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Conserved domains on  [gi|505360885|ref|WP_015547987|]
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MULTISPECIES: FN3 domain-containing metallophosphoesterase family protein [Alistipes]

Protein Classification

FN3 domain-containing metallophosphoesterase family protein( domain architecture ID 12179906)

FN3 domain-containing metallophosphoesterase contains an active site consisting of two metal ions (usually manganese, iron, or zinc), and may catalyze the hydrolysis of a phosphate-containing substrate

CATH:  3.60.21.10|2.60.40.10
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0042578|GO:0005515
PubMed:  25837850|7833045|8981327
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
150-345 4.11e-29

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


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 113.25  E-value: 4.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 150 FWMVNDIH-------ARDSVFQLLIKEAPEAQPDFVCLNGDLASQTETEQtlWDAclgsASKILTPAGIPLAVTRGNHEN 222
Cdd:COG1409    3 FAHISDLHlgapdgsDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEE--YAA----AREILARLGVPVYVVPGNHDI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 223 RGAYAQHWLDYF-PTPTGETYYTFRRGPAFFIVLDGCEDKpdndpRYYGmgdwnEYRRQQAEWLKgvvnsDEFRAAP--V 299
Cdd:COG1409   77 RAAMAEAYREYFgDLPPGGLYYSFDYGGVRFIGLDSNVPG-----RSSG-----ELGPEQLAWLE-----EELAAAPakP 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 505360885 300 RIVLMH--MIPGKEDSWYGEQQIRRLFIPELAGKGIDLMLCGHYHRYH 345
Cdd:COG1409  142 VIVFLHhpPYSTGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRYE 189
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 36-106 6.56e-05

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


:

Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 41.24  E-value: 6.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505360885   36 LNVTEDG--FTVVWDAKADAIG-WVE--LAPMDGSHFYSAERPRYYDshlGLCRVGRMHRVRIEGLQPGTTYRYRI 106
Cdd:pfam16656   6 LSLTGDStsMTVSWVTPSAVTSpVVQygTSSSALTSTATATSSTYTT---GDGGTGYIHRATLTGLEPGTTYYYRV 78
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
150-345 4.11e-29

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 113.25  E-value: 4.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 150 FWMVNDIH-------ARDSVFQLLIKEAPEAQPDFVCLNGDLASQTETEQtlWDAclgsASKILTPAGIPLAVTRGNHEN 222
Cdd:COG1409    3 FAHISDLHlgapdgsDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEE--YAA----AREILARLGVPVYVVPGNHDI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 223 RGAYAQHWLDYF-PTPTGETYYTFRRGPAFFIVLDGCEDKpdndpRYYGmgdwnEYRRQQAEWLKgvvnsDEFRAAP--V 299
Cdd:COG1409   77 RAAMAEAYREYFgDLPPGGLYYSFDYGGVRFIGLDSNVPG-----RSSG-----ELGPEQLAWLE-----EELAAAPakP 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 505360885 300 RIVLMH--MIPGKEDSWYGEQQIRRLFIPELAGKGIDLMLCGHYHRYH 345
Cdd:COG1409  142 VIVFLHhpPYSTGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRYE 189
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 174-343 2.50e-08

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: 54.63  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 174 QPDFVCLNGDL--ASQTETEQTLWDACLGSASKILTPAgIPLAVTRGNHE--NR--GAYAQHWLDYFptptGETYYTFRR 247
Cdd:cd07395   50 KPKFVVVCGDLvhAMPGEEFREQQVSDLKDVLSKLDPD-IPLVCVCGNHDvgNTptPETIQRYRDDF----GDDYFSFWV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 248 GPAFFIVLdgcedkpdNDPRYYGMGDWNEYRRQQAEWLKGVVNSDEFRAAPVRIVLMHmIP------GKEDSWYG-EQQI 320
Cdd:cd07395  125 GGVFFIVL--------NSQLFKDPSKVPELASAQDQWLEEQLQIARESDAKHVVVFQH-IPlfledpDEEDDYFNiPKSV 195

                        170       180
                 ....*....|....*....|...
gi 505360885 321 RRLFIPELAGKGIDLMLCGHYHR 343
Cdd:cd07395  196 RRELLDKFKKAGVKAVFSGHYHR 218
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 36-106 6.56e-05

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 41.24  E-value: 6.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505360885   36 LNVTEDG--FTVVWDAKADAIG-WVE--LAPMDGSHFYSAERPRYYDshlGLCRVGRMHRVRIEGLQPGTTYRYRI 106
Cdd:pfam16656   6 LSLTGDStsMTVSWVTPSAVTSpVVQygTSSSALTSTATATSSTYTT---GDGGTGYIHRATLTGLEPGTTYYYRV 78
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 150-234 1.30e-03

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: 38.35  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885  150 FWMVNDIHA---RDSVFQLLIKEAPEAQPDFVCLNGDLAS-QTETEQTLWDACLGsaskiltPAGIPLAVTRGNHENRGA 225
Cdd:pfam00149   3 ILVIGDLHLpgqLDDLLELLKKLLEEGKPDLVLHAGDLVDrGPPSEEVLELLERL-------IKYVPVYLVRGNHDFDYG 75


                  ....*....
gi 505360885  226 YAQHWLDYF 234
Cdd:pfam00149  76 ECLRLYPYL 84
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
150-345 4.11e-29

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 113.25  E-value: 4.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 150 FWMVNDIH-------ARDSVFQLLIKEAPEAQPDFVCLNGDLASQTETEQtlWDAclgsASKILTPAGIPLAVTRGNHEN 222
Cdd:COG1409    3 FAHISDLHlgapdgsDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEE--YAA----AREILARLGVPVYVVPGNHDI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 223 RGAYAQHWLDYF-PTPTGETYYTFRRGPAFFIVLDGCEDKpdndpRYYGmgdwnEYRRQQAEWLKgvvnsDEFRAAP--V 299
Cdd:COG1409   77 RAAMAEAYREYFgDLPPGGLYYSFDYGGVRFIGLDSNVPG-----RSSG-----ELGPEQLAWLE-----EELAAAPakP 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 505360885 300 RIVLMH--MIPGKEDSWYGEQQIRRLFIPELAGKGIDLMLCGHYHRYH 345
Cdd:COG1409  142 VIVFLHhpPYSTGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHRYE 189
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 174-343 2.50e-08

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: 54.63  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 174 QPDFVCLNGDL--ASQTETEQTLWDACLGSASKILTPAgIPLAVTRGNHE--NR--GAYAQHWLDYFptptGETYYTFRR 247
Cdd:cd07395   50 KPKFVVVCGDLvhAMPGEEFREQQVSDLKDVLSKLDPD-IPLVCVCGNHDvgNTptPETIQRYRDDF----GDDYFSFWV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 248 GPAFFIVLdgcedkpdNDPRYYGMGDWNEYRRQQAEWLKGVVNSDEFRAAPVRIVLMHmIP------GKEDSWYG-EQQI 320
Cdd:cd07395  125 GGVFFIVL--------NSQLFKDPSKVPELASAQDQWLEEQLQIARESDAKHVVVFQH-IPlfledpDEEDDYFNiPKSV 195

                        170       180
                 ....*....|....*....|...
gi 505360885 321 RRLFIPELAGKGIDLMLCGHYHR 343
Cdd:cd07395  196 RRELLDKFKKAGVKAVFSGHYHR 218
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 161-344 9.58e-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: 53.07  E-value: 9.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 161 SVFQLLIKEApeAQPDFVCLNGDLASQTETE-QTLWDACLGSASKILtpAGIPLAVTRGNHE---NRGAYAQHWLDY--- 233
Cdd:cd00839   22 NTLDHLEKEL--GNYDAIIHVGDIAYADGYNnGSRWDTFMRQIEPLA--SYVPYMVAPGNHEadyNGSTSKIKFFMPgrg 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 234 -FPTPTGET---YYTFRRGPAFFIVLDGcEdkpdndpRYYGMGDwneYRRQQAEWLKgvvnsDEFRAA-----PVRIVLM 304
Cdd:cd00839   98 mPPSPSGSTenlWYSFDVGPVHFISLST-E-------TDFLKGD---NISPQYDWLE-----ADLAKVdrsrtPWIIVMG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 505360885 305 H-----MIPGKEDSwYGEQQIRRLFIPELAGKGIDLMLCGHYHRY 344
Cdd:cd00839  162 HrpmycSNDDDADC-IEGEKMREALEDLFYKYGVDLVLSGHVHAY 205
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
155-342 2.72e-07

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 51.33  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 155 DIHARDSVFQL----LIKEAPEAQPDFVCLNGDLASQTETEqtlWDACLGSASKILTPAGIpLAVTrGNHEnRGAYAQHW 230
Cdd:COG1408   50 DLHLGPFIGGErlerLVEKINALKPDLVVLTGDLVDGSVAE---LEALLELLKKLKAPLGV-YAVL-GNHD-YYAGLEEL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 231 LDYFpTPTG------ETYYTFRRGPAFFIVldgcedkpdndpryyGMGDWNEYRRQQ-AEWLKGVvnsdefRAAPVRIVL 303
Cdd:COG1408  124 RAAL-EEAGvrvlrnEAVTLERGGDRLNLA---------------GVDDPHAGRFPDlEKALAGV------PPDAPRILL 181

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 505360885 304 MHmIPGkedswygeqqirrlFIPELAGKGIDLMLCGHYH 342
Cdd:COG1408  182 AH-NPD--------------VFDEAAAAGVDLQLSGHTH 205
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
155-343 7.10e-06

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 46.55  E-value: 7.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 155 DIHARDSVFQLLIKEAPEAQPDFVCLNGDLASQTETEQTlwDACLGSASKIltpaGIPLAVTRGNHENR------GAYAQ 228
Cdd:COG2129    7 DLHGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEA--REVLEELAAL----GVPVLAVPGNHDDPevldalEESGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 229 HWLDyfptptGETyytfrrgpaffIVLDGCedkpdndpRYYGMG-----DWNEYRRQQAEWLKGVVnsDEFRAAPVRIVL 303
Cdd:COG2129   81 HNLH------GRV-----------VEIGGL--------RIAGLGgsrptPFGTPYEYTEEEIEERL--AKLREKDVDILL 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 505360885 304 MHMIP-------GKEDSWYGEQQIRRLfipeLAGKGIDLMLCGHYHR 343
Cdd:COG2129  134 THAPPygttldrVEDGPHVGSKALREL----IEEFQPKLVLHGHIHE 176
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
158-352 9.97e-06

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 46.44  E-value: 9.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 158 ARDSVFQLLIKEAPEAQPDFVCLNGDL---ASQTETEQTLWDACLGSASKiltpAGIPLAVTRGNHEN--RGAYAQHWLD 232
Cdd:COG0420   23 DQLAALDRLVDLAIEEKVDAVLIAGDLfdsANPSPEAVRLLAEALRRLSE----AGIPVVLIAGNHDSpsRLSAGSPLLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 233 ----YFPTPTGETYYTFRRGPAFFIvldgcedkpdndpryYGMgDWNEYRRQQAewLKGVVNS--DEFRAAPVRIVLMH- 305
Cdd:COG0420   99 nlgvHVFGSVEPEPVELEDGLGVAV---------------YGL-PYLRPSDEEA--LRDLLERlpRALDPGGPNILLLHg 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 505360885 306 MIPGKEDSwygeqqiRRLFIPE-----LAGKGIDLMLCGHYHRYHWIDDGSR 352
Cdd:COG0420  161 FVAGASGS-------RDIYVAPvplsaLPAAGFDYVALGHIHRPQVLGGDPR 205
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 36-106 6.56e-05

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 41.24  E-value: 6.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505360885   36 LNVTEDG--FTVVWDAKADAIG-WVE--LAPMDGSHFYSAERPRYYDshlGLCRVGRMHRVRIEGLQPGTTYRYRI 106
Cdd:pfam16656   6 LSLTGDStsMTVSWVTPSAVTSpVVQygTSSSALTSTATATSSTYTT---GDGGTGYIHRATLTGLEPGTTYYYRV 78
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 173-343 1.27e-03

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: 39.95  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 173 AQPDFVCLNGDLASQTETEQtlwdacLGSASKILTPAGIPLAVTRGNHENRGAYaqhwLDYFPTPTGET----YYTFRRG 248
Cdd:cd07402   38 PRPDLVVVTGDLSDDGSPES------YERLRELLAPLPAPVYWIPGNHDDRAAM----REALPEPPYDDngpvQYVVDFG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885 249 PAFFIVLDGCEdkpdNDPRYYGMGDwneyrrQQAEWLKgvvnsDEFRAAPVR--IVLMH---MIPGkeDSWYgeQQIRRL 323
Cdd:cd07402  108 GWRLILLDTSV----PGVHHGELSD------EQLDWLE-----AALAEAPDRptLIFLHhppFPLG--IPWM--DAIRLR 168

                        170       180
                 ....*....|....*....|....*
gi 505360885 324 FIPELAG-----KGIDLMLCGHYHR 343
Cdd:cd07402  169 NSQALFAvlarhPQVKAILCGHIHR 193
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 150-234 1.30e-03

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: 38.35  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505360885  150 FWMVNDIHA---RDSVFQLLIKEAPEAQPDFVCLNGDLAS-QTETEQTLWDACLGsaskiltPAGIPLAVTRGNHENRGA 225
Cdd:pfam00149   3 ILVIGDLHLpgqLDDLLELLKKLLEEGKPDLVLHAGDLVDrGPPSEEVLELLERL-------IKYVPVYLVRGNHDFDYG 75


                  ....*....
gi 505360885  226 YAQHWLDYF 234
Cdd:pfam00149  76 ECLRLYPYL 84
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 172-220 2.13e-03

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 39.20  E-value: 2.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505360885 172 EAQPDFVCLNGDL----ASQTETEQTLWDaclgsasKILTP---AGIPLAVTRGNH 220
Cdd:cd07383   40 EEKPDLVVLTGDLitgeNTADDNATSYLD-------KAVSPlveRGIPWAATFGNH 88
 
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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