NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1133829855|ref|WP_076208352|]
View 

metallophosphoesterase family protein [Mycolicibacterium fortuitum]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 3-186 1.52e-53

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.


The actual alignment was detected with superfamily member cd07390:

Pssm-ID: 472684  Cd Length: 170  Bit Score: 168.31  E-value: 1.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855   3 YFTADLHLAHPKLAS--LRGFETVAAHDAAVMAPLHQLDPSQDTLWVLGDICAGGVASKEsALAQLSTLQVPMHLVTGNH 80
Cdd:cd07390     2 YFTSDTHFGHPNVIRytNRPFDNVEEMNKVIINNWNNTVGPDDIVYHLGDFALGTNKANE-ALEILSLLNGHIHLIRGNH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855  81 DPVHPMYRgaqkhfadyAAVFESVQQVGRTKVSGEGVMLSHFPYAEVPDrfsrksfdqyqlPNLGMWLIHGHSHSDQRRS 160
Cdd:cd07390    81 DKSLLMYR---------PLFFESVQQYVRIEHGGRRFYLSHYPYRGPDS------------PDFDGWLIHGHVHSNSPDE 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1133829855 161 G-----KRSICVSLEAWDRRPASAEEIAAEM 186
Cdd:cd07390   140 GpfvydPRQINVGVEAWDYRPVSLEEIEDLI 170
 
Name Accession Description Interval E-value
MPP_AQ1575 cd07390
Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes ...
 3-186 1.52e-53

Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to AQ1575, an uncharacterized Aquifex aeolicus protein. AQ1575 may play an accessory role in DNA repair, based on the close proximity of its gene to Holliday junction resolvasome genes. 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: 277336  Cd Length: 170  Bit Score: 168.31  E-value: 1.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855   3 YFTADLHLAHPKLAS--LRGFETVAAHDAAVMAPLHQLDPSQDTLWVLGDICAGGVASKEsALAQLSTLQVPMHLVTGNH 80
Cdd:cd07390     2 YFTSDTHFGHPNVIRytNRPFDNVEEMNKVIINNWNNTVGPDDIVYHLGDFALGTNKANE-ALEILSLLNGHIHLIRGNH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855  81 DPVHPMYRgaqkhfadyAAVFESVQQVGRTKVSGEGVMLSHFPYAEVPDrfsrksfdqyqlPNLGMWLIHGHSHSDQRRS 160
Cdd:cd07390    81 DKSLLMYR---------PLFFESVQQYVRIEHGGRRFYLSHYPYRGPDS------------PDFDGWLIHGHVHSNSPDE 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1133829855 161 G-----KRSICVSLEAWDRRPASAEEIAAEM 186
Cdd:cd07390   140 GpfvydPRQINVGVEAWDYRPVSLEEIEDLI 170
COG4186 COG4186
Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily ...
 1-187 1.65e-44

Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily [General function prediction only];


Pssm-ID: 443340  Cd Length: 167  Bit Score: 145.03  E-value: 1.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855   1 MDYFTADLHLAHPKLASL--RGFETVAAHDAAVMAPLHQLDPSQDTLWVLGDICAGGVAskESALAQLSTLQVPMHLVTG 78
Cdd:COG4186     1 MIYFTSDTHFGHANIIKFcpRPFASVEEMDEALIANWNATVGPDDTVYHLGDFAFGGSA--EEAREILRRLNGRKHLIRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855  79 NHDPVHPMYRgaqkhfadyAAVFESVQQVGRTKVSGEGVMLSHFPYaevpdrfsrksfDQYQLPNLGMWLIHGHSH-SDQ 157
Cdd:COG4186    79 NHDGKLLLRL---------PAGFASVQDYAEIKLGGRRLLLCHYPL------------RTWNGADRGAWHLHGHVHgNRL 137

                         170       180       190
                  ....*....|....*....|....*....|
gi 1133829855 158 RRSGKRSICVSLEAWDRRPASAEEIAAEMQ 187
Cdd:COG4186   138 LKPTRRSINVGVDAWDYRPVSLEEILERLD 167
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
33-81 8.15e-04

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 38.99  E-value: 8.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1133829855  33 APLHQL------DPSQDTLWVLGDICAGGVASKEsALAQLSTLQVPMHLVTGNHD 81
Cdd:PRK00166   14 DELQRLlekidfDPAKDTLWLVGDLVNRGPDSLE-VLRFVKSLGDSAVTVLGNHD 67
 
Name Accession Description Interval E-value
MPP_AQ1575 cd07390
Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes ...
 3-186 1.52e-53

Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to AQ1575, an uncharacterized Aquifex aeolicus protein. AQ1575 may play an accessory role in DNA repair, based on the close proximity of its gene to Holliday junction resolvasome genes. 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: 277336  Cd Length: 170  Bit Score: 168.31  E-value: 1.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855   3 YFTADLHLAHPKLAS--LRGFETVAAHDAAVMAPLHQLDPSQDTLWVLGDICAGGVASKEsALAQLSTLQVPMHLVTGNH 80
Cdd:cd07390     2 YFTSDTHFGHPNVIRytNRPFDNVEEMNKVIINNWNNTVGPDDIVYHLGDFALGTNKANE-ALEILSLLNGHIHLIRGNH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855  81 DPVHPMYRgaqkhfadyAAVFESVQQVGRTKVSGEGVMLSHFPYAEVPDrfsrksfdqyqlPNLGMWLIHGHSHSDQRRS 160
Cdd:cd07390    81 DKSLLMYR---------PLFFESVQQYVRIEHGGRRFYLSHYPYRGPDS------------PDFDGWLIHGHVHSNSPDE 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1133829855 161 G-----KRSICVSLEAWDRRPASAEEIAAEM 186
Cdd:cd07390   140 GpfvydPRQINVGVEAWDYRPVSLEEIEDLI 170
COG4186 COG4186
Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily ...
 1-187 1.65e-44

Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily [General function prediction only];


Pssm-ID: 443340  Cd Length: 167  Bit Score: 145.03  E-value: 1.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855   1 MDYFTADLHLAHPKLASL--RGFETVAAHDAAVMAPLHQLDPSQDTLWVLGDICAGGVAskESALAQLSTLQVPMHLVTG 78
Cdd:COG4186     1 MIYFTSDTHFGHANIIKFcpRPFASVEEMDEALIANWNATVGPDDTVYHLGDFAFGGSA--EEAREILRRLNGRKHLIRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855  79 NHDPVHPMYRgaqkhfadyAAVFESVQQVGRTKVSGEGVMLSHFPYaevpdrfsrksfDQYQLPNLGMWLIHGHSH-SDQ 157
Cdd:COG4186    79 NHDGKLLLRL---------PAGFASVQDYAEIKLGGRRLLLCHYPL------------RTWNGADRGAWHLHGHVHgNRL 137

                         170       180       190
                  ....*....|....*....|....*....|
gi 1133829855 158 RRSGKRSICVSLEAWDRRPASAEEIAAEMQ 187
Cdd:COG4186   138 LKPTRRSINVGVDAWDYRPVSLEEILERLD 167
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
7-99 2.39e-06

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 46.22  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855   7 DLHLAHPklaslRGFETVAAHDAAVMApLHQLDPsqDTLWVLGDIC-AGGVASKESALAQLSTLQVPMHLVTGNHDPVHP 85
Cdd:COG1409     8 DLHLGAP-----DGSDTAEVLAAALAD-INAPRP--DFVVVTGDLTdDGEPEEYAAAREILARLGVPVYVVPGNHDIRAA 79

                          90
                  ....*....|....
gi 1133829855  86 MYRGAQKHFADYAA 99
Cdd:COG1409    80 MAEAYREYFGDLPP 93
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 7-96 3.30e-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: 45.73  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855   7 DLHLAHPKLASLRGFETVAAHDAAVmAPLHQLDPSQDTLWVLGDICAGG-VASKESALAQLSTLQVPMHLVTGNHDPVHP 85
Cdd:cd07402     6 DTHLFAPGEGALLGVDTAARLAAAV-AQVNALHPRPDLVVVTGDLSDDGsPESYERLRELLAPLPAPVYWIPGNHDDRAA 84

                          90
                  ....*....|.
gi 1133829855  86 MYRGAQKHFAD 96
Cdd:cd07402    85 MREALPEPPYD 95
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
43-154 2.47e-04

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 39.90  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855  43 DTLWVLGDICAGGVASKEsALAQLStlQVPMHLVTGNHDpvhpmyrgaqkhfADYAAVFESVQQVGRTKVSGEGVMLSH- 121
Cdd:COG0622    28 DLIVHLGDLVGYGPDPPE-VLDLLR--ELPIVAVRGNHD-------------GAVLRGLRSLPETLRLELEGVRILLVHg 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1133829855 122 FPYAEVPDRFSRKSFDQYQLPNLGMWLIHGHSH 154
Cdd:COG0622    92 SPNEYLLPDTPAERLRALAAEGDADVVVCGHTH 124
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
33-81 8.15e-04

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 38.99  E-value: 8.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1133829855  33 APLHQL------DPSQDTLWVLGDICAGGVASKEsALAQLSTLQVPMHLVTGNHD 81
Cdd:PRK00166   14 DELQRLlekidfDPAKDTLWLVGDLVNRGPDSLE-VLRFVKSLGDSAVTVLGNHD 67
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
4-82 1.35e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 38.07  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133829855   4 FTADLHLAHPKLASLRGFETVAAHDAAVMAplhqldpsqdtlwvlGDICAGG-VASKESALAQLSTLQVPMHLVTGNHDP 82
Cdd:COG2129     4 AVSDLHGNFDLLEKLLELARAEDADLVILA---------------GDLTDFGtAEEAREVLEELAALGVPVLAVPGNHDD 68
 
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