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Conserved domains on  [gi|2092133461|ref|XP_043393970|]
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metallophosphoesterase domain-containing protein 1 [Chelonia mydas]

Protein Classification

metallophosphatase domain-containing protein( domain architecture ID 10164504)

metallophosphatase domain-containing protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to human metallophosphoesterase MPPED2 that may play a role in the development of the nervous system

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 ...
 67-279 8.88e-65

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: 199.78  E-value: 8.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461  67 RFVCISDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNHELTFDqefmadlikqdfyyf 146
Cdd:cd07379     1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461 147 psvsklkpesyenvqslltnciylqdsevtvrgfriygspwqpwfygwgfnlprgqallekwnliPDGIDILITHGPPLG 226
Cdd:cd07379    66 -----------------------------------------------------------------PEGTDILVTHGPPYG 80

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2092133461 227 FLDWVPKKmQRVGCVELLNTVQrRIQPRLHVFGHIHEGYGVMA----DGTTTYVNAS 279
Cdd:cd07379    81 HLDLGSSG-QRLGCEELLNTVQ-RVRPKLHVFGHIHEGYGIERvpdtDGETTFVNAS 135
 
Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 67-279 8.88e-65

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: 199.78  E-value: 8.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461  67 RFVCISDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNHELTFDqefmadlikqdfyyf 146
Cdd:cd07379     1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461 147 psvsklkpesyenvqslltnciylqdsevtvrgfriygspwqpwfygwgfnlprgqallekwnliPDGIDILITHGPPLG 226
Cdd:cd07379    66 -----------------------------------------------------------------PEGTDILVTHGPPYG 80

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2092133461 227 FLDWVPKKmQRVGCVELLNTVQrRIQPRLHVFGHIHEGYGVMA----DGTTTYVNAS 279
Cdd:cd07379    81 HLDLGSSG-QRLGCEELLNTVQ-RVRPKLHVFGHIHEGYGIERvpdtDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
67-279 4.40e-35

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 125.90  E-value: 4.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461  67 RFVCISDTHSRTDP-------IQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYeYKIVIAGNHEltfdqefmadli 139
Cdd:COG2129     1 KILAVSDLHGNFDLlekllelARAEDADLVILAGDLTDFGTAEEAREVLEELAALGV-PVLAVPGNHD------------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461 140 kqdfyyFPSVSKLKPESyenvqslltNCIYLQDSEVTVRGFRIYGS------PWQPWFYgwgfnlPRGQALLEKW-NLIP 212
Cdd:COG2129    68 ------DPEVLDALEES---------GVHNLHGRVVEIGGLRIAGLggsrptPFGTPYE------YTEEEIEERLaKLRE 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092133461 213 DGIDILITHGPPLGFLDWVPKKMQRVGCVELLNTVqRRIQPRLHVFGHIHEGYGVMADGTTTYVNAS 279
Cdd:COG2129   127 KDVDILLTHAPPYGTTLDRVEDGPHVGSKALRELI-EEFQPKLVLHGHIHESRGVDKIGGTRVVNPG 192
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 67-131 4.14e-04

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: 39.12  E-value: 4.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092133461  67 RFVCISDTHSR---------TDPIQMPYG-DVLIHAGDFTELGLPSEvkKFNEWLGSL-PYEYKIVIAGNHELTFD 131
Cdd:pfam00149   2 RILVIGDLHLPgqlddllelLKKLLEEGKpDLVLHAGDLVDRGPPSE--EVLELLERLiKYVPVYLVRGNHDFDYG 75
 
Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 67-279 8.88e-65

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: 199.78  E-value: 8.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461  67 RFVCISDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNHELTFDqefmadlikqdfyyf 146
Cdd:cd07379     1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461 147 psvsklkpesyenvqslltnciylqdsevtvrgfriygspwqpwfygwgfnlprgqallekwnliPDGIDILITHGPPLG 226
Cdd:cd07379    66 -----------------------------------------------------------------PEGTDILVTHGPPYG 80

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2092133461 227 FLDWVPKKmQRVGCVELLNTVQrRIQPRLHVFGHIHEGYGVMA----DGTTTYVNAS 279
Cdd:cd07379    81 HLDLGSSG-QRLGCEELLNTVQ-RVRPKLHVFGHIHEGYGIERvpdtDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
67-279 4.40e-35

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 125.90  E-value: 4.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461  67 RFVCISDTHSRTDP-------IQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYeYKIVIAGNHEltfdqefmadli 139
Cdd:COG2129     1 KILAVSDLHGNFDLlekllelARAEDADLVILAGDLTDFGTAEEAREVLEELAALGV-PVLAVPGNHD------------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461 140 kqdfyyFPSVSKLKPESyenvqslltNCIYLQDSEVTVRGFRIYGS------PWQPWFYgwgfnlPRGQALLEKW-NLIP 212
Cdd:COG2129    68 ------DPEVLDALEES---------GVHNLHGRVVEIGGLRIAGLggsrptPFGTPYE------YTEEEIEERLaKLRE 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092133461 213 DGIDILITHGPPLGFLDWVPKKMQRVGCVELLNTVqRRIQPRLHVFGHIHEGYGVMADGTTTYVNAS 279
Cdd:COG2129   127 KDVDILLTHAPPYGTTLDRVEDGPHVGSKALRELI-EEFQPKLVLHGHIHESRGVDKIGGTRVVNPG 192
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
66-281 2.68e-12

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 65.10  E-value: 2.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461  66 TRFVCISDTHSRTDPIQMPYG--------------DVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYkIVIAGNHELTFD 131
Cdd:COG1409     1 FRFAHISDLHLGAPDGSDTAEvlaaaladinaprpDFVVVTGDLTDDGEPEEYAAAREILARLGVPV-YVVPGNHDIRAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461 132 -----QEFMADLIKQDFYYFpsvsklkpesyenvqslltnciylqdseVTVRGFRIYG--SPWQPWFYGWgfnLPRGQ-A 203
Cdd:COG1409    80 maeayREYFGDLPPGGLYYS----------------------------FDYGGVRFIGldSNVPGRSSGE---LGPEQlA 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092133461 204 LLEKW-NLIPDGIDILITHGPPLGFLDWVPKKMQRvGCVELLNTVQRRiQPRLHVFGHIHEGYGVMADGTTTYVNASVC 281
Cdd:COG1409   129 WLEEElAAAPAKPVIVFLHHPPYSTGSGSDRIGLR-NAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTG 205
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 71-279 3.35e-10

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: 58.48  E-value: 3.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461  71 ISDTHSRTDPIQMPY-----GDVLIHAGDFTELGLPSEVKKFNEWLGSLpyeYKIVIA--GNheltFDQEFMADlikqdf 143
Cdd:cd07392     4 ISDVHGDVPKLKKIKlkaeeADAVIVAGDITHFGPGEEAIEALNLLLAI---GAPVLAvpGN----CDTPEVLG------ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461 144 yyfpsvsklkpesyenvqSLLTNCIYLQDSEVTVRGFRIYG------SPwqpwfygwgFNLPRG------QALLEKWNLI 211
Cdd:cd07392    71 ------------------ELNSAGLNIHGKVVEVGGYIFVGvggsnpTP---------FNTPFEyseeeiYSKLGLLNVK 123

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2092133461 212 PDGIDILITHGPPLG-FLDWVPKkMQRVGCVELLNTVQRRiQPRLHVFGHIHEGYGVMADGTTTYVNAS 279
Cdd:cd07392   124 LPGRLILVTHAPPYGtAVDRVSS-GVHVGSKAIRKFIEEF-QPLLCICGHIHESRGIDKIGNTLVVNPG 190
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 216-278 3.62e-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: 45.72  E-value: 3.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092133461 216 DILITHGPPLGFLDWVPKKMQRvgCVELLNTVQRRIQPRLHVFGHIHEGYGVMAD-GTTTYVNA 278
Cdd:cd00838    68 DILVTHGPPYDPLDEGSPGEDP--GSEALLELLDKYGPDLVLSGHTHVPGRREVDkGGTLVVNP 129
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 87-126 7.77e-05

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: 41.90  E-value: 7.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2092133461  87 DVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNH 126
Cdd:cd07400    32 DLVVVTGDLTQRARPAEFEEAREFLDALEPEPVVVVPGNH 71
MPP_DR1119 cd07393
Deinococcus radiodurans DR1119 and related proteins, metallophosphatase domain; DR1119 is an ...
 86-262 7.92e-05

Deinococcus radiodurans DR1119 and related proteins, metallophosphatase domain; DR1119 is an uncharacterized Deinococcus radiodurans 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: 277339 [Multi-domain]  Cd Length: 238  Bit Score: 43.25  E-value: 7.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461  86 GDVLIHAGDFTELGLPSEVKKFNEWLGSLPyEYKIVIAGNHEltfdqefmadlikqdfYYFPSVSKLKPESYENVQSLLT 165
Cdd:cd07393    43 EDIVLIPGDISWAMNLKEALKDLTWINDLP-GIKILLKGNHD----------------YWWPSKSKARRALEEEFLALKF 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092133461 166 NCIYLqDSEVTVRGFRIYGSPWQPWFYGWGFNLPRG----------QALLEKWNLI--------PDGIDILITHGPPL-- 225
Cdd:cd07393   106 HKAYI-DDKVVVGGTRLWDNPYNCWPIINKQLKEETlkveiderccQRELERLNFAlkamnelrEDKIKILMLHHPPAne 184

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2092133461 226 -GFLDWVPKKMQRVGcvellntvqrriqPRLHVFGHIH 262
Cdd:cd07393   185 dGDINPIFKLILESR-------------VDICLFGHIH 209
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 69-130 1.59e-04

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: 40.71  E-value: 1.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2092133461  69 VCISDTHSRTD---------PIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNHELTF 130
Cdd:cd00838     1 LVISDIHGNLEaleavleaaLAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHDILV 71
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 67-131 4.14e-04

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: 39.12  E-value: 4.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092133461  67 RFVCISDTHSR---------TDPIQMPYG-DVLIHAGDFTELGLPSEvkKFNEWLGSL-PYEYKIVIAGNHELTFD 131
Cdd:pfam00149   2 RILVIGDLHLPgqlddllelLKKLLEEGKpDLVLHAGDLVDRGPPSE--EVLELLERLiKYVPVYLVRGNHDFDYG 75
 
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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