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Conserved domains on  [gi|487747735|ref|WP_001829843|]
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MULTISPECIES: DNA repair exonuclease [Staphylococcus]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 11417965)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc), such as exonuclease SbcCD subunit D is a component of SbcCD, which is involved in double-strand DNA break detection and repair by homologous recombination and non-homologous end joining of damaged DNA

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0042578|GO:0046872|GO:0003677
PubMed:  25837850|8003970
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-245 5.97e-68

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


:

Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 215.16  E-value: 5.97e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   2 VKFIHCADLHLDSPFKSKSYLspnifEDVqksaYESFKNIVDLALKQEVDFIIIAGDLFDSENRTLRAEVFLNEQFERLR 81
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASRR-----EDQ----LAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735  82 KEQIFVYICHGNHDPLTSK-ITSQWP--NNVSVFSNQVETYQAItKSGETIYIHGFSYQNDASYENK---IDAYPSSQGQ 155
Cdd:COG0420   72 EAGIPVVLIAGNHDSPSRLsAGSPLLenLGVHVFGSVEPEPVEL-EDGLGVAVYGLPYLRPSDEEALrdlLERLPRALDP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735 156 KGIHIGVLHGTYSKSSV-KDRYT-EFRLEDLNQRLYHYWALGHIHQREQLSDMPVINYPGNIQGRHFNELGEKGCLLVE- 232
Cdd:COG0420  151 GGPNILLLHGFVAGASGsRDIYVaPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVEl 230

                        250
                 ....*....|...
gi 487747735 233 GDHLKLTTQFYPT 245
Cdd:COG0420  231 DAGGLVSVEFVPL 243
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-245 5.97e-68

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 215.16  E-value: 5.97e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   2 VKFIHCADLHLDSPFKSKSYLspnifEDVqksaYESFKNIVDLALKQEVDFIIIAGDLFDSENRTLRAEVFLNEQFERLR 81
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASRR-----EDQ----LAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735  82 KEQIFVYICHGNHDPLTSK-ITSQWP--NNVSVFSNQVETYQAItKSGETIYIHGFSYQNDASYENK---IDAYPSSQGQ 155
Cdd:COG0420   72 EAGIPVVLIAGNHDSPSRLsAGSPLLenLGVHVFGSVEPEPVEL-EDGLGVAVYGLPYLRPSDEEALrdlLERLPRALDP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735 156 KGIHIGVLHGTYSKSSV-KDRYT-EFRLEDLNQRLYHYWALGHIHQREQLSDMPVINYPGNIQGRHFNELGEKGCLLVE- 232
Cdd:COG0420  151 GGPNILLLHGFVAGASGsRDIYVaPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVEl 230

                        250
                 ....*....|...
gi 487747735 233 GDHLKLTTQFYPT 245
Cdd:COG0420  231 DAGGLVSVEFVPL 243
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 3-221 1.96e-60

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: 193.64  E-value: 1.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   3 KFIHCADLHLDSPFKSKSylspnifeDVQKSAYESFKNIVDLALKQEVDFIIIAGDLFDSENRTLRAEVFLNEQFERLRK 82
Cdd:cd00840    1 RFLHTADWHLGYPLYGLS--------RREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735  83 EQIFVYICHGNHDPLTSkitsqwpnnvsvfsnqvetyqaitksgetIYIHGFSYQNDASYENKID---AYPSSQGQKGIH 159
Cdd:cd00840   73 AGIPVFVIAGNHDSPAR-----------------------------VAIYGLPYLRDERLERLFEdleLRPRLLKPDWFN 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487747735 160 IGVLHGTYSKSSVKDRYTEFRLEDLNQRLYHYWALGHIHQR-EQLSDMPVINYPGNIQGRHFN 221
Cdd:cd00840  124 ILLLHQGVDGAGPSDSERPIVPEDLLPDGFDYVALGHIHKPqIIEGGGPPIVYPGSPEPTSFS 186
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 3-225 2.83e-12

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: 66.29  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735    3 KFIHCADLHLDSPFKSKSylspnIFEDVQKSAYEsfknIVDLALKQEVDFIIIAGDLFDSENRTLRAEVFLNEQFERLRK 82
Cdd:TIGR00619   2 RILHTSDWHLGKTLEGVS-----RLAEQKAFLDD----LLEFAKAEQVDALLVAGDVFDTANPPAEAQELFNAFFVNLSD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   83 EQIF-VYICHGNHDP-----LTSKITSQwpNNVSVFSNQVETYQAI----TKSGETIYIHGFSYQNDA----SYENKID- 147
Cdd:TIGR00619  73 TGIRpIVVISGNHDSaqrlsAAKKLLAE--LGVFVVGSPGHDPQILllkdGTNGEGLCVGLFLLPREAiltrAGLDGFGl 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735  148 ---------------AYPSSQGQKGI------HIGVLHGTYS---KSSVKDRYTEFRLEDLNQRLYHywALGHIHQREQL 203
Cdd:TIGR00619 151 elllahtdvklrqaaEALKLRLDQDLpkillaHLFTAGATKSdaeRRIYIGTLYAFPLQNFPEADYI--ALGHIHIHKIS 228

                         250       260
                  ....*....|....*....|..
gi 487747735  204 SDMPVINYPGNIQGRHFNELGE 225
Cdd:TIGR00619 229 KGRERVRYSGSPFPLSFDEAGK 250
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 3-95 6.62e-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: 44.90  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735    3 KFIHCADLHLDSPFksksylspnifedvqksayESFKNIVDLALKQE-VDFIIIAGDLFDSENRTLRAEVFLNEQFERLR 81
Cdd:pfam00149   2 RILVIGDLHLPGQL-------------------DDLLELLKKLLEEGkPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP 62

                          90
                  ....*....|....
gi 487747735   82 keqifVYICHGNHD 95
Cdd:pfam00149  63 -----VYLVRGNHD 71
PRK10966 PRK10966
exonuclease subunit SbcD; Provisional
 3-95 2.04e-03

exonuclease subunit SbcD; Provisional


Pssm-ID: 182871 [Multi-domain]  Cd Length: 407  Bit Score: 39.92  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   3 KFIHCADLHLDSPFKSKSylspnifedvQKSAYESFKN-IVDLALKQEVDFIIIAGDLFD-----SENRTLraevfLNEQ 76
Cdd:PRK10966   2 RILHTSDWHLGQNFYSKS----------RAAEHQAFLDwLLEQVQEHQVDAIIVAGDIFDtgsppSYAREL-----YNRF 66

                         90
                 ....*....|....*....
gi 487747735  77 FERLRKEQIFVYICHGNHD 95
Cdd:PRK10966  67 VVNLQQTGCQLVVLAGNHD 85
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-245 5.97e-68

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 215.16  E-value: 5.97e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   2 VKFIHCADLHLDSPFKSKSYLspnifEDVqksaYESFKNIVDLALKQEVDFIIIAGDLFDSENRTLRAEVFLNEQFERLR 81
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASRR-----EDQ----LAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735  82 KEQIFVYICHGNHDPLTSK-ITSQWP--NNVSVFSNQVETYQAItKSGETIYIHGFSYQNDASYENK---IDAYPSSQGQ 155
Cdd:COG0420   72 EAGIPVVLIAGNHDSPSRLsAGSPLLenLGVHVFGSVEPEPVEL-EDGLGVAVYGLPYLRPSDEEALrdlLERLPRALDP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735 156 KGIHIGVLHGTYSKSSV-KDRYT-EFRLEDLNQRLYHYWALGHIHQREQLSDMPVINYPGNIQGRHFNELGEKGCLLVE- 232
Cdd:COG0420  151 GGPNILLLHGFVAGASGsRDIYVaPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVEl 230

                        250
                 ....*....|...
gi 487747735 233 GDHLKLTTQFYPT 245
Cdd:COG0420  231 DAGGLVSVEFVPL 243
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 3-221 1.96e-60

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: 193.64  E-value: 1.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   3 KFIHCADLHLDSPFKSKSylspnifeDVQKSAYESFKNIVDLALKQEVDFIIIAGDLFDSENRTLRAEVFLNEQFERLRK 82
Cdd:cd00840    1 RFLHTADWHLGYPLYGLS--------RREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735  83 EQIFVYICHGNHDPLTSkitsqwpnnvsvfsnqvetyqaitksgetIYIHGFSYQNDASYENKID---AYPSSQGQKGIH 159
Cdd:cd00840   73 AGIPVFVIAGNHDSPAR-----------------------------VAIYGLPYLRDERLERLFEdleLRPRLLKPDWFN 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487747735 160 IGVLHGTYSKSSVKDRYTEFRLEDLNQRLYHYWALGHIHQR-EQLSDMPVINYPGNIQGRHFN 221
Cdd:cd00840  124 ILLLHQGVDGAGPSDSERPIVPEDLLPDGFDYVALGHIHKPqIIEGGGPPIVYPGSPEPTSFS 186
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 3-225 2.83e-12

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: 66.29  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735    3 KFIHCADLHLDSPFKSKSylspnIFEDVQKSAYEsfknIVDLALKQEVDFIIIAGDLFDSENRTLRAEVFLNEQFERLRK 82
Cdd:TIGR00619   2 RILHTSDWHLGKTLEGVS-----RLAEQKAFLDD----LLEFAKAEQVDALLVAGDVFDTANPPAEAQELFNAFFVNLSD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   83 EQIF-VYICHGNHDP-----LTSKITSQwpNNVSVFSNQVETYQAI----TKSGETIYIHGFSYQNDA----SYENKID- 147
Cdd:TIGR00619  73 TGIRpIVVISGNHDSaqrlsAAKKLLAE--LGVFVVGSPGHDPQILllkdGTNGEGLCVGLFLLPREAiltrAGLDGFGl 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735  148 ---------------AYPSSQGQKGI------HIGVLHGTYS---KSSVKDRYTEFRLEDLNQRLYHywALGHIHQREQL 203
Cdd:TIGR00619 151 elllahtdvklrqaaEALKLRLDQDLpkillaHLFTAGATKSdaeRRIYIGTLYAFPLQNFPEADYI--ALGHIHIHKIS 228

                         250       260
                  ....*....|....*....|..
gi 487747735  204 SDMPVINYPGNIQGRHFNELGE 225
Cdd:TIGR00619 229 KGRERVRYSGSPFPLSFDEAGK 250
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
2-95 7.40e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 52.77  E-value: 7.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   2 VKFIHCADLHLDSPFKSKSYlspnifedvqksayESFKNIVDLALKQEVDFIIIAGDLFDSENRtlraevflnEQFERLR 81
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTA--------------EVLAAALADINAPRPDFVVVTGDLTDDGEP---------EEYAAAR 57

                         90
                 ....*....|....*...
gi 487747735  82 KE----QIFVYICHGNHD 95
Cdd:COG1409   58 EIlarlGVPVYVVPGNHD 75
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
2-133 2.08e-06

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 48.64  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   2 VKFIHCADLHLDsPFKSKSYLspnifedvqksayesfKNIVDLALKQEVDFIIIAGDLFDSENRTLRAevfLNEQFERLR 81
Cdd:COG1408   43 LRIVQLSDLHLG-PFIGGERL----------------ERLVEKINALKPDLVVLTGDLVDGSVAELEA---LLELLKKLK 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 487747735  82 KEQIfVYICHGNHD------PLTSKITSqwpNNVSVFSNQVETyqaITKSGETIYIHG 133
Cdd:COG1408  103 APLG-VYAVLGNHDyyagleELRAALEE---AGVRVLRNEAVT---LERGGDRLNLAG 153
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 3-95 6.62e-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: 44.90  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735    3 KFIHCADLHLDSPFksksylspnifedvqksayESFKNIVDLALKQE-VDFIIIAGDLFDSENRTLRAEVFLNEQFERLR 81
Cdd:pfam00149   2 RILVIGDLHLPGQL-------------------DDLLELLKKLLEEGkPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP 62

                          90
                  ....*....|....
gi 487747735   82 keqifVYICHGNHD 95
Cdd:pfam00149  63 -----VYLVRGNHD 71
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
3-96 3.91e-05

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 44.24  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   3 KFIHCADLHLDspfksksylspnifedvqksaYESFKNIVDLALKQEVDFIIIAGDLFDsENRTLRAEVFLNEqferLRK 82
Cdd:COG2129    1 KILAVSDLHGN---------------------FDLLEKLLELARAEDADLVILAGDLTD-FGTAEEAREVLEE----LAA 54

                         90
                 ....*....|....
gi 487747735  83 EQIFVYICHGNHDP 96
Cdd:COG2129   55 LGVPVLAVPGNHDD 68
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 4-95 5.98e-04

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: 41.11  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   4 FIHCADLHLDSPfKSKSYLSpnifEDvqksAYESFKNIVD--LALKQEVDFIIIAGDLFDsENRTLRAEVFLnEQFERLR 81
Cdd:cd07402    1 IAQISDTHLFAP-GEGALLG----VD----TAARLAAAVAqvNALHPRPDLVVVTGDLSD-DGSPESYERLR-ELLAPLP 69

                         90
                 ....*....|....
gi 487747735  82 KEqifVYICHGNHD 95
Cdd:cd07402   70 AP---VYWIPGNHD 80
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 5-95 8.22e-04

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: 39.17  E-value: 8.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   5 IHCADLHLDSPFKSKsylspnifedvqksayesfKNIVDLALKQEVDFIIIAGDLFDSenrtLRAEVFLNEQFERLRKEQ 84
Cdd:cd00838    1 LVISDIHGNLEALEA-------------------VLEAALAKAEKPDLVICLGDLVDY----GPDPEEVELKALRLLLAG 57

                         90
                 ....*....|.
gi 487747735  85 IFVYICHGNHD 95
Cdd:cd00838   58 IPVYVVPGNHD 68
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 3-95 1.24e-03

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: 39.96  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   3 KFIHCADLHLdSPFKSKSYLspnifedvqksayesfKNIVDLALKQEVDFIIIAGDLFDSENRTLRAEVflnEQFERLRK 82
Cdd:cd07385    3 RIVQLSDIHL-GPFVGRTRL----------------QKVVRKVNELNPDLIVITGDLVDGDVSVLRLLA---SPLSKLKA 62

                         90
                 ....*....|....*
gi 487747735  83 EQ--IFVYichGNHD 95
Cdd:cd07385   63 PLgvYFVL---GNHD 74
PRK10966 PRK10966
exonuclease subunit SbcD; Provisional
 3-95 2.04e-03

exonuclease subunit SbcD; Provisional


Pssm-ID: 182871 [Multi-domain]  Cd Length: 407  Bit Score: 39.92  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747735   3 KFIHCADLHLDSPFKSKSylspnifedvQKSAYESFKN-IVDLALKQEVDFIIIAGDLFD-----SENRTLraevfLNEQ 76
Cdd:PRK10966   2 RILHTSDWHLGQNFYSKS----------RAAEHQAFLDwLLEQVQEHQVDAIIVAGDIFDtgsppSYAREL-----YNRF 66

                         90
                 ....*....|....*....
gi 487747735  77 FERLRKEQIFVYICHGNHD 95
Cdd:PRK10966  67 VVNLQQTGCQLVVLAGNHD 85
 
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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