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Conserved domains on  [gi|2265268929|ref|WP_253304040|]
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metallophosphoesterase [Thermococcus aggregans]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10005392)

metallophosphoesterase family 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:0016787|GO:0046872|GO:0042578
PubMed:  25837850|8003970
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-209 5.08e-78

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


:

Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 232.98  E-value: 5.08e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   2 RIIAVTDIHGKANKVRELLEHLKGQEFDLILIAGDITHFGGRESAYNILKEFLDFGKSFYAVMGNCDGRDVLELLEELNI 81
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDDPEVLDALEESGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  82 -GLHGKRVEFNGVGITGIGGSNITPFSTIWEFSEEEIWEILTRNY-KDGDIILSHVPPKDTNVDKTFVGTHAGSKSLRKF 159
Cdd:COG2129    81 hNLHGRVVEIGGLRIAGLGGSRPTPFGTPYEYTEEEIEERLAKLReKDVDILLTHAPPYGTTLDRVEDGPHVGSKALREL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2265268929 160 IEEKQPPLVICGHIHEGTGIDKIGETMIVNPGPLSRGHYAVIDFDEKEKK 209
Cdd:COG2129   161 IEEFQPKLVLHGHIHESRGVDKIGGTRVVNPGSLAEGYYALIDLEDRSVE 210
 
Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-209 5.08e-78

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 232.98  E-value: 5.08e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   2 RIIAVTDIHGKANKVRELLEHLKGQEFDLILIAGDITHFGGRESAYNILKEFLDFGKSFYAVMGNCDGRDVLELLEELNI 81
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDDPEVLDALEESGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  82 -GLHGKRVEFNGVGITGIGGSNITPFSTIWEFSEEEIWEILTRNY-KDGDIILSHVPPKDTNVDKTFVGTHAGSKSLRKF 159
Cdd:COG2129    81 hNLHGRVVEIGGLRIAGLGGSRPTPFGTPYEYTEEEIEERLAKLReKDVDILLTHAPPYGTTLDRVEDGPHVGSKALREL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2265268929 160 IEEKQPPLVICGHIHEGTGIDKIGETMIVNPGPLSRGHYAVIDFDEKEKK 209
Cdd:COG2129   161 IEEFQPKLVLHGHIHESRGVDKIGGTRVVNPGSLAEGYYALIDLEDRSVE 210
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 3-191 2.64e-75

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: 225.27  E-value: 2.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   3 IIAVTDIHGKANKVRELLehLKGQEFDLILIAGDITHFGGRESAYNILKEFLDFGKSFYAVMGNCDGRDVLELLEELNIG 82
Cdd:cd07392     1 ILAISDVHGDVPKLKKIK--LKAEEADAVIVAGDITHFGPGEEAIEALNLLLAIGAPVLAVPGNCDTPEVLGELNSAGLN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  83 LHGKRVEFNGVGITGIGGSNITPFSTIWEFSEEEIWEILTRNY---KDGDIILSHVPPKDTNVDKTFVGTHAGSKSLRKF 159
Cdd:cd07392    79 IHGKVVEVGGYIFVGVGGSNPTPFNTPFEYSEEEIYSKLGLLNvklPGRLILVTHAPPYGTAVDRVSSGVHVGSKAIRKF 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2265268929 160 IEEKQPPLVICGHIHEGTGIDKIGETMIVNPG 191
Cdd:cd07392   159 IEEFQPLLCICGHIHESRGIDKIGNTLVVNPG 190
Metallophos_3 pfam14582
Metallophosphoesterase, calcineurin superfamily; Members of this family are part of the ...
 2-207 2.50e-14

Metallophosphoesterase, calcineurin superfamily; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 405297 [Multi-domain]  Cd Length: 259  Bit Score: 69.54  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   2 RIIAVTDIHGKANKVRELLEHLKGQEFDLILIAGDITHFGGRESAY-----------------------NILKEFLD-FG 57
Cdd:pfam14582   7 KVLAISDFHGETELLERLVGKIEDKSPDALVLVGDLVKGQARADEYlsaqeegrepdkeeilneknedfKLYDKFFRtLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  58 ----KSFYaVMGNCDGRDVLELLEELNI--------GLHGKRVEFNG-VGITGIGGSnitpfstIWEFSEEEI------- 117
Cdd:pfam14582  87 eldvPVFY-VPGPMDAPLDVFLREAYNAeyvfpnihGVHESFAFKPGeVLIAGMGGE-------ITDGSKEEFfrlqypa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929 118 WE---ILTRNYKDGD---IILSHVPPKDTNV-DKTFvgTHAGSKSLRKFIEEKQPPLVICGHIHEGTGIDKIGETMIVNP 190
Cdd:pfam14582 159 WEaeyRLKVLKELKPyrkVFLLHTPPTGQLDaHKGP--KHAGSDVVNELIKTHNPEVVFVGHAHKAHGKEQLGKTLVVNP 236

                         250
                  ....*....|....*..
gi 2265268929 191 GPLSRGHYAVIDFDEKE 207
Cdd:pfam14582 237 GALKEGDFAVVDLENKE 253
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-88 3.31e-08

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 51.22  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   1 MRIIAVTDIHGKaNKVRELLEHLKGQE--FDLILIAGDIThfggresAYNILKEFLDFGKSFYAVMGNCDGrDVLELLEE 78
Cdd:TIGR00040   1 MKILVISDTHGP-LRATELPVELFNLEsnVDLVIHAGDLT-------SPFVLKEFEDLAAKVIAVRGNNDG-ERDELPEE 71

                          90
                  ....*....|
gi 2265268929  79 LNIGLHGKRV 88
Cdd:TIGR00040  72 EIFEAEGIDF 81
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-68 5.24e-05

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 42.16  E-value: 5.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2265268929   1 MRIIAVTDIHGKANKVRELLEHLKGQEFDLILIAGDITHFGGRE---SAYN--ILKEFL-DFGKSFYAVMGNCD 68
Cdd:PRK09453    1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDVLYHGPRNplpEGYApkKVAELLnAYADKIIAVRGNCD 74
 
Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-209 5.08e-78

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 232.98  E-value: 5.08e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   2 RIIAVTDIHGKANKVRELLEHLKGQEFDLILIAGDITHFGGRESAYNILKEFLDFGKSFYAVMGNCDGRDVLELLEELNI 81
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDDPEVLDALEESGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  82 -GLHGKRVEFNGVGITGIGGSNITPFSTIWEFSEEEIWEILTRNY-KDGDIILSHVPPKDTNVDKTFVGTHAGSKSLRKF 159
Cdd:COG2129    81 hNLHGRVVEIGGLRIAGLGGSRPTPFGTPYEYTEEEIEERLAKLReKDVDILLTHAPPYGTTLDRVEDGPHVGSKALREL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2265268929 160 IEEKQPPLVICGHIHEGTGIDKIGETMIVNPGPLSRGHYAVIDFDEKEKK 209
Cdd:COG2129   161 IEEFQPKLVLHGHIHESRGVDKIGGTRVVNPGSLAEGYYALIDLEDRSVE 210
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 3-191 2.64e-75

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: 225.27  E-value: 2.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   3 IIAVTDIHGKANKVRELLehLKGQEFDLILIAGDITHFGGRESAYNILKEFLDFGKSFYAVMGNCDGRDVLELLEELNIG 82
Cdd:cd07392     1 ILAISDVHGDVPKLKKIK--LKAEEADAVIVAGDITHFGPGEEAIEALNLLLAIGAPVLAVPGNCDTPEVLGELNSAGLN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  83 LHGKRVEFNGVGITGIGGSNITPFSTIWEFSEEEIWEILTRNY---KDGDIILSHVPPKDTNVDKTFVGTHAGSKSLRKF 159
Cdd:cd07392    79 IHGKVVEVGGYIFVGVGGSNPTPFNTPFEYSEEEIYSKLGLLNvklPGRLILVTHAPPYGTAVDRVSSGVHVGSKAIRKF 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2265268929 160 IEEKQPPLVICGHIHEGTGIDKIGETMIVNPG 191
Cdd:cd07392   159 IEEFQPLLCICGHIHESRGIDKIGNTLVVNPG 190
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-205 7.35e-19

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 81.66  E-value: 7.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   1 MRIIAVTDIH-------GKANKVRELLEHLKGQEFDLILIAGDITHFGGRESaYNILKEFLD-FGKSFYAVMGNCDGRDV 72
Cdd:COG1409     1 FRFAHISDLHlgapdgsDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEE-YAAAREILArLGVPVYVVPGNHDIRAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  73 L--ELLEELNIGLHGKR---VEFNGVGITGIgGSNItPFSTIWEFSEEEI-W--EILTRNYKDGDIILSHVPPKDTNVDK 144
Cdd:COG1409    80 MaeAYREYFGDLPPGGLyysFDYGGVRFIGL-DSNV-PGRSSGELGPEQLaWleEELAAAPAKPVIVFLHHPPYSTGSGS 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2265268929 145 TFVGTHaGSKSLRKFIEEKQPPLVICGHIHEGTGIDKIGETMIVNPG----PLSRGHYAVIDFDE 205
Cdd:COG1409   158 DRIGLR-NAEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGStggqVRLPPGYRVIEVDG 221
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-211 3.67e-18

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 78.42  E-value: 3.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   2 RIIAVTDIHGKANKVRELLEHLKGQEFDLILIAGDITHFGGRESAynILKEFLDFGksFYAVMGNCDgRDVLELLEELNI 81
Cdd:COG0622     1 KIAVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPE--VLDLLRELP--IVAVRGNHD-GAVLRGLRSLPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  82 GLhgkRVEFNGVgitgiggsnitpfstiwefseeeiweiltrnykdgDIILSHVPPKDtnvdktFVGTHAGSKSLRKFIE 161
Cdd:COG0622    76 TL---RLELEGV-----------------------------------RILLVHGSPNE------YLLPDTPAERLRALAA 111

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2265268929 162 EKQPPLVICGHIHEgTGIDKIGETMIVNPG--PLSRGH----YAVIDFDEKEKKVK 211
Cdd:COG0622   112 EGDADVVVCGHTHI-PFVRRVGGVLLVNPGsvGQPRDGdpasYAILDIDDGEWSVE 166
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-211 6.71e-15

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain 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: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 69.22  E-value: 6.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   2 RIIAVTDIHGKANKVRELLEHLKGQeFDLILIAGDIT-HFggresaynILKEFLDFGKSFYAVMGNCDG-RDVLELLEEL 79
Cdd:cd00841     1 KIGVISDTHGNLEAIEKALELFEDG-VDAVIHAGDFVsPF--------VLNALLELKAPLIAVRGNNDGeVDQLLGRPIL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  80 niglhgkrvefngvgitgiggsnitpfstiwefSEEEIWEIltrnyKDGDIILSHvppkdtnvdktfvGTHAGSKSLRKF 159
Cdd:cd00841    72 ---------------------------------PEFLTLEI-----GGLRILLTH-------------GHLFGVLEALYL 100

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2265268929 160 IEEKQPPLVICGHIHEgTGIDKIGETMIVNPG----PLSRGH-YAVIDFDEKEKKVK 211
Cdd:cd00841   101 AKEGGADVVVFGHTHV-PVIERVGGTLLLNPGsvsgPRGGRPtYAILDIEKLEVEII 156
Metallophos_3 pfam14582
Metallophosphoesterase, calcineurin superfamily; Members of this family are part of the ...
 2-207 2.50e-14

Metallophosphoesterase, calcineurin superfamily; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 405297 [Multi-domain]  Cd Length: 259  Bit Score: 69.54  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   2 RIIAVTDIHGKANKVRELLEHLKGQEFDLILIAGDITHFGGRESAY-----------------------NILKEFLD-FG 57
Cdd:pfam14582   7 KVLAISDFHGETELLERLVGKIEDKSPDALVLVGDLVKGQARADEYlsaqeegrepdkeeilneknedfKLYDKFFRtLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  58 ----KSFYaVMGNCDGRDVLELLEELNI--------GLHGKRVEFNG-VGITGIGGSnitpfstIWEFSEEEI------- 117
Cdd:pfam14582  87 eldvPVFY-VPGPMDAPLDVFLREAYNAeyvfpnihGVHESFAFKPGeVLIAGMGGE-------ITDGSKEEFfrlqypa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929 118 WE---ILTRNYKDGD---IILSHVPPKDTNV-DKTFvgTHAGSKSLRKFIEEKQPPLVICGHIHEGTGIDKIGETMIVNP 190
Cdd:pfam14582 159 WEaeyRLKVLKELKPyrkVFLLHTPPTGQLDaHKGP--KHAGSDVVNELIKTHNPEVVFVGHAHKAHGKEQLGKTLVVNP 236

                         250
                  ....*....|....*..
gi 2265268929 191 GPLSRGHYAVIDFDEKE 207
Cdd:pfam14582 237 GALKEGDFAVVDLENKE 253
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 121-189 7.02e-13

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: 63.42  E-value: 7.02e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2265268929 121 LTRNYKDGDIILSHVPPKDTnVDKTFVGTHAGSKSLRKFIEEKQPPLVICGHIHEGTGI----DKIGETMIVN 189
Cdd:cd07379    62 LTLDPEGTDILVTHGPPYGH-LDLGSSGQRLGCEELLNTVQRVRPKLHVFGHIHEGYGIervpDTDGETTFVN 133
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-206 6.11e-12

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 61.17  E-value: 6.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   1 MRIIAVTDIHGKANKVRELLEHLKGqEFDLILIAGDIthfggreSAYNILKEFLDFGKsFYAVMGNCDgrdvlelLEELN 80
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKG-VVDLIIHAGDI-------VAPEVLEELLELAP-VLAVRGNND-------AAAEF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  81 IGLHGKRVEFNgvgitgIGGsnitpfstiwefseeeiweiltrnykdGDIILSHVPPKDTNVDKTFVGTHAGskslrkfi 160
Cdd:pfam12850  65 ATDLPEEAVLE------LGG---------------------------VKILLTHGHGVKDALARLLRRAEEG-------- 103

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2265268929 161 eekqPPLVICGHIHEgTGIDKIGETMIVNPGPL------SRGHYAVIDFDEK 206
Cdd:pfam12850 104 ----VAVVVYGHTHV-PGVERIGGVLFVNPGSVggprfgDPPTYALLDIDDG 150
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 4-191 7.75e-11

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: 57.66  E-value: 7.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   4 IAVTDIHGKANKVRELLEH--LKGQEFDLILIAGDITHFGGRESAY-NILKEFLDFGKSFYAVMGNcdgrdvlelleeln 80
Cdd:cd00838     1 LVISDIHGNLEALEAVLEAalAKAEKPDLVICLGDLVDYGPDPEEVeLKALRLLLAGIPVYVVPGN-------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  81 iglHgkrvefngvgitgiggsnitpfstiwefseeeiweiltrnykdgDIILSHVPPKDTNvDKTFVGTHAGSKSLRKFI 160
Cdd:cd00838    67 ---H--------------------------------------------DILVTHGPPYDPL-DEGSPGEDPGSEALLELL 98

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2265268929 161 EEKQPPLVICGHIHEGTGID-KIGETMIVNPG 191
Cdd:cd00838    99 DKYGPDLVLSGHTHVPGRREvDKGGTLVVNPG 130
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-98 6.92e-09

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 51.83  E-value: 6.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   1 MRIIAVTDIH--GKANKVRELLEHLKGQE-FDLILIAGDITHFGGRESAYNILKEFLDFGKSFYAVMGNCDGR--DVLEL 75
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLEEGkPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHDFDygECLRL 80

                          90       100
                  ....*....|....*....|....*.
gi 2265268929  76 LEELNIGLHGKRVE---FNGVGITGI 98
Cdd:pfam00149  81 YPYLGLLARPWKRFlevFNFLPLAGI 106
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 2-191 1.58e-08

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: 53.05  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   2 RIIAVTDIH----GKANKVRELLEHLKGQEFDLILIAGDIthFGGRESAYNILKEFLDFGKS---FYAVMGN-----CDG 69
Cdd:cd07385     3 RIVQLSDIHlgpfVGRTRLQKVVRKVNELNPDLIVITGDL--VDGDVSVLRLLASPLSKLKAplgVYFVLGNhdyysGDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  70 RDVLELLEELNIG-LHGKRVEFNGVGIT-GIGGSNITPFSTIWEFSEEEIWEILTRNYKdgdIILSHVPpkdtnvdktfv 147
Cdd:cd07385    81 EVWIAALEKAGITvLRNESVELSRDGATiGLAGSGVDDIGGHGEDLEKALKGLDENDPV---ILLAHNP----------- 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2265268929 148 gthagskslrKFIEEKQPP---LVICGHIHEG------------------TGIDKIGETM--IVNPG 191
Cdd:cd07385   147 ----------DAAEEAQRPgvdLVLSGHTHGGqifppnygvlsklgfpydSGLYQIGGTTylYVSRG 203
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-88 3.31e-08

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 51.22  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   1 MRIIAVTDIHGKaNKVRELLEHLKGQE--FDLILIAGDIThfggresAYNILKEFLDFGKSFYAVMGNCDGrDVLELLEE 78
Cdd:TIGR00040   1 MKILVISDTHGP-LRATELPVELFNLEsnVDLVIHAGDLT-------SPFVLKEFEDLAAKVIAVRGNNDG-ERDELPEE 71

                          90
                  ....*....|
gi 2265268929  79 LNIGLHGKRV 88
Cdd:TIGR00040  72 EIFEAEGIDF 81
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
1-81 7.77e-07

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 48.25  E-value: 7.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   1 MRIIAVTDIHGK----ANKVRELLEHLKGQEFDLILIAGDIT--HFGGRESAYNILKEFLD-FGKsfYAVMGN----CDG 69
Cdd:COG1408    43 LRIVQLSDLHLGpfigGERLERLVEKINALKPDLVVLTGDLVdgSVAELEALLELLKKLKApLGV--YAVLGNhdyyAGL 120

                          90
                  ....*....|..
gi 2265268929  70 RDVLELLEELNI 81
Cdd:COG1408   121 EELRAALEEAGV 132
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 3-174 3.25e-06

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 46.50  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   3 IIAVTDIHGKANKVRELL------------EHLK--GQEFDLILIAGDITHFgGRESAYNILKEFLD-FGKSFYAVMGNC 67
Cdd:cd07402     1 IAQISDTHLFAPGEGALLgvdtaarlaaavAQVNalHPRPDLVVVTGDLSDD-GSPESYERLRELLApLPAPVYWIPGNH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  68 DGRDVL-ELLEELNIGLHG--KRVEFNGvGITGIGGSNITPFSTIWEFSEEEI-W--EILTRNYKDGDIILSHVPPKDTN 141
Cdd:cd07402    80 DDRAAMrEALPEPPYDDNGpvQYVVDFG-GWRLILLDTSVPGVHHGELSDEQLdWleAALAEAPDRPTLIFLHHPPFPLG 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2265268929 142 VDK----TFVGTHAGSKSLRKFieeKQPPLVICGHIH 174
Cdd:cd07402   159 IPWmdaiRLRNSQALFAVLARH---PQVKAILCGHIH 192
MPP_Tt1561 cd07388
Thermus thermophilus Tt1561 and related proteins, metallophosphatase domain; This family ...
 111-210 2.71e-05

Thermus thermophilus Tt1561 and related proteins, metallophosphatase domain; This family includes bacterial proteins related to Tt1561 (also known as Aq1956 in Aquifex aeolicus), an uncharacterized Thermus thermophilus protein. The conserved 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, and is thought to allow for productive metal coordination. However, the active site residues required for phosphoesterase activity in other members of this superfamily are poorly conserved in this functionally uncharacterized family.


Pssm-ID: 277334 [Multi-domain]  Cd Length: 224  Bit Score: 43.80  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929 111 EFSEEEIWEILTRNYkdgdIILSHVPPKDTNVDktfvgtHAGSKSLRKFIEEKQPPLVICGHIheGTGIDKIGETMIVNP 190
Cdd:cd07388   136 EYRLKALWELKDYPK----IFLFHTPPYHKGLN------EQGSHEVAHLIKTHNPLLVLVAGK--GQKHELLGASWVVVP 203

                          90       100
                  ....*....|....*....|
gi 2265268929 191 GPLSRGHYAVIDFDEKEKKV 210
Cdd:cd07388   204 GDLSEGEYSLLDLRARKLET 223
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-68 5.24e-05

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 42.16  E-value: 5.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2265268929   1 MRIIAVTDIHGKANKVRELLEHLKGQEFDLILIAGDITHFGGRE---SAYN--ILKEFL-DFGKSFYAVMGNCD 68
Cdd:PRK09453    1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDVLYHGPRNplpEGYApkKVAELLnAYADKIIAVRGNCD 74
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
1-209 3.95e-04

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 40.28  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929   1 MRIIAVTDIH-GK-----------ANKVRELLEHLKGQEFDLILIAGDITH-----FGGRESAYNILKEFLDFGKSFYAV 63
Cdd:COG0420     1 MRFLHTADWHlGKplhgasrredqLAALDRLVDLAIEEKVDAVLIAGDLFDsanpsPEAVRLLAEALRRLSEAGIPVVLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929  64 MGNCDGRDVLE----LLEELNIGLHGkRVEFNGVGITGIGGSNITPFStiweFSEEEIWEILTRNYKDgdiILSHVPPKD 139
Cdd:COG0420    81 AGNHDSPSRLSagspLLENLGVHVFG-SVEPEPVELEDGLGVAVYGLP----YLRPSDEEALRDLLER---LPRALDPGG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265268929 140 TNVdktFV--GTHAGSKSLRKFIEEKQPP---------LVICGHIHEGTGIDkiGETMIVNPG-PLSRghyaviDFDEKE 207
Cdd:COG0420   153 PNI---LLlhGFVAGASGSRDIYVAPVPLsalpaagfdYVALGHIHRPQVLG--GDPRIRYSGsPEPR------SFSEAG 221


                  ..
gi 2265268929 208 KK 209
Cdd:COG0420   222 GK 223
 
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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