NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958743436|ref|XP_038952910|]
View 

metallophosphoesterase 1 isoform X4 [Rattus norvegicus]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10169250)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)| bifunctional metallophosphatase/5'-nucleotidase contains an N-terminal metallophosphoesterase family domain that contains an active site consisting of two metal ions (usually manganese, iron, or zinc), and a 5'-nucleotidase C-terminal domain; similar to Escherichia coli UshA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 70-301 1.74e-77

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: 235.43  E-value: 1.74e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  70 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSHVQLK 149
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 150 VVIGNHDIGFHYHFVMVNSVAMEgdgcticseaeaelreisrklncsqevqgssqcdheprlplSAPVLLQHYPLYRasd 229
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFE-----------------------------------------KVFILLQHYPLYR--- 116

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958743436 230 ancsgedaappeersvpfeekydvlsreasqkLLWWLRPRLILSGHTHSACEVLHPGGAPEVSVPSFSWRNR 301
Cdd:cd08165   117 --------------------------------LLQWLKPRLVLSGHTHSACEVLHYGGIPEISVPSFSWRNR 156
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 70-301 1.74e-77

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: 235.43  E-value: 1.74e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  70 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSHVQLK 149
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 150 VVIGNHDIGFHYHFVMVNSVAMEgdgcticseaeaelreisrklncsqevqgssqcdheprlplSAPVLLQHYPLYRasd 229
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFE-----------------------------------------KVFILLQHYPLYR--- 116

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958743436 230 ancsgedaappeersvpfeekydvlsreasqkLLWWLRPRLILSGHTHSACEVLHPGGAPEVSVPSFSWRNR 301
Cdd:cd08165   117 --------------------------------LLQWLKPRLVLSGHTHSACEVLHYGGIPEISVPSFSWRNR 156
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
72-306 3.57e-09

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 56.62  E-value: 3.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  72 LADTHLLGEIRGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQrmfrhgshVQLKVV 151
Cdd:COG1409     6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG--------VPVYVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 152 IGNHDI------------------GFHY-------HFVMVNSVAMEGDGCTICSE----AEAELREISRKLNcsqevqgs 202
Cdd:COG1409    71 PGNHDIraamaeayreyfgdlppgGLYYsfdyggvRFIGLDSNVPGRSSGELGPEqlawLEEELAAAPAKPV-------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 203 sqcdheprlplsapVLLQHYPLYRasdancsgedaappeerSVPFEEKYDVLSREASQKLLWWLRPRLILSGHTHSAcEV 282
Cdd:COG1409   143 --------------IVFLHHPPYS-----------------TGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRY-ER 190

                         250       260
                  ....*....|....*....|....
gi 1958743436 283 LHPGGAPEVSVPSFSWRNRNNPSF 306
Cdd:COG1409   191 TRRDGVPYIVAGSTGGQVRLPPGY 214
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 67-160 2.93e-05

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: 42.97  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  67 LKAMFLADTHLLGEIRG--HWLDKLRREwqmerafqtalwlLQPEVVFILGDVFDEGKWSsaqawaddlHRFQRMFRH-G 143
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDllELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS---------EEVLELLERlI 58

                          90
                  ....*....|....*..
gi 1958743436 144 SHVQLKVVIGNHDIGFH 160
Cdd:pfam00149  59 KYVPVYLVRGNHDFDYG 75
 
Name Accession Description Interval E-value
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 70-301 1.74e-77

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: 235.43  E-value: 1.74e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  70 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSHVQLK 149
Cdd:cd08165     1 MFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPSDTPLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 150 VVIGNHDIGFHYHFVMVNSVAMEgdgcticseaeaelreisrklncsqevqgssqcdheprlplSAPVLLQHYPLYRasd 229
Cdd:cd08165    81 VVAGNHDIGFHYEMTTYKVHRFE-----------------------------------------KVFILLQHYPLYR--- 116

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958743436 230 ancsgedaappeersvpfeekydvlsreasqkLLWWLRPRLILSGHTHSACEVLHPGGAPEVSVPSFSWRNR 301
Cdd:cd08165   117 --------------------------------LLQWLKPRLVLSGHTHSACEVLHYGGIPEISVPSFSWRNR 156
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 70-301 2.55e-44

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: 2.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  70 MFLADTHLLGEIRGHW-------LDKLRREWQMERAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRH 142
Cdd:cd07384     1 LLIADPQILDETSYPPrpkpalrLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 143 GS-----HVQLKVVIGNHDIGFHYhfvmvnsvamegdgcticseaEAELREISRKLNcsqevqgssqcdheprlplSAPV 217
Cdd:cd07384    81 KSpgslgSIPVIFIPGNHDIGYGG---------------------EAVFPEKVDRFE-------------------KYFI 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 218 LLQHYPLYRasdancsgedaappeersvpfeekydvlsreasqkLLWWLRPRLILSGHTHSACEVLH---PGGAPEVSVP 294
Cdd:cd07384   121 LLTHIPLYR-----------------------------------LLDSIKPVLILSGHDHDYCEVVHkssPGSVKEITVK 165


                  ....*..
gi 1958743436 295 SFSWRNR 301
Cdd:cd07384   166 SFSWRMG 172
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 61-298 1.22e-19

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: 87.07  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  61 GRQEPVLK-AMFLADTHLlgeirghwldklRREW-QMERAfqtalwlLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQR 138
Cdd:cd08163    16 GRPWILNTlTEHFVDQYL------------RRNWrYLQKQ-------LKPDSTFFLGDLFDGGREWADEYWKKEYFRFNR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 139 MFRHgSHVQLKVVI--GNHDIGF------------HYHFVMVNSVAMEG-------DGCTICSEAEAELREISRKLNCSQ 197
Cdd:cd08163    77 IFDP-KPLRKMIESlpGNHDIGFgngvklpvrqrfESYFGPTSRVIDVGnhtfvivDTISLSNNDNPQVYQPAREFLHSF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 198 EVQGSSQcdhEPRlplsapVLLQHYPLYRASDANCsgedaAPPEERSVPFEEKY-----DVLSREASQKLLWWLRPRLIL 272
Cdd:cd08163   156 EAMKVNS---KPR------ILLTHVPLYRPPNTSC-----GPLREKKTPLPYGYgyqyqNVLEPSLSESILKAINPVAAF 221

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958743436 273 SGHTHSACEVLHP-------GGAPEVSVPSFSW 298
Cdd:cd08163   222 SGDDHDYCEVVHEyqfdgkeGSAREITVKSISM 254
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
72-306 3.57e-09

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 56.62  E-value: 3.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  72 LADTHLLGEIRGHWLDKLRrewqmerAFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQrmfrhgshVQLKVV 151
Cdd:COG1409     6 ISDLHLGAPDGSDTAEVLA-------AALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG--------VPVYVV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 152 IGNHDI------------------GFHY-------HFVMVNSVAMEGDGCTICSE----AEAELREISRKLNcsqevqgs 202
Cdd:COG1409    71 PGNHDIraamaeayreyfgdlppgGLYYsfdyggvRFIGLDSNVPGRSSGELGPEqlawLEEELAAAPAKPV-------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 203 sqcdheprlplsapVLLQHYPLYRasdancsgedaappeerSVPFEEKYDVLSREASQKLLWWLRPRLILSGHTHSAcEV 282
Cdd:COG1409   143 --------------IVFLHHPPYS-----------------TGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRY-ER 190

                         250       260
                  ....*....|....*....|....
gi 1958743436 283 LHPGGAPEVSVPSFSWRNRNNPSF 306
Cdd:COG1409   191 TRRDGVPYIVAGSTGGQVRLPPGY 214
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 70-171 6.36e-09

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: 55.14  E-value: 6.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  70 MFLADTHLLGEIRGHWLDKLRREWQMER----AFQTALWLLQPEVVFILGDVFDEGKWSSAQAWADDLHRFQRMFRHGSH 145
Cdd:cd08166     1 LLVADPQILGYENEKFGLGEISRWDSDRylakTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQRFIGIFPLKRG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958743436 146 VQLKVVIGNHDIG-------------FHYHFVMVNSVAM 171
Cdd:cd08166    81 KNAIYIPGDNDIGgeseiiiesrvrrFNNYFIMLSHVPL 119
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 67-309 1.24e-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: 45.73  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  67 LKAMFLADTHLLGEIRGHWLDKLRREwqmerafqtaLWLLQPEVVFILGDVFDEGKWssaqawadDLHRFQRMFRhgshv 146
Cdd:cd07385     2 LRIVQLSDIHLGPFVGRTRLQKVVRK----------VNELNPDLIVITGDLVDGDVS--------VLRLLASPLS----- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 147 QLK------VVIGNHDIGFHYHFVMVNsvAMEGDGCTICsEAEAELREISRKLNCSQEVQGSSQCDHEP-------RLPL 213
Cdd:cd07385    59 KLKaplgvyFVLGNHDYYSGDVEVWIA--ALEKAGITVL-RNESVELSRDGATIGLAGSGVDDIGGHGEdlekalkGLDE 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436 214 SAPV-LLQHYPLYRasdancsgEDAAPPeersvpfeeKYDvlsreasqkllwwlrprLILSGHTHsacevlhpGGapEVS 292
Cdd:cd07385   136 NDPViLLAHNPDAA--------EEAQRP---------GVD-----------------LVLSGHTH--------GG--QIF 171

                         250
                  ....*....|....*..
gi 1958743436 293 VPSFSWRNRNNPSFIMG 309
Cdd:cd07385   172 PPNYGVLSKLGFPYDSG 188
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 67-160 2.93e-05

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: 42.97  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  67 LKAMFLADTHLLGEIRG--HWLDKLRREwqmerafqtalwlLQPEVVFILGDVFDEGKWSsaqawaddlHRFQRMFRH-G 143
Cdd:pfam00149   1 MRILVIGDLHLPGQLDDllELLKKLLEE-------------GKPDLVLHAGDLVDRGPPS---------EEVLELLERlI 58

                          90
                  ....*....|....*..
gi 1958743436 144 SHVQLKVVIGNHDIGFH 160
Cdd:pfam00149  59 KYVPVYLVRGNHDFDYG 75
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
73-156 9.61e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 43.36  E-value: 9.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  73 ADTHLlgeirghwlDKLRREWQMERAFQTAL-WLL------QPEVVFILGDVFDegkwsSAQAWADDLHRFQRMFRHGSH 145
Cdd:COG0420     7 ADWHL---------GKPLHGASRREDQLAALdRLVdlaieeKVDAVLIAGDLFD-----SANPSPEAVRLLAEALRRLSE 72

                          90
                  ....*....|...
gi 1958743436 146 VQLKVVI--GNHD 156
Cdd:COG0420    73 AGIPVVLiaGNHD 85
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 71-186 1.33e-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: 38.40  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  71 FLADTHLlgeiRGHWLDKLRREWQMERAfqtalwllQPEVVFILGDVFDEGKWSSAQAWADDLHRFqrmfrhgSHVQLKV 150
Cdd:cd00838     2 VISDIHG----NLEALEAVLEAALAKAE--------KPDLVICLGDLVDYGPDPEEVELKALRLLL-------AGIPVYV 62

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958743436 151 VIGNHDIGFhYHFVMVNSVAMEGDGCTICSEAEAEL 186
Cdd:cd00838    63 VPGNHDILV-THGPPYDPLDEGSPGEDPGSEALLEL 97
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 70-173 3.15e-03

Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. 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: 277337  Cd Length: 175  Bit Score: 38.06  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743436  70 MFLADTHLlG---EIRGHWLDKLRRewQMERAFQTALWLLQ---PEVVFILGDVFDEGKWSSAQAWADdlhrFQRMFRHG 143
Cdd:cd07391     1 LVIADLHL-GyeeELRRQGINLPRR--QKERLLERLDRLLEelgPDRLVILGDLKHSFGRVSRQERRE----VPFFRLLA 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958743436 144 SHVQLKVVIGNHDIGFHYHFVMVNSVAMEG 173
Cdd:cd07391    74 KDVDVILIRGNHDGGLEEILSDVNVVVVEG 103
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH