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Conserved domains on  [gi|507083769|ref|WP_016154517|]
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MULTISPECIES: 3',5'-cyclic-AMP phosphodiesterase [Citrobacter]

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: 532.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769   1 MESLLTLPLAGEARVRILQITDTHLFAEKHETLLGVNTWDSYQSVLDAIHAESPEYDLIVATGDLAQDQSAAAYQHFAEG 80
Cdd:PRK11148   1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  81 IASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERNTL 160
Cdd:PRK11148  81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769 161 LLLHHHPLPAGCSWLDQHSLRNAAELDNVLVNYPRAKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTIS 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 507083769 241 PGWRTLELFADGTLQTQVRRLQGNRFHPDTASEGY 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: 532.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769   1 MESLLTLPLAGEARVRILQITDTHLFAEKHETLLGVNTWDSYQSVLDAIHAESPEYDLIVATGDLAQDQSAAAYQHFAEG 80
Cdd:PRK11148   1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  81 IASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERNTL 160
Cdd:PRK11148  81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769 161 LLLHHHPLPAGCSWLDQHSLRNAAELDNVLVNYPRAKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTIS 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 507083769 241 PGWRTLELFADGTLQTQVRRLQGNRFHPDTASEGY 275
Cdd:PRK11148 241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 17-253 4.42e-91

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: 269.53  E-value: 4.42e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  17 ILQITDTHLFAEKHETLLGVNTWDSYQSVLDAIHAESPEYDLIVATGDLAQDQSAAAYQHFAEGIASFRAPCVWLPGNHD 96
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  97 FQPAMYSALQDAG---ISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERNTLLLLHHHPLPAGCS 173
Cdd:cd07402   81 DRAAMREALPEPPyddNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769 174 WLDQHSLRNAAELDNVLVNYPRAKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTISPGWRTLELFADGT 253
Cdd:cd07402  161 WMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHADGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
15-264 4.16e-57

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 182.58  E-value: 4.16e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  15 VRILQITDTHLFAEKhetllGVNTWDSYQSVLDAIHAESPeyDLIVATGDLAQDQSAAAYQHFAEGIASFRAPCVWLPGN 94
Cdd:COG1409    1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADINAPRP--DFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  95 HDFQPAM----YSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERNT--------LLL 162
Cdd:COG1409   74 HDIRAAMaeayREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVivflhhppYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769 163 LhhhplpagcSWLDQHSLRNAAELDNVLVNYpRAKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPhcsnftldtiSPG 242
Cdd:COG1409  154 G---------SGSDRIGLRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL----------PPG 213

                        250       260
                 ....*....|....*....|..
gi 507083769 243 WRTLELFADGtLQTQVRRLQGN 264
Cdd:COG1409  214 YRVIEVDGDG-LTVEVRRVDGG 234
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-133 2.72e-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: 51.06  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769   16 RILQITDTHLFAEkhetllgvntWDSYQSVLDAIHAEsPEYDLIVATGDLAQ--DQSAAAYQHFAEGIAsfRAPCVWLPG 93
Cdd:pfam00149   2 RILVIGDLHLPGQ----------LDDLLELLKKLLEE-GKPDLVLHAGDLVDrgPPSEEVLELLERLIK--YVPVYLVRG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 507083769   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: 532.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769   1 MESLLTLPLAGEARVRILQITDTHLFAEKHETLLGVNTWDSYQSVLDAIHAESPEYDLIVATGDLAQDQSAAAYQHFAEG 80
Cdd:PRK11148   1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  81 IASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERNTL 160
Cdd:PRK11148  81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769 161 LLLHHHPLPAGCSWLDQHSLRNAAELDNVLVNYPRAKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTIS 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 507083769 241 PGWRTLELFADGTLQTQVRRLQGNRFHPDTASEGY 275
Cdd:PRK11148 241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 17-253 4.42e-91

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: 269.53  E-value: 4.42e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  17 ILQITDTHLFAEKHETLLGVNTWDSYQSVLDAIHAESPEYDLIVATGDLAQDQSAAAYQHFAEGIASFRAPCVWLPGNHD 96
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  97 FQPAMYSALQDAG---ISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERNTLLLLHHHPLPAGCS 173
Cdd:cd07402   81 DRAAMREALPEPPyddNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769 174 WLDQHSLRNAAELDNVLVNYPRAKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPHCSNFTLDTISPGWRTLELFADGT 253
Cdd:cd07402  161 WMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHADGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
15-264 4.16e-57

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 182.58  E-value: 4.16e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  15 VRILQITDTHLFAEKhetllGVNTWDSYQSVLDAIHAESPeyDLIVATGDLAQDQSAAAYQHFAEGIASFRAPCVWLPGN 94
Cdd:COG1409    1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADINAPRP--DFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  95 HDFQPAM----YSALQDAGISPAKRVFIGEQWQILLLDSQVFGVPHGELSEFQLEWLERKLADAPERNT--------LLL 162
Cdd:COG1409   74 HDIRAAMaeayREYFGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVivflhhppYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769 163 LhhhplpagcSWLDQHSLRNAAELDNVLVNYpRAKYLLCGHIHQELDLDWNGRRLLATPSTCVQFKPhcsnftldtiSPG 242
Cdd:COG1409  154 G---------SGSDRIGLRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL----------PPG 213

                        250       260
                 ....*....|....*....|..
gi 507083769 243 WRTLELFADGtLQTQVRRLQGN 264
Cdd:COG1409  214 YRVIEVDGDG-LTVEVRRVDGG 234
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
16-215 2.50e-13

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 67.35  E-value: 2.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  16 RILQITDTHLFAEKHETLLGvntwdsyqsvldaiHAESPEYDLIVATGDLAQDQSAAAYQHFAEGIASFRAPCVWLPGNH 95
Cdd:COG2129    1 KILAVSDLHGNFDLLEKLLE--------------LARAEDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  96 DFqPAMYSALQDAGispakrvfigeqwqILLLDSQVF---GV-----------PHGELSEFQLEWLERKLAD-------- 153
Cdd:COG2129   67 DD-PEVLDALEESG--------------VHNLHGRVVeigGLriaglggsrptPFGTPYEYTEEEIEERLAKlrekdvdi 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507083769 154 ----APERNTLLLLHHHPLPAGCSwldqhSLRNAAELDNVlvnypraKYLLCGHIHQELDLDWNGR 215
Cdd:COG2129  132 llthAPPYGTTLDRVEDGPHVGSK-----ALRELIEEFQP-------KLVLHGHIHESRGVDKIGG 185
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
7-110 1.41e-10

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 60.19  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769   7 LPlAGEARVRILQITDTHlfaekhetlLGVNTWDSY-QSVLDAIHAESPeyDLIVATGDLAqDQSAAAYQHFAEGIASFR 85
Cdd:COG1408   36 LP-PAFDGLRIVQLSDLH---------LGPFIGGERlERLVEKINALKP--DLVVLTGDLV-DGSVAELEALLELLKKLK 102

                         90       100       110
                 ....*....|....*....|....*....|..
gi 507083769  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 2.72e-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: 51.06  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769   16 RILQITDTHLFAEkhetllgvntWDSYQSVLDAIHAEsPEYDLIVATGDLAQ--DQSAAAYQHFAEGIAsfRAPCVWLPG 93
Cdd:pfam00149   2 RILVIGDLHLPGQ----------LDDLLELLKKLLEE-GKPDLVLHAGDLVDrgPPSEEVLELLERLIK--YVPVYLVRG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 507083769   94 NHDFQPAMYSALQDA-GISPAKRVFIGEQWQILLLDSQVFG 133
Cdd:pfam00149  69 NHDFDYGECLRLYPYlGLLARPWKRFLEVFNFLPLAGILSG 109
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 16-112 2.81e-07

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: 49.97  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  16 RILQITDTHLFAEKHETLLgvntwdsyQSVLDAIHAESPeyDLIVATGDLAqDQSAAAYQHFAEGIASFRAP----CVWl 91
Cdd:cd07385    3 RIVQLSDIHLGPFVGRTRL--------QKVVRKVNELNP--DLIVITGDLV-DGDVSVLRLLASPLSKLKAPlgvyFVL- 70

                         90       100
                 ....*....|....*....|....*
gi 507083769  92 pGNHDF----QPAMYSALQDAGISP 112
Cdd:cd07385   71 -GNHDYysgdVEVWIAALEKAGITV 94
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 57-205 5.04e-07

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: 49.64  E-value: 5.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  57 DLIVATGDL-----AQDQSAAAYQHFAEGIASFRAPCVWLPGNHDFQPAMYSALQDAGISPAKRVF-----IGEQWQILL 126
Cdd:cd07396   48 AFVVQLGDIidgynAKDRSKEALDAVLSILDRLKGPVHHVLGNHEFYNFPREYLNHLKTLNGEDAYyysfsPGPGFRFLV 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507083769 127 LDSQVFgvpHGELSEFQLEWLERKLADAPERNTLLLLHHHPLPAGCSWLDQHSLRNAAELDNVLVNYPRAKYLLCGHIH 205
Cdd:cd07396  128 LDFVKF---NGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWNYEEVLAILESYPCVKACFSGHNH 203
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 18-97 8.57e-07

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: 47.26  E-value: 8.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  18 LQITDTHLfaekhetllgvnTWDSYQSVLDAIHAESPEYDLIVATGDLAQD-QSAAAYQHFAEGIASFRAPCVWLPGNHD 96
Cdd:cd00838    1 LVISDIHG------------NLEALEAVLEAALAKAEKPDLVICLGDLVDYgPDPEEVELKALRLLLAGIPVYVVPGNHD 68


                 .
gi 507083769  97 F 97
Cdd:cd00838   69 I 69
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 34-152 6.22e-06

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: 46.52  E-value: 6.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  34 LGVNTWDSYQSvLDAIHAESPEYDLIVATGDLAQD--QSAA----AYQHFAEGIASfRAPCVWLPGNHD----FQPAMYS 103
Cdd:cd00839   13 MGQNTNNSTNT-LDHLEKELGNYDAIIHVGDIAYAdgYNNGsrwdTFMRQIEPLAS-YVPYMVAPGNHEadynGSTSKIK 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 507083769 104 ALQDAGISPAKRVFIGEQW---------QILLLDSQVFGVPHGELSEfQLEWLERKLA 152
Cdd:cd00839   91 FFMPGRGMPPSPSGSTENLwysfdvgpvHFISLSTETDFLKGDNISP-QYDWLEADLA 147
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 17-119 1.09e-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: 41.92  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  17 ILQITDTHlfaekhetllgvntwDSYQSvLDAIHAESPEYDLIVATGDLAQDQSAAAYQHFAEGIASFRAPCVWLPGNHD 96
Cdd:cd07392    1 ILAISDVH---------------GDVPK-LKKIKLKAEEADAVIVAGDITHFGPGEEAIEALNLLLAIGAPVLAVPGNCD 64

                         90       100
                 ....*....|....*....|....
gi 507083769  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 1.14e-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: 41.87  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  16 RILQITDTHL-FAEKHETLLGvntWDSYQSVLDAI-HAESPEYDLIVATGDLAQDQ--SAAAYQHFAEGIASFRA---PC 88
Cdd:cd00840    1 RFLHTADWHLgYPLYGLSRRE---EDFFKAFEEIVdLAIEEKVDFVLIAGDLFDSNnpSPEALKLAIEGLRRLCEagiPV 77


                 ....*....
gi 507083769  89 VWLPGNHDF 97
Cdd:cd00840   78 FVIAGNHDS 86
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
15-206 1.45e-04

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 42.21  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  15 VRILQITDTHLFAEKHETLLGVNTWDSYQSVLDAIHAESPeyDLIVATGDL--AQDQSAAAYQHFAEGIASFRA---PCV 89
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASRREDQLAALDRLVDLAIEEKV--DAVLIAGDLfdSANPSPEAVRLLAEALRRLSEagiPVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  90 WLPGNHDFQP---AMYSALQDAGIspakRVFIGEQWQILLLDS----QVFGVPHgeLSEFQLEWLERKLADAPERNTLLL 162
Cdd:COG0420   79 LIAGNHDSPSrlsAGSPLLENLGV----HVFGSVEPEPVELEDglgvAVYGLPY--LRPSDEEALRDLLERLPRALDPGG 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 507083769 163 LHHHPLPAGCSWLDQHSLRNAAELDNVLVNYPRAKYLLCGHIHQ 206
Cdd:COG0420  153 PNILLLHGFVAGASGSRDIYVAPVPLSALPAAGFDYVALGHIHR 196
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 17-96 2.75e-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: 39.97  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  17 ILQITDTHLFAEKHETLLGVNtwdsyqsVLDAIHAESPeyDLIVATGDLAQDQSAAAYQ---HFAEGIASFraPCVWLPG 93
Cdd:cd07400    1 IAHISDLHFGEERKPEVLELN-------LLDEINALKP--DLVVVTGDLTQRARPAEFEearEFLDALEPE--PVVVVPG 69


                 ...
gi 507083769  94 NHD 96
Cdd:cd07400   70 NHD 72
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 16-96 6.24e-03

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 36.89  E-value: 6.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083769  16 RILQITDTHlFAEKHETLLG-----VNTWDSYQSVLDAihaESPeyDLIVATGDLAqDQSAAAYQHFAEGIASFRAPCVW 90
Cdd:cd07383    4 KILQFADLH-FGEGEWTCWEgceadLKTVEFIESVLDE---EKP--DLVVLTGDLI-TGENTADDNATSYLDKAVSPLVE 76

                         90
                 ....*....|...
gi 507083769  91 --LP-----GNHD 96
Cdd:cd07383   77 rgIPwaatfGNHD 89
 
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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