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Conserved domains on  [gi|1040960989|ref|WP_065177583|]
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MULTISPECIES: calcineurin-like phosphoesterase family protein [Stenotrophomonas]

Protein Classification

CpdA and MetallophosC domain-containing protein( domain architecture ID 11708028)

protein containing domains Peptidase_M14NE-CP-C_like, 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 ...
 350-513 2.56e-43

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: 151.30  E-value: 2.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 350 NVGANCGAFWSGvKDAAGVPDsaMSDGTPKGYALLDVAGNgSYKLQYRVAGKPASEQIGLHAPKVLRQGAYP--AWGVYA 427
Cdd:pfam16370   1 NHGAACGAWWSG-LDENGIAI--CRDGTPNGYAVYEVDGN-DYKWYYKATGEPEDYQMRIYAPGEVYRGAYYsgPNEVVA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 428 NVYMGEDASVVEYRVDgGAWQPMKQVSQPDPRLMVENVADDL-ADSLRGYDRSPEATASPHLWRGALPTdlavGSHKVEV 506
Cdd:pfam16370  77 NVWNGDPGWKVEWYED-GKWMPMERVSGYDPLHIVEWSAGYYtSESLPKGRRFASPKKSSHLWRAKLPS----GAHTIEV 151


                  ....*..
gi 1040960989 507 RSTQPDG 513
Cdd:pfam16370 152 KATDRFG 158
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
140-390 9.91e-27

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


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 108.24  E-value: 9.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 140 LVFTDSQTASLKdiGYYQQSIVSPLVGQTKAR---MGTTLGDIVNDDLT-LYPAINKVTTSLGVPWFHVPGNHDLDFDAA 215
Cdd:COG1409     4 AHISDLHLGAPD--GSDTAEVLAAALADINAPrpdFVVVTGDLTDDGEPeEYAAAREILARLGVPVYVVPGNHDIRAAMA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 216 sdehslDSWRNIYGPDT-----YAVEEGGASFVFLDDVVYDpnarpKYVGGLREDQFAFLASYLKGlHKDRLLVLGMHIP 290
Cdd:COG1409    82 ------EAYREYFGDLPpgglyYSFDYGGVRFIGLDSNVPG-----RSSGELGPEQLAWLEEELAA-APAKPVIVFLHHP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 291 LFDAAPGRETFRHADRQRLFDLLKDFRNVLVLSGHSHTQQHVYhgkadgWNGdkpLHEYNVGANCGAFWsgvkdaagvpd 370
Cdd:COG1409   150 PYSTGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRYERTR------RDG---VPYIVAGSTGGQVR----------- 209

                         250       260
                  ....*....|....*....|
gi 1040960989 371 samsdgTPKGYALLDVAGNG 390
Cdd:COG1409   210 ------LPPGYRVIEVDGDG 223
Peptidase_M14NE-CP-C_like super family cl21470
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
 44-100 1.97e-10

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


The actual alignment was detected with superfamily member pfam16371:

Pssm-ID: 473874  Cd Length: 73  Bit Score: 56.79  E-value: 1.97e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1040960989  44 GLAGVQVSNGETIVKTAADGSYSLPVRDGQT-VFVIKPDAYSFPKATDGLPSFWRHFR 100
Cdd:pfam16371   4 GLAGVVVSDGYNFTKTDANGRYTLPDDKKAKfVYISTPAGYEVPTDDGITPRFYKPLD 61
 
Name Accession Description Interval E-value
MetallophosC pfam16370
C terminal of Calcineurin-like phosphoesterase; This is the C-terminal of Calcineurin-like ...
 350-513 2.56e-43

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: 151.30  E-value: 2.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 350 NVGANCGAFWSGvKDAAGVPDsaMSDGTPKGYALLDVAGNgSYKLQYRVAGKPASEQIGLHAPKVLRQGAYP--AWGVYA 427
Cdd:pfam16370   1 NHGAACGAWWSG-LDENGIAI--CRDGTPNGYAVYEVDGN-DYKWYYKATGEPEDYQMRIYAPGEVYRGAYYsgPNEVVA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 428 NVYMGEDASVVEYRVDgGAWQPMKQVSQPDPRLMVENVADDL-ADSLRGYDRSPEATASPHLWRGALPTdlavGSHKVEV 506
Cdd:pfam16370  77 NVWNGDPGWKVEWYED-GKWMPMERVSGYDPLHIVEWSAGYYtSESLPKGRRFASPKKSSHLWRAKLPS----GAHTIEV 151


                  ....*..
gi 1040960989 507 RSTQPDG 513
Cdd:pfam16370 152 KATDRFG 158
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
140-390 9.91e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 108.24  E-value: 9.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 140 LVFTDSQTASLKdiGYYQQSIVSPLVGQTKAR---MGTTLGDIVNDDLT-LYPAINKVTTSLGVPWFHVPGNHDLDFDAA 215
Cdd:COG1409     4 AHISDLHLGAPD--GSDTAEVLAAALADINAPrpdFVVVTGDLTDDGEPeEYAAAREILARLGVPVYVVPGNHDIRAAMA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 216 sdehslDSWRNIYGPDT-----YAVEEGGASFVFLDDVVYDpnarpKYVGGLREDQFAFLASYLKGlHKDRLLVLGMHIP 290
Cdd:COG1409    82 ------EAYREYFGDLPpgglyYSFDYGGVRFIGLDSNVPG-----RSSGELGPEQLAWLEEELAA-APAKPVIVFLHHP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 291 LFDAAPGRETFRHADRQRLFDLLKDFRNVLVLSGHSHTQQHVYhgkadgWNGdkpLHEYNVGANCGAFWsgvkdaagvpd 370
Cdd:COG1409   150 PYSTGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRYERTR------RDG---VPYIVAGSTGGQVR----------- 209

                         250       260
                  ....*....|....*....|
gi 1040960989 371 samsdgTPKGYALLDVAGNG 390
Cdd:COG1409   210 ------LPPGYRVIEVDGDG 223
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 177-327 2.74e-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: 63.84  E-value: 2.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 177 GDIVND-DLTLYPAINKVTTSLGVPWFHVPGNHDldFDAASDEHSLDSWRNIYGPDTYAVEEGGASFVFLDDVVYDPNAr 255
Cdd:cd07402    47 GDLSDDgSPESYERLRELLAPLPAPVYWIPGNHD--DRAAMREALPEPPYDDNGPVQYVVDFGGWRLILLDTSVPGVHH- 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040960989 256 pkyvGGLREDQFAFLASYLKGlHKDRLLVLGMHIPLFD-AAPGRETFRHADRQRLFDLLKDFRNV-LVLSGHSH 327
Cdd:cd07402   124 ----GELSDEQLDWLEAALAE-APDRPTLIFLHHPPFPlGIPWMDAIRLRNSQALFAVLARHPQVkAILCGHIH 192
MetallophosN pfam16371
N terminal of Calcineurin-like phosphoesterase; This is the N-terminal of Calcineurin-like ...
 44-100 1.97e-10

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: 56.79  E-value: 1.97e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1040960989  44 GLAGVQVSNGETIVKTAADGSYSLPVRDGQT-VFVIKPDAYSFPKATDGLPSFWRHFR 100
Cdd:pfam16371   4 GLAGVVVSDGYNFTKTDANGRYTLPDDKKAKfVYISTPAGYEVPTDDGITPRFYKPLD 61
 
Name Accession Description Interval E-value
MetallophosC pfam16370
C terminal of Calcineurin-like phosphoesterase; This is the C-terminal of Calcineurin-like ...
 350-513 2.56e-43

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: 151.30  E-value: 2.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 350 NVGANCGAFWSGvKDAAGVPDsaMSDGTPKGYALLDVAGNgSYKLQYRVAGKPASEQIGLHAPKVLRQGAYP--AWGVYA 427
Cdd:pfam16370   1 NHGAACGAWWSG-LDENGIAI--CRDGTPNGYAVYEVDGN-DYKWYYKATGEPEDYQMRIYAPGEVYRGAYYsgPNEVVA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 428 NVYMGEDASVVEYRVDgGAWQPMKQVSQPDPRLMVENVADDL-ADSLRGYDRSPEATASPHLWRGALPTdlavGSHKVEV 506
Cdd:pfam16370  77 NVWNGDPGWKVEWYED-GKWMPMERVSGYDPLHIVEWSAGYYtSESLPKGRRFASPKKSSHLWRAKLPS----GAHTIEV 151


                  ....*..
gi 1040960989 507 RSTQPDG 513
Cdd:pfam16370 152 KATDRFG 158
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
140-390 9.91e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 108.24  E-value: 9.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 140 LVFTDSQTASLKdiGYYQQSIVSPLVGQTKAR---MGTTLGDIVNDDLT-LYPAINKVTTSLGVPWFHVPGNHDLDFDAA 215
Cdd:COG1409     4 AHISDLHLGAPD--GSDTAEVLAAALADINAPrpdFVVVTGDLTDDGEPeEYAAAREILARLGVPVYVVPGNHDIRAAMA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 216 sdehslDSWRNIYGPDT-----YAVEEGGASFVFLDDVVYDpnarpKYVGGLREDQFAFLASYLKGlHKDRLLVLGMHIP 290
Cdd:COG1409    82 ------EAYREYFGDLPpgglyYSFDYGGVRFIGLDSNVPG-----RSSGELGPEQLAWLEEELAA-APAKPVIVFLHHP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 291 LFDAAPGRETFRHADRQRLFDLLKDFRNVLVLSGHSHTQQHVYhgkadgWNGdkpLHEYNVGANCGAFWsgvkdaagvpd 370
Cdd:COG1409   150 PYSTGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRYERTR------RDG---VPYIVAGSTGGQVR----------- 209

                         250       260
                  ....*....|....*....|
gi 1040960989 371 samsdgTPKGYALLDVAGNG 390
Cdd:COG1409   210 ------LPPGYRVIEVDGDG 223
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 177-327 2.74e-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: 63.84  E-value: 2.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 177 GDIVND-DLTLYPAINKVTTSLGVPWFHVPGNHDldFDAASDEHSLDSWRNIYGPDTYAVEEGGASFVFLDDVVYDPNAr 255
Cdd:cd07402    47 GDLSDDgSPESYERLRELLAPLPAPVYWIPGNHD--DRAAMREALPEPPYDDNGPVQYVVDFGGWRLILLDTSVPGVHH- 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040960989 256 pkyvGGLREDQFAFLASYLKGlHKDRLLVLGMHIPLFD-AAPGRETFRHADRQRLFDLLKDFRNV-LVLSGHSH 327
Cdd:cd07402   124 ----GELSDEQLDWLEAALAE-APDRPTLIFLHHPPFPlGIPWMDAIRLRNSQALFAVLARHPQVkAILCGHIH 192
MetallophosN pfam16371
N terminal of Calcineurin-like phosphoesterase; This is the N-terminal of Calcineurin-like ...
 44-100 1.97e-10

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: 56.79  E-value: 1.97e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1040960989  44 GLAGVQVSNGETIVKTAADGSYSLPVRDGQT-VFVIKPDAYSFPKATDGLPSFWRHFR 100
Cdd:pfam16371   4 GLAGVVVSDGYNFTKTDANGRYTLPDDKKAKfVYISTPAGYEVPTDDGITPRFYKPLD 61
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 196-331 6.31e-09

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 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: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 57.34  E-value: 6.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 196 SLGVPWFHVPGNHDL--DFDAASDEHSLD-SWRNIYgPDTYAVEEGG-------ASFVFLDDVVY--------DPNARPK 257
Cdd:cd07378    72 SLQVPWYLVLGNHDHrgNVSAQIAYTQRPnSKRWNF-PNYYYDISFKfpssdvtVAFIMIDTVLLcgntddeaSGQPRGP 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040960989 258 YVGGLREDQFAFLASYLKGLHKDRLLVLGmHIPLFDAAPGRETfrHADRQRLFDLLKDFRNVLVLSGHSHTQQH 331
Cdd:cd07378   151 PNKKLAETQLAWLEKQLAASKADYKIVVG-HYPIYSSGEHGPT--KCLVDILLPLLKKYKVDAYLSGHDHNLQH 221
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 175-327 3.40e-07

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: 51.56  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 175 TLGDIVNDDLTLYP------AINKVTTSLGVPWFHVPGNHdlDFDAASDEHSLDSWRNIYGPDTYAVEEGGASFVFlddV 248
Cdd:cd07396    52 QLGDIIDGYNAKDRskealdAVLSILDRLKGPVHHVLGNH--EFYNFPREYLNHLKTLNGEDAYYYSFSPGPGFRF---L 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 249 VYDpnaRPKYVGGLREDQFAFLASYLK-GLHKD-RLLVLGmHIPLFDAApgreTFRHA---DRQRLFDLLKDFRNVL-VL 322
Cdd:cd07396   127 VLD---FVKFNGGIGEEQLAWLRNELTsADANGeKVIVLS-HLPIYPEA----ADPQCllwNYEEVLAILESYPCVKaCF 198


                  ....*
gi 1040960989 323 SGHSH 327
Cdd:cd07396   199 SGHNH 203
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 214-341 2.75e-06

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: 46.88  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 214 AASDEHSlDSWRNIYGPDTYAVEEGGASFV-FLDDVVYDPNARPKYVGGLREDQFAFL-ASYLKGLHkDrllVLGMHIPL 291
Cdd:cd00838     2 VISDIHG-NLEALEAVLEAALAKAEKPDLViCLGDLVDYGPDPEEVELKALRLLLAGIpVYVVPGNH-D---ILVTHGPP 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1040960989 292 FDAAPGRETFRHADRQRLFDLLKDFRNVLVLSGHSHTQQHVYHGKADGWN 341
Cdd:cd00838    77 YDPLDEGSPGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLV 126
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
176-327 5.40e-06

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 47.32  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 176 LGDIVND-DLTLYPAINKVTTSLGVPWFHVPGNHdlDFDAASDEHSLDSWRNIygpDTYAVEEGGASFVFLDDVVYDPNA 254
Cdd:COG2129    33 AGDLTDFgTAEEAREVLEELAALGVPVLAVPGNH--DDPEVLDALEESGVHNL---HGRVVEIGGLRIAGLGGSRPTPFG 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040960989 255 RPKYvggLREDQfafLASYLKGLHKDRLLVLGMHI-PLFDAAPGRETFRHADRQRLFDLLKDFRNVLVLSGHSH 327
Cdd:COG2129   108 TPYE---YTEEE---IEERLAKLREKDVDILLTHApPYGTTLDRVEDGPHVGSKALRELIEEFQPKLVLHGHIH 175
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 199-327 3.29e-05

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: 45.77  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 199 VPWFHVPGNHDLDFDAASDehSLDSWRNIYGPDTYAVEEGGASFVFLDDVVY-DPNARPKyvggLREDQFAFLASYLK-- 275
Cdd:cd07395    88 IPLVCVCGNHDVGNTPTPE--TIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFkDPSKVPE----LASAQDQWLEEQLQia 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1040960989 276 GLHKDRLLVLGMHIPLFDAAPGRET----FRHADRQRLFDLLKDFRNVLVLSGHSH 327
Cdd:cd07395   162 RESDAKHVVVFQHIPLFLEDPDEEDdyfnIPKSVRRELLDKFKKAGVKAVFSGHYH 217
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 201-330 7.12e-05

Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) is an uncharacterized Homo sapiens transmembrane protein with an N-terminal metallophosphatase domain. TMEM62 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: 277346 [Multi-domain]  Cd Length: 254  Bit Score: 44.66  E-value: 7.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 201 WFHVPGNHDLdFDAASdehsLDSWRNIY------GPD-----TYAVEEGGASFVFLDDVVYDPNARPkyvgglredqFAF 269
Cdd:cd07401    80 LFDIRGNHDL-FGIVS----FDSQNNYYrkysntGRDhshsfSSTTRFGNYSFIGFDPTIFPGPKRP----------FNF 144

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040960989 270 LASYLKgLHKDRLLVLGM------------HIPL-----FDAAPGRETFRhadrqrlfDLLKDFRNVLVLSGHSHTQQ 330
Cdd:cd07401   145 FGSLDK-KLLDRLEKELEksknskytiwfgHYPHsliisPSAKSSSKTFK--------DLLKKYNVTAYLCGHLHPLG 213
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 204-351 1.30e-03

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: 40.85  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 204 VPGNHDLDFDAASDEHSLDSWRNIYGPDTYAVEEGGASFVFLDDVVYDPNARPKYVGGLREdqfaFLASYLKGLHKDRLL 283
Cdd:cd08163    90 LPGNHDIGFGNGVKLPVRQRFESYFGPTSRVIDVGNHTFVIVDTISLSNNDNPQVYQPARE----FLHSFEAMKVNSKPR 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 284 VLGMHIPLF-DAA----PGRE-------TFRHA-----DRQRLFDLLKDFRNVLVLSGHSHTQQHVYHGKADGWNGDKPl 346
Cdd:cd08163   166 ILLTHVPLYrPPNtscgPLREkktplpyGYGYQyqnvlEPSLSESILKAINPVAAFSGDDHDYCEVVHEYQFDGKEGSA- 244


                  ....*
gi 1040960989 347 HEYNV 351
Cdd:cd08163   245 REITV 249
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
177-327 1.83e-03

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 40.16  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 177 GDIVNDDLTLYP----AINKVTTSLGVpwFHVPGNHDLdfdaasdEHSLDSWRNIYgpdtyavEEGGasFVFLDD--VVY 250
Cdd:COG1408    81 GDLVDGSVAELEalleLLKKLKAPLGV--YAVLGNHDY-------YAGLEELRAAL-------EEAG--VRVLRNeaVTL 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040960989 251 DPNARPKYVGGL---REDQFAFLASYLKGLHKDRLLVLGMHIPlfdaapgrETFRHADRQRlFDLlkdfrnvlVLSGHSH 327
Cdd:COG1408   143 ERGGDRLNLAGVddpHAGRFPDLEKALAGVPPDAPRILLAHNP--------DVFDEAAAAG-VDL--------QLSGHTH 205
 
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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