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Conserved domains on  [gi|489193561|ref|WP_003102894|]
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MULTISPECIES: metallophosphoesterase family protein [Pseudomonas]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10582454)

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

CATH:  3.60.21.10
Gene Ontology:  GO:0046872|GO:0042578
PubMed:  25837850
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 9-145 1.59e-44

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: 143.22  E-value: 1.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561    9 RIGLIADTHG--LLRPEALERLRGC-DQLIHAGDIGKPEILAELERLAPLSVVRGNNDTQ-DWAADIPERLLLKIGRLTL 84
Cdd:pfam12850   2 RIGIISDTHDnlALPEAALERLKGVvDLIIHAGDIVAPEVLEELLELAPVLAVRGNNDAAaEFATDLPEEAVLELGGVKI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489193561   85 YVLH------DLKRLdLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGSAGPRRFSLPIGIGVLEV 145
Cdd:pfam12850  82 LLTHghgvkdALARL-LRRAEEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDI 147
 
Name Accession Description Interval E-value
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 9-145 1.59e-44

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: 143.22  E-value: 1.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561    9 RIGLIADTHG--LLRPEALERLRGC-DQLIHAGDIGKPEILAELERLAPLSVVRGNNDTQ-DWAADIPERLLLKIGRLTL 84
Cdd:pfam12850   2 RIGIISDTHDnlALPEAALERLKGVvDLIIHAGDIVAPEVLEELLELAPVLAVRGNNDAAaEFATDLPEEAVLELGGVKI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489193561   85 YVLH------DLKRLdLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGSAGPRRFSLPIGIGVLEV 145
Cdd:pfam12850  82 LLTHghgvkdALARL-LRRAEEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDI 147
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
9-157 1.37e-38

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 129.27  E-value: 1.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561   9 RIGLIADTHGLLRP--EALERLR--GCDQLIHAGDIGK-----PEILAELERLaPLSVVRGNNDTQDWA--ADIPERLLL 77
Cdd:COG0622    1 KIAVISDTHGNLPAleAVLEDLEreGVDLIVHLGDLVGygpdpPEVLDLLREL-PIVAVRGNHDGAVLRglRSLPETLRL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561  78 KIGRLTLYVLH-----------DLKRLDLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGSAGPRRFSLPIGIGVLEVA 146
Cdd:COG0622   80 ELEGVRILLVHgspneyllpdtPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDGDPASYAILDID 159

                        170
                 ....*....|.
gi 489193561 147 GKKIEAELITL 157
Cdd:COG0622  160 DGEWSVEFVRV 170
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 9-155 8.31e-31

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: 108.51  E-value: 8.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561   9 RIGLIADTHG-LLRPE-ALERL-RGCDQLIHAGDIGKPEILAELERL-APLSVVRGNND----TQDWAADIPERLLLKIG 80
Cdd:cd00841    1 KIGVISDTHGnLEAIEkALELFeDGVDAVIHAGDFVSPFVLNALLELkAPLIAVRGNNDgevdQLLGRPILPEFLTLEIG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489193561  81 RLTLYVLH----DLKRLDLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGSAGPRRFSLPiGIGVLEVagKKIEAELI 155
Cdd:cd00841   81 GLRILLTHghlfGVLEALYLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGGRP-TYAILDI--EKLEVEII 156
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 9-153 8.09e-28

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: 100.91  E-value: 8.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561    9 RIGLIADTHGLLRP-----EALERLRGCDQLIHAGDIGKPEILAELERLA-PLSVVRGNNDtqDWAADIPERLLLKIGRL 82
Cdd:TIGR00040   2 KILVISDTHGPLRAtelpvELFNLESNVDLVIHAGDLTSPFVLKEFEDLAaKVIAVRGNND--GERDELPEEEIFEAEGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561   83 TLYVLH--------DLKRLDLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGS-AGPRRFSLPIgIGVLEVAGKKIEAE 153
Cdd:TIGR00040  80 DFGLVHgdlvyprgDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSlTGPRNGNTPS-YAILDVDKDKVTAL 158
PRK09453 PRK09453
phosphodiesterase; Provisional
 8-144 6.54e-14

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 65.66  E-value: 6.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561   8 LRIGLIADTHGLLRP--EALERLR--GCDQLIHAGDI---G---------KPEILAE-LERLA-PLSVVRGNNDtqdwaA 69
Cdd:PRK09453   1 MKLMFASDTHGSLPAteKALELFAqsGADWLVHLGDVlyhGprnplpegyAPKKVAElLNAYAdKIIAVRGNCD-----S 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561  70 DIPERLL----------LKIGRLTLYVLH-DLKRLDLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGSAgprrfSLPI 138
Cdd:PRK09453  76 EVDQMLLhfpimapyqqVLLEGKRLFLTHgHLYGPENLPALHDGDVLVYGHTHIPVAEKQGGIILFNPGSV-----SLPK 150

                        170
                 ....*....|.
gi 489193561 139 G-----IGVLE 144
Cdd:PRK09453 151 GgypasYGILD 161
 
Name Accession Description Interval E-value
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 9-145 1.59e-44

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: 143.22  E-value: 1.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561    9 RIGLIADTHG--LLRPEALERLRGC-DQLIHAGDIGKPEILAELERLAPLSVVRGNNDTQ-DWAADIPERLLLKIGRLTL 84
Cdd:pfam12850   2 RIGIISDTHDnlALPEAALERLKGVvDLIIHAGDIVAPEVLEELLELAPVLAVRGNNDAAaEFATDLPEEAVLELGGVKI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489193561   85 YVLH------DLKRLdLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGSAGPRRFSLPIGIGVLEV 145
Cdd:pfam12850  82 LLTHghgvkdALARL-LRRAEEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDI 147
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
9-157 1.37e-38

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 129.27  E-value: 1.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561   9 RIGLIADTHGLLRP--EALERLR--GCDQLIHAGDIGK-----PEILAELERLaPLSVVRGNNDTQDWA--ADIPERLLL 77
Cdd:COG0622    1 KIAVISDTHGNLPAleAVLEDLEreGVDLIVHLGDLVGygpdpPEVLDLLREL-PIVAVRGNHDGAVLRglRSLPETLRL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561  78 KIGRLTLYVLH-----------DLKRLDLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGSAGPRRFSLPIGIGVLEVA 146
Cdd:COG0622   80 ELEGVRILLVHgspneyllpdtPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDGDPASYAILDID 159

                        170
                 ....*....|.
gi 489193561 147 GKKIEAELITL 157
Cdd:COG0622  160 DGEWSVEFVRV 170
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 9-155 8.31e-31

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: 108.51  E-value: 8.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561   9 RIGLIADTHG-LLRPE-ALERL-RGCDQLIHAGDIGKPEILAELERL-APLSVVRGNND----TQDWAADIPERLLLKIG 80
Cdd:cd00841    1 KIGVISDTHGnLEAIEkALELFeDGVDAVIHAGDFVSPFVLNALLELkAPLIAVRGNNDgevdQLLGRPILPEFLTLEIG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489193561  81 RLTLYVLH----DLKRLDLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGSAGPRRFSLPiGIGVLEVagKKIEAELI 155
Cdd:cd00841   81 GLRILLTHghlfGVLEALYLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGGRP-TYAILDI--EKLEVEII 156
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 9-153 8.09e-28

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: 100.91  E-value: 8.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561    9 RIGLIADTHGLLRP-----EALERLRGCDQLIHAGDIGKPEILAELERLA-PLSVVRGNNDtqDWAADIPERLLLKIGRL 82
Cdd:TIGR00040   2 KILVISDTHGPLRAtelpvELFNLESNVDLVIHAGDLTSPFVLKEFEDLAaKVIAVRGNND--GERDELPEEEIFEAEGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561   83 TLYVLH--------DLKRLDLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGS-AGPRRFSLPIgIGVLEVAGKKIEAE 153
Cdd:TIGR00040  80 DFGLVHgdlvyprgDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSlTGPRNGNTPS-YAILDVDKDKVTAL 158
PRK09453 PRK09453
phosphodiesterase; Provisional
 8-144 6.54e-14

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 65.66  E-value: 6.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561   8 LRIGLIADTHGLLRP--EALERLR--GCDQLIHAGDI---G---------KPEILAE-LERLA-PLSVVRGNNDtqdwaA 69
Cdd:PRK09453   1 MKLMFASDTHGSLPAteKALELFAqsGADWLVHLGDVlyhGprnplpegyAPKKVAElLNAYAdKIIAVRGNCD-----S 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561  70 DIPERLL----------LKIGRLTLYVLH-DLKRLDLDPAAEGIDVVVAGHSHKPLKEERDGVLYLNPGSAgprrfSLPI 138
Cdd:PRK09453  76 EVDQMLLhfpimapyqqVLLEGKRLFLTHgHLYGPENLPALHDGDVLVYGHTHIPVAEKQGGIILFNPGSV-----SLPK 150

                        170
                 ....*....|.
gi 489193561 139 G-----IGVLE 144
Cdd:PRK09453 151 GgypasYGILD 161
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 8-113 2.88e-08

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: 49.13  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561    8 LRIGLIADTHGLLRPEALERL-------RGCDQLIHAGDI---GKP-----EILAELERLAPLSVVRGNNdtqDWAADIP 72
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDLLELlkklleeGKPDLVLHAGDLvdrGPPseevlELLERLIKYVPVYLVRGNH---DFDYGEC 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 489193561   73 ERLLLKIGRLTLYVLHDLKRLDLDPAAEgidvVVAGHSHKP 113
Cdd:pfam00149  78 LRLYPYLGLLARPWKRFLEVFNFLPLAG----ILSGHTHVP 114
MPP_Vps29 cd07394
Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting ...
 33-129 3.33e-07

Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting protein 29), also known as vacuolar membrane protein Pep11, is a subunit of the retromer complex which is responsible for the retrieval of mannose-6-phosphate receptors (MPRs) from the endosomes for retrograde transport back to the Golgi. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer complex assembly as well as a phosphatase with specificity for the cytoplasmic tail of the MPR. The retromer includes the following 5 subunits: Vps35, Vps26, Vps29, and a dimer of the sorting nexins Vps5 (Snx1), and Vps17 (Snx2). Vps29 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: 163637 [Multi-domain]  Cd Length: 178  Bit Score: 47.20  E-value: 3.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561  33 QLIHAGDIGKPEILAELERLAP-LSVVRGNNDTQdwaADIPERLLLKIGRLTLYVLH--------DLKRL-----DLDpa 98
Cdd:cd07394   32 HVLCTGNLCSKETYDYLKTIAPdVHIVRGDFDEN---LNYPETKVITVGQFKIGLIHghqvvpwgDPDSLaalqrQLD-- 106

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489193561  99 aegIDVVVAGHSHKPLKEERDGVLYLNPGSA 129
Cdd:cd07394  107 ---VDILISGHTHKFEAFEHEGKFFINPGSA 134
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
8-157 3.62e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 47.76  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561   8 LRIGLIADTH-----GLLRPEALERL------RGCDQLIHAGDI---GKPEILAELERL-----APLSVVRGNNDTQDWA 68
Cdd:COG1409    1 FRFAHISDLHlgapdGSDTAEVLAAAladinaPRPDFVVVTGDLtddGEPEEYAAAREIlarlgVPVYVVPGNHDIRAAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561  69 ADIPERLLLKIGRLTLYVLHD-------------------------LKRL--DLDPAAE--------------------- 100
Cdd:COG1409   81 AEAYREYFGDLPPGGLYYSFDyggvrfigldsnvpgrssgelgpeqLAWLeeELAAAPAkpvivflhhppystgsgsdri 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489193561 101 ---------------GIDVVVAGHSHKPLKEERDGVLYLNPGSAGPrRFSLPIGIGVLEVAGKKIEAELITL 157
Cdd:COG1409  161 glrnaeellallaryGVDLVLSGHVHRYERTRRDGVPYIVAGSTGG-QVRLPPGYRVIEVDGDGLTVEVRRV 231
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 11-127 6.15e-07

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: 46.11  E-value: 6.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561  11 GLIADTHGllRPEALERLRGC--------DQLIHAGDI----GKPE-----ILAELERLAPLSVVRGNNDTqdWAADIPE 73
Cdd:cd00838    1 LVISDIHG--NLEALEAVLEAalakaekpDLVICLGDLvdygPDPEevelkALRLLLAGIPVYVVPGNHDI--LVTHGPP 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489193561  74 RLLLKIGRLTLYVLHDLKRLDLDpaAEGIDVVVAGHSHKP--LKEERDGVLYLNPG 127
Cdd:cd00838   77 YDPLDEGSPGEDPGSEALLELLD--KYGPDLVLSGHTHVPgrREVDKGGTLVVNPG 130
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 9-113 9.09e-04

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: 37.22  E-value: 9.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193561   9 RIGLIADTHGLLRPEALERlrgCDQLIHAGDI---GKPEilaELErlaplsvvrgnnDTQDWAADIPERLLLKI-GRltl 84
Cdd:cd07379    1 RFVCISDTHSRHPTISIPD---GDVLIHAGDFtegGTPD---EVK------------KFLDWLKSLPHPHKIVIaGN--- 59

                         90       100
                 ....*....|....*....|....*....
gi 489193561  85 yvlHDLKrldLDPaaEGIDVVVaghSHKP 113
Cdd:cd07379   60 ---HDLT---LDP--EGTDILV---THGP 77
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 100-157 2.01e-03

2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms];


Pssm-ID: 440500 [Multi-domain]  Cd Length: 471  Bit Score: 37.53  E-value: 2.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489193561 100 EGIDVVVAGHSHKPLKEE---RDGVLYLNPGSAGprRFslpigIGVLEV----AGKKI---EAELITL 157
Cdd:COG0737  204 PGIDVILGGHTHTLLPEPvvvNGGTLIVQAGSYG--KY-----LGRLDLtlddDGGKVvsvSAELIPV 264
 
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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