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Conserved domains on  [gi|499232095|ref|WP_010929635|]
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phosphodiesterase [Bordetella pertussis]

Protein Classification

phosphodiesterase( domain architecture ID 10164715)

phosphodiesterase of the metallophosphatase (MPP) superfamily, related to Enterobacter aerogenes glycerophosphodiesterase Q and Escherichia coli 3',5'-cyclic AMP phosphodiesterase CpdA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 3-245 1.63e-103

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: 301.12  E-value: 1.63e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIRMPGQKAYRVVETDRYLPPAVAALNRLEPAPDLVIVSGDLTDFGRPQEYAHLKQMLDALRVPYHVLPGNHD 82
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  83 DRVQLAATFADHPYlrEAGEFVQYTIEDQPLRFIVLDTVVPQQSHGALCERRLQWLAQRLAEQPGRPTVIVMHHPPFRTG 162
Cdd:cd07402   81 DRAAMREALPEPPY--DDNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095 163 IAHMDAIGlLAGAPELEALVARHSNVERIMCGHLHRTIFQRFGGTIASTCPSPAHQVALDLRPDGPSAFVMEPPGFHLHE 242
Cdd:cd07402  159 IPWMDAIR-LRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHA 237


                 ...
gi 499232095 243 WRD 245
Cdd:cd07402  238 DGI 240
 
Name Accession Description Interval E-value
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 3-245 1.63e-103

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: 301.12  E-value: 1.63e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIRMPGQKAYRVVETDRYLPPAVAALNRLEPAPDLVIVSGDLTDFGRPQEYAHLKQMLDALRVPYHVLPGNHD 82
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  83 DRVQLAATFADHPYlrEAGEFVQYTIEDQPLRFIVLDTVVPQQSHGALCERRLQWLAQRLAEQPGRPTVIVMHHPPFRTG 162
Cdd:cd07402   81 DRAAMREALPEPPY--DDNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095 163 IAHMDAIGlLAGAPELEALVARHSNVERIMCGHLHRTIFQRFGGTIASTCPSPAHQVALDLRPDGPSAFVMEPPGFHLHE 242
Cdd:cd07402  159 IPWMDAIR-LRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHA 237


                 ...
gi 499232095 243 WRD 245
Cdd:cd07402  238 DGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-258 1.55e-66

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 206.85  E-value: 1.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   1 MLIAQISDLHIRMPgqkayRVVETDRYLPPAVAALNRlePAPDLVIVSGDLTDFGRPQEYAHLKQMLDALRVPYHVLPGN 80
Cdd:COG1409    1 FRFAHISDLHLGAP-----DGSDTAEVLAAALADINA--PRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  81 HDDRVQLAATFADHpYLREAGEFVQYTIEDQPLRFIVLDTVVPQQSHGALCERRLQWLAQRLAEQPGRPTVIVMHHPPFR 160
Cdd:COG1409   74 HDIRAAMAEAYREY-FGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVIVFLHHPPYS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095 161 TGIaHMDAIGlLAGAPELEALVARHsNVERIMCGHLHRTIFQRFGGTIASTCPSPAHQVALdlrpdgpsafvmePPGFHL 240
Cdd:COG1409  153 TGS-GSDRIG-LRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL-------------PPGYRV 216

                        250
                 ....*....|....*...
gi 499232095 241 HEWRDGALVTHHAYIESY 258
Cdd:COG1409  217 IEVDGDGLTVEVRRVDGG 234
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 3-197 2.12e-19

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


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 84.99  E-value: 2.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIRMPGQKAYRVVETDRYLPPAVAALNRLEPAPDLVIVSGDLTDFGRPQEYAHLKQMLDALRVPYHVLPGNHD 82
Cdd:PRK11148  17 ILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEGIAPLRKPCVWLPGNHD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  83 DRVQLAATFADHPYLRE----AGEFVQytiedqplrFIVLDTVVPQQSHGALCERRLQWLAQRLAEQPGRPTVIVMHHPP 158
Cdd:PRK11148  97 FQPAMYSALQDAGISPAkhvlIGEHWQ---------ILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTLVLLHHHP 167

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499232095 159 FRTGIAHMDAIGlLAGAPELEALVARHSNVERIMCGHLH 197
Cdd:PRK11148 168 LPAGCAWLDQHS-LRNAHELAEVLAKFPNVKAILCGHIH 205
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-84 4.10e-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: 50.67  E-value: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095    1 MLIAQISDLHIrmPGQkAYRVVETDRYLPPavaalnrlEPAPDLVIVSGDLTDFGRPQEYAHLKQMLDALRVPYHVLPGN 80
Cdd:pfam00149   1 MRILVIGDLHL--PGQ-LDDLLELLKKLLE--------EGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGN 69


                  ....
gi 499232095   81 HDDR 84
Cdd:pfam00149  70 HDFD 73
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 1-147 5.25e-03

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 37.40  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095    1 MLIAQISDLHIrmpGQKAYRVVEtdryLPPAVAALNRL-----EPAPDLVIVSGDLTDFGRP----QE--YAHLKQMLDA 69
Cdd:TIGR00619   1 MRILHTSDWHL---GKTLEGVSR----LAEQKAFLDDLlefakAEQVDALLVAGDVFDTANPpaeaQElfNAFFVNLSDT 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499232095   70 LRVPYHVLPGNHDDRVQLAATfadHPYLREAGEFVQYTIEDQPLRFIVLDTVVPQ-QSHGALCERRLQWLAQRLAEQPG 147
Cdd:TIGR00619  74 GIRPIVVISGNHDSAQRLSAA---KKLLAELGVFVVGSPGHDPQILLLKDGTNGEgLCVGLFLLPREAILTRAGLDGFG 149
 
Name Accession Description Interval E-value
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 3-245 1.63e-103

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: 301.12  E-value: 1.63e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIRMPGQKAYRVVETDRYLPPAVAALNRLEPAPDLVIVSGDLTDFGRPQEYAHLKQMLDALRVPYHVLPGNHD 82
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNHD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  83 DRVQLAATFADHPYlrEAGEFVQYTIEDQPLRFIVLDTVVPQQSHGALCERRLQWLAQRLAEQPGRPTVIVMHHPPFRTG 162
Cdd:cd07402   81 DRAAMREALPEPPY--DDNGPVQYVVDFGGWRLILLDTSVPGVHHGELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095 163 IAHMDAIGlLAGAPELEALVARHSNVERIMCGHLHRTIFQRFGGTIASTCPSPAHQVALDLRPDGPSAFVMEPPGFHLHE 242
Cdd:cd07402  159 IPWMDAIR-LRNSQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQFALDLDDFALDAEAPGPRNLLLHA 237


                 ...
gi 499232095 243 WRD 245
Cdd:cd07402  238 DGI 240
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-258 1.55e-66

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 206.85  E-value: 1.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   1 MLIAQISDLHIRMPgqkayRVVETDRYLPPAVAALNRlePAPDLVIVSGDLTDFGRPQEYAHLKQMLDALRVPYHVLPGN 80
Cdd:COG1409    1 FRFAHISDLHLGAP-----DGSDTAEVLAAALADINA--PRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  81 HDDRVQLAATFADHpYLREAGEFVQYTIEDQPLRFIVLDTVVPQQSHGALCERRLQWLAQRLAEQPGRPTVIVMHHPPFR 160
Cdd:COG1409   74 HDIRAAMAEAYREY-FGDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLAWLEEELAAAPAKPVIVFLHHPPYS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095 161 TGIaHMDAIGlLAGAPELEALVARHsNVERIMCGHLHRTIFQRFGGTIASTCPSPAHQVALdlrpdgpsafvmePPGFHL 240
Cdd:COG1409  153 TGS-GSDRIG-LRNAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRL-------------PPGYRV 216

                        250
                 ....*....|....*...
gi 499232095 241 HEWRDGALVTHHAYIESY 258
Cdd:COG1409  217 IEVDGDGLTVEVRRVDGG 234
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 3-197 2.12e-19

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


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 84.99  E-value: 2.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIRMPGQKAYRVVETDRYLPPAVAALNRLEPAPDLVIVSGDLTDFGRPQEYAHLKQMLDALRVPYHVLPGNHD 82
Cdd:PRK11148  17 ILQITDTHLFADEHETLLGVNTWESYQAVLEAIRAQQHEFDLIVATGDLAQDHSSEAYQHFAEGIAPLRKPCVWLPGNHD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  83 DRVQLAATFADHPYLRE----AGEFVQytiedqplrFIVLDTVVPQQSHGALCERRLQWLAQRLAEQPGRPTVIVMHHPP 158
Cdd:PRK11148  97 FQPAMYSALQDAGISPAkhvlIGEHWQ---------ILLLDSQVFGVPHGELSEYQLEWLERKLADAPERHTLVLLHHHP 167

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499232095 159 FRTGIAHMDAIGlLAGAPELEALVARHSNVERIMCGHLH 197
Cdd:PRK11148 168 LPAGCAWLDQHS-LRNAHELAEVLAKFPNVKAILCGHIH 205
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
3-208 1.07e-16

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 76.59  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIRMPgqkayrvvetdrYLPPAVAALNRlePAPDLVIVSGDLTDFGRPQEYAHLKQMLDALRVPYHVLPGNHD 82
Cdd:COG2129    2 ILAVSDLHGNFD------------LLEKLLELARA--EDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  83 DRVQLAAtfadhpyLREA------GEFVqyTIEDqpLRFIVLdTVVPQQSHGALCERRLQWLAQRLAE-QPGRPTVIVMH 155
Cdd:COG2129   68 DPEVLDA-------LEESgvhnlhGRVV--EIGG--LRIAGL-GGSRPTPFGTPYEYTEEEIEERLAKlREKDVDILLTH 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499232095 156 HPPFRTGIAHmDAIGLLAGAPELEALVARHsNVERIMCGHLHR-TIFQRFGGTI 208
Cdd:COG2129  136 APPYGTTLDR-VEDGPHVGSKALRELIEEF-QPKLVLHGHIHEsRGVDKIGGTR 187
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 3-82 3.32e-13

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: 65.01  E-value: 3.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIrmpgqkayrvvetDRYLPPAVAALNRLEPA----PDLVIVSGDLTDFGRPQEYAHLKQMLDALRV-PYHVL 77
Cdd:cd07400    1 IAHISDLHF-------------GEERKPEVLELNLLDEInalkPDLVVVTGDLTQRARPAEFEEAREFLDALEPePVVVV 67


                 ....*
gi 499232095  78 PGNHD 82
Cdd:cd07400   68 PGNHD 72
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 31-237 2.25e-12

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: 65.05  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  31 AVAALNRlEPAPDLVIVSGDLTDFGRPQEYAH-----LKQMLDALRVPYHVLPGNHDDRVqLAATFADHPYLREAGEFVQ 105
Cdd:cd07396   37 AVEEWNR-ESNLAFVVQLGDIIDGYNAKDRSKealdaVLSILDRLKGPVHHVLGNHEFYN-FPREYLNHLKTLNGEDAYY 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095 106 YTIEDQP-LRFIVLDTVvpqQSHGALCERRLQWLAQRL-----AEQPgrptVIVMHHPPFRTGIAhmDAIGLLAGAPELE 179
Cdd:cd07396  115 YSFSPGPgFRFLVLDFV---KFNGGIGEEQLAWLRNELtsadaNGEK----VIVLSHLPIYPEAA--DPQCLLWNYEEVL 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499232095 180 ALVARHSNVERIMCGHLHRtifqrfGGTiaSTCPSPAHQVALdlrpdgpSAFVMEPPG 237
Cdd:cd07396  186 AILESYPCVKACFSGHNHE------GGY--EQDSHGVHHVTL-------EGVLETPPD 228
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 31-198 3.98e-10

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 58.87  E-value: 3.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  31 AVAALNRLEPAPDLVIVSGDLTD--FGRPQEYAHLKQMLDALR-----VPYHVLPGNHD--DRVQlAATFADhpYLREAG 101
Cdd:cd07395   40 AVQAINKLNPKPKFVVVCGDLVHamPGEEFREQQVSDLKDVLSkldpdIPLVCVCGNHDvgNTPT-PETIQR--YRDDFG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095 102 -EFVQYTIEDqpLRFIVLDTVVPQQSHGA--LCERRLQWLAQRL--AEQPGRPTVIV-MHHPPFRTGIAHMDAIGLLAGA 175
Cdd:cd07395  117 dDYFSFWVGG--VFFIVLNSQLFKDPSKVpeLASAQDQWLEEQLqiARESDAKHVVVfQHIPLFLEDPDEEDDYFNIPKS 194

                        170       180
                 ....*....|....*....|....
gi 499232095 176 PELEALVARHSN-VERIMCGHLHR 198
Cdd:cd07395  195 VRRELLDKFKKAgVKAVFSGHYHR 218
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
3-157 4.46e-10

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 58.65  E-value: 4.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIR--MPGQKAYRVVEtdrylppavaALNRLEpaPDLVIVSGDLTDfGRPQEYAHLKQMLDALRVPYHVL--P 78
Cdd:COG1408   45 IVQLSDLHLGpfIGGERLERLVE----------KINALK--PDLVVLTGDLVD-GSVAELEALLELLKKLKAPLGVYavL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  79 GNHDDRVQLAATFAdhpYLREAG------EFVQYTIEDQPLRFIVLDTVVpqqshgalcERRLQWLAQRLAEQPGRPTVI 152
Cdd:COG1408  112 GNHDYYAGLEELRA---ALEEAGvrvlrnEAVTLERGGDRLNLAGVDDPH---------AGRFPDLEKALAGVPPDAPRI 179


                 ....*.
gi 499232095 153 VM-HHP 157
Cdd:COG1408  180 LLaHNP 185
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-84 4.10e-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: 50.67  E-value: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095    1 MLIAQISDLHIrmPGQkAYRVVETDRYLPPavaalnrlEPAPDLVIVSGDLTDFGRPQEYAHLKQMLDALRVPYHVLPGN 80
Cdd:pfam00149   1 MRILVIGDLHL--PGQ-LDDLLELLKKLLE--------EGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGN 69


                  ....
gi 499232095   81 HDDR 84
Cdd:pfam00149  70 HDFD 73
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
1-207 5.10e-08

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 52.61  E-value: 5.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   1 MLIAQISDLHIRMPGQKAYRvvETDRYlppavAALNRL-----EPAPDLVIVSGDLTDFGRPQEYAhLKQMLDALR---- 71
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASR--REDQL-----AALDRLvdlaiEEKVDAVLIAGDLFDSANPSPEA-VRLLAEALRrlse 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  72 --VPYHVLPGNHD--DRVQLAATFADHPYLREAGEFV--QYTIED-QPLRFIVLDTVVPQQshgalcERRLQWLAQRLAE 144
Cdd:COG0420   73 agIPVVLIAGNHDspSRLSAGSPLLENLGVHVFGSVEpePVELEDgLGVAVYGLPYLRPSD------EEALRDLLERLPR 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499232095 145 Q--PGRPTVIVMHHppFRTGIAHMDAIgllAGAP-ELEALvaRHSNVERIMCGHLHRtiFQRFGGT 207
Cdd:COG0420  147 AldPGGPNILLLHG--FVAGASGSRDI---YVAPvPLSAL--PAAGFDYVALGHIHR--PQVLGGD 203
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 69-197 1.81e-07

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: 51.17  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  69 ALRVPYHVLPGNHDDRV----QLAATFAD--------HPYLREAGEFvqyTIEDQPLRFIVLDTVV-------------P 123
Cdd:cd07378   72 SLQVPWYLVLGNHDHRGnvsaQIAYTQRPnskrwnfpNYYYDISFKF---PSSDVTVAFIMIDTVLlcgntddeasgqpR 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499232095 124 QQSHGALCERRLQWLAQRLAEQPGRPTVIVMHHPPFRTGiAHMDAIGLLAgapELEALVARHsNVERIMCGHLH 197
Cdd:cd07378  149 GPPNKKLAETQLAWLEKQLAASKADYKIVVGHYPIYSSG-EHGPTKCLVD---ILLPLLKKY-KVDAYLSGHDH 217
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 3-87 1.04e-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: 48.43  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIRMpgqkayrvVETDRYLPPAVAALNRLEpaPDLVIVSGDLTDfGRPQEYAHLKQMLDALRVPYHVL--PGN 80
Cdd:cd07385    4 IVQLSDIHLGP--------FVGRTRLQKVVRKVNELN--PDLIVITGDLVD-GDVSVLRLLASPLSKLKAPLGVYfvLGN 72


                 ....*..
gi 499232095  81 HDDRVQL 87
Cdd:cd07385   73 HDYYSGD 79
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 4-82 3.90e-06

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 45.34  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   4 AQISDLHIrmpgqkayrvveTDRYLPPAVAALNRLEPAPDLVIVSGDLTDFGRPQEYAHLKQMLD-ALRVPYHVLPGNHD 82
Cdd:cd00838    1 LVISDIHG------------NLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALRLlLAGIPVYVVPGNHD 68
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 3-83 1.03e-05

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: 45.36  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIrmpGQKAYRVVETDRYLPPAVAALNRL--EPAPDLVIVSGDL-TDFGRPQEYA--HLKQM---LDALRVPY 74
Cdd:cd07383    5 ILQFADLHF---GEGEWTCWEGCEADLKTVEFIESVldEEKPDLVVLTGDLiTGENTADDNAtsYLDKAvspLVERGIPW 81


                 ....*....
gi 499232095  75 HVLPGNHDD 83
Cdd:cd07383   82 AATFGNHDG 90
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 3-100 9.72e-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: 39.17  E-value: 9.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   3 IAQISDLHIrmpGQKAYRV--VETDRYlppavAALNRL-----EPAPDLVIVSGDLTDFGRPQEYAhLKQMLDALR---- 71
Cdd:cd00840    2 FLHTADWHL---GYPLYGLsrREEDFF-----KAFEEIvdlaiEEKVDFVLIAGDLFDSNNPSPEA-LKLAIEGLRrlce 72

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499232095  72 --VPYHVLPGNHDD--RVQLAATfadhPYLREA 100
Cdd:cd00840   73 agIPVFVIAGNHDSpaRVAIYGL----PYLRDE 101
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 7-195 1.01e-03

Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized Microscilla protein with a metallophosphatase domain. Microscilla proteins MS152, and MS153 are also included in this family. 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: 277349 [Multi-domain]  Cd Length: 201  Bit Score: 39.24  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095   7 SDLHIRMPGQKAYRVVETdrylppavaalnrLEPAPDLVIVSGDLtdfGRPQEYAHLKQMLDALRVPY-HVL--PGNHDD 83
Cdd:cd07404    5 SDLHLEVEQNLAKLKFFP-------------KVPDADILILAGDI---GRLTDAEAWDNFLDLQSFQFePVYyvPGNHEF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095  84 RVQ-LAATFADHPYLREAGEFVQY----TIEDQPLRFI--VLDTVVPQqSHGALCERRLQWLAqrlaeqpgRPTVIVMHH 156
Cdd:cd07404   69 YGGsLDITLDALRMAAQDLSNVHYlnnqEVVLDDVRILgcTLWSDFDP-DGEDIVQRKLNDFR--------GATVVVTHH 139

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 499232095 157 PPFRTGIAHMDAIGLLAGApelealvARHSNVERIMCGH 195
Cdd:cd07404  140 APSPRSTSDNYADGLPKNA-------AFHVDLKDLILAP 171
MPP_YvnB cd07399
Bacillus subtilis YvnB and related proteins, metallophosphatase domain; YvnB (BSU35040) is an ...
 43-82 2.82e-03

Bacillus subtilis YvnB and related proteins, metallophosphatase domain; YvnB (BSU35040) is an uncharacterized Bacillus subtilis protein with a metallophosphatase domain. This family includes bacterial and eukaryotic proteins similar to YvnB. YvnB 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: 277344 [Multi-domain]  Cd Length: 207  Bit Score: 37.86  E-value: 2.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 499232095  43 DLVIVSGDLTDFGRPQEY---AHLKQMLDALRVPYHVLPGNHD 82
Cdd:cd07399   37 DFVFHTGDVTDHGVDKEWevaAAAFNVLDDSGVPYSVLAGNHD 79
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 1-147 5.25e-03

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 37.40  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499232095    1 MLIAQISDLHIrmpGQKAYRVVEtdryLPPAVAALNRL-----EPAPDLVIVSGDLTDFGRP----QE--YAHLKQMLDA 69
Cdd:TIGR00619   1 MRILHTSDWHL---GKTLEGVSR----LAEQKAFLDDLlefakAEQVDALLVAGDVFDTANPpaeaQElfNAFFVNLSDT 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499232095   70 LRVPYHVLPGNHDDRVQLAATfadHPYLREAGEFVQYTIEDQPLRFIVLDTVVPQ-QSHGALCERRLQWLAQRLAEQPG 147
Cdd:TIGR00619  74 GIRPIVVISGNHDSAQRLSAA---KKLLAELGVFVVGSPGHDPQILLLKDGTNGEgLCVGLFLLPREAILTRAGLDGFG 149
 
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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