NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446160361|ref|WP_000238216|]
View 

exonuclease SbcCD subunit D [Staphylococcus aureus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-249 1.99e-68

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


:

Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 216.70  E-value: 1.99e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   2 VKFIHCSDLHLDSPFKSKShispkifedVQKSAYESFKNIVDIALQQDVDFVIIAGDLFDSENRTLRAEIFLKQQFERLQ 81
Cdd:COG0420    1 MRFLHTADWHLGKPLHGAS---------RREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361  82 NEQIFIYVCHGNHDPLSSK-ISSNWPD--NVSVFSNKVEtyEAIT-KSGETIYIHGFSYENRASYENK---IDEYPSSQG 154
Cdd:COG0420   72 EAGIPVVLIAGNHDSPSRLsAGSPLLEnlGVHVFGSVEP--EPVElEDGLGVAVYGLPYLRPSDEEALrdlLERLPRALD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361 155 QKGIHIGVLHGTYSKSSVN-ERYTEFI-LEDLNSKLYHYWALGHIHERQQLSDMPVINYSGNIQGRHFNEQGEKGCLLIE 232
Cdd:COG0420  150 PGGPNILLLHGFVAGASGSrDIYVAPVpLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVE 229

                        250
                 ....*....|....*...
gi 446160361 233 -GDHLKLKTKFYPTQYIR 249
Cdd:COG0420  230 lDAGGLVSVEFVPLPATR 247
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-249 1.99e-68

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 216.70  E-value: 1.99e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   2 VKFIHCSDLHLDSPFKSKShispkifedVQKSAYESFKNIVDIALQQDVDFVIIAGDLFDSENRTLRAEIFLKQQFERLQ 81
Cdd:COG0420    1 MRFLHTADWHLGKPLHGAS---------RREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361  82 NEQIFIYVCHGNHDPLSSK-ISSNWPD--NVSVFSNKVEtyEAIT-KSGETIYIHGFSYENRASYENK---IDEYPSSQG 154
Cdd:COG0420   72 EAGIPVVLIAGNHDSPSRLsAGSPLLEnlGVHVFGSVEP--EPVElEDGLGVAVYGLPYLRPSDEEALrdlLERLPRALD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361 155 QKGIHIGVLHGTYSKSSVN-ERYTEFI-LEDLNSKLYHYWALGHIHERQQLSDMPVINYSGNIQGRHFNEQGEKGCLLIE 232
Cdd:COG0420  150 PGGPNILLLHGFVAGASGSrDIYVAPVpLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVE 229

                        250
                 ....*....|....*...
gi 446160361 233 -GDHLKLKTKFYPTQYIR 249
Cdd:COG0420  230 lDAGGLVSVEFVPLPATR 247
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 3-221 2.75e-58

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: 188.25  E-value: 2.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   3 KFIHCSDLHLDSPFKSKSHispkifedVQKSAYESFKNIVDIALQQDVDFVIIAGDLFDSENRTLRAEIFLKQQFERLQN 82
Cdd:cd00840    1 RFLHTADWHLGYPLYGLSR--------REEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361  83 EQIFIYVCHGNHDPLSSkissnwpdnvsvfsnkvetyeaitksgetIYIHGFSYENRASYENKID---EYPSSQGQKGIH 159
Cdd:cd00840   73 AGIPVFVIAGNHDSPAR-----------------------------VAIYGLPYLRDERLERLFEdleLRPRLLKPDWFN 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446160361 160 IGVLHGTYSKSSVNERYTEFILEDLNSKLYHYWALGHIHERQQL-SDMPVINYSGNIQGRHFN 221
Cdd:cd00840  124 ILLLHQGVDGAGPSDSERPIVPEDLLPDGFDYVALGHIHKPQIIeGGGPPIVYPGSPEPTSFS 186
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 3-225 6.23e-11

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: 62.05  E-value: 6.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361    3 KFIHCSDLHLDSPFKSKShispkIFEDVQKSAYEsfknIVDIALQQDVDFVIIAGDLFDSENRTLRAEIFLKQQFERLQN 82
Cdd:TIGR00619   2 RILHTSDWHLGKTLEGVS-----RLAEQKAFLDD----LLEFAKAEQVDALLVAGDVFDTANPPAEAQELFNAFFVNLSD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   83 EQIF-IYVCHGNHDPlSSKISSNWP----DNVSVFSNKVETYEAI----TKSGETI----------YIHGFSYEN----- 138
Cdd:TIGR00619  73 TGIRpIVVISGNHDS-AQRLSAAKKllaeLGVFVVGSPGHDPQILllkdGTNGEGLcvglfllpreAILTRAGLDgfgle 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361  139 --RASYENKIDEYPSSQGQKGI---------HIGVLHGTYSkSSVNERYTEFILEDLNSKLY--HYWALGHIHERQQLSD 205
Cdd:TIGR00619 152 llLAHTDVKLRQAAEALKLRLDqdlpkillaHLFTAGATKS-DAERRIYIGTLYAFPLQNFPeaDYIALGHIHIHKISKG 230

                         250       260
                  ....*....|....*....|
gi 446160361  206 MPVINYSGNIQGRHFNEQGE 225
Cdd:TIGR00619 231 RERVRYSGSPFPLSFDEAGK 250
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 3-114 7.91e-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: 47.59  E-value: 7.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361    3 KFIHCSDLHLDSPFkskshispkifedvqksayESFKNIVD-IALQQDVDFVIIAGDLFDSENRTLRAEIFLKQQFERLQ 81
Cdd:pfam00149   2 RILVIGDLHLPGQL-------------------DDLLELLKkLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446160361   82 neqifIYVCHGNHD----------PLSSKISSNWPDNVSVFSN 114
Cdd:pfam00149  63 -----VYLVRGNHDfdygeclrlyPYLGLLARPWKRFLEVFNF 100
PRK10966 PRK10966
exonuclease subunit SbcD; Provisional
 3-95 4.27e-03

exonuclease subunit SbcD; Provisional


Pssm-ID: 182871 [Multi-domain]  Cd Length: 407  Bit Score: 39.15  E-value: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   3 KFIHCSDLHLDSPFKSKShispkifedvQKSAYESFKN-IVDIALQQDVDFVIIAGDLFD-----SENRTLRaeiflkQQ 76
Cdd:PRK10966   2 RILHTSDWHLGQNFYSKS----------RAAEHQAFLDwLLEQVQEHQVDAIIVAGDIFDtgsppSYARELY------NR 65

                         90       100
                 ....*....|....*....|
gi 446160361  77 F-ERLQNEQIFIYVCHGNHD 95
Cdd:PRK10966  66 FvVNLQQTGCQLVVLAGNHD 85
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-249 1.99e-68

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 216.70  E-value: 1.99e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   2 VKFIHCSDLHLDSPFKSKShispkifedVQKSAYESFKNIVDIALQQDVDFVIIAGDLFDSENRTLRAEIFLKQQFERLQ 81
Cdd:COG0420    1 MRFLHTADWHLGKPLHGAS---------RREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361  82 NEQIFIYVCHGNHDPLSSK-ISSNWPD--NVSVFSNKVEtyEAIT-KSGETIYIHGFSYENRASYENK---IDEYPSSQG 154
Cdd:COG0420   72 EAGIPVVLIAGNHDSPSRLsAGSPLLEnlGVHVFGSVEP--EPVElEDGLGVAVYGLPYLRPSDEEALrdlLERLPRALD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361 155 QKGIHIGVLHGTYSKSSVN-ERYTEFI-LEDLNSKLYHYWALGHIHERQQLSDMPVINYSGNIQGRHFNEQGEKGCLLIE 232
Cdd:COG0420  150 PGGPNILLLHGFVAGASGSrDIYVAPVpLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVE 229

                        250
                 ....*....|....*...
gi 446160361 233 -GDHLKLKTKFYPTQYIR 249
Cdd:COG0420  230 lDAGGLVSVEFVPLPATR 247
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 3-221 2.75e-58

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: 188.25  E-value: 2.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   3 KFIHCSDLHLDSPFKSKSHispkifedVQKSAYESFKNIVDIALQQDVDFVIIAGDLFDSENRTLRAEIFLKQQFERLQN 82
Cdd:cd00840    1 RFLHTADWHLGYPLYGLSR--------REEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361  83 EQIFIYVCHGNHDPLSSkissnwpdnvsvfsnkvetyeaitksgetIYIHGFSYENRASYENKID---EYPSSQGQKGIH 159
Cdd:cd00840   73 AGIPVFVIAGNHDSPAR-----------------------------VAIYGLPYLRDERLERLFEdleLRPRLLKPDWFN 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446160361 160 IGVLHGTYSKSSVNERYTEFILEDLNSKLYHYWALGHIHERQQL-SDMPVINYSGNIQGRHFN 221
Cdd:cd00840  124 ILLLHQGVDGAGPSDSERPIVPEDLLPDGFDYVALGHIHKPQIIeGGGPPIVYPGSPEPTSFS 186
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 3-225 6.23e-11

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: 62.05  E-value: 6.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361    3 KFIHCSDLHLDSPFKSKShispkIFEDVQKSAYEsfknIVDIALQQDVDFVIIAGDLFDSENRTLRAEIFLKQQFERLQN 82
Cdd:TIGR00619   2 RILHTSDWHLGKTLEGVS-----RLAEQKAFLDD----LLEFAKAEQVDALLVAGDVFDTANPPAEAQELFNAFFVNLSD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   83 EQIF-IYVCHGNHDPlSSKISSNWP----DNVSVFSNKVETYEAI----TKSGETI----------YIHGFSYEN----- 138
Cdd:TIGR00619  73 TGIRpIVVISGNHDS-AQRLSAAKKllaeLGVFVVGSPGHDPQILllkdGTNGEGLcvglfllpreAILTRAGLDgfgle 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361  139 --RASYENKIDEYPSSQGQKGI---------HIGVLHGTYSkSSVNERYTEFILEDLNSKLY--HYWALGHIHERQQLSD 205
Cdd:TIGR00619 152 llLAHTDVKLRQAAEALKLRLDqdlpkillaHLFTAGATKS-DAERRIYIGTLYAFPLQNFPeaDYIALGHIHIHKISKG 230

                         250       260
                  ....*....|....*....|
gi 446160361  206 MPVINYSGNIQGRHFNEQGE 225
Cdd:TIGR00619 231 RERVRYSGSPFPLSFDEAGK 250
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
2-95 1.89e-09

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 57.39  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   2 VKFIHCSDLHLDSPFKSKShispkifedvqksaYESFKNIVDIALQQDVDFVIIAGDLFDsenRTLRAEI-FLKQQFERL 80
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDT--------------AEVLAAALADINAPRPDFVVVTGDLTD---DGEPEEYaAAREILARL 63

                         90
                 ....*....|....*
gi 446160361  81 qneQIFIYVCHGNHD 95
Cdd:COG1409   64 ---GVPVYVVPGNHD 75
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 3-114 7.91e-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: 47.59  E-value: 7.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361    3 KFIHCSDLHLDSPFkskshispkifedvqksayESFKNIVD-IALQQDVDFVIIAGDLFDSENRTLRAEIFLKQQFERLQ 81
Cdd:pfam00149   2 RILVIGDLHLPGQL-------------------DDLLELLKkLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446160361   82 neqifIYVCHGNHD----------PLSSKISSNWPDNVSVFSN 114
Cdd:pfam00149  63 -----VYLVRGNHDfdygeclrlyPYLGLLARPWKRFLEVFNF 100
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
3-96 5.82e-05

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 43.85  E-value: 5.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   3 KFIHCSDLHLDspfkskshispkifedvqksaYESFKNIVDIALQQDVDFVIIAGDLFDSENRTLRAEIflkqqFERLQN 82
Cdd:COG2129    1 KILAVSDLHGN---------------------FDLLEKLLELARAEDADLVILAGDLTDFGTAEEAREV-----LEELAA 54

                         90
                 ....*....|....
gi 446160361  83 EQIFIYVCHGNHDP 96
Cdd:COG2129   55 LGVPVLAVPGNHDD 68
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 5-133 7.95e-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: 42.25  E-value: 7.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   5 IHCSDLHLDSPFKSKshispkifedvqksayesfKNIVDIALQQDVDFVIIAGDLFDSENRTLRAEIflkqQFERLQNEQ 84
Cdd:cd00838    1 LVISDIHGNLEALEA-------------------VLEAALAKAEKPDLVICLGDLVDYGPDPEEVEL----KALRLLLAG 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446160361  85 IFIYVCHGNHD-------PLSSKISSNWPDNVsvfsNKVETYEAITKSGETIYIHG 133
Cdd:cd00838   58 IPVYVVPGNHDilvthgpPYDPLDEGSPGEDP----GSEALLELLDKYGPDLVLSG 109
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 3-146 4.11e-04

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: 41.50  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   3 KFIHCSDLHLdSPFKSKSHIspkifedvqksayesfKNIVDIALQQDVDFVIIAGDLFDSENRTLRAEIflkQQFERLqN 82
Cdd:cd07385    3 RIVQLSDIHL-GPFVGRTRL----------------QKVVRKVNELNPDLIVITGDLVDGDVSVLRLLA---SPLSKL-K 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446160361  83 EQIFIYVCHGNHDPLSSkISSNWPD-----NVSVFSNKVETYEAITKSGETIYIHGFSYENRASYENKI 146
Cdd:cd07385   62 APLGVYFVLGNHDYYSG-DVEVWIAalekaGITVLRNESVELSRDGATIGLAGSGVDDIGGHGEDLEKA 129
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 4-95 7.04e-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: 40.72  E-value: 7.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   4 FIHCSDLHLdspfkskshISPKIFEDVQKSAYESFKNIVD--IALQQDVDFVIIAGDLFDseNRTLRAEIFLKQQFERLq 81
Cdd:cd07402    1 IAQISDTHL---------FAPGEGALLGVDTAARLAAAVAqvNALHPRPDLVVVTGDLSD--DGSPESYERLRELLAPL- 68

                         90
                 ....*....|....
gi 446160361  82 neQIFIYVCHGNHD 95
Cdd:cd07402   69 --PAPVYWIPGNHD 80
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 5-95 3.81e-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: 37.27  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   5 IHCSDLHLDSPFKSKSHispkifedvqksayesFKNIVDIALQQDVDFVIIAGDLfdsENRTLRAEIFL-KQQFERLQNE 83
Cdd:cd07400    2 AHISDLHFGEERKPEVL----------------ELNLLDEINALKPDLVVVTGDL---TQRARPAEFEEaREFLDALEPE 62

                         90
                 ....*....|..
gi 446160361  84 QifIYVCHGNHD 95
Cdd:cd07400   63 P--VVVVPGNHD 72
PRK10966 PRK10966
exonuclease subunit SbcD; Provisional
 3-95 4.27e-03

exonuclease subunit SbcD; Provisional


Pssm-ID: 182871 [Multi-domain]  Cd Length: 407  Bit Score: 39.15  E-value: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361   3 KFIHCSDLHLDSPFKSKShispkifedvQKSAYESFKN-IVDIALQQDVDFVIIAGDLFD-----SENRTLRaeiflkQQ 76
Cdd:PRK10966   2 RILHTSDWHLGQNFYSKS----------RAAEHQAFLDwLLEQVQEHQVDAIIVAGDIFDtgsppSYARELY------NR 65

                         90       100
                 ....*....|....*....|
gi 446160361  77 F-ERLQNEQIFIYVCHGNHD 95
Cdd:PRK10966  66 FvVNLQQTGCQLVVLAGNHD 85
acc_ester TIGR03729
putative phosphoesterase; Members of this protein family belong to the larger family pfam00149 ...
 8-100 4.52e-03

putative phosphoesterase; Members of this protein family belong to the larger family pfam00149 (calcineurin-like phosphoesterase), a family largely defined by small motifs of metal-chelating residues. The subfamily in this model shows a good but imperfect co-occurrence in species with domain TIGR03715 that defines a novel class of signal peptide typical of the accessory secretory system.


Pssm-ID: 163441 [Multi-domain]  Cd Length: 239  Bit Score: 38.44  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361    8 SDLHLDSPfkskshispkifedvQKSAYESFKNIVDIALQQDVDFVIIAGDLFDSENRTLraeiflkQQFERLQNEQ-IF 86
Cdd:TIGR03729   6 SDLHIDLN---------------HFDTEEMLETLAQYLKKQKIDHLHIAGDISNDFQRSL-------PFIEKLQELKgIK 63

                          90
                  ....*....|....
gi 446160361   87 IYVCHGNHDPLSSK 100
Cdd:TIGR03729  64 VTFNAGNHDMLKDL 77
MPP_DNA_pol_II_small_archeal_C cd07386
archeal DNA polymerase II, small subunit, C-terminal metallophosphatase domain; The small ...
 16-144 9.25e-03

archeal DNA polymerase II, small subunit, C-terminal metallophosphatase domain; The small subunit of the archeal DNA polymerase II contains a C-terminal metallophosphatase domain. This domain is thought to be functionally active because the active site residues required for phosphoesterase activity in other members of this superfamily are intact. The archeal replicative DNA polymerases are thought to possess intrinsic phosphatase activity that hydrolyzes the pyrophosphate released during nucleotide polymerization. This domain 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: 277332  Cd Length: 243  Bit Score: 37.28  E-value: 9.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361  16 FKSKSHISPKIF-EDvqksAYESF----KNIVDIAlqQDVDFVIIAGDLFD-------SENRTLRAEIFlkQQFERLQN- 82
Cdd:cd07386    3 FISDVHVGSKTFlED----AFEKFvrwlNGEDDSA--SRVKYLIIAGDLVDgigvypgQEEELEILDIY--EQYEEAAEy 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446160361  83 -----EQIFIYVCHGNHDP---------LSSKISSN-WPDNVSVFSNKVetyeAITKSGETIYI-HGFSYEN------RA 140
Cdd:cd07386   75 lsdvpSHIKIIIIPGNHDAvrqaepqpaLPEEIRKLfYPGNVEFLSNPA----LVKIHGVDVLIyHGRSLDDvvglipGL 150


                 ....
gi 446160361 141 SYEN 144
Cdd:cd07386  151 SYDK 154
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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