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Conserved domains on  [gi|1498517846|gb|RMI94109|]
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Metallo-dependent phosphatase-like protein [Yarrowia lipolytica]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10169246)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 91-348 1.18e-162

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. Cdc1 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: 277370  Cd Length: 257  Bit Score: 459.56  E-value: 1.18e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846  91 ALVADPQLVDDHTYPGRPASMMRLTEFVVDNYLRRNWVYIQKNLVPDTTIFLGDLFDGGRAWKDDKWYPEFDRWNRIFSL 170
Cdd:cd08163     1 ALVADPQLVDDHTYPGRPWILNTLTEHFVDQYLRRNWRYLQKQLKPDSTFFLGDLFDGGREWADEYWKKEYFRFNRIFDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 171 DPGQDVIWSLPGNHDIGYGNEIVPLALKRFEKHFGPLSREFDRGNHTFVQIDTISMENKNDSRIYEPPKEFVDEFRASQP 250
Cdd:cd08163    81 KPLRKMIESLPGNHDIGFGNGVKLPVRQRFESYFGPTSRVIDVGNHTFVIVDTISLSNNDNPQVYQPAREFLHSFEAMKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 251 RDKPAIVLTHVPFYRSEaNSNCGRQREKGHKLSYTVGHQYQTQLEPDVTNGLLTALNPVLVYSGDDHDACHVTHPFVFNG 330
Cdd:cd08163   161 NSKPRILLTHVPLYRPP-NTSCGPLREKKTPLPYGYGYQYQNVLEPSLSESILKAINPVAAFSGDDHDYCEVVHEYQFDG 239

                         250
                  ....*....|....*...
gi 1498517846 331 KNQVAHEYTVKSISMAMG 348
Cdd:cd08163   240 KEGSAREITVKSISMAMG 257
 
Name Accession Description Interval E-value
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 91-348 1.18e-162

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. Cdc1 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: 277370  Cd Length: 257  Bit Score: 459.56  E-value: 1.18e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846  91 ALVADPQLVDDHTYPGRPASMMRLTEFVVDNYLRRNWVYIQKNLVPDTTIFLGDLFDGGRAWKDDKWYPEFDRWNRIFSL 170
Cdd:cd08163     1 ALVADPQLVDDHTYPGRPWILNTLTEHFVDQYLRRNWRYLQKQLKPDSTFFLGDLFDGGREWADEYWKKEYFRFNRIFDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 171 DPGQDVIWSLPGNHDIGYGNEIVPLALKRFEKHFGPLSREFDRGNHTFVQIDTISMENKNDSRIYEPPKEFVDEFRASQP 250
Cdd:cd08163    81 KPLRKMIESLPGNHDIGFGNGVKLPVRQRFESYFGPTSRVIDVGNHTFVIVDTISLSNNDNPQVYQPAREFLHSFEAMKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 251 RDKPAIVLTHVPFYRSEaNSNCGRQREKGHKLSYTVGHQYQTQLEPDVTNGLLTALNPVLVYSGDDHDACHVTHPFVFNG 330
Cdd:cd08163   161 NSKPRILLTHVPLYRPP-NTSCGPLREKKTPLPYGYGYQYQNVLEPSLSESILKAINPVAAFSGDDHDYCEVVHEYQFDG 239

                         250
                  ....*....|....*...
gi 1498517846 331 KNQVAHEYTVKSISMAMG 348
Cdd:cd08163   240 KEGSAREITVKSISMAMG 257
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
136-266 9.26e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 52.77  E-value: 9.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 136 PDTTIFLGDLFDGGRAwkddkwyPEFDRWNRIfsLDPGQDVIWSLPGNHDIGYGNEivplalKRFEKHFGPLSRE----- 210
Cdd:COG1409    35 PDFVVVTGDLTDDGEP-------EEYAAAREI--LARLGVPVYVVPGNHDIRAAMA------EAYREYFGDLPPGglyys 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1498517846 211 FDRGNHTFVQIDTiSMENKNDSRIYEPPKEFVDEfRASQPRDKPAIVLTHVPFYRS 266
Cdd:COG1409   100 FDYGGVRFIGLDS-NVPGRSSGELGPEQLAWLEE-ELAAAPAKPVIVFLHHPPYST 153
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 121-225 7.97e-03

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: 36.42  E-value: 7.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 121 NYLRRNWVYIQKNLVPDTTIFLGDLFDGGRawKDDKWYPEFDRwnrifsLDPGQDVIWsLPGNHDIGYGNeivplaLKRF 200
Cdd:pfam00149  16 DDLLELLKKLLEEGKPDLVLHAGDLVDRGP--PSEEVLELLER------LIKYVPVYL-VRGNHDFDYGE------CLRL 80

                          90       100
                  ....*....|....*....|....*
gi 1498517846 201 EKHFGPLSREFDRGNHTFVQIDTIS 225
Cdd:pfam00149  81 YPYLGLLARPWKRFLEVFNFLPLAG 105
 
Name Accession Description Interval E-value
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 91-348 1.18e-162

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. Cdc1 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: 277370  Cd Length: 257  Bit Score: 459.56  E-value: 1.18e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846  91 ALVADPQLVDDHTYPGRPASMMRLTEFVVDNYLRRNWVYIQKNLVPDTTIFLGDLFDGGRAWKDDKWYPEFDRWNRIFSL 170
Cdd:cd08163     1 ALVADPQLVDDHTYPGRPWILNTLTEHFVDQYLRRNWRYLQKQLKPDSTFFLGDLFDGGREWADEYWKKEYFRFNRIFDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 171 DPGQDVIWSLPGNHDIGYGNEIVPLALKRFEKHFGPLSREFDRGNHTFVQIDTISMENKNDSRIYEPPKEFVDEFRASQP 250
Cdd:cd08163    81 KPLRKMIESLPGNHDIGFGNGVKLPVRQRFESYFGPTSRVIDVGNHTFVIVDTISLSNNDNPQVYQPAREFLHSFEAMKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 251 RDKPAIVLTHVPFYRSEaNSNCGRQREKGHKLSYTVGHQYQTQLEPDVTNGLLTALNPVLVYSGDDHDACHVTHPFVFNG 330
Cdd:cd08163   161 NSKPRILLTHVPLYRPP-NTSCGPLREKKTPLPYGYGYQYQNVLEPSLSESILKAINPVAAFSGDDHDYCEVVHEYQFDG 239

                         250
                  ....*....|....*...
gi 1498517846 331 KNQVAHEYTVKSISMAMG 348
Cdd:cd08163   240 KEGSAREITVKSISMAMG 257
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 91-348 2.23e-43

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. This group also contains Saccharomyces cerevisiae TED1 (Trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), which acts together with Emp24p and Erv25p in cargo exit from the ER, and human MPPE1. The human MPPE1 gene is a candidate susceptibility gene for bipolar disorder. These proteins 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: 277330 [Multi-domain]  Cd Length: 172  Bit Score: 150.58  E-value: 2.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846  91 ALVADPQLVDDHTYPGRPASMMRLTEFVVDNYLRRNWVYIQKNLVPDTTIFLGDLFDGGRAWKDDKWYPEFDRWNRIFSL 170
Cdd:cd07384     1 LLIADPQILDETSYPPRPKPALRLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 171 DPGQDV----IWSLPGNHDIGYGNEIV-PLALKRFEKHFgplsrefdrgnhtfvqidtismenkndsriyeppkefvdef 245
Cdd:cd07384    81 KSPGSLgsipVIFIPGNHDIGYGGEAVfPEKVDRFEKYF----------------------------------------- 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 246 rasqprdkpaIVLTHVPFYRseansncgrqrekghklsytvghqyqtqlepdvtngLLTALNPVLVYSGDDHDACHVTHp 325
Cdd:cd07384   120 ----------ILLTHIPLYR------------------------------------LLDSIKPVLILSGHDHDYCEVVH- 152

                         250       260
                  ....*....|....*....|...
gi 1498517846 326 fvfNGKNQVAHEYTVKSISMAMG 348
Cdd:cd07384   153 ---KSSPGSVKEITVKSFSWRMG 172
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 92-208 5.89e-16

uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; A functionally uncharacterized subgroup related to the metallophosphatase domain of Saccharomyces cerevisiae Cdc1, S. cerevisiae Ted1 and human MPPE1. Cdc1 is an endoplasmic reticulum-localized transmembrane lipid phosphatase and is a subunit of DNA polymerase delta. TED1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), acts together with Emp24p and Erv25p in cargo exit from the ER. The MPPE1 gene is a candidate susceptibility gene for Bipolar disorder. Proteins in this uncharacterized subgroup 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: 277373  Cd Length: 195  Bit Score: 75.94  E-value: 5.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846  92 LVADPQLV-DDHTYPGrpasMMRLTEFVVDNYLRRNWVYIQKNLVPDTTIFLGDLFDGGRAWKDDKWYPEFDRWNRIFSL 170
Cdd:cd08166     2 LVADPQILgYENEKFG----LGEISRWDSDRYLAKTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQRFIGIFPL 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1498517846 171 DPGQDVIWsLPGNHDIGYGNEIV-PLALKRFEKHFGPLS 208
Cdd:cd08166    78 KRGKNAIY-IPGDNDIGGESEIIiESRVRRFNNYFIMLS 115
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 93-348 6.56e-14

Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces cerevisiae Ted1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1) is a metallophosphatase domain-containing protein which acts together with Emp24p and Erv25p in cargo exit from the ER. Ted1 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: 277371  Cd Length: 193  Bit Score: 70.21  E-value: 6.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846  93 VADPQLVDDHTYPgRPASMMRLTEFVVDNYLRRNWVYIQKNLVPDTTIFLGDLFdgGRAWKDDKwypEFDR-----WNRI 167
Cdd:cd08164     3 LGDPQIEGDWPIT-NYGFKGRLDIFGNDYFLGHIYQMMQFRLKPTHVTVLGDLF--SSQWITDE---EFEKradryKKRI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 168 FSLDPGQD---------------VIWSLPGNHDIGYGNEIVPLALKRFEKHFgplsrefdrgnhtfvqidtismenknds 232
Cdd:cd08164    77 FGRSDWQVgnislaartfengdiLLINIAGNHDVGYAGESTEARISRFEQLF---------------------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 233 riyeppkefvdefrasqprdkpaIVLTHVPFYRSEANSncgrqrekghklsytvghqyqtqlepdvtnglltalNPVLVY 312
Cdd:cd08164   129 -----------------------ILLTHVPLYKFFLEG------------------------------------KPGLIL 149

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1498517846 313 SGDDHDACHVTHPFVFNGKNQV--------AHEYTVKSismAMG 348
Cdd:cd08164   150 TGHDHEGCDYEYPSNPSVTWATsleesgngVREYTVRS---MMG 190
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 123-324 2.79e-12

human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally uncharacterized metallophosphatase domain-containing protein. The MPPE1 gene is located on chromosome 18 and is a candidate susceptibility gene for Bipolar disorder. MPPE1 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: 277372 [Multi-domain]  Cd Length: 156  Bit Score: 64.40  E-value: 2.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 123 LRRNWVY---IQKN---LVPDTTIFLGDLFDGGRAWKDDKWYPEFDRWNRIFSLDPGQDVIwSLPGNHDIGYGNEIVPLA 196
Cdd:cd08165    20 LRREWQMeraFQTAlwlLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH-VVAGNHDIGFHYEMTTYK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 197 LKRFEKHFgplsrefdrgnhtfvqidtismenkndsriyeppkefvdefrasqprdkpaIVLTHVPFYRseansncgrqr 276
Cdd:cd08165    99 VHRFEKVF---------------------------------------------------ILLQHYPLYR----------- 116

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1498517846 277 ekghklsytvghqyqtqlepdvtngLLTALNPVLVYSGDDHDACHVTH 324
Cdd:cd08165   117 -------------------------LLQWLKPRLVLSGHTHSACEVLH 139
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
136-266 9.26e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 52.77  E-value: 9.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 136 PDTTIFLGDLFDGGRAwkddkwyPEFDRWNRIfsLDPGQDVIWSLPGNHDIGYGNEivplalKRFEKHFGPLSRE----- 210
Cdd:COG1409    35 PDFVVVTGDLTDDGEP-------EEYAAAREI--LARLGVPVYVVPGNHDIRAAMA------EAYREYFGDLPPGglyys 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1498517846 211 FDRGNHTFVQIDTiSMENKNDSRIYEPPKEFVDEfRASQPRDKPAIVLTHVPFYRS 266
Cdd:COG1409   100 FDYGGVRFIGLDS-NVPGRSSGELGPEQLAWLEE-ELAAAPAKPVIVFLHHPPYST 153
COG1407 COG1407
Metallophosphoesterase superfamily enzyme [General function prediction only];
136-187 2.98e-05

Metallophosphoesterase superfamily enzyme [General function prediction only];


Pssm-ID: 441017  Cd Length: 224  Bit Score: 45.25  E-value: 2.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1498517846 136 PDTTIFLGDLFDGgRAWKDDKWYPEFDRWnriFSLDPGQDVIWsLPGNHDIG 187
Cdd:COG1407    67 PDRLIILGDLFHD-FGGPSRQEWEELERL---LALHAGVEVIL-VRGNHDPG 113
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 125-271 4.34e-05

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: 44.58  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 125 RNWVYIQKNLVPDTTIFLGDLFDGGRawKDDKWYPEFDRWNRifsLDPGqdvIWSLPGNHDigYGNEIVPLALKRFEKH- 203
Cdd:cd07385    22 QKVVRKVNELNPDLIVITGDLVDGDV--SVLRLLASPLSKLK---APLG---VYFVLGNHD--YYSGDVEVWIAALEKAg 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1498517846 204 FGPL---SREFDRGNHTfVQIDTIsmenknDSRIYEPPKEFVDEFRASQPRDKPAIVLTHVPFYRSEANSN 271
Cdd:cd07385    92 ITVLrneSVELSRDGAT-IGLAGS------GVDDIGGHGEDLEKALKGLDENDPVILLAHNPDAAEEAQRP 155
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 121-225 7.97e-03

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: 36.42  E-value: 7.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498517846 121 NYLRRNWVYIQKNLVPDTTIFLGDLFDGGRawKDDKWYPEFDRwnrifsLDPGQDVIWsLPGNHDIGYGNeivplaLKRF 200
Cdd:pfam00149  16 DDLLELLKKLLEEGKPDLVLHAGDLVDRGP--PSEEVLELLER------LIKYVPVYL-VRGNHDFDYGE------CLRL 80

                          90       100
                  ....*....|....*....|....*
gi 1498517846 201 EKHFGPLSREFDRGNHTFVQIDTIS 225
Cdd:pfam00149  81 YPYLGLLARPWKRFLEVFNFLPLAG 105
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 119-186 8.54e-03

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: 36.48  E-value: 8.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1498517846 119 VDNYLRRNWVYIQKNLVPDTTIFLGDLFDGGRawkddkwYPEFDRWNRIFSLDPGQDVIWsLPGNHDI 186
Cdd:cd00838    10 LEALEAVLEAALAKAEKPDLVICLGDLVDYGP-------DPEEVELKALRLLLAGIPVYV-VPGNHDI 69
 
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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