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Conserved domains on  [gi|1239686986|gb|ASW80537|]
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YfcE family phosphodiesterase [Vibrio anguillarum]

Protein Classification

metallophosphoesterase( domain architecture ID 10013241)

metallophosphoesterase contains an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to Escherichia coli YfcE

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09453 PRK09453
phosphodiesterase; Provisional
 17-190 3.81e-106

phosphodiesterase; Provisional


:

Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 302.55  E-value: 3.81e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  17 MKLFFASDLHGSLPATEKVLSLFERSGADTLVLLGDLLNHGPRNPIPDGYNPTAVAECLNRWAPHIVAVRGNCDSEVDQM 96
Cdd:PRK09453    1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDVLYHGPRNPLPEGYAPKKVAELLNAYADKIIAVRGNCDSEVDQM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  97 LLDFPMMMDFCWVVLEsGTRFFLTHGHQYNAQNRPPLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPRNEFPPSYAI 176
Cdd:PRK09453   81 LLHFPIMAPYQQVLLE-GKRLFLTHGHLYGPENLPALHDGDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGGYPASYGI 159

                         170
                  ....*....|....
gi 1239686986 177 YTDGLFQVMGLEGQ 190
Cdd:PRK09453  160 LDDNVLSVIDLEGG 173
 
Name Accession Description Interval E-value
PRK09453 PRK09453
phosphodiesterase; Provisional
 17-190 3.81e-106

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 302.55  E-value: 3.81e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  17 MKLFFASDLHGSLPATEKVLSLFERSGADTLVLLGDLLNHGPRNPIPDGYNPTAVAECLNRWAPHIVAVRGNCDSEVDQM 96
Cdd:PRK09453    1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDVLYHGPRNPLPEGYAPKKVAELLNAYADKIIAVRGNCDSEVDQM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  97 LLDFPMMMDFCWVVLEsGTRFFLTHGHQYNAQNRPPLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPRNEFPPSYAI 176
Cdd:PRK09453   81 LLHFPIMAPYQQVLLE-GKRLFLTHGHLYGPENLPALHDGDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGGYPASYGI 159

                         170
                  ....*....|....
gi 1239686986 177 YTDGLFQVMGLEGQ 190
Cdd:PRK09453  160 LDDNVLSVIDLEGG 173
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
18-178 3.32e-50

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 160.47  E-value: 3.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  18 KLFFASDLHGSLPATEKVLSLFERSGADTLVLLGDLLNHGPrnpipdgyNPTAVAECLNRWapHIVAVRGNCDSEVDQML 97
Cdd:COG0622     1 KIAVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGP--------DPPEVLDLLREL--PIVAVRGNHDGAVLRGL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  98 LDFPMMMDFCWvvleSGTRFFLTHGHQYN----------AQNRPPLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPR 167
Cdd:COG0622    71 RSLPETLRLEL----EGVRILLVHGSPNEyllpdtpaerLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPR 146

                         170
                  ....*....|.
gi 1239686986 168 NEFPPSYAIYT 178
Cdd:COG0622   147 DGDPASYAILD 157
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 18-176 2.54e-41

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain family 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: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 137.02  E-value: 2.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  18 KLFFASDLHGSLPATEKVLSLFERsGADTLVLLGDLLNHGPRNPIpdgynptavaecLNRWAPhIVAVRGNCDSEVDQML 97
Cdd:cd00841     1 KIGVISDTHGNLEAIEKALELFED-GVDAVIHAGDFVSPFVLNAL------------LELKAP-LIAVRGNNDGEVDQLL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  98 lDFPMMMDFcWVVLESGTRFFLTHGHQY---NAQNRPPLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPRNEfPPSY 174
Cdd:cd00841    67 -GRPILPEF-LTLEIGGLRILLTHGHLFgvlEALYLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTY 143


                  ..
gi 1239686986 175 AI 176
Cdd:cd00841   144 AI 145
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 17-180 6.47e-30

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 107.84  E-value: 6.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  17 MKLFFASDLHGSLPATEKVLSLFER-SGADTLVLLGDLLnhgprnpipdgynPTAVAECLNRWAPHIVAVRGNCDSEVDQ 95
Cdd:TIGR00040   1 MKILVISDTHGPLRATELPVELFNLeSNVDLVIHAGDLT-------------SPFVLKEFEDLAAKVIAVRGNNDGERDE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  96 MLLDFPMMMDFCWVVLESGtRFFLTHGHQYNAQNRPPLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPRNEFPPSYA 175
Cdd:TIGR00040  68 LPEEEIFEAEGIDFGLVHG-DLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSYA 146


                  ....*
gi 1239686986 176 IYTDG 180
Cdd:TIGR00040 147 ILDVD 151
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 17-178 2.46e-26

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 98.54  E-value: 2.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  17 MKLFFASDLHGSLPATEKVLSLFeRSGADTLVLLGDLLNhgprnpipdgynPTAVAECLNRWAPHivAVRGNCDSEVdQM 96
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERL-KGVVDLIIHAGDIVA------------PEVLEELLELAPVL--AVRGNNDAAA-EF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  97 LLDFPmmmDFCWVVLEsGTRFFLTHGHQYNAQNRP----PLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPRNEFPP 172
Cdd:pfam12850  65 ATDLP---EEAVLELG-GVKILLTHGHGVKDALARllrrAEEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPP 140


                  ....*.
gi 1239686986 173 SYAIYT 178
Cdd:pfam12850 141 TYALLD 146
 
Name Accession Description Interval E-value
PRK09453 PRK09453
phosphodiesterase; Provisional
 17-190 3.81e-106

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 302.55  E-value: 3.81e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  17 MKLFFASDLHGSLPATEKVLSLFERSGADTLVLLGDLLNHGPRNPIPDGYNPTAVAECLNRWAPHIVAVRGNCDSEVDQM 96
Cdd:PRK09453    1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDVLYHGPRNPLPEGYAPKKVAELLNAYADKIIAVRGNCDSEVDQM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  97 LLDFPMMMDFCWVVLEsGTRFFLTHGHQYNAQNRPPLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPRNEFPPSYAI 176
Cdd:PRK09453   81 LLHFPIMAPYQQVLLE-GKRLFLTHGHLYGPENLPALHDGDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGGYPASYGI 159

                         170
                  ....*....|....
gi 1239686986 177 YTDGLFQVMGLEGQ 190
Cdd:PRK09453  160 LDDNVLSVIDLEGG 173
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
18-178 3.32e-50

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 160.47  E-value: 3.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  18 KLFFASDLHGSLPATEKVLSLFERSGADTLVLLGDLLNHGPrnpipdgyNPTAVAECLNRWapHIVAVRGNCDSEVDQML 97
Cdd:COG0622     1 KIAVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGP--------DPPEVLDLLREL--PIVAVRGNHDGAVLRGL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  98 LDFPMMMDFCWvvleSGTRFFLTHGHQYN----------AQNRPPLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPR 167
Cdd:COG0622    71 RSLPETLRLEL----EGVRILLVHGSPNEyllpdtpaerLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPR 146

                         170
                  ....*....|.
gi 1239686986 168 NEFPPSYAIYT 178
Cdd:COG0622   147 DGDPASYAILD 157
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 18-176 2.54e-41

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain family 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: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 137.02  E-value: 2.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  18 KLFFASDLHGSLPATEKVLSLFERsGADTLVLLGDLLNHGPRNPIpdgynptavaecLNRWAPhIVAVRGNCDSEVDQML 97
Cdd:cd00841     1 KIGVISDTHGNLEAIEKALELFED-GVDAVIHAGDFVSPFVLNAL------------LELKAP-LIAVRGNNDGEVDQLL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  98 lDFPMMMDFcWVVLESGTRFFLTHGHQY---NAQNRPPLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPRNEfPPSY 174
Cdd:cd00841    67 -GRPILPEF-LTLEIGGLRILLTHGHLFgvlEALYLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTY 143


                  ..
gi 1239686986 175 AI 176
Cdd:cd00841   144 AI 145
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 17-180 6.47e-30

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 107.84  E-value: 6.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  17 MKLFFASDLHGSLPATEKVLSLFER-SGADTLVLLGDLLnhgprnpipdgynPTAVAECLNRWAPHIVAVRGNCDSEVDQ 95
Cdd:TIGR00040   1 MKILVISDTHGPLRATELPVELFNLeSNVDLVIHAGDLT-------------SPFVLKEFEDLAAKVIAVRGNNDGERDE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  96 MLLDFPMMMDFCWVVLESGtRFFLTHGHQYNAQNRPPLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPRNEFPPSYA 175
Cdd:TIGR00040  68 LPEEEIFEAEGIDFGLVHG-DLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSYA 146


                  ....*
gi 1239686986 176 IYTDG 180
Cdd:TIGR00040 147 ILDVD 151
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 17-178 2.46e-26

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 98.54  E-value: 2.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  17 MKLFFASDLHGSLPATEKVLSLFeRSGADTLVLLGDLLNhgprnpipdgynPTAVAECLNRWAPHivAVRGNCDSEVdQM 96
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAALERL-KGVVDLIIHAGDIVA------------PEVLEELLELAPVL--AVRGNNDAAA-EF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  97 LLDFPmmmDFCWVVLEsGTRFFLTHGHQYNAQNRP----PLKKGDVLIHGHSHIPMAQGQDDVIIVNPGSATFPRNEFPP 172
Cdd:pfam12850  65 ATDLP---EEAVLELG-GVKILLTHGHGVKDALARllrrAEEGVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPP 140


                  ....*.
gi 1239686986 173 SYAIYT 178
Cdd:pfam12850 141 TYALLD 146
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
18-92 7.63e-11

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 58.87  E-value: 7.63e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239686986  18 KLFFASDLHGSLPATEKVLSLFERSGADTLVLLGDLLNHGPRNPIpdgynpTAVAECLNRWAPHIVAVRGNCDSE 92
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEA------REVLEELAALGVPVLAVPGNHDDP 69
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 21-161 3.96e-10

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: 55.35  E-value: 3.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  21 FASDLHGSLPATEKVLS--LFERSGADTLVLLGDLLNHGPRNPIPDGYNPTAVAECLNrwaphIVAVRGNCDsevdqmll 98
Cdd:cd00838     2 VISDIHGNLEALEAVLEaaLAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIP-----VYVVPGNHD-------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  99 dfpmmmdfcwvvlesgtrFFLTHGHQYN-------------AQNRPPLKKG--DVLIHGHSHIPMA--QGQDDVIIVNPG 161
Cdd:cd00838    69 ------------------ILVTHGPPYDpldegspgedpgsEALLELLDKYgpDLVLSGHTHVPGRreVDKGGTLVVNPG 130
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 17-147 2.29e-06

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: 44.90  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  17 MKLFFASDLH--GSLPATEKVLS-LFERSGADTLVLLGDLLNHGPRNPipdgynptavaECLNRWAP-----HIVAVRGN 88
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKkLLEEGKPDLVLHAGDLVDRGPPSE-----------EVLELLERlikyvPVYLVRGN 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1239686986  89 CDSEVDQMLLDFPmmmdfcwvvleSGTRFFLTHGHQYNAQNRPPLKKgdvLIHGHSHIP 147
Cdd:pfam00149  70 HDFDYGECLRLYP-----------YLGLLARPWKRFLEVFNFLPLAG---ILSGHTHVP 114
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 20-131 2.71e-06

Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an Escherichia coli UDP-2,3-diacylglucosamine hydrolase thought to catalyze the fourth step of lipid A biosynthesis, in which a precursor UDP-2,3-diacylglucosamine is hydrolyzed to yield 2,3-diacylglucosamine 1-phosphate and UMP. YbbF 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: 277343 [Multi-domain]  Cd Length: 217  Bit Score: 46.20  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  20 FFASDLHGSLPATEKVLSLFER-----SGADTLVLLGDLLN--HGPRNPIPDGYNPTAVAecLNRWAPH---IVAVRGNC 89
Cdd:cd07398     1 LFISDLHLGLRGCRADRLLDFLlveelDEADALYLLGDIFDlwIGDDSVVWPGAHRALAR--LLRLADRgteVIYVPGNH 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1239686986  90 DSEVDQMLLD--FPMMMDFCWVVLE-SGTRFFLTHGHQYNAQNRP 131
Cdd:cd07398    79 DFLLGRFFAEalGAILLPEPAEHLElDGKRLLVLHGDQLDTDDRA 123
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 33-145 1.16e-05

Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. The domain present in members of this family 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: 277337  Cd Length: 175  Bit Score: 43.84  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  33 EKVLSLFERSGADTLVLLGDLLNHGPRNPipdgynPTAVAECLNRWAPHIVA----VRGNCDSEVDQMLLDFPmmmdfcw 108
Cdd:cd07391    31 ERLDRLLEELGPDRLVILGDLKHSFGRVS------RQERREVPFFRLLAKDVdvilIRGNHDGGLEEILSDVN------- 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1239686986 109 VVLESGTR---FFLTHGHQYnaqnrPPLKKGDVLIHGHSH 145
Cdd:cd07391    98 VVVVEGYLlggYLIFHGHKE-----PDPLDAKLVIMGHEH 132
COG4186 COG4186
Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily ...
 45-145 1.80e-05

Uncharacterized conserved protein MJ1445, calcineurin-like phosphoesterase superfamily [General function prediction only];


Pssm-ID: 443340  Cd Length: 167  Bit Score: 43.34  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  45 DTLVLLGDLLNHGPRNPIpdgynptavAECLNRWAPHIVAVRGNCDSEVDQMLLDfpmmmDFCWV----VLE-SGTRFFL 119
Cdd:COG4186    45 DTVYHLGDFAFGGSAEEA---------REILRRLNGRKHLIRGNHDGKLLLRLPA-----GFASVqdyaEIKlGGRRLLL 110

                          90       100
                  ....*....|....*....|....*.
gi 1239686986 120 THghqYNAQNRPPLKKGDVLIHGHSH 145
Cdd:COG4186   111 CH---YPLRTWNGADRGAWHLHGHVH 133
MPP_AQ1575 cd07390
Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes ...
 45-145 7.67e-05

Aquifex aeolicus AQ1575 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to AQ1575, an uncharacterized Aquifex aeolicus protein. AQ1575 may play an accessory role in DNA repair, based on the close proximity of its gene to Holliday junction resolvasome genes. The domain present in members of this family 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: 277336  Cd Length: 170  Bit Score: 41.58  E-value: 7.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239686986  45 DTLVLLGDLLNHGprnpipdgyNPTAVAEC-LNRWAPHIVAVRGNCDSEVDQMLLDFPMMMDFCWVVLESGTRFFLTHgh 123
Cdd:cd07390    44 DIVYHLGDFALGT---------NKANEALEiLSLLNGHIHLIRGNHDKSLLMYRPLFFESVQQYVRIEHGGRRFYLSH-- 112

                          90       100
                  ....*....|....*....|..
gi 1239686986 124 qYNAQNRPPLKKGDVLIHGHSH 145
Cdd:cd07390   113 -YPYRGPDSPDFDGWLIHGHVH 133
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 23-90 1.57e-03

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. The domain present in members of this family 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: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 38.06  E-value: 1.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239686986  23 SDLHGSLPATEKvlSLFERSGADTLVLLGDLLNHGPRNpipdgynptAVAECLNRWAPH---IVAVRGNCD 90
Cdd:cd07392     5 SDVHGDVPKLKK--IKLKAEEADAVIVAGDITHFGPGE---------EAIEALNLLLAIgapVLAVPGNCD 64
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 23-88 8.99e-03

phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs 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: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 35.81  E-value: 8.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239686986  23 SDLHGSLPATEKVLSLFERSGADTLVLLGDLLNHGPRNpipdgynptavAECL-------NRWAPHIVAVRGN 88
Cdd:cd00144     4 GDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDS-----------VEVIdlllalkILYPDNVFLLRGN 65
 
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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