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Conserved domains on  [gi|490366854|ref|WP_004246518|]
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MULTISPECIES: metallophosphoesterase [Proteus]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

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
COG5555 super family cl44260
Cytolysin, a secreted calcineurin-like phosphatase [Intracellular trafficking, secretion, and ...
 5-297 2.79e-48

Cytolysin, a secreted calcineurin-like phosphatase [Intracellular trafficking, secretion, and vesicular transport];


The actual alignment was detected with superfamily member COG5555:

Pssm-ID: 444298 [Multi-domain]  Cd Length: 325  Bit Score: 163.88  E-value: 2.79e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854   5 QSTDYNIIVMSDPQPWRLDLDNNDPNNDQSRWETTVKSVRDSIQALHrEKSF-----------AFGIINGDLTEFGRRSQ 73
Cdd:COG5555   33 PAIDVTFLVVADTHAGRVASGLAPGCPEEGKTDKALERHVAALNGIA-GQAWppaiggvvgrpRGLLVGGDLTEDGQGRQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854  74 RESFRALF----APSPLGFNTYVGLGNHDYQNNVGDCAEPSNADYsmnacargmvfdmhyrIEEYRNYATSGNFRYDSSE 149
Cdd:COG5555  112 LDQFKARYglggGPGLLHMPVYEGLGNHDLDQNGPPWYRREVRDY----------------VEQRHRESVFYKPPVPVTE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854 150 YSGSKAYSWEYGDIHFVQLQNYPTYHVVLDhwsastinvTDSIDWLEKDLIQARNSNKTIILNFHDGNQHFPEK---SSQ 226
Cdd:COG5555  176 YHGSDCYSWDWGDLHLVQLHRAPGDEVKGD---------VSSLDWLKKDLAAAAADGRPVILFFHYGLEGFSTEywfASG 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490366854 227 EELTFFKYMLEHYGVKAVFVGHTHYVGQDNRYGgseifgdVPVYNSGALFKGDYLAVEIRGTELSITVYNG 297
Cdd:COG5555  247 PDRQALLDILKGYNVLGIFHGHYHTTGIYRWHG-------IDVYKPGAAKNGGFAVVRVTDGRMTVASYNA 310
 
Name Accession Description Interval E-value
COG5555 COG5555
Cytolysin, a secreted calcineurin-like phosphatase [Intracellular trafficking, secretion, and ...
 5-297 2.79e-48

Cytolysin, a secreted calcineurin-like phosphatase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444298 [Multi-domain]  Cd Length: 325  Bit Score: 163.88  E-value: 2.79e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854   5 QSTDYNIIVMSDPQPWRLDLDNNDPNNDQSRWETTVKSVRDSIQALHrEKSF-----------AFGIINGDLTEFGRRSQ 73
Cdd:COG5555   33 PAIDVTFLVVADTHAGRVASGLAPGCPEEGKTDKALERHVAALNGIA-GQAWppaiggvvgrpRGLLVGGDLTEDGQGRQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854  74 RESFRALF----APSPLGFNTYVGLGNHDYQNNVGDCAEPSNADYsmnacargmvfdmhyrIEEYRNYATSGNFRYDSSE 149
Cdd:COG5555  112 LDQFKARYglggGPGLLHMPVYEGLGNHDLDQNGPPWYRREVRDY----------------VEQRHRESVFYKPPVPVTE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854 150 YSGSKAYSWEYGDIHFVQLQNYPTYHVVLDhwsastinvTDSIDWLEKDLIQARNSNKTIILNFHDGNQHFPEK---SSQ 226
Cdd:COG5555  176 YHGSDCYSWDWGDLHLVQLHRAPGDEVKGD---------VSSLDWLKKDLAAAAADGRPVILFFHYGLEGFSTEywfASG 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490366854 227 EELTFFKYMLEHYGVKAVFVGHTHYVGQDNRYGgseifgdVPVYNSGALFKGDYLAVEIRGTELSITVYNG 297
Cdd:COG5555  247 PDRQALLDILKGYNVLGIFHGHYHTTGIYRWHG-------IDVYKPGAAKNGGFAVVRVTDGRMTVASYNA 310
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 134-250 1.04e-08

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: 55.38  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854 134 YRNYATSGNFRYDSSEYSGSkAYSWEYGDIHFVQLQNYptyhvvldHWSASTINVTDSIDWLEKDLIQArNSNKT--IIL 211
Cdd:cd00839   90 KFFMPGRGMPPSPSGSTENL-WYSFDVGPVHFISLSTE--------TDFLKGDNISPQYDWLEADLAKV-DRSRTpwIIV 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490366854 212 NFH-----DGNQHFPEKSSQEELTFFKYMLEHYGVKAVFVGHTH 250
Cdd:cd00839  160 MGHrpmycSNDDDADCIEGEKMREALEDLFYKYGVDLVLSGHVH 203
 
Name Accession Description Interval E-value
COG5555 COG5555
Cytolysin, a secreted calcineurin-like phosphatase [Intracellular trafficking, secretion, and ...
 5-297 2.79e-48

Cytolysin, a secreted calcineurin-like phosphatase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444298 [Multi-domain]  Cd Length: 325  Bit Score: 163.88  E-value: 2.79e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854   5 QSTDYNIIVMSDPQPWRLDLDNNDPNNDQSRWETTVKSVRDSIQALHrEKSF-----------AFGIINGDLTEFGRRSQ 73
Cdd:COG5555   33 PAIDVTFLVVADTHAGRVASGLAPGCPEEGKTDKALERHVAALNGIA-GQAWppaiggvvgrpRGLLVGGDLTEDGQGRQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854  74 RESFRALF----APSPLGFNTYVGLGNHDYQNNVGDCAEPSNADYsmnacargmvfdmhyrIEEYRNYATSGNFRYDSSE 149
Cdd:COG5555  112 LDQFKARYglggGPGLLHMPVYEGLGNHDLDQNGPPWYRREVRDY----------------VEQRHRESVFYKPPVPVTE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854 150 YSGSKAYSWEYGDIHFVQLQNYPTYHVVLDhwsastinvTDSIDWLEKDLIQARNSNKTIILNFHDGNQHFPEK---SSQ 226
Cdd:COG5555  176 YHGSDCYSWDWGDLHLVQLHRAPGDEVKGD---------VSSLDWLKKDLAAAAADGRPVILFFHYGLEGFSTEywfASG 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490366854 227 EELTFFKYMLEHYGVKAVFVGHTHYVGQDNRYGgseifgdVPVYNSGALFKGDYLAVEIRGTELSITVYNG 297
Cdd:COG5555  247 PDRQALLDILKGYNVLGIFHGHYHTTGIYRWHG-------IDVYKPGAAKNGGFAVVRVTDGRMTVASYNA 310
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
11-295 7.56e-16

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 75.11  E-value: 7.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854  11 IIVMSDPQpwrldldnndpnNDQSRWETTVKSVRDSIQALHREKsFAFGIINGDLTEFGRRSQRESFRALFAPspLGFNT 90
Cdd:COG1409    3 FAHISDLH------------LGAPDGSDTAEVLAAALADINAPR-PDFVVVTGDLTDDGEPEEYAAAREILAR--LGVPV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854  91 YVGLGNHDYqnnvgdcaepsnadysmnacargmvfdmhyrieeyRNYATSGNFRYDSSEYSGSKAYSWEYGDIHFVQL-- 168
Cdd:COG1409   68 YVVPGNHDI-----------------------------------RAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGLds 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854 169 QNYPTYHVVLDHwsastinvtDSIDWLEKDLiqARNSNKTIILNFHdgnQHFPEKSSQEELTFFKY------MLEHYGVK 242
Cdd:COG1409  113 NVPGRSSGELGP---------EQLAWLEEEL--AAAPAKPVIVFLH---HPPYSTGSGSDRIGLRNaeellaLLARYGVD 178

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490366854 243 AVFVGHTHYVGQDNRYGgseifgdVPVYNSGAL-----FKGDYLAVEIRGTELSITVY 295
Cdd:COG1409  179 LVLSGHVHRYERTRRDG-------VPYIVAGSTggqvrLPPGYRVIEVDGDGLTVEVR 229
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 134-250 1.04e-08

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: 55.38  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854 134 YRNYATSGNFRYDSSEYSGSkAYSWEYGDIHFVQLQNYptyhvvldHWSASTINVTDSIDWLEKDLIQArNSNKT--IIL 211
Cdd:cd00839   90 KFFMPGRGMPPSPSGSTENL-WYSFDVGPVHFISLSTE--------TDFLKGDNISPQYDWLEADLAKV-DRSRTpwIIV 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490366854 212 NFH-----DGNQHFPEKSSQEELTFFKYMLEHYGVKAVFVGHTH 250
Cdd:cd00839  160 MGHrpmycSNDDDADCIEGEKMREALEDLFYKYGVDLVLSGHVH 203
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 45-251 8.33e-05

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: 43.04  E-value: 8.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854  45 DSIQALHREksFAFGIINGDLTEFGRRSQRESFRALFAPspLGFNTYVGLGNHDYQNNvgdcaepsnadysMNAcargmV 124
Cdd:cd07402   31 AQVNALHPR--PDLVVVTGDLSDDGSPESYERLRELLAP--LPAPVYWIPGNHDDRAA-------------MRE-----A 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854 125 FDMHYrieeyrnYATSGNFRYdsseysgskAYSWEYGDIHFVQLQNYPTYHVVLDhwsastinvTDSIDWLEKDLIQARN 204
Cdd:cd07402   89 LPEPP-------YDDNGPVQY---------VVDFGGWRLILLDTSVPGVHHGELS---------DEQLDWLEAALAEAPD 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490366854 205 SNKTIILN---FHDGNQHFPEKSSQEELTFFKYMLEHYGVKAVFVGHTHY 251
Cdd:cd07402  144 RPTLIFLHhppFPLGIPWMDAIRLRNSQALFAVLARHPQVKAILCGHIHR 193
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 134-250 1.49e-04

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: 42.35  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854 134 YRNYatSGNFRYDSSEYSgskaYSWEYGDIHFVQL--QNYPTYHVVLDHWSASTinvTDSIDWLEKDLIQARNSNKTIIL 211
Cdd:cd07401  102 YRKY--SNTGRDHSHSFS----STTRFGNYSFIGFdpTIFPGPKRPFNFFGSLD---KKLLDRLEKELEKSKNSKYTIWF 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490366854 212 NfhdgnqHFP-----EKSSQEELTFFKYMLEHYGVKAVFVGHTH 250
Cdd:cd07401  173 G------HYPhsliiSPSAKSSSKTFKDLLKKYNVTAYLCGHLH 210
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 5-250 1.26e-03

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: 39.61  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854   5 QSTDYNIIVMSDPQPwrLDLDNNDPNNDQSRWETTVKSVRDSIQALHR-EKSFAFGIINGDLTE----FGRRSQRES--- 76
Cdd:cd07395    1 WKGPFYFIQGADPQL--GLIKQNNIGNGGDEWDKEIELTEQAVQAINKlNPKPKFVVVCGDLVHampgEEFREQQVSdlk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854  77 --FRALFAPSPLgfnTYVGlGNHDyqnnVGDCAEPSNadysmnacargmvfdmhyrIEEYRNyatsgNFrydsseysGSK 154
Cdd:cd07395   79 dvLSKLDPDIPL---VCVC-GNHD----VGNTPTPET-------------------IQRYRD-----DF--------GDD 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366854 155 AYSWEYGDIHFVQL--QNYPTYHVVLDHWSASTinvtdsiDWLEKDLIQARNSNKTIILNFhdgnQHFPE--KSSQEELT 230
Cdd:cd07395  119 YFSFWVGGVFFIVLnsQLFKDPSKVPELASAQD-------QWLEEQLQIARESDAKHVVVF----QHIPLflEDPDEEDD 187

                        250       260       270
                 ....*....|....*....|....*....|
gi 490366854 231 FF-------KYMLE---HYGVKAVFVGHTH 250
Cdd:cd07395  188 YFnipksvrRELLDkfkKAGVKAVFSGHYH 217
 
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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