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Conserved domains on  [gi|1045279779|gb|ANU64460|]
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hypothetical protein A4V02_12510 [Muribaculum intestinale]

Protein Classification

MetallophosN and MetallophosC domain-containing protein( domain architecture ID 12177660)

protein containing domains MetallophosN, CpdA, and MetallophosC

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MetallophosC pfam16370
C terminal of Calcineurin-like phosphoesterase; This is the C-terminal of Calcineurin-like ...
 359-523 5.01e-27

C terminal of Calcineurin-like phosphoesterase; This is the C-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.


:

Pssm-ID: 435306  Cd Length: 160  Bit Score: 107.00  E-value: 5.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 359 GGWWPAgfkPHMPNLPVCFDGAPWGFGIWDFASGTPHHIYKGFQLPTDFQIRAYDLNQVSIDdqdlstaylpGNSANKDV 438
Cdd:pfam16370   7 GAWWSG---LDENGIAICRDGTPNGYAVYEVDGNDYKWYYKATGEPEDYQMRIYAPGEVYRG----------AYYSGPNE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 439 VLANIWAYEPGCTVKMYENGRELTVKRVKTQDP-----YLIQKYLVPIKKEYTKWNsgmNPEETAHLFRAQASTADSPVT 513
Cdd:pfam16370  74 VVANVWNGDPGWKVEWYEDGKWMPMERVSGYDPlhiveWSAGYYTSESLPKGRRFA---SPKKSSHLWRAKLPSGAHTIE 150

                         170
                  ....*....|
gi 1045279779 514 IEFTDLSGRK 523
Cdd:pfam16370 151 VKATDRFGRT 160
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
135-366 7.06e-24

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


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 100.15  E-value: 7.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 135 IIAIADPQISNRCGdvellkNMIVPDVNRAIDSLKAKGTSPIVITlGDLICDVFVADgYGYTLDLFNKdfkVNAPLYHTM 214
Cdd:COG1409     3 FAHISDLHLGAPDG------SDTAEVLAAALADINAPRPDFVVVT-GDLTDDGEPEE-YAAAREILAR---LGVPVYVVP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 215 GNHDYDPFMTGDIpgLSNWLYIN-GPSYYSFNRGGAHFIVVNNMVYQEGT-ALKADQLDWIAKDLATIKDKtaPLFITMH 292
Cdd:COG1409    72 GNHDIRAAMAEAY--REYFGDLPpGGLYYSFDYGGVRFIGLDSNVPGRSSgELGPEQLAWLEEELAAAPAK--PVIVFLH 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045279779 293 -GIFLTYPEAEGVNVskvyrfdEGGPQLGALLSEFtNVK-VFSGHSHksHFQHTPEGNIREYNYAGANGGWW-PAGF 366
Cdd:COG1409   148 hPPYSTGSGSDRIGL-------RNAEELLALLARY-GVDlVLSGHVH--RYERTRRDGVPYIVAGSTGGQVRlPPGY 214
MetallophosN pfam16371
N terminal of Calcineurin-like phosphoesterase; This is the N-terminal of Calcineurin-like ...
 52-124 1.30e-18

N terminal of Calcineurin-like phosphoesterase; This is the N-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.


:

Pssm-ID: 435307  Cd Length: 73  Bit Score: 79.91  E-value: 1.30e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1045279779  52 TGTPLADVVVSDGYNLTTTDVNGKYIMKSEVALGYIFVSTPDGYEPAAfLDNNRPKFWQQVRKTNG-KSVDFIL 124
Cdd:pfam16371   1 NGKGLAGVVVSDGYNFTKTDANGRYTLPDDKKAKFVYISTPAGYEVPT-DDGITPRFYKPLDDKEKvKRYDFTL 73
 
Name Accession Description Interval E-value
MetallophosC pfam16370
C terminal of Calcineurin-like phosphoesterase; This is the C-terminal of Calcineurin-like ...
 359-523 5.01e-27

C terminal of Calcineurin-like phosphoesterase; This is the C-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.


Pssm-ID: 435306  Cd Length: 160  Bit Score: 107.00  E-value: 5.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 359 GGWWPAgfkPHMPNLPVCFDGAPWGFGIWDFASGTPHHIYKGFQLPTDFQIRAYDLNQVSIDdqdlstaylpGNSANKDV 438
Cdd:pfam16370   7 GAWWSG---LDENGIAICRDGTPNGYAVYEVDGNDYKWYYKATGEPEDYQMRIYAPGEVYRG----------AYYSGPNE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 439 VLANIWAYEPGCTVKMYENGRELTVKRVKTQDP-----YLIQKYLVPIKKEYTKWNsgmNPEETAHLFRAQASTADSPVT 513
Cdd:pfam16370  74 VVANVWNGDPGWKVEWYEDGKWMPMERVSGYDPlhiveWSAGYYTSESLPKGRRFA---SPKKSSHLWRAKLPSGAHTIE 150

                         170
                  ....*....|
gi 1045279779 514 IEFTDLSGRK 523
Cdd:pfam16370 151 VKATDRFGRT 160
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
135-366 7.06e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 100.15  E-value: 7.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 135 IIAIADPQISNRCGdvellkNMIVPDVNRAIDSLKAKGTSPIVITlGDLICDVFVADgYGYTLDLFNKdfkVNAPLYHTM 214
Cdd:COG1409     3 FAHISDLHLGAPDG------SDTAEVLAAALADINAPRPDFVVVT-GDLTDDGEPEE-YAAAREILAR---LGVPVYVVP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 215 GNHDYDPFMTGDIpgLSNWLYIN-GPSYYSFNRGGAHFIVVNNMVYQEGT-ALKADQLDWIAKDLATIKDKtaPLFITMH 292
Cdd:COG1409    72 GNHDIRAAMAEAY--REYFGDLPpGGLYYSFDYGGVRFIGLDSNVPGRSSgELGPEQLAWLEEELAAAPAK--PVIVFLH 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045279779 293 -GIFLTYPEAEGVNVskvyrfdEGGPQLGALLSEFtNVK-VFSGHSHksHFQHTPEGNIREYNYAGANGGWW-PAGF 366
Cdd:COG1409   148 hPPYSTGSGSDRIGL-------RNAEELLALLARY-GVDlVLSGHVH--RYERTRRDGVPYIVAGSTGGQVRlPPGY 214
MetallophosN pfam16371
N terminal of Calcineurin-like phosphoesterase; This is the N-terminal of Calcineurin-like ...
 52-124 1.30e-18

N terminal of Calcineurin-like phosphoesterase; This is the N-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.


Pssm-ID: 435307  Cd Length: 73  Bit Score: 79.91  E-value: 1.30e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1045279779  52 TGTPLADVVVSDGYNLTTTDVNGKYIMKSEVALGYIFVSTPDGYEPAAfLDNNRPKFWQQVRKTNG-KSVDFIL 124
Cdd:pfam16371   1 NGKGLAGVVVSDGYNFTKTDANGRYTLPDDKKAKFVYISTPAGYEVPT-DDGITPRFYKPLDDKEKvKRYDFTL 73
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 215-337 4.91e-12

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: 66.94  E-value: 4.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 215 GNHDYDP----------FMTGDIPGLSNwlYINGPSYYSFNRGGAHFIVVNNMVYQEGTALKADQLDWIAKDLATIKDKT 284
Cdd:cd00839    76 GNHEADYngstskikffMPGRGMPPSPS--GSTENLWYSFDVGPVHFISLSTETDFLKGDNISPQYDWLEADLAKVDRSR 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1045279779 285 APLFITM-H-GIFLTYPEAEGVNVSKVYRfdeggPQLGALLSEFtNVK-VFSGHSH 337
Cdd:cd00839   154 TPWIIVMgHrPMYCSNDDDADCIEGEKMR-----EALEDLFYKY-GVDlVLSGHVH 203
 
Name Accession Description Interval E-value
MetallophosC pfam16370
C terminal of Calcineurin-like phosphoesterase; This is the C-terminal of Calcineurin-like ...
 359-523 5.01e-27

C terminal of Calcineurin-like phosphoesterase; This is the C-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.


Pssm-ID: 435306  Cd Length: 160  Bit Score: 107.00  E-value: 5.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 359 GGWWPAgfkPHMPNLPVCFDGAPWGFGIWDFASGTPHHIYKGFQLPTDFQIRAYDLNQVSIDdqdlstaylpGNSANKDV 438
Cdd:pfam16370   7 GAWWSG---LDENGIAICRDGTPNGYAVYEVDGNDYKWYYKATGEPEDYQMRIYAPGEVYRG----------AYYSGPNE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 439 VLANIWAYEPGCTVKMYENGRELTVKRVKTQDP-----YLIQKYLVPIKKEYTKWNsgmNPEETAHLFRAQASTADSPVT 513
Cdd:pfam16370  74 VVANVWNGDPGWKVEWYEDGKWMPMERVSGYDPlhiveWSAGYYTSESLPKGRRFA---SPKKSSHLWRAKLPSGAHTIE 150

                         170
                  ....*....|
gi 1045279779 514 IEFTDLSGRK 523
Cdd:pfam16370 151 VKATDRFGRT 160
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
135-366 7.06e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 100.15  E-value: 7.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 135 IIAIADPQISNRCGdvellkNMIVPDVNRAIDSLKAKGTSPIVITlGDLICDVFVADgYGYTLDLFNKdfkVNAPLYHTM 214
Cdd:COG1409     3 FAHISDLHLGAPDG------SDTAEVLAAALADINAPRPDFVVVT-GDLTDDGEPEE-YAAAREILAR---LGVPVYVVP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 215 GNHDYDPFMTGDIpgLSNWLYIN-GPSYYSFNRGGAHFIVVNNMVYQEGT-ALKADQLDWIAKDLATIKDKtaPLFITMH 292
Cdd:COG1409    72 GNHDIRAAMAEAY--REYFGDLPpGGLYYSFDYGGVRFIGLDSNVPGRSSgELGPEQLAWLEEELAAAPAK--PVIVFLH 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1045279779 293 -GIFLTYPEAEGVNVskvyrfdEGGPQLGALLSEFtNVK-VFSGHSHksHFQHTPEGNIREYNYAGANGGWW-PAGF 366
Cdd:COG1409   148 hPPYSTGSGSDRIGL-------RNAEELLALLARY-GVDlVLSGHVH--RYERTRRDGVPYIVAGSTGGQVRlPPGY 214
MetallophosN pfam16371
N terminal of Calcineurin-like phosphoesterase; This is the N-terminal of Calcineurin-like ...
 52-124 1.30e-18

N terminal of Calcineurin-like phosphoesterase; This is the N-terminal of Calcineurin-like phosphoesterases. It is around 150 residues in length from various Bacteroides species. The function of this family is unknown.


Pssm-ID: 435307  Cd Length: 73  Bit Score: 79.91  E-value: 1.30e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1045279779  52 TGTPLADVVVSDGYNLTTTDVNGKYIMKSEVALGYIFVSTPDGYEPAAfLDNNRPKFWQQVRKTNG-KSVDFIL 124
Cdd:pfam16371   1 NGKGLAGVVVSDGYNFTKTDANGRYTLPDDKKAKFVYISTPAGYEVPT-DDGITPRFYKPLDDKEKvKRYDFTL 73
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 215-337 4.91e-12

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: 66.94  E-value: 4.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 215 GNHDYDP----------FMTGDIPGLSNwlYINGPSYYSFNRGGAHFIVVNNMVYQEGTALKADQLDWIAKDLATIKDKT 284
Cdd:cd00839    76 GNHEADYngstskikffMPGRGMPPSPS--GSTENLWYSFDVGPVHFISLSTETDFLKGDNISPQYDWLEADLAKVDRSR 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1045279779 285 APLFITM-H-GIFLTYPEAEGVNVSKVYRfdeggPQLGALLSEFtNVK-VFSGHSH 337
Cdd:cd00839   154 TPWIIVMgHrPMYCSNDDDADCIEGEKMR-----EALEDLFYKY-GVDlVLSGHVH 203
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 163-337 7.93e-11

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: 62.30  E-value: 7.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 163 RAIDSLKAKGTSP--IVITlGDLiCDVFVADGYGYTLDLFNKdfkVNAPLYHTMGNHDYDPFMtgdIPGLSNWLYI-NGP 239
Cdd:cd07402    28 AAVAQVNALHPRPdlVVVT-GDL-SDDGSPESYERLRELLAP---LPAPVYWIPGNHDDRAAM---REALPEPPYDdNGP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 240 SYYSFNRGGAHFIVVNNMVY-QEGTALKADQLDWIAKDLATIKDKtaPLFITMH------GIfltyPEAEGVNVskvyrf 312
Cdd:cd07402   100 VQYVVDFGGWRLILLDTSVPgVHHGELSDEQLDWLEAALAEAPDR--PTLIFLHhppfplGI----PWMDAIRL------ 167

                         170       180
                  ....*....|....*....|....*.
gi 1045279779 313 dEGGPQLGALLSEFTNVK-VFSGHSH 337
Cdd:cd07402   168 -RNSQALFAVLARHPQVKaILCGHIH 192
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 163-338 3.86e-08

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: 54.26  E-value: 3.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 163 RAIDSLKAKGTSPIVITLGDLICDVFVADGYGYTLDLFNKDF-KVNAPLYHTMGNHDYDPF------MTGDIPGLSNwly 235
Cdd:cd07396    36 RAVEEWNRESNLAFVVQLGDIIDGYNAKDRSKEALDAVLSILdRLKGPVHHVLGNHEFYNFpreylnHLKTLNGEDA--- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 236 ingpSYYSFNRG-GAHFIVVNNMVYQEGtaLKADQLDWIAKDLATIKDKTAPLFITMHgiFLTYPEAEGvNVSKVYRFDE 314
Cdd:cd07396   113 ----YYYSFSPGpGFRFLVLDFVKFNGG--IGEEQLAWLRNELTSADANGEKVIVLSH--LPIYPEAAD-PQCLLWNYEE 183

                         170       180
                  ....*....|....*....|....*
gi 1045279779 315 ggpqLGALLSEFTNVK-VFSGHSHK 338
Cdd:cd07396   184 ----VLAILESYPCVKaCFSGHNHE 204
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 131-338 1.36e-06

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 50.01  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 131 NPLGIIAIADPQI----SNRCG--------DVELLKNMIvpdvnRAIDSLKAKgtsP-IVITLGDLICDVFVADGYgytl 197
Cdd:cd07395     3 GPFYFIQGADPQLglikQNNIGnggdewdkEIELTEQAV-----QAINKLNPK---PkFVVVCGDLVHAMPGEEFR---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 198 DLFNKDFK-------VNAPLYHTMGNHDydpfmTGDIP---GLSNWLYINGPSYYSFNRGGAHFIVVNNMVYQEGT---A 264
Cdd:cd07395    71 EQQVSDLKdvlskldPDIPLVCVCGNHD-----VGNTPtpeTIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSkvpE 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 265 LKADQLDWIAKDL--ATIKDKTAPLFITMHGIFLTYPEAEG--VNVSKVYRFDeggpqlgaLLSEFTN--VK-VFSGHSH 337
Cdd:cd07395   146 LASAQDQWLEEQLqiARESDAKHVVVFQHIPLFLEDPDEEDdyFNIPKSVRRE--------LLDKFKKagVKaVFSGHYH 217


                  .
gi 1045279779 338 K 338
Cdd:cd07395   218 R 218
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 195-348 4.71e-03

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase 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: 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: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 39.20  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 195 YTLDLFNKDFKvNAPLYHTMGNHDYDPFMTGDIPGLS-NWLY----------INGPSYYSFNRGG---------AHFIVV 254
Cdd:cd00842    98 NLTNLLKKYFP-NVPVYPALGNHDSYPVNQFPPHSNSpSWLYdalaelwkpwLPTEAKETFKKGGyysvdvkdgLRVISL 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045279779 255 NNMVY-------QEGTALKADQLDWIAKDLATIKDKTAPLFITMH---GIFLTYPeaegvNVSKVYRfdeggpqlgALLS 324
Cdd:cd00842   177 NTNLYykknfwlYSNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHippGLNSYDA-----DWSERFY---------QIIN 242

                         170       180
                  ....*....|....*....|....*.
gi 1045279779 325 EFTNVKV--FSGHSHKSHFQHTPEGN 348
Cdd:cd00842   243 RYSDTIAgqFFGHTHRDEFRVFYDDK 268
 
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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