NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|544686028|ref|WP_021117792|]
View 

3',5'-cyclic-AMP phosphodiesterase [Glaesserella parasuis]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 1-275 6.67e-152

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


The actual alignment was detected with superfamily member PRK11148:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 275  Bit Score: 425.12  E-value: 6.67e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028   1 MDDSYIFPLSSPIIRILQITDSHLFASDTCELLGVNTTQSFQAVLNMIMKESFEYDLILATGDLVQDHNREAYHRFAKMV 80
Cdd:PRK11148   2 ESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  81 KPLVKPLFWVAGNHDLQPQMRNALSIYsQIKPEKHILVGDHWQIILLDSHIQDSPKGRLEFSELAFLKRKLEVHPERYSL 160
Cdd:PRK11148  82 APLRKPCVWLPGNHDFQPAMYSALQDA-GISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028 161 IVLHHNILPTNSAWLDQHSLSNVNDLLATLKAFPKVKAIVHGHIHQEVDAQWNGYRILSTPSTCIQFKPHCNDFTLDAIP 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 544686028 241 QGWRELCLNIDGFIDTVVKRLDNNNFLPNFKALGY 275
Cdd:PRK11148 241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
 
Name Accession Description Interval E-value
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 1-275 6.67e-152

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


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 425.12  E-value: 6.67e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028   1 MDDSYIFPLSSPIIRILQITDSHLFASDTCELLGVNTTQSFQAVLNMIMKESFEYDLILATGDLVQDHNREAYHRFAKMV 80
Cdd:PRK11148   2 ESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  81 KPLVKPLFWVAGNHDLQPQMRNALSIYsQIKPEKHILVGDHWQIILLDSHIQDSPKGRLEFSELAFLKRKLEVHPERYSL 160
Cdd:PRK11148  82 APLRKPCVWLPGNHDFQPAMYSALQDA-GISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028 161 IVLHHNILPTNSAWLDQHSLSNVNDLLATLKAFPKVKAIVHGHIHQEVDAQWNGYRILSTPSTCIQFKPHCNDFTLDAIP 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 544686028 241 QGWRELCLNIDGFIDTVVKRLDNNNFLPNFKALGY 275
Cdd:PRK11148 241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 16-253 1.02e-81

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: 245.65  E-value: 1.02e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  16 ILQITDSHLFASDTCELLGVNTTQSFQAVLNMIMKESFEYDLILATGDLVQDHNREAYHRFAKMVKPLVKPLFWVAGNHD 95
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  96 LQPQMRNAL--SIYSQIKPEKHILVGDHWQIILLDSHIQDSPKGRLEFSELAFLKRKLEVHPERYSLIVLHHNILPTNSA 173
Cdd:cd07402   81 DRAAMREALpePPYDDNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028 174 WLDQHSLSNVNDLLATLKAFPKVKAIVHGHIHQEVDAQWNGYRILSTPSTCIQFKPHCNDFTLDAIPQGWRELCLNIDGF 253
Cdd:cd07402  161 WMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHADGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
14-264 1.94e-53

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 173.34  E-value: 1.94e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  14 IRILQITDSHLFASDtcellGVNTTQSFQAVLNMImkESFEYDLILATGDLVQDHNREAYHRFAKMVKPLVKPLFWVAGN 93
Cdd:COG1409    1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADI--NAPRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  94 HDLQPQM-RNALSIYSQIKPEK--HILVGDHWQIILLDSHIQDSPKGRLEFSELAFLKRKLEVHPERYSLIVLHHNILPT 170
Cdd:COG1409   74 HDIRAAMaEAYREYFGDLPPGGlyYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVIVFLHHPPYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028 171 NSaWLDQHSLSNVNDLLATLKAFpKVKAIVHGHIHQEVDAQWNGYRILSTPSTCIQFKPhcndftldaiPQGWRELCLNI 250
Cdd:COG1409  154 GS-GSDRIGLRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL----------PPGYRVIEVDG 221

                        250
                 ....*....|....
gi 544686028 251 DGfIDTVVKRLDNN 264
Cdd:COG1409  222 DG-LTVEVRRVDGG 234
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 14-96 1.04e-06

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: 46.44  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028   14 IRILQITDSHLFASDtcellgvnttQSFQAVLNMImKESFEYDLILATGDLVQDHNREayHRFAKMVKPLVK--PLFWVA 91
Cdd:pfam00149   1 MRILVIGDLHLPGQL----------DDLLELLKKL-LEEGKPDLVLHAGDLVDRGPPS--EEVLELLERLIKyvPVYLVR 67


                  ....*
gi 544686028   92 GNHDL 96
Cdd:pfam00149  68 GNHDF 72
 
Name Accession Description Interval E-value
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 1-275 6.67e-152

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


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 425.12  E-value: 6.67e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028   1 MDDSYIFPLSSPIIRILQITDSHLFASDTCELLGVNTTQSFQAVLNMIMKESFEYDLILATGDLVQDHNREAYHRFAKMV 80
Cdd:PRK11148   2 ESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  81 KPLVKPLFWVAGNHDLQPQMRNALSIYsQIKPEKHILVGDHWQIILLDSHIQDSPKGRLEFSELAFLKRKLEVHPERYSL 160
Cdd:PRK11148  82 APLRKPCVWLPGNHDFQPAMYSALQDA-GISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028 161 IVLHHNILPTNSAWLDQHSLSNVNDLLATLKAFPKVKAIVHGHIHQEVDAQWNGYRILSTPSTCIQFKPHCNDFTLDAIP 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 544686028 241 QGWRELCLNIDGFIDTVVKRLDNNNFLPNFKALGY 275
Cdd:PRK11148 241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 16-253 1.02e-81

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: 245.65  E-value: 1.02e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  16 ILQITDSHLFASDTCELLGVNTTQSFQAVLNMIMKESFEYDLILATGDLVQDHNREAYHRFAKMVKPLVKPLFWVAGNHD 95
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  96 LQPQMRNAL--SIYSQIKPEKHILVGDHWQIILLDSHIQDSPKGRLEFSELAFLKRKLEVHPERYSLIVLHHNILPTNSA 173
Cdd:cd07402   81 DRAAMREALpePPYDDNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028 174 WLDQHSLSNVNDLLATLKAFPKVKAIVHGHIHQEVDAQWNGYRILSTPSTCIQFKPHCNDFTLDAIPQGWRELCLNIDGF 253
Cdd:cd07402  161 WMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHADGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
14-264 1.94e-53

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 173.34  E-value: 1.94e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  14 IRILQITDSHLFASDtcellGVNTTQSFQAVLNMImkESFEYDLILATGDLVQDHNREAYHRFAKMVKPLVKPLFWVAGN 93
Cdd:COG1409    1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADI--NAPRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  94 HDLQPQM-RNALSIYSQIKPEK--HILVGDHWQIILLDSHIQDSPKGRLEFSELAFLKRKLEVHPERYSLIVLHHNILPT 170
Cdd:COG1409   74 HDIRAAMaEAYREYFGDLPPGGlyYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVIVFLHHPPYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028 171 NSaWLDQHSLSNVNDLLATLKAFpKVKAIVHGHIHQEVDAQWNGYRILSTPSTCIQFKPhcndftldaiPQGWRELCLNI 250
Cdd:COG1409  154 GS-GSDRIGLRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL----------PPGYRVIEVDG 221

                        250
                 ....*....|....
gi 544686028 251 DGfIDTVVKRLDNN 264
Cdd:COG1409  222 DG-LTVEVRRVDGG 234
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
14-95 1.96e-09

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 56.73  E-value: 1.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  14 IRILQITDSHLfasdtcellGVNTTQSF-QAVLNMIMKEsfEYDLILATGDLVqDHNREAYHRFAKMVKPLVKPL--FWV 90
Cdd:COG1408   43 LRIVQLSDLHL---------GPFIGGERlERLVEKINAL--KPDLVVLTGDLV-DGSVAELEALLELLKKLKAPLgvYAV 110


                 ....*
gi 544686028  91 AGNHD 95
Cdd:COG1408  111 LGNHD 115
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
15-206 6.08e-08

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 51.94  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  15 RILQITDSHLfasdtcellgvnTTQSFQAVLNMIMKEsfEYDLILATGDLVQDHNREAYHRFAKMVKPLVKPLFWVAGNH 94
Cdd:COG2129    1 KILAVSDLHG------------NFDLLEKLLELARAE--DADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  95 DLqPQMRNALSiysqiKPEKHILVGDHWQI----ILLDSHIQDSPKGR-LEFSELAFLKRKLEVHPERYSLIVLHH---N 166
Cdd:COG2129   67 DD-PEVLDALE-----ESGVHNLHGRVVEIgglrIAGLGGSRPTPFGTpYEYTEEEIEERLAKLREKDVDILLTHAppyG 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 544686028 167 ILPTNSAWLDQHSLSNVNDLLATLkafpKVKAIVHGHIHQ 206
Cdd:COG2129  141 TTLDRVEDGPHVGSKALRELIEEF----QPKLVLHGHIHE 176
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 14-96 1.04e-06

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: 46.44  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028   14 IRILQITDSHLFASDtcellgvnttQSFQAVLNMImKESFEYDLILATGDLVQDHNREayHRFAKMVKPLVK--PLFWVA 91
Cdd:pfam00149   1 MRILVIGDLHLPGQL----------DDLLELLKKL-LEEGKPDLVLHAGDLVDRGPPS--EEVLELLERLIKyvPVYLVR 67


                  ....*
gi 544686028   92 GNHDL 96
Cdd:pfam00149  68 GNHDF 72
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 14-166 3.47e-06

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: 46.89  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  14 IRILQITDSHLFASDTCELLgvnttqsfQAVLNMImkESFEYDLILATGDLVqDHNREAYHRFAKMVKPLVKPL--FWVA 91
Cdd:cd07385    2 LRIVQLSDIHLGPFVGRTRL--------QKVVRKV--NELNPDLIVITGDLV-DGDVSVLRLLASPLSKLKAPLgvYFVL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  92 GNHDlqpqmrnalsIYSQIKPE---------------KHILVGDHWQIILLDSHIQDSPKGRLEFSELAFLKRklevhPE 156
Cdd:cd07385   71 GNHD----------YYSGDVEVwiaalekagitvlrnESVELSRDGATIGLAGSGVDDIGGHGEDLEKALKGL-----DE 135

                        170
                 ....*....|
gi 544686028 157 RYSLIVLHHN 166
Cdd:cd07385  136 NDPVILLAHN 145
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 15-95 1.60e-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: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  15 RILQITDSHL-FASDTCELLGVNTTQSFQAVLNMIMKEsfEYDLILATGDLVQDHN--REAYHRFAKMVKPLVK---PLF 88
Cdd:cd00840    1 RFLHTADWHLgYPLYGLSRREEDFFKAFEEIVDLAIEE--KVDFVLIAGDLFDSNNpsPEALKLAIEGLRRLCEagiPVF 78


                 ....*..
gi 544686028  89 WVAGNHD 95
Cdd:cd00840   79 VIAGNHD 85
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 56-205 6.68e-04

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 40.01  E-value: 6.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  56 DLILATGDLV-----QDHNREAYHRFAKMVKPLVKPLFWVAGNHDL---------QPQMRNALSIYSQikpekHILVGDH 121
Cdd:cd07396   48 AFVVQLGDIIdgynaKDRSKEALDAVLSILDRLKGPVHHVLGNHEFynfpreylnHLKTLNGEDAYYY-----SFSPGPG 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028 122 WQIILLDshIQDSpKGRLEFSELAFLKRKLEV--HPERYSLIVLHHNILPTNSAwlDQHSLSNVNDLLATLKAFPKVKAI 199
Cdd:cd07396  123 FRFLVLD--FVKF-NGGIGEEQLAWLRNELTSadANGEKVIVLSHLPIYPEAAD--PQCLLWNYEEVLAILESYPCVKAC 197


                 ....*.
gi 544686028 200 VHGHIH 205
Cdd:cd07396  198 FSGHNH 203
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 17-96 3.73e-03

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: 36.86  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  17 LQITDSHLfasdtcellgvnTTQSFQAVLNMIMKESFEYDLILATGDLVQDHNR-EAYHRFAKMVKPLVKPLFWVAGNHD 95
Cdd:cd00838    1 LVISDIHG------------NLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDpEEVELKALRLLLAGIPVYVVPGNHD 68


                 .
gi 544686028  96 L 96
Cdd:cd00838   69 I 69
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 56-205 5.18e-03

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 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: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 37.69  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  56 DLILATGDL-----VQDHNREAYHR-FAKMV--KPLVKPLFWVAGNHDLQpqmRNALsiySQIKPEKHILvGDHW----- 122
Cdd:cd07378   38 DFILSLGDNfyddgVKDVDDPRFQEtFEDVYsaPSLQVPWYLVLGNHDHR---GNVS---AQIAYTQRPN-SKRWnfpny 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028 123 ---------------QIILLDS--------HIQDSPKGRLEF-----SELAFLKRKLEVHPERYSLIVLHHNILpTNSAW 174
Cdd:cd07378  111 yydisfkfpssdvtvAFIMIDTvllcgntdDEASGQPRGPPNkklaeTQLAWLEKQLAASKADYKIVVGHYPIY-SSGEH 189

                        170       180       190
                 ....*....|....*....|....*....|.
gi 544686028 175 LDQHSLsnVNDLLATLKAFpKVKAIVHGHIH 205
Cdd:cd07378  190 GPTKCL--VDILLPLLKKY-KVDAYLSGHDH 217
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
14-167 5.99e-03

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 37.20  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  14 IRILQITDSHLfasDTcELLGVNTTQSFQAVLNMIMK--ESFEYDLILATGDLVqDHNR---EAYHRFAKMVKPLVK--- 85
Cdd:COG0420    1 MRFLHTADWHL---GK-PLHGASRREDQLAALDRLVDlaIEEKVDAVLIAGDLF-DSANpspEAVRLLAEALRRLSEagi 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544686028  86 PLFWVAGNHD-------LQPQMRNA-LSIYSQIKPEKHILVGDHWQIILLDSHIQDSPKGRLEfSELAFLKRKLEvhPER 157
Cdd:COG0420   76 PVVLIAGNHDspsrlsaGSPLLENLgVHVFGSVEPEPVELEDGLGVAVYGLPYLRPSDEEALR-DLLERLPRALD--PGG 152

                        170
                 ....*....|
gi 544686028 158 YSLIVLHHNI 167
Cdd:COG0420  153 PNILLLHGFV 162
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH