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Conserved domains on  [gi|446738457|ref|WP_000815713|]
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MULTISPECIES: DNA repair exonuclease [Bacillus]

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];
4-242 8.55e-83

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


:

Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 254.07  E-value: 8.55e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   4 VKFIHAADLHLDSPFKGmemnvpqsiwERMKQSTFESFERIIDKAIQERVDFVLLAGDLYDAETRSLRAQVFVREQMKRL 83
Cdd:COG0420    1 MRFLHTADWHLGKPLHG----------ASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457  84 SQYDIPVFIIHGNHDHLGGSWAAIEFPE--NVHVFTEPYVEEKSFYNNGEllASIYGFSYLQQAVTDNMTAQFTKMS--- 158
Cdd:COG0420   71 SEAGIPVVLIAGNHDSPSRLSAGSPLLEnlGVHVFGSVEPEPVELEDGLG--VAVYGLPYLRPSDEEALRDLLERLPral 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457 159 -DAPFHIGMLHGSVEGDAEHNR--YAPFQIRELKEKQFDYWALGHIHKREILSEEPYIIYSGNIQGRHRKETGEKGAYLI 235
Cdd:COG0420  149 dPGGPNILLLHGFVAGASGSRDiyVAPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLV 228


                 ....*..
gi 446738457 236 ELTKQGT 242
Cdd:COG0420  229 ELDAGGL 235
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
4-242 8.55e-83

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 254.07  E-value: 8.55e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   4 VKFIHAADLHLDSPFKGmemnvpqsiwERMKQSTFESFERIIDKAIQERVDFVLLAGDLYDAETRSLRAQVFVREQMKRL 83
Cdd:COG0420    1 MRFLHTADWHLGKPLHG----------ASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457  84 SQYDIPVFIIHGNHDHLGGSWAAIEFPE--NVHVFTEPYVEEKSFYNNGEllASIYGFSYLQQAVTDNMTAQFTKMS--- 158
Cdd:COG0420   71 SEAGIPVVLIAGNHDSPSRLSAGSPLLEnlGVHVFGSVEPEPVELEDGLG--VAVYGLPYLRPSDEEALRDLLERLPral 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457 159 -DAPFHIGMLHGSVEGDAEHNR--YAPFQIRELKEKQFDYWALGHIHKREILSEEPYIIYSGNIQGRHRKETGEKGAYLI 235
Cdd:COG0420  149 dPGGPNILLLHGFVAGASGSRDiyVAPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLV 228


                 ....*..
gi 446738457 236 ELTKQGT 242
Cdd:COG0420  229 ELDAGGL 235
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 5-223 1.41e-59

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: 192.10  E-value: 1.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   5 KFIHAADLHLDSPFKGmemnvpqsiWERMKQSTFESFERIIDKAIQERVDFVLLAGDLYDAETRSLRAQVFVREQMKRLS 84
Cdd:cd00840    1 RFLHTADWHLGYPLYG---------LSRREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLC 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457  85 QYDIPVFIIHGNHDHLGGswaaiefpenvhvftepyveeksfynngellASIYGFSYLQQAVTDNMT----AQFTKMSDA 160
Cdd:cd00840   72 EAGIPVFVIAGNHDSPAR-------------------------------VAIYGLPYLRDERLERLFedleLRPRLLKPD 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446738457 161 PFHIGMLHGSVEGDAEHNRYAPFQIRELKEKQFDYWALGHIHKR-EILSEEPYIIYSGNIQGRH 223
Cdd:cd00840  121 WFNILLLHQGVDGAGPSDSERPIVPEDLLPDGFDYVALGHIHKPqIIEGGGPPIVYPGSPEPTS 184
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 5-138 1.19e-09

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: 55.68  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457    5 KFIHAADLHLDSPFkgmemnvpqsiwermkqstfESFERIIDKAIQE-RVDFVLLAGDLYDAETRSLRAQVFVREQMKRl 83
Cdd:pfam00149   2 RILVIGDLHLPGQL--------------------DDLLELLKKLLEEgKPDLVLHAGDLVDRGPPSEEVLELLERLIKY- 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446738457   84 sqydIPVFIIHGNHDHLGGSWaaIEFPENVHVFTEPYVEEKSFYNNGELLASIYG 138
Cdd:pfam00149  61 ----VPVYLVRGNHDFDYGEC--LRLYPYLGLLARPWKRFLEVFNFLPLAGILSG 109
mre11 TIGR00583
DNA repair protein (mre11); All proteins in this family for which functions are known are ...
 34-102 6.31e-05

DNA repair protein (mre11); All proteins in this family for which functions are known are subunits of a nuclease complex made up of multiple proteins including MRE11 and RAD50 homologs. The functions of this nuclease complex include recombinational repair and non-homolgous end joining. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). The proteins in this family are distantly related to proteins in the SbcCD complex of bacteria. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273153 [Multi-domain]  Cd Length: 405  Bit Score: 44.83  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   34 KQSTFESFERIIDKAIQERVDFVLLAGDLYDAE----------TRSLR-----------------AQVFVREQMKRLSQY 86
Cdd:TIGR00583  24 GDDSWNTFEEVLQIAKEQDVDMILLGGDLFHENkpsrkslyqvLRSLRlyclgdkpceleflsdaSVVFNQSAFGNVNYE 103

                          90       100
                  ....*....|....*....|..
gi 446738457   87 D------IPVFIIHGNHDHLGG 102
Cdd:TIGR00583 104 DpninvaIPVFSIHGNHDDPSG 125
PRK05340 PRK05340
UDP-2,3-diacylglucosamine hydrolase; Provisional
 6-103 8.72e-03

UDP-2,3-diacylglucosamine hydrolase; Provisional


Pssm-ID: 235420  Cd Length: 241  Bit Score: 37.48  E-value: 8.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   6 FIhaADLHLdSPfkgmemnvpqsiwERmkQSTFESFERIID-KAIQERVDFVLlaGDLYDA-----ETRSLRAQVfvREQ 79
Cdd:PRK05340   5 FI--SDLHL-SP-------------ER--PAITAAFLRFLRgEARQADALYIL--GDLFEAwigddDPSPFAREI--AAA 62

                         90       100
                 ....*....|....*....|....
gi 446738457  80 MKRLSQYDIPVFIIHGNHDHLGGS 103
Cdd:PRK05340  63 LKALSDSGVPCYFMHGNRDFLLGK 86
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
4-242 8.55e-83

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 254.07  E-value: 8.55e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   4 VKFIHAADLHLDSPFKGmemnvpqsiwERMKQSTFESFERIIDKAIQERVDFVLLAGDLYDAETRSLRAQVFVREQMKRL 83
Cdd:COG0420    1 MRFLHTADWHLGKPLHG----------ASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457  84 SQYDIPVFIIHGNHDHLGGSWAAIEFPE--NVHVFTEPYVEEKSFYNNGEllASIYGFSYLQQAVTDNMTAQFTKMS--- 158
Cdd:COG0420   71 SEAGIPVVLIAGNHDSPSRLSAGSPLLEnlGVHVFGSVEPEPVELEDGLG--VAVYGLPYLRPSDEEALRDLLERLPral 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457 159 -DAPFHIGMLHGSVEGDAEHNR--YAPFQIRELKEKQFDYWALGHIHKREILSEEPYIIYSGNIQGRHRKETGEKGAYLI 235
Cdd:COG0420  149 dPGGPNILLLHGFVAGASGSRDiyVAPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLV 228


                 ....*..
gi 446738457 236 ELTKQGT 242
Cdd:COG0420  229 ELDAGGL 235
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 5-223 1.41e-59

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: 192.10  E-value: 1.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   5 KFIHAADLHLDSPFKGmemnvpqsiWERMKQSTFESFERIIDKAIQERVDFVLLAGDLYDAETRSLRAQVFVREQMKRLS 84
Cdd:cd00840    1 RFLHTADWHLGYPLYG---------LSRREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLC 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457  85 QYDIPVFIIHGNHDHLGGswaaiefpenvhvftepyveeksfynngellASIYGFSYLQQAVTDNMT----AQFTKMSDA 160
Cdd:cd00840   72 EAGIPVFVIAGNHDSPAR-------------------------------VAIYGLPYLRDERLERLFedleLRPRLLKPD 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446738457 161 PFHIGMLHGSVEGDAEHNRYAPFQIRELKEKQFDYWALGHIHKR-EILSEEPYIIYSGNIQGRH 223
Cdd:cd00840  121 WFNILLLHQGVDGAGPSDSERPIVPEDLLPDGFDYVALGHIHKPqIIEGGGPPIVYPGSPEPTS 184
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
4-106 5.51e-11

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 62.02  E-value: 5.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   4 VKFIHAADLHLDSPfKGMEmnvpqsiwermkqsTFESFERIIDKAIQERVDFVLLAGDL-YDAETRSLRAqvfVREQMKR 82
Cdd:COG1409    1 FRFAHISDLHLGAP-DGSD--------------TAEVLAAALADINAPRPDFVVVTGDLtDDGEPEEYAA---AREILAR 62

                         90       100
                 ....*....|....*....|....
gi 446738457  83 LsqyDIPVFIIHGNHDHLGGSWAA 106
Cdd:COG1409   63 L---GVPVYVVPGNHDIRAAMAEA 83
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 5-138 1.19e-09

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: 55.68  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457    5 KFIHAADLHLDSPFkgmemnvpqsiwermkqstfESFERIIDKAIQE-RVDFVLLAGDLYDAETRSLRAQVFVREQMKRl 83
Cdd:pfam00149   2 RILVIGDLHLPGQL--------------------DDLLELLKKLLEEgKPDLVLHAGDLVDRGPPSEEVLELLERLIKY- 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446738457   84 sqydIPVFIIHGNHDHLGGSWaaIEFPENVHVFTEPYVEEKSFYNNGELLASIYG 138
Cdd:pfam00149  61 ----VPVYLVRGNHDFDYGEC--LRLYPYLGLLARPWKRFLEVFNFLPLAGILSG 109
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
5-115 1.06e-08

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 55.02  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   5 KFIHAADLHLDspfkgmemnvpqsiwermkqstFESFERIIDKAIQERVDFVLLAGDLYDAETRSlRAQVFVREqmkrLS 84
Cdd:COG2129    1 KILAVSDLHGN----------------------FDLLEKLLELARAEDADLVILAGDLTDFGTAE-EAREVLEE----LA 53

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446738457  85 QYDIPVFIIHGNHDHLgGSWAAIEfPENVHV 115
Cdd:COG2129   54 ALGVPVLAVPGNHDDP-EVLDALE-ESGVHN 82
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
4-202 1.36e-08

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 55.57  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   4 VKFIHAADLHLDSPFKGmemnvpqsiwermkqstfESFERIIDKAIQERVDFVLLAGDLYDAETRSLRAqvfVREQMKRL 83
Cdd:COG1408   43 LRIVQLSDLHLGPFIGG------------------ERLERLVEKINALKPDLVVLTGDLVDGSVAELEA---LLELLKKL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457  84 SQYDiPVFIIHGNHDHLGG--SWAA------IEFPENVHVftepyveekSFYNNGELLAsIYGFSYLQQAVTDNMTAQFT 155
Cdd:COG1408  102 KAPL-GVYAVLGNHDYYAGleELRAaleeagVRVLRNEAV---------TLERGGDRLN-LAGVDDPHAGRFPDLEKALA 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446738457 156 KMSDAPFHIGMLHgsvegdaehnryAPFQIRELKEKQFDyWAL-GHIH 202
Cdd:COG1408  171 GVPPDAPRILLAH------------NPDVFDEAAAAGVD-LQLsGHTH 205
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 6-111 7.63e-06

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: 46.89  E-value: 7.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   6 FIHAADLHLDSPfKGMEMNVpqsiwermkQSTFESFERIIDK--AIQERVDFVLLAGDLYD-AETRSLraQVFvREQMKR 82
Cdd:cd07402    1 IAQISDTHLFAP-GEGALLG---------VDTAARLAAAVAQvnALHPRPDLVVVTGDLSDdGSPESY--ERL-RELLAP 67

                         90       100
                 ....*....|....*....|....*....
gi 446738457  83 LsqyDIPVFIIHGNHDHLGGSWAAieFPE 111
Cdd:cd07402   68 L---PAPVYWIPGNHDDRAAMREA--LPE 91
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 35-129 1.08e-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: 44.57  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457  35 QSTFESFERIIDKAI--QERVDFVLLAGDLYDAETRSlraqVFVREQMKRLSQYDIPVFIIHGNHDHL---GGSWAAIEF 109
Cdd:cd00838    7 HGNLEALEAVLEAALakAEKPDLVICLGDLVDYGPDP----EEVELKALRLLLAGIPVYVVPGNHDILvthGPPYDPLDE 82

                         90       100
                 ....*....|....*....|
gi 446738457 110 PENVHVFTEPYVEEKSFYNN 129
Cdd:cd00838   83 GSPGEDPGSEALLELLDKYG 102
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 5-102 4.25e-05

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 44.58  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   5 KFIHAADLHLDspfkgmemnvpqsiwermKQSTFESFERIIDKAIQERVDFVLLAGDLYDAETRSLRAQVFVREQMKRls 84
Cdd:cd07385    3 RIVQLSDIHLG------------------PFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKA-- 62

                         90
                 ....*....|....*...
gi 446738457  85 qyDIPVFIIHGNHDHLGG 102
Cdd:cd07385   63 --PLGVYFVLGNHDYYSG 78
LpxH COG2908
UDP-2,3-diacylglucosamine pyrophosphatase LpxH [Cell wall/membrane/envelope biogenesis];
6-123 4.36e-05

UDP-2,3-diacylglucosamine pyrophosphatase LpxH [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442152 [Multi-domain]  Cd Length: 238  Bit Score: 44.40  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   6 FIhaADLHLDSPFkgmemnvPQSIWERmkqstFESF-ERIIDKAiqervDFVLLAGDLYDA--ETRSLRAQVFVR--EQM 80
Cdd:COG2908    5 FI--SDLHLGTPG-------PQAITAA-----LLDFlRSIAHDA-----DALYLLGDIFDFwiGDDDVWPPGHNRvlQKL 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446738457  81 KRLSQYDIPVFIIHGNHDHLGGSWAAIEFpeNVHVFTEPYVEE 123
Cdd:COG2908   66 LELADKGTPVYYIPGNHDFLLGDYFAKEL--GATLLPDPIHLT 106
mre11 TIGR00583
DNA repair protein (mre11); All proteins in this family for which functions are known are ...
 34-102 6.31e-05

DNA repair protein (mre11); All proteins in this family for which functions are known are subunits of a nuclease complex made up of multiple proteins including MRE11 and RAD50 homologs. The functions of this nuclease complex include recombinational repair and non-homolgous end joining. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). The proteins in this family are distantly related to proteins in the SbcCD complex of bacteria. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273153 [Multi-domain]  Cd Length: 405  Bit Score: 44.83  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   34 KQSTFESFERIIDKAIQERVDFVLLAGDLYDAE----------TRSLR-----------------AQVFVREQMKRLSQY 86
Cdd:TIGR00583  24 GDDSWNTFEEVLQIAKEQDVDMILLGGDLFHENkpsrkslyqvLRSLRlyclgdkpceleflsdaSVVFNQSAFGNVNYE 103

                          90       100
                  ....*....|....*....|..
gi 446738457   87 D------IPVFIIHGNHDHLGG 102
Cdd:TIGR00583 104 DpninvaIPVFSIHGNHDDPSG 125
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
39-206 7.87e-04

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 40.28  E-value: 7.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457  39 ESFERIIDKAIQERVDFVLLAGDL--YDAETRslraqvFVREQMKRLsqydiPVFIIHGNHDHLGGSWAAiEFPENVHVF 116
Cdd:COG0622   13 PALEAVLEDLEREGVDLIVHLGDLvgYGPDPP------EVLDLLREL-----PIVAVRGNHDGAVLRGLR-SLPETLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457 117 TEpyveeksfynngellasiygfsylqqavtdnmtaqftkmsdaPFHIGMLHGSVEGDAEHNRYAPFQIRELKEKQFDYW 196
Cdd:COG0622   81 LE------------------------------------------GVRILLVHGSPNEYLLPDTPAERLRALAAEGDADVV 118

                        170
                 ....*....|
gi 446738457 197 ALGHIHKREI 206
Cdd:COG0622  119 VCGHTHIPFV 128
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 42-98 1.88e-03

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: 39.20  E-value: 1.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446738457  42 ERIIDkaiQERVDFVLLAGDLYDAE-TRSLRAQVFVREQMKRLSQYDIPVFIIHGNHD 98
Cdd:cd07383   35 ESVLD---EEKPDLVVLTGDLITGEnTADDNATSYLDKAVSPLVERGIPWAATFGNHD 89
PRK05340 PRK05340
UDP-2,3-diacylglucosamine hydrolase; Provisional
 6-103 8.72e-03

UDP-2,3-diacylglucosamine hydrolase; Provisional


Pssm-ID: 235420  Cd Length: 241  Bit Score: 37.48  E-value: 8.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446738457   6 FIhaADLHLdSPfkgmemnvpqsiwERmkQSTFESFERIID-KAIQERVDFVLlaGDLYDA-----ETRSLRAQVfvREQ 79
Cdd:PRK05340   5 FI--SDLHL-SP-------------ER--PAITAAFLRFLRgEARQADALYIL--GDLFEAwigddDPSPFAREI--AAA 62

                         90       100
                 ....*....|....*....|....
gi 446738457  80 MKRLSQYDIPVFIIHGNHDHLGGS 103
Cdd:PRK05340  63 LKALSDSGVPCYFMHGNRDFLLGK 86
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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