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Conserved domains on  [gi|496082008|ref|WP_008806515|]
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MULTISPECIES: 3',5'-cyclic-AMP phosphodiesterase [Klebsiella]

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 496082008   1 MESLLNLPLAGEARVRILQITDTHLFAEKHETLLGINTWESYQAVLSAIHASQRPCDLIVATGDLAQDHSSAAYQHFAEG 80
Cdd:PRK11148   1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  81 IASFAAPCVWLPGNHDFQPAMYSTLQASGISPAKRVFLGDHWQILLLDSQVFGVPHGELSDFQLEWLEHKLAEAPERYTL 160
Cdd:PRK11148  81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008 161 LLLHHHPLPAGCSWLDQHSLRNAGALDRALSAWPRVRHLLCGHIHQELDLDWNGRRMMATPSTCVQFKPHCANFTLDTVS 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 496082008 241 PGWRWLELHPDGTLTTEVCRLEGAEFHPDIASEGY 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 496082008   1 MESLLNLPLAGEARVRILQITDTHLFAEKHETLLGINTWESYQAVLSAIHASQRPCDLIVATGDLAQDHSSAAYQHFAEG 80
Cdd:PRK11148   1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  81 IASFAAPCVWLPGNHDFQPAMYSTLQASGISPAKRVFLGDHWQILLLDSQVFGVPHGELSDFQLEWLEHKLAEAPERYTL 160
Cdd:PRK11148  81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008 161 LLLHHHPLPAGCSWLDQHSLRNAGALDRALSAWPRVRHLLCGHIHQELDLDWNGRRMMATPSTCVQFKPHCANFTLDTVS 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 496082008 241 PGWRWLELHPDGTLTTEVCRLEGAEFHPDIASEGY 275
Cdd:PRK11148 241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 17-253 1.18e-90

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: 268.38  E-value: 1.18e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  17 ILQITDTHLFAEKHETLLGINTWESYQAVLSAIHASQRPCDLIVATGDLAQDHSSAAYQHFAEGIASFAAPCVWLPGNHD 96
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  97 FQPAMYSTL---QASGISPAKRVFLGDHWQILLLDSQVFGVPHGELSDFQLEWLEHKLAEAPERYTLLLLHHHPLPAGCS 173
Cdd:cd07402   81 DRAAMREALpepPYDDNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008 174 WLDQHSLRNAGALDRALSAWPRVRHLLCGHIHQELDLDWNGRRMMATPSTCVQFKPHCANFTLDTVSPGWRWLELHPDGT 253
Cdd:cd07402  161 WMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHADGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
15-264 3.67e-55

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 177.96  E-value: 3.67e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  15 VRILQITDTHLFAEKhetllGINTWESYQAVLSAIHAsqRPCDLIVATGDLAQDHSSAAYQHFAEGIASFAAPCVWLPGN 94
Cdd:COG1409    1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADINA--PRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  95 HDFQPAMYSTLQA--SGISPAKR--VFLGDHWQILLLDSQVFGVPHGELSDFQLEWLEHKLAEAPER----------YTL 160
Cdd:COG1409   74 HDIRAAMAEAYREyfGDLPPGGLyySFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKpvivflhhppYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008 161 LllhhhplpagcSWLDQHSLRNAGALDRALSAWpRVRHLLCGHIHQELDLDWNGRRMMATPSTCVQFKPhcanftldtvS 240
Cdd:COG1409  154 G-----------SGSDRIGLRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL----------P 211

                        250       260
                 ....*....|....*....|....
gi 496082008 241 PGWRWLELHPDGtLTTEVCRLEGA 264
Cdd:COG1409  212 PGYRVIEVDGDG-LTVEVRRVDGG 234
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-133 2.54e-07

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: 48.36  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008   16 RILQITDTHLFAEkhetllgintWESYQAVLSAIHASQRPcDLIVATGDLAQDHS-SAAYQHFAEGIASFAaPCVWLPGN 94
Cdd:pfam00149   2 RILVIGDLHLPGQ----------LDDLLELLKKLLEEGKP-DLVLHAGDLVDRGPpSEEVLELLERLIKYV-PVYLVRGN 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 496082008   95 HDFQPAMYSTLQA-SGISPAKRVFLGDHWQILLLDSQVFG 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 496082008   1 MESLLNLPLAGEARVRILQITDTHLFAEKHETLLGINTWESYQAVLSAIHASQRPCDLIVATGDLAQDHSSAAYQHFAEG 80
Cdd:PRK11148   1 MESLLTLPLAGEARVRILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  81 IASFAAPCVWLPGNHDFQPAMYSTLQASGISPAKRVFLGDHWQILLLDSQVFGVPHGELSDFQLEWLEHKLAEAPERYTL 160
Cdd:PRK11148  81 IAPLRKPCVWLPGNHDFQPAMYSALQDAGISPAKHVLIGEHWQILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008 161 LLLHHHPLPAGCSWLDQHSLRNAGALDRALSAWPRVRHLLCGHIHQELDLDWNGRRMMATPSTCVQFKPHCANFTLDTVS 240
Cdd:PRK11148 161 VLLHHHPLPAGCAWLDQHSLRNAHELAEVLAKFPNVKAILCGHIHQELDLDWNGRRLLATPSTCVQFKPHCTNFTLDTVA 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 496082008 241 PGWRWLELHPDGTLTTEVCRLEGAEFHPDIASEGY 275
Cdd:PRK11148 241 PGWRELELHADGSLETEVHRLADTEFLPDTASEGY 275
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 17-253 1.18e-90

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: 268.38  E-value: 1.18e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  17 ILQITDTHLFAEKHETLLGINTWESYQAVLSAIHASQRPCDLIVATGDLAQDHSSAAYQHFAEGIASFAAPCVWLPGNHD 96
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  97 FQPAMYSTL---QASGISPAKRVFLGDHWQILLLDSQVFGVPHGELSDFQLEWLEHKLAEAPERYTLLLLHHHPLPAGCS 173
Cdd:cd07402   81 DRAAMREALpepPYDDNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008 174 WLDQHSLRNAGALDRALSAWPRVRHLLCGHIHQELDLDWNGRRMMATPSTCVQFKPHCANFTLDTVSPGWRWLELHPDGT 253
Cdd:cd07402  161 WMDAIRLRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHADGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
15-264 3.67e-55

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 177.96  E-value: 3.67e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  15 VRILQITDTHLFAEKhetllGINTWESYQAVLSAIHAsqRPCDLIVATGDLAQDHSSAAYQHFAEGIASFAAPCVWLPGN 94
Cdd:COG1409    1 FRFAHISDLHLGAPD-----GSDTAEVLAAALADINA--PRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  95 HDFQPAMYSTLQA--SGISPAKR--VFLGDHWQILLLDSQVFGVPHGELSDFQLEWLEHKLAEAPER----------YTL 160
Cdd:COG1409   74 HDIRAAMAEAYREyfGDLPPGGLyySFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKpvivflhhppYST 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008 161 LllhhhplpagcSWLDQHSLRNAGALDRALSAWpRVRHLLCGHIHQELDLDWNGRRMMATPSTCVQFKPhcanftldtvS 240
Cdd:COG1409  154 G-----------SGSDRIGLRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL----------P 211

                        250       260
                 ....*....|....*....|....
gi 496082008 241 PGWRWLELHPDGtLTTEVCRLEGA 264
Cdd:COG1409  212 PGYRVIEVDGDG-LTVEVRRVDGG 234
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
16-215 1.01e-09

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 56.95  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  16 RILQITDTHLFAEKHETLLGIntwesyqavlsaihASQRPCDLIVATGDLAQDHSSAAYQHFAEGIASFAAPCVWLPGNH 95
Cdd:COG2129    1 KILAVSDLHGNFDLLEKLLEL--------------ARAEDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  96 DFqPAMYSTLQASGIspakrvflgdHWqillLDSQVF--------GVPHGELSDFQ------LEWLEHKLAE-------- 153
Cdd:COG2129   67 DD-PEVLDALEESGV----------HN----LHGRVVeigglriaGLGGSRPTPFGtpyeytEEEIEERLAKlrekdvdi 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082008 154 ----APERYTLLLLHHHPLPAGCSwldqhslrnagALDRALSAWpRVRHLLCGHIHQELDLDWNGR 215
Cdd:COG2129  132 llthAPPYGTTLDRVEDGPHVGSK-----------ALRELIEEF-QPKLVLHGHIHESRGVDKIGG 185
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
6-110 3.89e-09

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 55.96  E-value: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008   6 NLPlAGEARVRILQITDTHlfaekhetlLGINTWESY-QAVLSAIhASQRPcDLIVATGDLAqDHSSAAYQHFAEGIASF 84
Cdd:COG1408   35 KLP-PAFDGLRIVQLSDLH---------LGPFIGGERlERLVEKI-NALKP-DLVVLTGDLV-DGSVAELEALLELLKKL 101

                         90       100       110
                 ....*....|....*....|....*....|...
gi 496082008  85 AAPC----VWlpGNHDF---QPAMYSTLQASGI 110
Cdd:COG1408  102 KAPLgvyaVL--GNHDYyagLEELRAALEEAGV 132
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-133 2.54e-07

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: 48.36  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008   16 RILQITDTHLFAEkhetllgintWESYQAVLSAIHASQRPcDLIVATGDLAQDHS-SAAYQHFAEGIASFAaPCVWLPGN 94
Cdd:pfam00149   2 RILVIGDLHLPGQ----------LDDLLELLKKLLEEGKP-DLVLHAGDLVDRGPpSEEVLELLERLIKYV-PVYLVRGN 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 496082008   95 HDFQPAMYSTLQA-SGISPAKRVFLGDHWQILLLDSQVFG 133
Cdd:pfam00149  70 HDFDYGECLRLYPyLGLLARPWKRFLEVFNFLPLAGILSG 109
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 16-135 2.02e-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: 44.58  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  16 RILQITDTHLFAEKHETLLgintwesyQAVLSAIhASQRPcDLIVATGDLAqDHSSAAYQHFAEGIASFAAP----CVWl 91
Cdd:cd07385    3 RIVQLSDIHLGPFVGRTRL--------QKVVRKV-NELNP-DLIVITGDLV-DGDVSVLRLLASPLSKLKAPlgvyFVL- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496082008  92 pGNHDF----QPAMYSTLQASGISP---AKRVFLGDHWQILLLDSQVFGVP 135
Cdd:cd07385   71 -GNHDYysgdVEVWIAALEKAGITVlrnESVELSRDGATIGLAGSGVDDIG 120
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 18-97 7.07e-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: 41.87  E-value: 7.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  18 LQITDTHLfaekhetllginTWESYQAVLSAIHASQRPCDLIVATGDLAQDHS-SAAYQHFAEGIASFAAPCVWLPGNHD 96
Cdd:cd00838    1 LVISDIHG------------NLEALEAVLEAALAKAEKPDLVICLGDLVDYGPdPEEVELKALRLLLAGIPVYVVPGNHD 68


                 .
gi 496082008  97 F 97
Cdd:cd00838   69 I 69
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 51-205 1.82e-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: 41.93  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  51 ASQRPCDLIVATGDL-----AQDHSSAAYQHFAEGIASFAAPCVWLPGNHDFQPAMYSTLQASGISPAKRVF-----LGD 120
Cdd:cd07396   42 NRESNLAFVVQLGDIidgynAKDRSKEALDAVLSILDRLKGPVHHVLGNHEFYNFPREYLNHLKTLNGEDAYyysfsPGP 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008 121 HWQILLLDSQVFgvpHGELSDFQLEWLEHKLAEAPERYTLLLLHHHPLPAGCSWLDQHSLRNAGALDRALSAWPRVRHLL 200
Cdd:cd07396  122 GFRFLVLDFVKF---NGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWNYEEVLAILESYPCVKACF 198


                 ....*
gi 496082008 201 CGHIH 205
Cdd:cd07396  199 SGHNH 203
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
15-154 6.49e-04

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 40.28  E-value: 6.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  15 VRILQITDTHLfaekHETLLGINTWESYQAVLSAI--HASQRPCDLIVATGDL--AQDHSSAAYQHFAEGIASFAA---P 87
Cdd:COG0420    1 MRFLHTADWHL----GKPLHGASRREDQLAALDRLvdLAIEEKVDAVLIAGDLfdSANPSPEAVRLLAEALRRLSEagiP 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082008  88 CVWLPGNHDFQP---AMYSTLQASGIspakRVFLGDHWQILLLDS----QVFGVPHGELSDFQ-----LEWLEHKLAEA 154
Cdd:COG0420   77 VVLIAGNHDSPSrlsAGSPLLENLGV----HVFGSVEPEPVELEDglgvAVYGLPYLRPSDEEalrdlLERLPRALDPG 151
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 17-137 1.83e-03

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


Pssm-ID: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 37.66  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  17 ILQITDTHLFAEKHETLLGINtwesyqaVLSAIHAsQRPcDLIVATGDLAQDHSSAAYQHFAEGIASFAA-PCVWLPGNH 95
Cdd:cd07400    1 IAHISDLHFGEERKPEVLELN-------LLDEINA-LKP-DLVVVTGDLTQRARPAEFEEAREFLDALEPePVVVVPGNH 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 496082008  96 DFQPAMYSTLQASGISPAKRVFLGDHWQIL--LLDSQVFGVPHG 137
Cdd:cd07400   72 DAIVALHHPLLPPPDTGRERNVLLDAGDALklLKELGVDLVLHG 115
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 34-154 4.51e-03

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: 38.05  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  34 LGINTWESYQAvLSAIHASQRPCDLIVATGDLA-QDHSSAA-----YQHFAEGIASfAAPCVWLPGNHD-----FQPAMY 102
Cdd:cd00839   13 MGQNTNNSTNT-LDHLEKELGNYDAIIHVGDIAyADGYNNGsrwdtFMRQIEPLAS-YVPYMVAPGNHEadyngSTSKIK 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082008 103 STLQASGISPAKrvflGDHWQ------------ILLLDSQVFGVPHGELSDfQLEWLEHKLAEA 154
Cdd:cd00839   91 FFMPGRGMPPSP----SGSTEnlwysfdvgpvhFISLSTETDFLKGDNISP-QYDWLEADLAKV 149
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 16-97 8.87e-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: 36.48  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082008  16 RILQITDTHL-FAEKHETLLGintWESYQAVLSAI-HASQRPCDLIVATGDLAqDHS--SAAYQHFA-EGIASFAA---P 87
Cdd:cd00840    1 RFLHTADWHLgYPLYGLSRRE---EDFFKAFEEIVdLAIEEKVDFVLIAGDLF-DSNnpSPEALKLAiEGLRRLCEagiP 76

                         90
                 ....*....|
gi 496082008  88 CVWLPGNHDF 97
Cdd:cd00840   77 VFVIAGNHDS 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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