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Conserved domains on  [gi|2277053498|gb|KAI5559760|]
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hypothetical protein BDE02_17G135000 [Populus trichocarpa]

Protein Classification

metallophosphoesterase( domain architecture ID 11988119)

metallophosphoesterase contains an active site consisting of two metal ions (usually manganese, iron, or zinc)

CATH:  3.60.21.10
Gene Ontology:  GO:0046872|GO:0016787
PubMed:  25837850
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YaeI super family cl43414
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
52-174 1.23e-08

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


The actual alignment was detected with superfamily member COG1408:

Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 55.19  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  52 LPPPPLSRDALGFRVFVLSDLHTDYPENMNWVKSL--STKAYKNDLLLLAGDV----AETYHNFYSTMSLLKDRFqHVFY 125
Cdd:COG1408    31 VPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLveKINALKPDLVVLTGDLvdgsVAELEALLELLKKLKAPL-GVYA 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2277053498 126 VPGNHDLWcrsepEGHPYYLDSLDKLN-KLL-DACRGLGVQTRPMVLYGLG 174
Cdd:COG1408   110 VLGNHDYY-----AGLEELRAALEEAGvRVLrNEAVTLERGGDRLNLAGVD 155
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
52-174 1.23e-08

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 55.19  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  52 LPPPPLSRDALGFRVFVLSDLHTDYPENMNWVKSL--STKAYKNDLLLLAGDV----AETYHNFYSTMSLLKDRFqHVFY 125
Cdd:COG1408    31 VPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLveKINALKPDLVVLTGDLvdgsVAELEALLELLKKLKAPL-GVYA 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2277053498 126 VPGNHDLWcrsepEGHPYYLDSLDKLN-KLL-DACRGLGVQTRPMVLYGLG 174
Cdd:COG1408   110 VLGNHDYY-----AGLEELRAALEEAGvRVLrNEAVTLERGGDRLNLAGVD 155
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 64-156 1.56e-08

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 52.22  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  64 FRVFVLSDLHTD--YPENMNWVKSLStKAYKNDLLLLAGDVAETYHNFYSTMSLLKD--RFQHVFYVPGNHDLWCRSEPE 139
Cdd:pfam00149   1 MRILVIGDLHLPgqLDDLLELLKKLL-EEGKPDLVLHAGDLVDRGPPSEEVLELLERliKYVPVYLVRGNHDFDYGECLR 79

                          90
                  ....*....|....*..
gi 2277053498 140 GHPYYLDSLDKLNKLLD 156
Cdd:pfam00149  80 LYPYLGLLARPWKRFLE 96
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 68-134 1.20e-06

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 46.88  E-value: 1.20e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  68 VLSDLHTDYPENMNWVKSLSTKAYKNDLLLLAGDVAE--TYHNFYS-TMSLLKDRFQHVFYVPGNHDLWC 134
Cdd:cd00838     2 VISDIHGNLEALEAVLEAALAKAEKPDLVICLGDLVDygPDPEEVElKALRLLLAGIPVYVVPGNHDILV 71
acc_ester TIGR03729
putative phosphoesterase; Members of this protein family belong to the larger family pfam00149 ...
 65-133 4.76e-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: 38.06  E-value: 4.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2277053498  65 RVFVLSDLHTDY----PENMnwVKSLST--KAYKNDLLLLAGDVAETYH---NFYSTMSLLKDrfQHVFYVPGNHDLW 133
Cdd:TIGR03729   1 KIAFSSDLHIDLnhfdTEEM--LETLAQylKKQKIDHLHIAGDISNDFQrslPFIEKLQELKG--IKVTFNAGNHDML 74
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
52-174 1.23e-08

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 55.19  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  52 LPPPPLSRDALGFRVFVLSDLHTDYPENMNWVKSL--STKAYKNDLLLLAGDV----AETYHNFYSTMSLLKDRFqHVFY 125
Cdd:COG1408    31 VPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLveKINALKPDLVVLTGDLvdgsVAELEALLELLKKLKAPL-GVYA 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2277053498 126 VPGNHDLWcrsepEGHPYYLDSLDKLN-KLL-DACRGLGVQTRPMVLYGLG 174
Cdd:COG1408   110 VLGNHDYY-----AGLEELRAALEEAGvRVLrNEAVTLERGGDRLNLAGVD 155
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 64-156 1.56e-08

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 52.22  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  64 FRVFVLSDLHTD--YPENMNWVKSLStKAYKNDLLLLAGDVAETYHNFYSTMSLLKD--RFQHVFYVPGNHDLWCRSEPE 139
Cdd:pfam00149   1 MRILVIGDLHLPgqLDDLLELLKKLL-EEGKPDLVLHAGDLVDRGPPSEEVLELLERliKYVPVYLVRGNHDFDYGECLR 79

                          90
                  ....*....|....*..
gi 2277053498 140 GHPYYLDSLDKLNKLLD 156
Cdd:pfam00149  80 LYPYLGLLARPWKRFLE 96
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
64-133 5.53e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 52.77  E-value: 5.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  64 FRVFVLSDLHTDYPENMNWVKSLST-----KAYKNDLLLLAGDVAET-----YHNFYSTMSLLKDRfqhVFYVPGNHDLW 133
Cdd:COG1409     1 FRFAHISDLHLGAPDGSDTAEVLAAaladiNAPRPDFVVVTGDLTDDgepeeYAAAREILARLGVP---VYVVPGNHDIR 77
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
65-176 8.42e-07

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 48.86  E-value: 8.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  65 RVFVLSDLHTDYPenmNWVKSLST-KAYKNDLLLLAGDVAE--TYHNFYSTMSLLKDRFQHVFYVPGNHDlwcrsepegH 141
Cdd:COG2129     1 KILAVSDLHGNFD---LLEKLLELaRAEDADLVILAGDLTDfgTAEEAREVLEELAALGVPVLAVPGNHD---------D 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2277053498 142 PYYLDSLDKLN-KLLDAcrglgvqtRPMVLYGLGIV 176
Cdd:COG2129    69 PEVLDALEESGvHNLHG--------RVVEIGGLRIA 96
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 68-134 1.20e-06

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 46.88  E-value: 1.20e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  68 VLSDLHTDYPENMNWVKSLSTKAYKNDLLLLAGDVAE--TYHNFYS-TMSLLKDRFQHVFYVPGNHDLWC 134
Cdd:cd00838     2 VISDIHGNLEALEAVLEAALAKAEKPDLVICLGDLVDygPDPEEVElKALRLLLAGIPVYVVPGNHDILV 71
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 68-140 1.65e-06

Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized Microscilla protein with a metallophosphatase domain. Microscilla proteins MS152, and MS153 are also included in this family. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277349 [Multi-domain]  Cd Length: 201  Bit Score: 48.10  E-value: 1.65e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2277053498  68 VLSDLHTDYPENMNWVKSLStKAYKNDLLLLAGDVAET--YHNFYSTMSLLKDRFQHVFYVPGNHDLWCRSEPEG 140
Cdd:cd07404     3 IASDLHLEVEQNLAKLKFFP-KVPDADILILAGDIGRLtdAEAWDNFLDLQSFQFEPVYYVPGNHEFYGGSLDIT 76
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
64-131 1.58e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 45.67  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  64 FRVFVLSDLHTDYPENMNWVKSLSTKAYKN----------DLLLLAGDV-------AETYHNFYSTMSLLKDRFQHVFYV 126
Cdd:COG0420     1 MRFLHTADWHLGKPLHGASRREDQLAALDRlvdlaieekvDAVLIAGDLfdsanpsPEAVRLLAEALRRLSEAGIPVVLI 80


                  ....*
gi 2277053498 127 PGNHD 131
Cdd:COG0420    81 AGNHD 85
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 63-133 3.42e-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: 44.19  E-value: 3.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2277053498  63 GFRVFVLSDLH---TDYPENMN-WVKSlsTKAYKNDLLLLAGDVAET----YHNFYSTMSLLKDRFQhVFYVPGNHDLW 133
Cdd:cd07385     1 GLRIVQLSDIHlgpFVGRTRLQkVVRK--VNELNPDLIVITGDLVDGdvsvLRLLASPLSKLKAPLG-VYFVLGNHDYY 76
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 65-131 8.36e-05

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: 42.64  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277053498  65 RVFVLSDLHTDYPEN------------MNWVKSLSTKAyKNDLLLLAGDV-------AETYHNFYSTMSLLKDRFQHVFY 125
Cdd:cd00840     1 RFLHTADWHLGYPLYglsrreedffkaFEEIVDLAIEE-KVDFVLIAGDLfdsnnpsPEALKLAIEGLRRLCEAGIPVFV 79


                  ....*.
gi 2277053498 126 VPGNHD 131
Cdd:cd00840    80 IAGNHD 85
acc_ester TIGR03729
putative phosphoesterase; Members of this protein family belong to the larger family pfam00149 ...
 65-133 4.76e-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: 38.06  E-value: 4.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2277053498  65 RVFVLSDLHTDY----PENMnwVKSLST--KAYKNDLLLLAGDVAETYH---NFYSTMSLLKDrfQHVFYVPGNHDLW 133
Cdd:TIGR03729   1 KIAFSSDLHIDLnhfdTEEM--LETLAQylKKQKIDHLHIAGDISNDFQrslPFIEKLQELKG--IKVTFNAGNHDML 74
 
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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