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Conserved domains on  [gi|113204627|ref|NP_001037835|]
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metallophosphoesterase domain-containing protein 1 precursor [Homo sapiens]

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 ...
 91-303 5.05e-66

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: 204.02  E-value: 5.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627  91 RFVCVSDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNHELTFDqefmadlikqdfyyf 170
Cdd:cd07379    1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627 171 psvsklkpenyenvqslltnciylqdsevtvrgfriygspwqpwfygwgfnlprgqallekwnliPEGVDILITHGPPLG 250
Cdd:cd07379   66 -----------------------------------------------------------------PEGTDILVTHGPPYG 80

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 113204627 251 FLDWVPKKmQRVGCVELLNTVQrRVQPRLHVFGHIHEGYGVMA----DGTTTYVNAS 303
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 ...
 91-303 5.05e-66

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: 204.02  E-value: 5.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627  91 RFVCVSDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNHELTFDqefmadlikqdfyyf 170
Cdd:cd07379    1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627 171 psvsklkpenyenvqslltnciylqdsevtvrgfriygspwqpwfygwgfnlprgqallekwnliPEGVDILITHGPPLG 250
Cdd:cd07379   66 -----------------------------------------------------------------PEGTDILVTHGPPYG 80

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 113204627 251 FLDWVPKKmQRVGCVELLNTVQrRVQPRLHVFGHIHEGYGVMA----DGTTTYVNAS 303
Cdd:cd07379   81 HLDLGSSG-QRLGCEELLNTVQ-RVRPKLHVFGHIHEGYGIERvpdtDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
91-303 6.18e-36

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 128.98  E-value: 6.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627  91 RFVCVSDTHSRTDP-------IQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYeYKIVIAGNHEltfDQEFMADLI 163
Cdd:COG2129    1 KILAVSDLHGNFDLlekllelARAEDADLVILAGDLTDFGTAEEAREVLEELAALGV-PVLAVPGNHD---DPEVLDALE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627 164 KqdfyyfpsvsklkpenyenvqsllTNCIYLQDSEVTVRGFRIYGS------PWQPWFYgwgfnlPRGQALLEKW-NLIP 236
Cdd:COG2129   77 E------------------------SGVHNLHGRVVEIGGLRIAGLggsrptPFGTPYE------YTEEEIEERLaKLRE 126

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113204627 237 EGVDILITHGPPLGFLDWVPKKMQRVGCVELLNTVqRRVQPRLHVFGHIHEGYGVMADGTTTYVNAS 303
Cdd:COG2129  127 KDVDILLTHAPPYGTTLDRVEDGPHVGSKALRELI-EEFQPKLVLHGHIHESRGVDKIGGTRVVNPG 192
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 91-155 4.82e-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: 4.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113204627   91 RFVCVSDTHSR---------TDPIQMPYG-DVLIHAGDFTELGLPSEvkKFNEWLGSL-PYEYKIVIAGNHELTFD 155
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 ...
 91-303 5.05e-66

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: 204.02  E-value: 5.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627  91 RFVCVSDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNHELTFDqefmadlikqdfyyf 170
Cdd:cd07379    1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627 171 psvsklkpenyenvqslltnciylqdsevtvrgfriygspwqpwfygwgfnlprgqallekwnliPEGVDILITHGPPLG 250
Cdd:cd07379   66 -----------------------------------------------------------------PEGTDILVTHGPPYG 80

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 113204627 251 FLDWVPKKmQRVGCVELLNTVQrRVQPRLHVFGHIHEGYGVMA----DGTTTYVNAS 303
Cdd:cd07379   81 HLDLGSSG-QRLGCEELLNTVQ-RVRPKLHVFGHIHEGYGIERvpdtDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
91-303 6.18e-36

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 128.98  E-value: 6.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627  91 RFVCVSDTHSRTDP-------IQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYeYKIVIAGNHEltfDQEFMADLI 163
Cdd:COG2129    1 KILAVSDLHGNFDLlekllelARAEDADLVILAGDLTDFGTAEEAREVLEELAALGV-PVLAVPGNHD---DPEVLDALE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627 164 KqdfyyfpsvsklkpenyenvqsllTNCIYLQDSEVTVRGFRIYGS------PWQPWFYgwgfnlPRGQALLEKW-NLIP 236
Cdd:COG2129   77 E------------------------SGVHNLHGRVVEIGGLRIAGLggsrptPFGTPYE------YTEEEIEERLaKLRE 126

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113204627 237 EGVDILITHGPPLGFLDWVPKKMQRVGCVELLNTVqRRVQPRLHVFGHIHEGYGVMADGTTTYVNAS 303
Cdd:COG2129  127 KDVDILLTHAPPYGTTLDRVEDGPHVGSKALRELI-EEFQPKLVLHGHIHESRGVDKIGGTRVVNPG 192
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
90-305 1.40e-11

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 63.17  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627  90 TRFVCVSDTHSRTDPIQMPYG--------------DVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYkIVIAGNHEltfD 155
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAEvlaaaladinaprpDFVVVTGDLTDDGEPEEYAAAREILARLGVPV-YVVPGNHD---I 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627 156 QEFMADLIKQDFYYFPSvsklKPENYenvqslltnciylqdsEVTVRGFRIYG--SPWQPWFYGWgfnLPRGQ-ALLEKW 232
Cdd:COG1409   77 RAAMAEAYREYFGDLPP----GGLYY----------------SFDYGGVRFIGldSNVPGRSSGE---LGPEQlAWLEEE 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113204627 233 -NLIPEGVDILITHGPPLGFLDWVPKKMQRvGCVELLNTVQRRvQPRLHVFGHIHEGYGVMADGTTTYVNASVC 305
Cdd:COG1409  134 lAAAPAKPVIVFLHHPPYSTGSGSDRIGLR-NAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTG 205
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 95-303 2.47e-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: 58.86  E-value: 2.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627  95 VSDTHSRTDPIQMPY-----GDVLIHAGDFTELGLPSEVKKFNEWLGSLpyeYKIVIA--GNheltFDQEFMADlikqdf 167
Cdd:cd07392    4 ISDVHGDVPKLKKIKlkaeeADAVIVAGDITHFGPGEEAIEALNLLLAI---GAPVLAvpGN----CDTPEVLG------ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627 168 yyfpsvsklkpenyenvqSLLTNCIYLQDSEVTVRGFRIYG------SPwqpwfygwgFNLPRG------QALLEKWNLI 235
Cdd:cd07392   71 ------------------ELNSAGLNIHGKVVEVGGYIFVGvggsnpTP---------FNTPFEyseeeiYSKLGLLNVK 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113204627 236 PEGVDILITHGPPLG-FLDWVPKkMQRVGCvELLNTVQRRVQPRLHVFGHIHEGYGVMADGTTTYVNAS 303
Cdd:cd07392  124 LPGRLILVTHAPPYGtAVDRVSS-GVHVGS-KAIRKFIEEFQPLLCICGHIHESRGIDKIGNTLVVNPG 190
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 240-302 3.10e-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: 3.10e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113204627 240 DILITHGPPLGFLDWVPKKMQRvgCVELLNTVQRRVQPRLHVFGHIHEGYGVMAD-GTTTYVNA 302
Cdd:cd00838   68 DILVTHGPPYDPLDEGSPGEDP--GSEALLELLDKYGPDLVLSGHTHVPGRREVDkGGTLVVNP 129
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 111-150 6.76e-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: 42.28  E-value: 6.76e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 113204627 111 DVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNH 150
Cdd:cd07400   32 DLVVVTGDLTQRARPAEFEEAREFLDALEPEPVVVVPGNH 71
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 93-154 1.93e-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: 1.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113204627  93 VCVSDTHSRTD---------PIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGSLPYEYKIVIAGNHELTF 154
Cdd:cd00838    1 LVISDIHGNLEaleavleaaLAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHDILV 71
MPP_DR1119 cd07393
Deinococcus radiodurans DR1119 and related proteins, metallophosphatase domain; DR1119 is an ...
 110-286 2.85e-04

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: 41.71  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627 110 GDVLIHAGDFTELGLPSEVKKFNEWLGSLPyEYKIVIAGNHEltfdqefmadlikqdfYYFPSVSKLKPENYENVQSLLT 189
Cdd:cd07393   43 EDIVLIPGDISWAMNLKEALKDLTWINDLP-GIKILLKGNHD----------------YWWPSKSKARRALEEEFLALKF 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113204627 190 NCIYLqDSEVTVRGFRIYGSPWQPWFYGWGFNLPRG----------QALLEKWNLI--------PEGVDILITHGPPL-- 249
Cdd:cd07393  106 HKAYI-DDKVVVGGTRLWDNPYNCWPIINKQLKEETlkveiderccQRELERLNFAlkamnelrEDKIKILMLHHPPAne 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 113204627 250 -GFLDWVPKKMQRVGcvellntvqrrvqPRLHVFGHIH 286
Cdd:cd07393  185 dGDINPIFKLILESR-------------VDICLFGHIH 209
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 91-155 4.82e-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: 4.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113204627   91 RFVCVSDTHSR---------TDPIQMPYG-DVLIHAGDFTELGLPSEvkKFNEWLGSL-PYEYKIVIAGNHELTFD 155
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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