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Conserved domains on  [gi|1972289863|ref|NP_001379681|]
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Calcineurin-like phosphoesterase domain-containing protein [Caenorhabditis elegans]

Protein Classification

metallophosphatase domain-containing protein( domain architecture ID 12955154)

metallophosphatase domain-containing protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0042578|GO:0046872|GO:0016311
PubMed:  8003970|25837850

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 49-248 3.12e-49

Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein 239) is thought to play a role in central nervous system development, but its specific role in unknown. 239FB is expressed predominantly in human fetal brain from a gene located in the chromosome 11p13 region associated with the mental retardation component of the WAGR (Wilms tumor, Aniridia, Genitourinary anomalies, Mental retardation) syndrome. Orthologous brp-like (brain protein 239-like) proteins have been identified in the invertebrate amphioxus group and in vertebrates. 239FB 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: 277325 [Multi-domain]  Cd Length: 135  Bit Score: 158.95  E-value: 3.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  49 KVVCISDTHEQLHNVTVPDGDVLIHAGDFTNNGKREELIKFNEEMTRFPHKYKLVVAGNHELGFDhdenqgerqdadkgl 128
Cdd:cd07379     1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 129 gtedgyniltnvtylqdkgvtidgvtffgssyhplrgfpfyrnraeqlaecwkavPNDTNVLITHTPPLGYLDQ-FGDER 207
Cdd:cd07379    66 -------------------------------------------------------PEGTDILVTHGPPYGHLDLgSSGQR 90

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1972289863 208 WGCRDLLKTVERIQPAYHIFGHVHEQHGVLS----NGNTTFINAA 248
Cdd:cd07379    91 LGCEELLNTVQRVRPKLHVFGHIHEGYGIERvpdtDGETTFVNAS 135
SbcD super family cl33866
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
69-194 1.03e-03

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


The actual alignment was detected with superfamily member COG0420:

Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 39.51  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  69 DVLIHAGDFTNNGKR--EELIKFNEEMTRFpHKYK---LVVAGNHElgfdhdenQGERQDADKGLGTEDGYNILTNVtyl 143
Cdd:COG0420    41 DAVLIAGDLFDSANPspEAVRLLAEALRRL-SEAGipvVLIAGNHD--------SPSRLSAGSPLLENLGVHVFGSV--- 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972289863 144 QDKGVTID---GVTFFGSSYHPLRGFPFYRNRAEQLAEcwKAVPNDTNVLITHT 194
Cdd:COG0420   109 EPEPVELEdglGVAVYGLPYLRPSDEEALRDLLERLPR--ALDPGGPNILLLHG 160
 
Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 49-248 3.12e-49

Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein 239) is thought to play a role in central nervous system development, but its specific role in unknown. 239FB is expressed predominantly in human fetal brain from a gene located in the chromosome 11p13 region associated with the mental retardation component of the WAGR (Wilms tumor, Aniridia, Genitourinary anomalies, Mental retardation) syndrome. Orthologous brp-like (brain protein 239-like) proteins have been identified in the invertebrate amphioxus group and in vertebrates. 239FB 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: 277325 [Multi-domain]  Cd Length: 135  Bit Score: 158.95  E-value: 3.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  49 KVVCISDTHEQLHNVTVPDGDVLIHAGDFTNNGKREELIKFNEEMTRFPHKYKLVVAGNHELGFDhdenqgerqdadkgl 128
Cdd:cd07379     1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 129 gtedgyniltnvtylqdkgvtidgvtffgssyhplrgfpfyrnraeqlaecwkavPNDTNVLITHTPPLGYLDQ-FGDER 207
Cdd:cd07379    66 -------------------------------------------------------PEGTDILVTHGPPYGHLDLgSSGQR 90

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1972289863 208 WGCRDLLKTVERIQPAYHIFGHVHEQHGVLS----NGNTTFINAA 248
Cdd:cd07379    91 LGCEELLNTVQRVRPKLHVFGHIHEGYGIERvpdtDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
49-254 6.96e-42

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 142.85  E-value: 6.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  49 KVVCISDTHEQLHNVT-------VPDGDVLIHAGDFTNNGKREELIKFNEEMTRFPhKYKLVVAGNHelgfDHDENQGER 121
Cdd:COG2129     1 KILAVSDLHGNFDLLEkllelarAEDADLVILAGDLTDFGTAEEAREVLEELAALG-VPVLAVPGNH----DDPEVLDAL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 122 QDAdkglgtedgyniltNVTYLQDKGVTIDGVTFFGSSYHPLRGF--PFYRNRAEQLAECWKAVPNDTNVLITHTPPLGY 199
Cdd:COG2129    76 EES--------------GVHNLHGRVVEIGGLRIAGLGGSRPTPFgtPYEYTEEEIEERLAKLREKDVDILLTHAPPYGT 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972289863 200 -LDQFGDERW-GCRDLLKTVERIQPAYHIFGHVHEQHGVLSNGNTTFINAAQCNKGN 254
Cdd:COG2129   142 tLDRVEDGPHvGSKALRELIEEFQPKLVLHGHIHESRGVDKIGGTRVVNPGSLAEGY 198
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 48-117 4.43e-06

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: 44.90  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  48 LKVVCISDTH--------EQLHNVTVPDG--DVLIHAGDFTNNGKR-EELIKFNEEMTRFPHKYklVVAGNHELGFDHDE 116
Cdd:pfam00149   1 MRILVIGDLHlpgqlddlLELLKKLLEEGkpDLVLHAGDLVDRGPPsEEVLELLERLIKYVPVY--LVRGNHDFDYGECL 78


                  .
gi 1972289863 117 N 117
Cdd:pfam00149  79 R 79
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
69-194 1.03e-03

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 39.51  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  69 DVLIHAGDFTNNGKR--EELIKFNEEMTRFpHKYK---LVVAGNHElgfdhdenQGERQDADKGLGTEDGYNILTNVtyl 143
Cdd:COG0420    41 DAVLIAGDLFDSANPspEAVRLLAEALRRL-SEAGipvVLIAGNHD--------SPSRLSAGSPLLENLGVHVFGSV--- 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972289863 144 QDKGVTID---GVTFFGSSYHPLRGFPFYRNRAEQLAEcwKAVPNDTNVLITHT 194
Cdd:COG0420   109 EPEPVELEdglGVAVYGLPYLRPSDEEALRDLLERLPR--ALDPGGPNILLLHG 160
acc_ester TIGR03729
putative phosphoesterase; Members of this protein family belong to the larger family pfam00149 ...
 69-248 2.84e-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: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  69 DVLIHAGDFTNNGKR-----EELIKFNEEMTRFphkyklvVAGNHELGFDHDENQGERQDadkglgtEDGYNILTNVTYL 143
Cdd:TIGR03729  34 DHLHIAGDISNDFQRslpfiEKLQELKGIKVTF-------NAGNHDMLKDLTYEEIESND-------SPLYLHNRFIDIP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 144 QDKGVTIDGVTFFGSSYHPLR--------GFPFYRNR---------------AEQLAECWKAVPNDTNVLITH-TPPLGY 199
Cdd:TIGR03729 100 NTQWRIIGNNGWYDYSFSNDKtskeilrwKKSFWFDRrikrpmsdpertaivLKQLKKQLNQLDNKQVIFVTHfVPHRDF 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972289863 200 LDQFGD-ERW-------GCRDLLKTVERIQPAYHIFGHVHEQHGVLSNGNTTFINAA 248
Cdd:TIGR03729 180 IYVPMDhRRFdmfnaflGSQHFGQLLVKYEIKDVIFGHLHRRFGPLTIGGTTYHNRP 236
 
Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 49-248 3.12e-49

Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein 239) is thought to play a role in central nervous system development, but its specific role in unknown. 239FB is expressed predominantly in human fetal brain from a gene located in the chromosome 11p13 region associated with the mental retardation component of the WAGR (Wilms tumor, Aniridia, Genitourinary anomalies, Mental retardation) syndrome. Orthologous brp-like (brain protein 239-like) proteins have been identified in the invertebrate amphioxus group and in vertebrates. 239FB 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: 277325 [Multi-domain]  Cd Length: 135  Bit Score: 158.95  E-value: 3.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  49 KVVCISDTHEQLHNVTVPDGDVLIHAGDFTNNGKREELIKFNEEMTRFPHKYKLVVAGNHELGFDhdenqgerqdadkgl 128
Cdd:cd07379     1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 129 gtedgyniltnvtylqdkgvtidgvtffgssyhplrgfpfyrnraeqlaecwkavPNDTNVLITHTPPLGYLDQ-FGDER 207
Cdd:cd07379    66 -------------------------------------------------------PEGTDILVTHGPPYGHLDLgSSGQR 90

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1972289863 208 WGCRDLLKTVERIQPAYHIFGHVHEQHGVLS----NGNTTFINAA 248
Cdd:cd07379    91 LGCEELLNTVQRVRPKLHVFGHIHEGYGIERvpdtDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
49-254 6.96e-42

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 142.85  E-value: 6.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  49 KVVCISDTHEQLHNVT-------VPDGDVLIHAGDFTNNGKREELIKFNEEMTRFPhKYKLVVAGNHelgfDHDENQGER 121
Cdd:COG2129     1 KILAVSDLHGNFDLLEkllelarAEDADLVILAGDLTDFGTAEEAREVLEELAALG-VPVLAVPGNH----DDPEVLDAL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 122 QDAdkglgtedgyniltNVTYLQDKGVTIDGVTFFGSSYHPLRGF--PFYRNRAEQLAECWKAVPNDTNVLITHTPPLGY 199
Cdd:COG2129    76 EES--------------GVHNLHGRVVEIGGLRIAGLGGSRPTPFgtPYEYTEEEIEERLAKLREKDVDILLTHAPPYGT 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972289863 200 -LDQFGDERW-GCRDLLKTVERIQPAYHIFGHVHEQHGVLSNGNTTFINAAQCNKGN 254
Cdd:COG2129   142 tLDRVEDGPHvGSKALRELIEEFQPKLVLHGHIHESRGVDKIGGTRVVNPGSLAEGY 198
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
48-248 2.73e-12

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 64.71  E-value: 2.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  48 LKVVCISDTH----------EQLHNVT----VPDGDVLIHAGDFTNNGKREELIKFNEEMTRFPHKYkLVVAGNHELGFD 113
Cdd:COG1409     1 FRFAHISDLHlgapdgsdtaEVLAAALadinAPRPDFVVVTGDLTDDGEPEEYAAAREILARLGVPV-YVVPGNHDIRAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 114 HDENQGERqdadkgLGTEDGynilTNVTYLqdkgVTIDGVTFFG-SSYHPlrGFPFYRNRAEQLAecW-----KAVPNDT 187
Cdd:COG1409    80 MAEAYREY------FGDLPP----GGLYYS----FDYGGVRFIGlDSNVP--GRSSGELGPEQLA--WleeelAAAPAKP 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972289863 188 NVLITHTPPLGYLDQFGDERWGCRD-LLKTVERIQPAYHIFGHVHeQHGVLSNGNTTFINAA 248
Cdd:COG1409   142 VIVFLHHPPYSTGSGSDRIGLRNAEeLLALLARYGVDLVLSGHVH-RYERTRRDGVPYIVAG 202
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 50-247 1.10e-11

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. 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: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 62.33  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  50 VVCISDTHEQL----HNVTVPDG-DVLIHAGDFTNNGKREELIKFNEEMTRFpHKYKLVVAGNhelgFDHDENQGErqda 124
Cdd:cd07392     1 ILAISDVHGDVpklkKIKLKAEEaDAVIVAGDITHFGPGEEAIEALNLLLAI-GAPVLAVPGN----CDTPEVLGE---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 125 dkglgtedGYNILTNVTylqDKGVTIDGVTFFG---SSYHPlrgF--PFYRNRAEQLAECWKAVPN--DTNVLITHTPPL 197
Cdd:cd07392    72 --------LNSAGLNIH---GKVVEVGGYIFVGvggSNPTP---FntPFEYSEEEIYSKLGLLNVKlpGRLILVTHAPPY 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1972289863 198 G-YLDQ-FGDERWGCRDLLKTVERIQPAYHIFGHVHEQHGVLSNGNTTFINA 247
Cdd:cd07392   138 GtAVDRvSSGVHVGSKAIRKFIEEFQPLLCICGHIHESRGIDKIGNTLVVNP 189
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 48-117 4.43e-06

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: 44.90  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  48 LKVVCISDTH--------EQLHNVTVPDG--DVLIHAGDFTNNGKR-EELIKFNEEMTRFPHKYklVVAGNHELGFDHDE 116
Cdd:pfam00149   1 MRILVIGDLHlpgqlddlLELLKKLLEEGkpDLVLHAGDLVDRGPPsEEVLELLERLIKYVPVY--LVRGNHDFDYGECL 78


                  .
gi 1972289863 117 N 117
Cdd:pfam00149  79 R 79
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 53-231 8.77e-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: 8.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  53 ISDTH----------------------EQLhNVTVPDGDVLIHAGDFTNNGKREELIKFNEEMTRFPHKYkLVVAGNHEl 110
Cdd:cd07402     4 ISDTHlfapgegallgvdtaarlaaavAQV-NALHPRPDLVVVTGDLSDDGSPESYERLRELLAPLPAPV-YWIPGNHD- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 111 gfdhdenqgERQDADKGLGTEDgYNILTNVTYLQD----KGVTIDGVTFfgssyhplrGFPFYRNRAEQLAecW-----K 181
Cdd:cd07402    81 ---------DRAAMREALPEPP-YDDNGPVQYVVDfggwRLILLDTSVP---------GVHHGELSDEQLD--WleaalA 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972289863 182 AVPNDTNVLITHTPPL----GYLDQFGderwgCRD---LLKTVER-IQPAYHIFGHVH 231
Cdd:cd07402   140 EAPDRPTLIFLHHPPFplgiPWMDAIR-----LRNsqaLFAVLARhPQVKAILCGHIH 192
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 65-231 1.66e-05

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: 44.63  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  65 VPDGDVLIHAGDfTNNGKREELIKFNEEMTRFPHKYKLVVAGNHELGFDHDENQGERQDADKglgtedgyNILTNVTYLQ 144
Cdd:cd07404    24 VPDADILILAGD-IGRLTDAEAWDNFLDLQSFQFEPVYYVPGNHEFYGGSLDITLDALRMAA--------QDLSNVHYLN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 145 DKGVTIDGVTFFGSSYHplRGFPfyrnrAEQLAECwKAVPND---TNVLITHTPPlgYLDQFGDERWGCR--------DL 213
Cdd:cd07404    95 NQEVVLDDVRILGCTLW--SDFD-----PDGEDIV-QRKLNDfrgATVVVTHHAP--SPRSTSDNYADGLpknaafhvDL 164

                         170
                  ....*....|....*...
gi 1972289863 214 LKTVERIQPAYHIFGHVH 231
Cdd:cd07404   165 KDLILAPPIDLWIHGHTH 182
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 189-247 2.15e-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: 43.02  E-value: 2.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972289863 189 VLITHTPPLGYLD-QFGDERWGCRDLLKTVERIQPAYHIFGHVHEQHG-VLSNGNTTFINA 247
Cdd:cd00838    69 ILVTHGPPYDPLDeGSPGEDPGSEALLELLDKYGPDLVLSGHTHVPGRrEVDKGGTLVVNP 129
MPP_NostocDevT-like cd07397
Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative ...
 48-248 7.74e-04

Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative protein phosphatase from Nostoc PCC 7120 (Anabaena PCC 7120). DevT mutants form mature heterocysts, but they are unable to fix N(2) and must be supplied with a source of combined nitrogen in order to survive. Anabaena DevT shows homology to phosphatases of the PPP family and displays a Mn(2+)-dependent phosphatase activity. DevT is constitutively expressed in both vegetative cells and heterocysts, and is not regulated by NtcA. The heterocyst regulator HetR may exert a certain inhibition on the expression of devT. Under diazotrophic growth conditions, DevT protein accumulates specifically in mature heterocysts. The role that DevT plays in a late essential step of heterocyst differentiation is still unknown. 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: 277342 [Multi-domain]  Cd Length: 245  Bit Score: 39.97  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  48 LKVVCISDTH-------EQLHNVTVPDGDVLIhaGDFTNngkrEELikfneEMTR------FPhkyKLVVAGNHELGFDH 114
Cdd:cd07397     1 VRIAIVGDVHgqwdaedERALRLLQPDLVLFV--GDFGN----ENV-----QLVRriasldLP---KAVILGNHDAWYTA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 115 DENQGERQDADKGLGTEDGYNIL--TNVTY----LQDKGVTIDGVTFFGSSYHPLRGFPFYRNR---------AEQLAEC 179
Cdd:cd07397    67 TRWGRCPYDRSKGDRVQQQLEILgdEHVGYgrldFPSLKLSVVGGRPFSKGGGRWLSKRFLSAVygvisleesAQRIADA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 180 WKAVPNDTNVLI-THTPPLGYLDQFGD-------ER---WGCRDLLKTVERIQPA-YHI----FGHVHEQ--HG------ 235
Cdd:cd07397   147 AKAAPEDHPLIFlAHNGPSGLGSRPEDicgkdwkPPggdHGDPDLAEAIAQVQAQgRRVplvvFGHMHHQlkRGnkglrm 226

                         250
                  ....*....|....*
gi 1972289863 236 --VLSNGNTTFINAA 248
Cdd:cd07397   227 mhVDDRTGTVYLNAA 241
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 69-108 8.43e-04

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: 38.81  E-value: 8.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1972289863  69 DVLIHAGDFTNNGKREELIKFNEEMTRFPHKYKLVVAGNH 108
Cdd:cd07400    32 DLVVVTGDLTQRARPAEFEEAREFLDALEPEPVVVVPGNH 71
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
69-194 1.03e-03

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 39.51  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  69 DVLIHAGDFTNNGKR--EELIKFNEEMTRFpHKYK---LVVAGNHElgfdhdenQGERQDADKGLGTEDGYNILTNVtyl 143
Cdd:COG0420    41 DAVLIAGDLFDSANPspEAVRLLAEALRRL-SEAGipvVLIAGNHD--------SPSRLSAGSPLLENLGVHVFGSV--- 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972289863 144 QDKGVTID---GVTFFGSSYHPLRGFPFYRNRAEQLAEcwKAVPNDTNVLITHT 194
Cdd:COG0420   109 EPEPVELEdglGVAVYGLPYLRPSDEEALRDLLERLPR--ALDPGGPNILLLHG 160
MPP_TTHA0053 cd07403
Thermus thermophilus TTHA0053 and related proteins, metallophosphatase domain; TTHA0053 is an ...
 185-231 1.15e-03

Thermus thermophilus TTHA0053 and related proteins, metallophosphatase domain; TTHA0053 is an uncharacterized Thermus thermophilus protein with a domain that 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: 277348  Cd Length: 130  Bit Score: 38.26  E-value: 1.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1972289863 185 NDTNVLITHTPPLGYLDQFGDERWGCRDLLKTVERIQPAYHIFGHVH 231
Cdd:cd07403    55 HGLDVLLTHAPPLGPSAGEDFAHRGFRAFLLFIRLFRPRYLIHGHTH 101
acc_ester TIGR03729
putative phosphoesterase; Members of this protein family belong to the larger family pfam00149 ...
 69-248 2.84e-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: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863  69 DVLIHAGDFTNNGKR-----EELIKFNEEMTRFphkyklvVAGNHELGFDHDENQGERQDadkglgtEDGYNILTNVTYL 143
Cdd:TIGR03729  34 DHLHIAGDISNDFQRslpfiEKLQELKGIKVTF-------NAGNHDMLKDLTYEEIESND-------SPLYLHNRFIDIP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972289863 144 QDKGVTIDGVTFFGSSYHPLR--------GFPFYRNR---------------AEQLAECWKAVPNDTNVLITH-TPPLGY 199
Cdd:TIGR03729 100 NTQWRIIGNNGWYDYSFSNDKtskeilrwKKSFWFDRrikrpmsdpertaivLKQLKKQLNQLDNKQVIFVTHfVPHRDF 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972289863 200 LDQFGD-ERW-------GCRDLLKTVERIQPAYHIFGHVHEQHGVLSNGNTTFINAA 248
Cdd:TIGR03729 180 IYVPMDhRRFdmfnaflGSQHFGQLLVKYEIKDVIFGHLHRRFGPLTIGGTTYHNRP 236
 
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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