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Conserved domains on  [gi|446568165|ref|WP_000645511|]
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MULTISPECIES: metallophosphoesterase [Bacillus]

Protein Classification

metallophosphoesterase( domain architecture ID 10096151)

metallophosphoesterase contains 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_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-151 5.79e-39

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: 129.70  E-value: 5.79e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165   2 KALIVSDSHSSVKELQQLKEKYEGKVDIMIHCGDSE----LTSAHEELQGFHVVKGNCD--------YANFQDEIVTDVD 69
Cdd:cd00841    1 KIGVISDTHGNLEAIEKALELFEDGVDAVIHAGDFVspfvLNALLELKAPLIAVRGNNDgevdqllgRPILPEFLTLEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165  70 GIRFLVVHGHRHNVKMTLqtlaYHAEEVGAQVACFGHSHVLGAELIEGVLFINPGSILLPRQRvEKTFALLEMDEnqMEV 149
Cdd:cd00841   81 GLRILLTHGHLFGVLEAL----YLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTYAILDIEK--LEV 153


                 ..
gi 446568165 150 RF 151
Cdd:cd00841  154 EI 155
 
Name Accession Description Interval E-value
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-151 5.79e-39

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: 129.70  E-value: 5.79e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165   2 KALIVSDSHSSVKELQQLKEKYEGKVDIMIHCGDSE----LTSAHEELQGFHVVKGNCD--------YANFQDEIVTDVD 69
Cdd:cd00841    1 KIGVISDTHGNLEAIEKALELFEDGVDAVIHAGDFVspfvLNALLELKAPLIAVRGNNDgevdqllgRPILPEFLTLEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165  70 GIRFLVVHGHRHNVKMTLqtlaYHAEEVGAQVACFGHSHVLGAELIEGVLFINPGSILLPRQRvEKTFALLEMDEnqMEV 149
Cdd:cd00841   81 GLRILLTHGHLFGVLEAL----YLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTYAILDIEK--LEV 153


                 ..
gi 446568165 150 RF 151
Cdd:cd00841  154 EI 155
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-145 8.08e-37

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: 123.96  E-value: 8.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165    1 MKALIVSDSHSSVKELQQLKEKYEGKVDIMIHCGDSELTSAHEELQ---GFHVVKGNCDYAN-----FQDEIVTDVDGIR 72
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKGVVDLIIHAGDIVAPEVLEELLelaPVLAVRGNNDAAAefatdLPEEAVLELGGVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446568165   73 FLVVHGHrhNVKMTLQTLAYHAEEVGAqVACFGHSHVLGAELIEGVLFINPGSILLPRQRVEKTFALLEMDEN 145
Cdd:pfam12850  81 ILLTHGH--GVKDALARLLRRAEEGVA-VVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDIDDG 150
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-167 5.37e-32

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 112.70  E-value: 5.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165   2 KALIVSDSHSSVKELQQLKEKYEG-KVDIMIHCGDSELTSAH-----EELQ--GFHVVKGNCDYA------NFQDEIVTD 67
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEDLEReGVDLIVHLGDLVGYGPDppevlDLLRelPIVAVRGNHDGAvlrglrSLPETLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165  68 VDGIRFLVVHGHRHNV---KMTLQTLAYHAEEVGAQVACFGHSHVLGAELIEGVLFINPGSILLPRQRVEKTFALLEMDE 144
Cdd:COG0622   81 LEGVRILLVHGSPNEYllpDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDGDPASYAILDIDD 160

                        170       180
                 ....*....|....*....|...
gi 446568165 145 NQMEVRFETLDGqLVEQAVFKRG 167
Cdd:COG0622  161 GEWSVEFVRVPY-DIEAAIREAG 182
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-150 8.45e-31

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: 109.00  E-value: 8.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165    1 MKALIVSDSHSSVKELQQLKE--KYEGKVDIMIHCGDSE----LTSAHEELQGFHVVKGNCD--YANFQDEIVTDVDGIR 72
Cdd:TIGR00040   1 MKILVISDTHGPLRATELPVElfNLESNVDLVIHAGDLTspfvLKEFEDLAAKVIAVRGNNDgeRDELPEEEIFEAEGID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446568165   73 FLVVHGHRHNVKMTLQTLAYHAEEVGAQVACFGHSHVLGAELIEGVLFINPGSILLPRQRVEKTFALLEMDENQMEVR 150
Cdd:TIGR00040  81 FGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSYAILDVDKDKVTAL 158
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-159 9.25e-18

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 76.06  E-value: 9.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165   1 MKALIVSDSHSSVKELQQLKEKYE-GKVDIMIHCGD----------------SELTsahEELQGFHV----VKGNCD--- 56
Cdd:PRK09453   1 MKLMFASDTHGSLPATEKALELFAqSGADWLVHLGDvlyhgprnplpegyapKKVA---ELLNAYADkiiaVRGNCDsev 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165  57 ------YANFQDEIVTDVDGIRFLVVHGHRhnvkmtlqtlaYHAEEVGAQVAC----FGHSHVLGAELIEGVLFINPGSI 126
Cdd:PRK09453  78 dqmllhFPIMAPYQQVLLEGKRLFLTHGHL-----------YGPENLPALHDGdvlvYGHTHIPVAEKQGGIILFNPGSV 146

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446568165 127 LLPRQRVEKTFALLEMDenqmEVRFETLDGQLV 159
Cdd:PRK09453 147 SLPKGGYPASYGILDDN----VLSVIDLEGGEV 175
 
Name Accession Description Interval E-value
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 2-151 5.79e-39

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: 129.70  E-value: 5.79e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165   2 KALIVSDSHSSVKELQQLKEKYEGKVDIMIHCGDSE----LTSAHEELQGFHVVKGNCD--------YANFQDEIVTDVD 69
Cdd:cd00841    1 KIGVISDTHGNLEAIEKALELFEDGVDAVIHAGDFVspfvLNALLELKAPLIAVRGNNDgevdqllgRPILPEFLTLEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165  70 GIRFLVVHGHRHNVKMTLqtlaYHAEEVGAQVACFGHSHVLGAELIEGVLFINPGSILLPRQRvEKTFALLEMDEnqMEV 149
Cdd:cd00841   81 GLRILLTHGHLFGVLEAL----YLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTYAILDIEK--LEV 153


                 ..
gi 446568165 150 RF 151
Cdd:cd00841  154 EI 155
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 1-145 8.08e-37

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: 123.96  E-value: 8.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165    1 MKALIVSDSHSSVKELQQLKEKYEGKVDIMIHCGDSELTSAHEELQ---GFHVVKGNCDYAN-----FQDEIVTDVDGIR 72
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERLKGVVDLIIHAGDIVAPEVLEELLelaPVLAVRGNNDAAAefatdLPEEAVLELGGVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446568165   73 FLVVHGHrhNVKMTLQTLAYHAEEVGAqVACFGHSHVLGAELIEGVLFINPGSILLPRQRVEKTFALLEMDEN 145
Cdd:pfam12850  81 ILLTHGH--GVKDALARLLRRAEEGVA-VVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDIDDG 150
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-167 5.37e-32

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 112.70  E-value: 5.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165   2 KALIVSDSHSSVKELQQLKEKYEG-KVDIMIHCGDSELTSAH-----EELQ--GFHVVKGNCDYA------NFQDEIVTD 67
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEDLEReGVDLIVHLGDLVGYGPDppevlDLLRelPIVAVRGNHDGAvlrglrSLPETLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165  68 VDGIRFLVVHGHRHNV---KMTLQTLAYHAEEVGAQVACFGHSHVLGAELIEGVLFINPGSILLPRQRVEKTFALLEMDE 144
Cdd:COG0622   81 LEGVRILLVHGSPNEYllpDTPAERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDGDPASYAILDIDD 160

                        170       180
                 ....*....|....*....|...
gi 446568165 145 NQMEVRFETLDGqLVEQAVFKRG 167
Cdd:COG0622  161 GEWSVEFVRVPY-DIEAAIREAG 182
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 1-150 8.45e-31

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: 109.00  E-value: 8.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165    1 MKALIVSDSHSSVKELQQLKE--KYEGKVDIMIHCGDSE----LTSAHEELQGFHVVKGNCD--YANFQDEIVTDVDGIR 72
Cdd:TIGR00040   1 MKILVISDTHGPLRATELPVElfNLESNVDLVIHAGDLTspfvLKEFEDLAAKVIAVRGNNDgeRDELPEEEIFEAEGID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446568165   73 FLVVHGHRHNVKMTLQTLAYHAEEVGAQVACFGHSHVLGAELIEGVLFINPGSILLPRQRVEKTFALLEMDENQMEVR 150
Cdd:TIGR00040  81 FGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSYAILDVDKDKVTAL 158
PRK09453 PRK09453
phosphodiesterase; Provisional
 1-159 9.25e-18

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 76.06  E-value: 9.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165   1 MKALIVSDSHSSVKELQQLKEKYE-GKVDIMIHCGD----------------SELTsahEELQGFHV----VKGNCD--- 56
Cdd:PRK09453   1 MKLMFASDTHGSLPATEKALELFAqSGADWLVHLGDvlyhgprnplpegyapKKVA---ELLNAYADkiiaVRGNCDsev 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165  57 ------YANFQDEIVTDVDGIRFLVVHGHRhnvkmtlqtlaYHAEEVGAQVAC----FGHSHVLGAELIEGVLFINPGSI 126
Cdd:PRK09453  78 dqmllhFPIMAPYQQVLLEGKRLFLTHGHL-----------YGPENLPALHDGdvlvYGHTHIPVAEKQGGIILFNPGSV 146

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446568165 127 LLPRQRVEKTFALLEMDenqmEVRFETLDGQLV 159
Cdd:PRK09453 147 SLPKGGYPASYGILDDN----VLSVIDLEGGEV 175
MPP_Vps29 cd07394
Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting ...
 48-126 2.85e-09

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: 53.37  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165  48 FHVVKGNCD-YANFQDEIVTDVDGIRFLVVHGHRHNVKMTLQTLAYHAEEVGAQVACFGHSHVLGAELIEGVLFINPGSI 126
Cdd:cd07394   55 VHIVRGDFDeNLNYPETKVITVGQFKIGLIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSA 134
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 4-124 6.89e-05

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: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446568165   4 LIVSDSHSSVKELQQLKEK---YEGKVDIMIHCGD----------SELTSAHEELQGF--HVVKGNCDyanfqdeivtdv 68
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAalaKAEKPDLVICLGDlvdygpdpeeVELKALRLLLAGIpvYVVPGNHD------------ 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446568165  69 dgirFLVVHGHRHNVKMTL--------QTLAYHAEEVGAQVACFGHSHVLGAELIE--GVLFINPG 124
Cdd:cd00838   69 ----ILVTHGPPYDPLDEGspgedpgsEALLELLDKYGPDLVLSGHTHVPGRREVDkgGTLVVNPG 130
 
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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