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Conserved domains on  [gi|517994775|ref|WP_019164983|]
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DNA repair exonuclease [Staphylococcus delphini]

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];
2-249 4.74e-69

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


:

Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 217.86  E-value: 4.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   2 VKFLHCADLHLDSPFaskrylnptILKDVENSAYESFKNIIDLALREEVDFVIISGDLFDQHNRTLKAEVFLKSQFERLQ 81
Cdd:COG0420    1 MRFLHTADWHLGKPL---------HGASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775  82 KEQIFVYIVHGNHDPLS-DEIKTKWPE--NVTVFSNQVETYQAItKTGETVHLHGFSYEKR---ESYENKIDAYPTNENR 155
Cdd:COG0420   72 EAGIPVVLIAGNHDSPSrLSAGSPLLEnlGVHVFGSVEPEPVEL-EDGLGVAVYGLPYLRPsdeEALRDLLERLPRALDP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775 156 NVVHIGVLHGTYSKSEAS-DRYT-EFRLEDLNAKLYHYWALGHIHLRQQLSDLPEIHYPGNIQGRHFKEQGEKGCLIVE- 232
Cdd:COG0420  151 GGPNILLLHGFVAGASGSrDIYVaPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVEl 230

                        250
                 ....*....|....*..
gi 517994775 233 GDHVALKTRFVPTQFIR 249
Cdd:COG0420  231 DAGGLVSVEFVPLPATR 247
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-249 4.74e-69

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 217.86  E-value: 4.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   2 VKFLHCADLHLDSPFaskrylnptILKDVENSAYESFKNIIDLALREEVDFVIISGDLFDQHNRTLKAEVFLKSQFERLQ 81
Cdd:COG0420    1 MRFLHTADWHLGKPL---------HGASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775  82 KEQIFVYIVHGNHDPLS-DEIKTKWPE--NVTVFSNQVETYQAItKTGETVHLHGFSYEKR---ESYENKIDAYPTNENR 155
Cdd:COG0420   72 EAGIPVVLIAGNHDSPSrLSAGSPLLEnlGVHVFGSVEPEPVEL-EDGLGVAVYGLPYLRPsdeEALRDLLERLPRALDP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775 156 NVVHIGVLHGTYSKSEAS-DRYT-EFRLEDLNAKLYHYWALGHIHLRQQLSDLPEIHYPGNIQGRHFKEQGEKGCLIVE- 232
Cdd:COG0420  151 GGPNILLLHGFVAGASGSrDIYVaPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVEl 230

                        250
                 ....*....|....*..
gi 517994775 233 GDHVALKTRFVPTQFIR 249
Cdd:COG0420  231 DAGGLVSVEFVPLPATR 247
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 3-220 1.13e-52

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: 173.61  E-value: 1.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   3 KFLHCADLHLDSPFASkrylnptiLKDVENSAYESFKNIIDLALREEVDFVIISGDLFDQHNRTLKAEVFLKSQFERLQK 82
Cdd:cd00840    1 RFLHTADWHLGYPLYG--------LSRREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775  83 EQIFVYIVHGNHDPLSdeiktkwpenvtvfsnqvetyqaitktgeTVHLHGFSYEKRESYENKID---AYPTNENRNVVH 159
Cdd:cd00840   73 AGIPVFVIAGNHDSPA-----------------------------RVAIYGLPYLRDERLERLFEdleLRPRLLKPDWFN 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517994775 160 IGVLHGTYSKSEASDRYTEFRLEDLNAKLYHYWALGHIHLRQQL-SDLPEIHYPGNIQGRHF 220
Cdd:cd00840  124 ILLLHQGVDGAGPSDSERPIVPEDLLPDGFDYVALGHIHKPQIIeGGGPPIVYPGSPEPTSF 185
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 3-107 2.45e-07

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 48.75  E-value: 2.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775    3 KFLHCADLHLDSPFaskrylnptilkdvensayESFKNIIDLALREE-VDFVIISGDLFDQHNRTLKAEVFLKSQFERLQ 81
Cdd:pfam00149   2 RILVIGDLHLPGQL-------------------DDLLELLKKLLEEGkPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP 62

                          90       100
                  ....*....|....*....|....*.
gi 517994775   82 keqifVYIVHGNHDPLSDEIKTKWPE 107
Cdd:pfam00149  63 -----VYLVRGNHDFDYGECLRLYPY 83
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
2-249 4.74e-69

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 217.86  E-value: 4.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   2 VKFLHCADLHLDSPFaskrylnptILKDVENSAYESFKNIIDLALREEVDFVIISGDLFDQHNRTLKAEVFLKSQFERLQ 81
Cdd:COG0420    1 MRFLHTADWHLGKPL---------HGASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775  82 KEQIFVYIVHGNHDPLS-DEIKTKWPE--NVTVFSNQVETYQAItKTGETVHLHGFSYEKR---ESYENKIDAYPTNENR 155
Cdd:COG0420   72 EAGIPVVLIAGNHDSPSrLSAGSPLLEnlGVHVFGSVEPEPVEL-EDGLGVAVYGLPYLRPsdeEALRDLLERLPRALDP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775 156 NVVHIGVLHGTYSKSEAS-DRYT-EFRLEDLNAKLYHYWALGHIHLRQQLSDLPEIHYPGNIQGRHFKEQGEKGCLIVE- 232
Cdd:COG0420  151 GGPNILLLHGFVAGASGSrDIYVaPVPLSALPAAGFDYVALGHIHRPQVLGGDPRIRYSGSPEPRSFSEAGGKGVLLVEl 230

                        250
                 ....*....|....*..
gi 517994775 233 GDHVALKTRFVPTQFIR 249
Cdd:COG0420  231 DAGGLVSVEFVPLPATR 247
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 3-220 1.13e-52

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: 173.61  E-value: 1.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   3 KFLHCADLHLDSPFASkrylnptiLKDVENSAYESFKNIIDLALREEVDFVIISGDLFDQHNRTLKAEVFLKSQFERLQK 82
Cdd:cd00840    1 RFLHTADWHLGYPLYG--------LSRREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775  83 EQIFVYIVHGNHDPLSdeiktkwpenvtvfsnqvetyqaitktgeTVHLHGFSYEKRESYENKID---AYPTNENRNVVH 159
Cdd:cd00840   73 AGIPVFVIAGNHDSPA-----------------------------RVAIYGLPYLRDERLERLFEdleLRPRLLKPDWFN 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517994775 160 IGVLHGTYSKSEASDRYTEFRLEDLNAKLYHYWALGHIHLRQQL-SDLPEIHYPGNIQGRHF 220
Cdd:cd00840  124 ILLLHQGVDGAGPSDSERPIVPEDLLPDGFDYVALGHIHKPQIIeGGGPPIVYPGSPEPTSF 185
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
2-95 1.24e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 52.00  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   2 VKFLHCADLHLDSPFASKrylnptilkdvensAYESFKNIIDLALREEVDFVIISGDLFDQHnrtlkaevfLKSQFERLQ 81
Cdd:COG1409    1 FRFAHISDLHLGAPDGSD--------------TAEVLAAALADINAPRPDFVVVTGDLTDDG---------EPEEYAAAR 57

                         90
                 ....*....|....*...
gi 517994775  82 KE----QIFVYIVHGNHD 95
Cdd:COG1409   58 EIlarlGVPVYVVPGNHD 75
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 3-107 2.45e-07

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 48.75  E-value: 2.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775    3 KFLHCADLHLDSPFaskrylnptilkdvensayESFKNIIDLALREE-VDFVIISGDLFDQHNRTLKAEVFLKSQFERLQ 81
Cdd:pfam00149   2 RILVIGDLHLPGQL-------------------DDLLELLKKLLEEGkPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP 62

                          90       100
                  ....*....|....*....|....*.
gi 517994775   82 keqifVYIVHGNHDPLSDEIKTKWPE 107
Cdd:pfam00149  63 -----VYLVRGNHDFDYGECLRLYPY 83
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
3-96 4.98e-06

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 46.93  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   3 KFLHCADLHLDspfaskrylnptilkdvensaYESFKNIIDLALREEVDFVIISGDLFDqHNRTLKAEVFLksqfERLQK 82
Cdd:COG2129    1 KILAVSDLHGN---------------------FDLLEKLLELARAEDADLVILAGDLTD-FGTAEEAREVL----EELAA 54

                         90
                 ....*....|....
gi 517994775  83 EQIFVYIVHGNHDP 96
Cdd:COG2129   55 LGVPVLAVPGNHDD 68
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 5-133 6.75e-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: 6.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   5 LHCADLHLdspfaskrylnptilkdveNSAYESFKNIIDLALREEVDFVIISGDLFDqHNRTLKAEVFlksQFERLQKEQ 84
Cdd:cd00838    1 LVISDIHG-------------------NLEALEAVLEAALAKAEKPDLVICLGDLVD-YGPDPEEVEL---KALRLLLAG 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517994775  85 IFVYIVHGNHD-------PLSDEIKTKWPENVtvfsNQVETYQAITKTGETVHLHG 133
Cdd:cd00838   58 IPVYVVPGNHDilvthgpPYDPLDEGSPGEDP----GSEALLELLDKYGPDLVLSG 109
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 4-95 1.22e-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: 43.04  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   4 FLHCADLHLDSPFASKRYLNPTilkdvensaYESFKNIID--LALREEVDFVIISGDLFDQHnrTLKAEVFLKSQFERLQ 81
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGVDT---------AARLAAAVAqvNALHPRPDLVVVTGDLSDDG--SPESYERLRELLAPLP 69

                         90
                 ....*....|....
gi 517994775  82 KEqifVYIVHGNHD 95
Cdd:cd07402   70 AP---VYWIPGNHD 80
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 8-110 4.24e-04

Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277337  Cd Length: 175  Bit Score: 40.76  E-value: 4.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   8 ADLHL--DSPFASKRYLNPTILKDvensayESFKNIIDLALREEVDFVIISGDLFdqHNRT-LKAEVFLKSQFERLQKEQ 84
Cdd:cd07391    4 ADLHLgyEEELRRQGINLPRRQKE------RLLERLDRLLEELGPDRLVILGDLK--HSFGrVSRQERREVPFFRLLAKD 75

                         90       100
                 ....*....|....*....|....*.
gi 517994775  85 IFVYIVHGNHDPLSDEIKTKWPENVT 110
Cdd:cd07391   76 VDVILIRGNHDGGLEEILSDVNVVVV 101
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 3-95 5.86e-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: 41.11  E-value: 5.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   3 KFLHCADLHLdSPFASKRYLnptilkdvensayesfKNIIDLALREEVDFVIISGDLFDQHNRTLKAEV----FLKSQFE 78
Cdd:cd07385    3 RIVQLSDIHL-GPFVGRTRL----------------QKVVRKVNELNPDLIVITGDLVDGDVSVLRLLAsplsKLKAPLG 65

                         90
                 ....*....|....*..
gi 517994775  79 rlqkeqifVYIVHGNHD 95
Cdd:cd07385   66 --------VYFVLGNHD 74
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 5-95 4.74e-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: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517994775   5 LHCADLHLDSPFASKRYlnptilkdvensayesFKNIIDLALREEVDFVIISGDLFdqhNRTLKAEVFLKSQF-ERLQKE 83
Cdd:cd07400    2 AHISDLHFGEERKPEVL----------------ELNLLDEINALKPDLVVVTGDLT---QRARPAEFEEAREFlDALEPE 62

                         90
                 ....*....|..
gi 517994775  84 QifVYIVHGNHD 95
Cdd:cd07400   63 P--VVVVPGNHD 72
 
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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