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Conserved domains on  [gi|1264379983|ref|WP_097990196.1|]
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lamin tail domain-containing protein

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10747867)

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_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 1402-1657 5.82e-78

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.


The actual alignment was detected with superfamily member cd07399:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 207  Bit Score: 256.65  E-value: 5.82e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1402 YTFVWMSDTQYYSESYPYIYKSQVDWIAAQKDPLNIKYVFHTGDFVDKSyQEFQWQRADEYMKVLENAKVPYGVLAGNHD 1481
Cdd:cd07399      1 FTLVWLPDTQYYFELYPDILKAQTEWIVDERENKNIDFVFHTGDVTDHG-VDKEWEVAAAAFNVLDDSGVPYSVLAGNHD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1482 vnhkdedytayskyfgnwrfkdkpfygesykdnrghydlisvkgndfIMLYMGWGVTDEDIQWMKEVLQKYPNRKAILSF 1561
Cdd:cd07399     80 -----------------------------------------------LVLALGWGPSDEVLAWANEVLKKHPDRPAILNT 112

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1562 HEYLLVSGNRSP---IGDKIFNEVVKPNKNVLAVLSGHYHDSETLVDEiddnGDGIVDRKVYQMLADYQGGPEGGQGYMR 1638
Cdd:cd07399    113 HEYMLSDDGRMPegnIGERIWDELVKKNPNVFMVLSGHYHPAGRTTLV----GDGDAGRDVHQMLANYQGRPEGGQGYLR 188

                          250
                   ....*....|....*....
gi 1264379983 1639 LLQFDTIANKMYVKTYSPY 1657
Cdd:cd07399    189 LLDFDVKKQKVDVKTYSPY 207
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 340-418 6.04e-10

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


:

Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 58.20  E-value: 6.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264379983  340 VMITELMPDTINVNGkdgyEFIEIYNNSSEAIQLKDYKLIYKYSETgsedWNFTENATIPSKGTKVFWIKNEGNAALSK 418
Cdd:pfam00932    7 VVISEVVYDGSGGND----EFIELYNTGSKAVDLSGWKLQDASGGT----YTFPNGTTLAPGQTVVVWTGSGTNSATAG 77
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 615-751 4.15e-08

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


:

Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 52.81  E-value: 4.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983  615 PQSVPPFLITEVTPDttnvGKADGYEFIEVYNNSTQDLNFKDYTIRYRYPSEgpegdliwGSTPDDVVIPSGQSLVFWII 694
Cdd:pfam00932    1 SSATGDVVISEVVYD----GSGGNDEFIELYNTGSKAVDLSGWKLQDASGGT--------YTFPNGTTLAPGQTVVVWTG 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1264379983  695 NGENNEKTVADFNkqfgvnlvenknivriySNGMANGSARGIVVVTKTGTEIASAYY 751
Cdd:pfam00932   69 SGTNSATAGYWGP-----------------SNAVWNNGGDAVALYDANGELVDSVGY 108
 
Name Accession Description Interval E-value
MPP_YvnB cd07399
Bacillus subtilis YvnB and related proteins, metallophosphatase domain; YvnB (BSU35040) is an ...
 1402-1657 5.82e-78

Bacillus subtilis YvnB and related proteins, metallophosphatase domain; YvnB (BSU35040) is an uncharacterized Bacillus subtilis protein with a metallophosphatase domain. This family includes bacterial and eukaryotic proteins similar to YvnB. YvnB 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: 277344 [Multi-domain]  Cd Length: 207  Bit Score: 256.65  E-value: 5.82e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1402 YTFVWMSDTQYYSESYPYIYKSQVDWIAAQKDPLNIKYVFHTGDFVDKSyQEFQWQRADEYMKVLENAKVPYGVLAGNHD 1481
Cdd:cd07399      1 FTLVWLPDTQYYFELYPDILKAQTEWIVDERENKNIDFVFHTGDVTDHG-VDKEWEVAAAAFNVLDDSGVPYSVLAGNHD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1482 vnhkdedytayskyfgnwrfkdkpfygesykdnrghydlisvkgndfIMLYMGWGVTDEDIQWMKEVLQKYPNRKAILSF 1561
Cdd:cd07399     80 -----------------------------------------------LVLALGWGPSDEVLAWANEVLKKHPDRPAILNT 112

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1562 HEYLLVSGNRSP---IGDKIFNEVVKPNKNVLAVLSGHYHDSETLVDEiddnGDGIVDRKVYQMLADYQGGPEGGQGYMR 1638
Cdd:cd07399    113 HEYMLSDDGRMPegnIGERIWDELVKKNPNVFMVLSGHYHPAGRTTLV----GDGDAGRDVHQMLANYQGRPEGGQGYLR 188

                          250
                   ....*....|....*....
gi 1264379983 1639 LLQFDTIANKMYVKTYSPY 1657
Cdd:cd07399    189 LLDFDVKKQKVDVKTYSPY 207
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1402-1602 3.66e-19

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 88.59  E-value: 3.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1402 YTFVWMSDTQYYSESYPYIYKSqVDWIAAQKDPLNIKYVFHTGDFVDKSYQEfQWQRADEymkVLENAKVPYGVLAGNHD 1481
Cdd:COG1409      1 FRFAHISDLHLGAPDGSDTAEV-LAAALADINAPRPDFVVVTGDLTDDGEPE-EYAAARE---ILARLGVPVYVVPGNHD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1482 VNHKDEDytAYSKYFGnwrfkDKPFYGESYKDNRGHYDLISVKGNDFiMLYMGWgVTDEDIQWMKEVLQKYPNRKAILSF 1561
Cdd:COG1409     76 IRAAMAE--AYREYFG-----DLPPGGLYYSFDYGGVRFIGLDSNVP-GRSSGE-LGPEQLAWLEEELAAAPAKPVIVFL 146

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1264379983 1562 HEYLLVSG---NRSPIGD-KIFNEVVKPNkNVLAVLSGHYHDSET 1602
Cdd:COG1409    147 HHPPYSTGsgsDRIGLRNaEELLALLARY-GVDLVLSGHVHRYER 190
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 340-418 6.04e-10

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 58.20  E-value: 6.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264379983  340 VMITELMPDTINVNGkdgyEFIEIYNNSSEAIQLKDYKLIYKYSETgsedWNFTENATIPSKGTKVFWIKNEGNAALSK 418
Cdd:pfam00932    7 VVISEVVYDGSGGND----EFIELYNTGSKAVDLSGWKLQDASGGT----YTFPNGTTLAPGQTVVVWTGSGTNSATAG 77
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 615-751 4.15e-08

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 52.81  E-value: 4.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983  615 PQSVPPFLITEVTPDttnvGKADGYEFIEVYNNSTQDLNFKDYTIRYRYPSEgpegdliwGSTPDDVVIPSGQSLVFWII 694
Cdd:pfam00932    1 SSATGDVVISEVVYD----GSGGNDEFIELYNTGSKAVDLSGWKLQDASGGT--------YTFPNGTTLAPGQTVVVWTG 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1264379983  695 NGENNEKTVADFNkqfgvnlvenknivriySNGMANGSARGIVVVTKTGTEIASAYY 751
Cdd:pfam00932   69 SGTNSATAGYWGP-----------------SNAVWNNGGDAVALYDANGELVDSVGY 108
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1402-1517 1.31e-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: 46.05  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1402 YTFVWMSDTQYYSEsypyiYKSQVDWIAAQKDPLNIKYVFHTGDFVDKSYQEFQWQRADEYMKvlenAKVPYGVLAGNHD 1481
Cdd:pfam00149    1 MRILVIGDLHLPGQ-----LDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLI----KYVPVYLVRGNHD 71

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1264379983 1482 VNHKD--EDYTAYSKYFGNWRFKDKPFYGESYKDN-RGH 1517
Cdd:pfam00149   72 FDYGEclRLYPYLGLLARPWKRFLEVFNFLPLAGIlSGH 110
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 1538-1624 6.40e-03

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 40.69  E-value: 6.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1538 TDEDIQWMKEVLQKYPNRKAILSFHEYLLVSGnrSPIGDK-------IFNEVVKPNKNVLAVLSGHYHdsetlvDEIDDN 1610
Cdd:PRK11148   140 SEYQLEWLERKLADAPERHTLVLLHHHPLPAG--CAWLDQhslrnahELAEVLAKFPNVKAILCGHIH------QELDLD 211

                           90
                   ....*....|....
gi 1264379983 1611 GDGivdrkvYQMLA 1624
Cdd:PRK11148   212 WNG------RRLLA 219
 
Name Accession Description Interval E-value
MPP_YvnB cd07399
Bacillus subtilis YvnB and related proteins, metallophosphatase domain; YvnB (BSU35040) is an ...
 1402-1657 5.82e-78

Bacillus subtilis YvnB and related proteins, metallophosphatase domain; YvnB (BSU35040) is an uncharacterized Bacillus subtilis protein with a metallophosphatase domain. This family includes bacterial and eukaryotic proteins similar to YvnB. YvnB 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: 277344 [Multi-domain]  Cd Length: 207  Bit Score: 256.65  E-value: 5.82e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1402 YTFVWMSDTQYYSESYPYIYKSQVDWIAAQKDPLNIKYVFHTGDFVDKSyQEFQWQRADEYMKVLENAKVPYGVLAGNHD 1481
Cdd:cd07399      1 FTLVWLPDTQYYFELYPDILKAQTEWIVDERENKNIDFVFHTGDVTDHG-VDKEWEVAAAAFNVLDDSGVPYSVLAGNHD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1482 vnhkdedytayskyfgnwrfkdkpfygesykdnrghydlisvkgndfIMLYMGWGVTDEDIQWMKEVLQKYPNRKAILSF 1561
Cdd:cd07399     80 -----------------------------------------------LVLALGWGPSDEVLAWANEVLKKHPDRPAILNT 112

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1562 HEYLLVSGNRSP---IGDKIFNEVVKPNKNVLAVLSGHYHDSETLVDEiddnGDGIVDRKVYQMLADYQGGPEGGQGYMR 1638
Cdd:cd07399    113 HEYMLSDDGRMPegnIGERIWDELVKKNPNVFMVLSGHYHPAGRTTLV----GDGDAGRDVHQMLANYQGRPEGGQGYLR 188

                          250
                   ....*....|....*....
gi 1264379983 1639 LLQFDTIANKMYVKTYSPY 1657
Cdd:cd07399    189 LLDFDVKKQKVDVKTYSPY 207
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1402-1602 3.66e-19

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 88.59  E-value: 3.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1402 YTFVWMSDTQYYSESYPYIYKSqVDWIAAQKDPLNIKYVFHTGDFVDKSYQEfQWQRADEymkVLENAKVPYGVLAGNHD 1481
Cdd:COG1409      1 FRFAHISDLHLGAPDGSDTAEV-LAAALADINAPRPDFVVVTGDLTDDGEPE-EYAAARE---ILARLGVPVYVVPGNHD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1482 VNHKDEDytAYSKYFGnwrfkDKPFYGESYKDNRGHYDLISVKGNDFiMLYMGWgVTDEDIQWMKEVLQKYPNRKAILSF 1561
Cdd:COG1409     76 IRAAMAE--AYREYFG-----DLPPGGLYYSFDYGGVRFIGLDSNVP-GRSSGE-LGPEQLAWLEEELAAAPAKPVIVFL 146

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1264379983 1562 HEYLLVSG---NRSPIGD-KIFNEVVKPNkNVLAVLSGHYHDSET 1602
Cdd:COG1409    147 HHPPYSTGsgsDRIGLRNaEELLALLARY-GVDLVLSGHVHRYER 190
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 340-418 6.04e-10

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 58.20  E-value: 6.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264379983  340 VMITELMPDTINVNGkdgyEFIEIYNNSSEAIQLKDYKLIYKYSETgsedWNFTENATIPSKGTKVFWIKNEGNAALSK 418
Cdd:pfam00932    7 VVISEVVYDGSGGND----EFIELYNTGSKAVDLSGWKLQDASGGT----YTFPNGTTLAPGQTVVVWTGSGTNSATAG 77
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 615-751 4.15e-08

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 52.81  E-value: 4.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983  615 PQSVPPFLITEVTPDttnvGKADGYEFIEVYNNSTQDLNFKDYTIRYRYPSEgpegdliwGSTPDDVVIPSGQSLVFWII 694
Cdd:pfam00932    1 SSATGDVVISEVVYD----GSGGNDEFIELYNTGSKAVDLSGWKLQDASGGT--------YTFPNGTTLAPGQTVVVWTG 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1264379983  695 NGENNEKTVADFNkqfgvnlvenknivriySNGMANGSARGIVVVTKTGTEIASAYY 751
Cdd:pfam00932   69 SGTNSATAGYWGP-----------------SNAVWNNGGDAVALYDANGELVDSVGY 108
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 1439-1598 5.71e-08

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 55.75  E-value: 5.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1439 YVFHTGDFVDksyqefqWQRADEY---MKVLENAKVPYGVLAGNHDvnhkdeDYTAYSKYFgnwrfKDKPfygesYKDNR 1515
Cdd:cd07402     42 LVVVTGDLSD-------DGSPESYerlRELLAPLPAPVYWIPGNHD------DRAAMREAL-----PEPP-----YDDNG 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1516 GHYDLISVKGNDFIML-------YMGWgVTDEDIQWMKEVLQKYPNRKAILSFHEYLLVSGnrSPIGDKI-------FNE 1581
Cdd:cd07402     99 PVQYVVDFGGWRLILLdtsvpgvHHGE-LSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLG--IPWMDAIrlrnsqaLFA 175

                          170
                   ....*....|....*..
gi 1264379983 1582 VVKPNKNVLAVLSGHYH 1598
Cdd:cd07402    176 VLARHPQVKAILCGHIH 192
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 1402-1598 2.59e-07

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 54.23  E-value: 2.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1402 YTFVWMSD---TQYYSesypyiyKSQVDWIAAQKDplNIKYVFHTGDFvdkSY---QEFQWqRADEYMKVLEN--AKVPY 1473
Cdd:cd00839      5 LKFAVFGDmgqNTNNS-------TNTLDHLEKELG--NYDAIIHVGDI---AYadgYNNGS-RWDTFMRQIEPlaSYVPY 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1474 GVLAGNHDVNHKDEDYTAYSKYFGNWRF------KDKPFYgeSYkdNRGhydliSVKgndFIML--YMGWGVTD---EDI 1542
Cdd:cd00839     72 MVAPGNHEADYNGSTSKIKFFMPGRGMPpspsgsTENLWY--SF--DVG-----PVH---FISLstETDFLKGDnisPQY 139

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1264379983 1543 QWMKEVLQKYpNRKA----ILSFHEYLLVSGNrsPIGDKIFNEVVKP------NKN-VLAVLSGHYH 1598
Cdd:cd00839    140 DWLEADLAKV-DRSRtpwiIVMGHRPMYCSND--DDADCIEGEKMREaledlfYKYgVDLVLSGHVH 203
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 1436-1606 6.10e-06

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 49.64  E-value: 6.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1436 NIKYVFHTGDFVDKSYQEFQWQRA-DEYMKVLENAKVPYGVLAGNHDVNHKDEDYTAYSKYFGnwrfKDKPFYgesykdn 1514
Cdd:cd07396     46 NLAFVVQLGDIIDGYNAKDRSKEAlDAVLSILDRLKGPVHHVLGNHEFYNFPREYLNHLKTLN----GEDAYY------- 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1515 rghYDLISVKGNDFIML----YMGwGVTDEDIQWMKEVLQ--KYPNRKAILSFHeYLLVSGNRSPIGDkIFN-----EVV 1583
Cdd:cd07396    115 ---YSFSPGPGFRFLVLdfvkFNG-GIGEEQLAWLRNELTsaDANGEKVIVLSH-LPIYPEAADPQCL-LWNyeevlAIL 188

                          170       180
                   ....*....|....*....|...
gi 1264379983 1584 KPNKNVLAVLSGHYHDSETLVDE 1606
Cdd:cd07396    189 ESYPCVKACFSGHNHEGGYEQDS 211
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1402-1517 1.31e-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: 46.05  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1402 YTFVWMSDTQYYSEsypyiYKSQVDWIAAQKDPLNIKYVFHTGDFVDKSYQEFQWQRADEYMKvlenAKVPYGVLAGNHD 1481
Cdd:pfam00149    1 MRILVIGDLHLPGQ-----LDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLI----KYVPVYLVRGNHD 71

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1264379983 1482 VNHKD--EDYTAYSKYFGNWRFKDKPFYGESYKDN-RGH 1517
Cdd:pfam00149   72 FDYGEclRLYPYLGLLARPWKRFLEVFNFLPLAGIlSGH 110
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 1405-1482 7.88e-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: 44.18  E-value: 7.88e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264379983 1405 VWMSDTQYYSESYPYIYKsqvdwiAAQKDPLNIKYVFHTGDFVDKSYQEFQWQRADEYmkvLENAKVPYGVLAGNHDV 1482
Cdd:cd00838      1 LVISDIHGNLEALEAVLE------AALAKAEKPDLVICLGDLVDYGPDPEEVELKALR---LLLAGIPVYVVPGNHDI 69
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 1538-1624 6.40e-03

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 40.69  E-value: 6.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379983 1538 TDEDIQWMKEVLQKYPNRKAILSFHEYLLVSGnrSPIGDK-------IFNEVVKPNKNVLAVLSGHYHdsetlvDEIDDN 1610
Cdd:PRK11148   140 SEYQLEWLERKLADAPERHTLVLLHHHPLPAG--CAWLDQhslrnahELAEVLAKFPNVKAILCGHIH------QELDLD 211

                           90
                   ....*....|....
gi 1264379983 1611 GDGivdrkvYQMLA 1624
Cdd:PRK11148   212 WNG------RRLLA 219
 
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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