17 ILQITDTHlfaekhetllgvntwESYQAVLSAIHAENRAcDLIVATGDLAQDQSSAAYQHFAEGIASFSAPCVWLPGNHD 96
Cdd:cd07392     1 ILAISDVH---------------GDVPKLKKIKLKAEEA-DAVIVAGDITHFGPGEEAIEALNLLLAIGAPVLAVPGNCD 64

                          90
                  ....*....|....*
gi 1541543846  97 fQPAMYSSLQDAGIS 111
Cdd:cd07392    65 -TPEVLGELNSAGLN 78
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 16-97 1.08e-03

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: 39.17  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541543846  16 RILQITDTHL-FAEKHETLLGvntWESYQAVLSAI-HAENRACDLIVATGDLAQDQS-SAAYQHFAegIASFSA------ 86
Cdd:cd00840     1 RFLHTADWHLgYPLYGLSRRE---EDFFKAFEEIVdLAIEEKVDFVLIAGDLFDSNNpSPEALKLA--IEGLRRlceagi 75

                          90
                  ....*....|.
gi 1541543846  87 PCVWLPGNHDF 97
Cdd:cd00840    76 PVFVIAGNHDS 86
 
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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