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Conserved domains on  [gi|510924913|ref|WP_016245666|]
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phosphodiesterase YaeI [Escherichia coli]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10013779)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)| bifunctional metallophosphatase/5'-nucleotidase contains an N-terminal metallophosphoesterase family domain that contains an active site consisting of two metal ions (usually manganese, iron, or zinc), and a 5'-nucleotidase C-terminal domain; similar to Escherichia coli UshA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 1-270 0e+00

phosphodiesterase YaeI; Provisional


:

Pssm-ID: 236899  Cd Length: 271  Bit Score: 509.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913   1 MISRRCLLLAAAATLTAGSGFGYMRYWEPGWLELTHQRIAFFKDKAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKP 80
Cdd:PRK11340   2 MISRRRLLQAAAATIATSSGFGYMHYWEPGWFELIRHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  81 DLILLGGDYVLFDMPLNFSAFSNVLSPLAECAPTFACFGNHDRPVGTEKNHLIGETLKSAGITVLFNQATVIATPNRQFE 160
Cdd:PRK11340  82 DLILLGGDYVLFDMPLNFSAFSDVLSPLAECAPTFACFGNHDRPVGTEKNHLIGETLKSAGITVLFNQATVIATPNRQFE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 161 LVGTGDLWAGQCKPPPASEANLPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVEDKRYVAGLNAFG 240
Cdd:PRK11340 162 LVGTGDLWAGQCKPPPASEANLPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVEDKRYVAGLNAFG 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 510924913 241 ERHIYTTRGVGSLYGLRLNCRPEVTMLELV 270
Cdd:PRK11340 242 ERQIYTTRGVGSLYGLRLNCRPEVTMLELV 271
 
Name Accession Description Interval E-value
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 1-270 0e+00

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 509.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913   1 MISRRCLLLAAAATLTAGSGFGYMRYWEPGWLELTHQRIAFFKDKAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKP 80
Cdd:PRK11340   2 MISRRRLLQAAAATIATSSGFGYMHYWEPGWFELIRHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  81 DLILLGGDYVLFDMPLNFSAFSNVLSPLAECAPTFACFGNHDRPVGTEKNHLIGETLKSAGITVLFNQATVIATPNRQFE 160
Cdd:PRK11340  82 DLILLGGDYVLFDMPLNFSAFSDVLSPLAECAPTFACFGNHDRPVGTEKNHLIGETLKSAGITVLFNQATVIATPNRQFE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 161 LVGTGDLWAGQCKPPPASEANLPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVEDKRYVAGLNAFG 240
Cdd:PRK11340 162 LVGTGDLWAGQCKPPPASEANLPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVEDKRYVAGLNAFG 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 510924913 241 ERHIYTTRGVGSLYGLRLNCRPEVTMLELV 270
Cdd:PRK11340 242 ERQIYTTRGVGSLYGLRLNCRPEVTMLELV 271
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
21-270 3.08e-76

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 232.38  E-value: 3.08e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  21 FGYMRYWEPGWLELTHQRIAFFKDKAA--PFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDYVlFDMPLNF 98
Cdd:COG1408   13 LAYGLYIEPRRLRVRRYTVPIPKLPPAfdGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGDLV-DGSVAEL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  99 SAFSNVLSPLAECAPTFACFGNHDRPVGTEKnhlIGETLKSAGITVLFNQATVIATPNRQFELVGTGDLWAGQCKPPPA- 177
Cdd:COG1408   92 EALLELLKKLKAPLGVYAVLGNHDYYAGLEE---LRAALEEAGVRVLRNEAVTLERGGDRLNLAGVDDPHAGRFPDLEKa 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 178 ---SEANLPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVE-DKRYVAGLNAFGERHIYTTRGVG-S 252
Cdd:COG1408  169 lagVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIGALLTPVRlGRKYVAGLYREGGTQLYVSRGLGtS 248

                        250
                 ....*....|....*...
gi 510924913 253 LYGLRLNCRPEVTMLELV 270
Cdd:COG1408  249 GPPVRFGCPPEITLITLK 266
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 48-269 9.07e-49

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE 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: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 160.91  E-value: 9.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  48 PFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDYVlFDMPLNFSAFSNVLSPLAECAPTFACFGNHDRPVGT 127
Cdd:cd07385    1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLV-DGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 128 EKNHLigETLKSAGITVLFNQATVIATPNRQFELVGTGDLWAGQCKPPP-----ASEANLPRLVLAHNPDSKEVMRDEPW 202
Cdd:cd07385   80 VEVWI--AALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGGHGEDLekalkGLDENDPVILLAHNPDAAEEAQRPGV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510924913 203 DLMLCGHTHGGQLRVPLVGepFAPVEDKRYVAGLNAFGER-HIYTTRGVG-SLYGLRLNCRPEVTMLEL 269
Cdd:cd07385  158 DLVLSGHTHGGQIFPPNYG--VLSKLGFPYDSGLYQIGGTtYLYVSRGLGtWGPPIRLGCPPEITLITL 224
lipid_A_LpxG NF033458
UDP-2,3-diacylglucosamine diphosphatase LpxG; Members of this family are LpxG, the lipid A ...
 21-270 6.00e-31

UDP-2,3-diacylglucosamine diphosphatase LpxG; Members of this family are LpxG, the lipid A biosynthesis enzyme UDP-2,3-diacylglucosamine diphosphatase ()EC 3.6.1.54). This family is unrelated to the more common LpxH, or to LpxI, which share the same activity.


Pssm-ID: 380300 [Multi-domain]  Cd Length: 321  Bit Score: 117.13  E-value: 6.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  21 FGYMRYWEPGWLELTHQRIAFFKDKAA--PFKILFLADLHYSRFVP---LSLISDAIAlgiEQKPDLILLGGDYVL---F 92
Cdd:NF033458  15 GIWARFIEPNLLRVSKLTWKLPKKPAHlhGLRIVQISDLHFNKSVPqkfLKKVSRKIK---SLSPDILVFTGDFLCrakL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  93 DMPLNFSAFSNVL-SPLAecapTFACFGNHD-----------------------------------RPVG---------- 126
Cdd:NF033458  92 EDKERLKAFLNSLhAPLG----CFAILGNHDydsyvsrnikgdidvippsssrplkrafisllqglFPSGhykyaenlkp 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 127 TEKNHLIGETLKSAGITVLFNQATVIatPNrQFELVGTGDLWAGQCKPPPA---SEANLPRLVLAHNPDSKEVMRDEPWD 203
Cdd:NF033458 168 QEPHPELLTLLKNTPFRLLHNETHQI--PD-TLNIVGLGDLFAKQFDPEKAfknYNPTLPGIILSHNPDTIPLLEDYPGD 244

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510924913 204 LMLCGHTHGGQLRVP------LVGEPFAPVEDKRYVAGLNAF--GERHIYTTRGVGSLYGLRLNCRPEVTMLELV 270
Cdd:NF033458 245 LILSGHTHGPQINLPwpkfanKIWNKFSGLENPHLARGLFLFseGKKQLYVNRGLGGLKRFRFFSPPEICLMTCK 319
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 49-122 9.19e-07

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: 46.82  E-value: 9.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510924913   49 FKILFLADLHYS-RFVPLSLISDAIAlgIEQKPDLILLGGDYVlfDMPLNFSAFSNVLSPLAECAPTFACFGNHD 122
Cdd:pfam00149   1 MRILVIGDLHLPgQLDDLLELLKKLL--EEGKPDLVLHAGDLV--DRGPPSEEVLELLERLIKYVPVYLVRGNHD 71
 
Name Accession Description Interval E-value
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 1-270 0e+00

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 509.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913   1 MISRRCLLLAAAATLTAGSGFGYMRYWEPGWLELTHQRIAFFKDKAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKP 80
Cdd:PRK11340   2 MISRRRLLQAAAATIATSSGFGYMHYWEPGWFELIRHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  81 DLILLGGDYVLFDMPLNFSAFSNVLSPLAECAPTFACFGNHDRPVGTEKNHLIGETLKSAGITVLFNQATVIATPNRQFE 160
Cdd:PRK11340  82 DLILLGGDYVLFDMPLNFSAFSDVLSPLAECAPTFACFGNHDRPVGTEKNHLIGETLKSAGITVLFNQATVIATPNRQFE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 161 LVGTGDLWAGQCKPPPASEANLPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVEDKRYVAGLNAFG 240
Cdd:PRK11340 162 LVGTGDLWAGQCKPPPASEANLPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVEDKRYVAGLNAFG 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 510924913 241 ERHIYTTRGVGSLYGLRLNCRPEVTMLELV 270
Cdd:PRK11340 242 ERQIYTTRGVGSLYGLRLNCRPEVTMLELV 271
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
21-270 3.08e-76

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 232.38  E-value: 3.08e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  21 FGYMRYWEPGWLELTHQRIAFFKDKAA--PFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDYVlFDMPLNF 98
Cdd:COG1408   13 LAYGLYIEPRRLRVRRYTVPIPKLPPAfdGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGDLV-DGSVAEL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  99 SAFSNVLSPLAECAPTFACFGNHDRPVGTEKnhlIGETLKSAGITVLFNQATVIATPNRQFELVGTGDLWAGQCKPPPA- 177
Cdd:COG1408   92 EALLELLKKLKAPLGVYAVLGNHDYYAGLEE---LRAALEEAGVRVLRNEAVTLERGGDRLNLAGVDDPHAGRFPDLEKa 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 178 ---SEANLPRLVLAHNPDSKEVMRDEPWDLMLCGHTHGGQLRVPLVGEPFAPVE-DKRYVAGLNAFGERHIYTTRGVG-S 252
Cdd:COG1408  169 lagVPPDAPRILLAHNPDVFDEAAAAGVDLQLSGHTHGGQIRLPGIGALLTPVRlGRKYVAGLYREGGTQLYVSRGLGtS 248

                        250
                 ....*....|....*...
gi 510924913 253 LYGLRLNCRPEVTMLELV 270
Cdd:COG1408  249 GPPVRFGCPPEITLITLK 266
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 48-269 9.07e-49

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE 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: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 160.91  E-value: 9.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  48 PFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDYVlFDMPLNFSAFSNVLSPLAECAPTFACFGNHDRPVGT 127
Cdd:cd07385    1 GLRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLV-DGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 128 EKNHLigETLKSAGITVLFNQATVIATPNRQFELVGTGDLWAGQCKPPP-----ASEANLPRLVLAHNPDSKEVMRDEPW 202
Cdd:cd07385   80 VEVWI--AALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGGHGEDLekalkGLDENDPVILLAHNPDAAEEAQRPGV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510924913 203 DLMLCGHTHGGQLRVPLVGepFAPVEDKRYVAGLNAFGER-HIYTTRGVG-SLYGLRLNCRPEVTMLEL 269
Cdd:cd07385  158 DLVLSGHTHGGQIFPPNYG--VLSKLGFPYDSGLYQIGGTtYLYVSRGLGtWGPPIRLGCPPEITLITL 224
lipid_A_LpxG NF033458
UDP-2,3-diacylglucosamine diphosphatase LpxG; Members of this family are LpxG, the lipid A ...
 21-270 6.00e-31

UDP-2,3-diacylglucosamine diphosphatase LpxG; Members of this family are LpxG, the lipid A biosynthesis enzyme UDP-2,3-diacylglucosamine diphosphatase ()EC 3.6.1.54). This family is unrelated to the more common LpxH, or to LpxI, which share the same activity.


Pssm-ID: 380300 [Multi-domain]  Cd Length: 321  Bit Score: 117.13  E-value: 6.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  21 FGYMRYWEPGWLELTHQRIAFFKDKAA--PFKILFLADLHYSRFVP---LSLISDAIAlgiEQKPDLILLGGDYVL---F 92
Cdd:NF033458  15 GIWARFIEPNLLRVSKLTWKLPKKPAHlhGLRIVQISDLHFNKSVPqkfLKKVSRKIK---SLSPDILVFTGDFLCrakL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  93 DMPLNFSAFSNVL-SPLAecapTFACFGNHD-----------------------------------RPVG---------- 126
Cdd:NF033458  92 EDKERLKAFLNSLhAPLG----CFAILGNHDydsyvsrnikgdidvippsssrplkrafisllqglFPSGhykyaenlkp 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 127 TEKNHLIGETLKSAGITVLFNQATVIatPNrQFELVGTGDLWAGQCKPPPA---SEANLPRLVLAHNPDSKEVMRDEPWD 203
Cdd:NF033458 168 QEPHPELLTLLKNTPFRLLHNETHQI--PD-TLNIVGLGDLFAKQFDPEKAfknYNPTLPGIILSHNPDTIPLLEDYPGD 244

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510924913 204 LMLCGHTHGGQLRVP------LVGEPFAPVEDKRYVAGLNAF--GERHIYTTRGVGSLYGLRLNCRPEVTMLELV 270
Cdd:NF033458 245 LILSGHTHGPQINLPwpkfanKIWNKFSGLENPHLARGLFLFseGKKQLYVNRGLGGLKRFRFFSPPEICLMTCK 319
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
50-213 8.74e-11

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 60.03  E-value: 8.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  50 KILFLADLHYSRfvplSLISDAIALGIEQKPDLILLGGDYVLFDMPlnfSAFSNVLSPLAEC-APTFACFGNHDRPvgte 128
Cdd:COG2129    1 KILAVSDLHGNF----DLLEKLLELARAEDADLVILAGDLTDFGTA---EEAREVLEELAALgVPVLAVPGNHDDP---- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 129 knhLIGETLKSAGITVLFNQATVIATpnrqFELVGTGDLWAGQ-CKPPPASEANL-----------PRLVLAHNP---DS 193
Cdd:COG2129   70 ---EVLDALEESGVHNLHGRVVEIGG----LRIAGLGGSRPTPfGTPYEYTEEEIeerlaklrekdVDILLTHAPpygTT 142

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 510924913 194 KEVMRDEPW---------------DLMLCGHTHGG 213
Cdd:COG2129  143 LDRVEDGPHvgskalrelieefqpKLVLHGHIHES 177
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
49-211 5.79e-09

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 55.08  E-value: 5.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  49 FKILFLADLHYSR---FVPLSLISDAIALGIEQKPDLILLGGDYVLFDMPLNFSAFSNVLSPLAecAPTFACFGNHDRPV 125
Cdd:COG1409    1 FRFAHISDLHLGApdgSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG--VPVYVVPGNHDIRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 126 GTEKN---HLIGETLKSAGITVLFNQATVIATpNRQFELVGTGDLWAGQ-------CKPPPASeanlPRLVLAHNP---- 191
Cdd:COG1409   79 AMAEAyreYFGDLPPGGLYYSFDYGGVRFIGL-DSNVPGRSSGELGPEQlawleeeLAAAPAK----PVIVFLHHPpyst 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 510924913 192 ---DSKEVMRDEPW----------DLMLCGHTH 211
Cdd:COG1409  154 gsgSDRIGLRNAEEllallarygvDLVLSGHVH 186
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
49-214 2.17e-08

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 53.76  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  49 FKILFLADLHY-SRFVPLSLISD-------AIALGIEQKPDLILLGGDyvLFDMPlNFSA-----FSNVLSPLAEC-APT 114
Cdd:COG0420    1 MRFLHTADWHLgKPLHGASRREDqlaaldrLVDLAIEEKVDAVLIAGD--LFDSA-NPSPeavrlLAEALRRLSEAgIPV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 115 FACFGNHDRPVGTEKNHLIgetLKSAGITVLfnqATVIATPnrqFELVGTGDLW-AGQCKPPPASEANL----------- 182
Cdd:COG0420   78 VLIAGNHDSPSRLSAGSPL---LENLGVHVF---GSVEPEP---VELEDGLGVAvYGLPYLRPSDEEALrdllerlpral 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 510924913 183 ----PRLVLAH--------------NPDSKEVMRDEPWDLMLCGHTHGGQ 214
Cdd:COG0420  149 dpggPNILLLHgfvagasgsrdiyvAPVPLSALPAAGFDYVALGHIHRPQ 198
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 49-122 9.19e-07

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: 46.82  E-value: 9.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510924913   49 FKILFLADLHYS-RFVPLSLISDAIAlgIEQKPDLILLGGDYVlfDMPLNFSAFSNVLSPLAECAPTFACFGNHD 122
Cdd:pfam00149   1 MRILVIGDLHLPgQLDDLLELLKKLL--EEGKPDLVLHAGDLV--DRGPPSEEVLELLERLIKYVPVYLVRGNHD 71
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
50-211 1.07e-06

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 47.99  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  50 KILFLADLHySRFVPLSLISDAIAlgiEQKPDLILLGGDYVlfdmplNFSAFSN-VLSPLAEcAPTFACFGNHDRPVGTE 128
Cdd:COG0622    1 KIAVISDTH-GNLPALEAVLEDLE---REGVDLIVHLGDLV------GYGPDPPeVLDLLRE-LPIVAVRGNHDGAVLRG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913 129 KNHL-IGETLKSAGITVLFnqatVIATPNRQFelvgtgdlwagqckPPPASEANLprlvlahnpdsKEVMRDEPWDLMLC 207
Cdd:COG0622   70 LRSLpETLRLELEGVRILL----VHGSPNEYL--------------LPDTPAERL-----------RALAAEGDADVVVC 120


                 ....
gi 510924913 208 GHTH 211
Cdd:COG0622  121 GHTH 124
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 50-126 5.58e-06

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 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: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 45.72  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  50 KILFLADLH--YSRFVPLSLISD-------AIALGIEQKPDLILLGGDyvLFD--MPlNFSA---FSNVLSPLAE-CAPT 114
Cdd:cd00840    1 RFLHTADWHlgYPLYGLSRREEDffkafeeIVDLAIEEKVDFVLIAGD--LFDsnNP-SPEAlklAIEGLRRLCEaGIPV 77

                         90
                 ....*....|..
gi 510924913 115 FACFGNHDRPVG 126
Cdd:cd00840   78 FVIAGNHDSPAR 89
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 52-122 1.84e-04

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: 40.33  E-value: 1.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510924913  52 LFLADLHYSRFVPLSLISDAIALgiEQKPDLILLGGDYVLFDMPLNFsAFSNVLSPLAECAPTFACFGNHD 122
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAALAK--AEKPDLVICLGDLVDYGPDPEE-VELKALRLLLAGIPVYVVPGNHD 68
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 49-124 9.69e-04

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: 9.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  49 FKILFLADLHYSRFV------------PLSLISDAIAlgiEQKPDLILLGGDyvLFD----MPLNF-SAFSNVLSPLAEC 111
Cdd:cd07383    3 FKILQFADLHFGEGEwtcwegceadlkTVEFIESVLD---EEKPDLVVLTGD--LITgentADDNAtSYLDKAVSPLVER 77

                         90
                 ....*....|....
gi 510924913 112 APTFA-CFGNHDRP 124
Cdd:cd07383   78 GIPWAaTFGNHDGY 91
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 50-126 1.59e-03

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: 38.06  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510924913   50 KILFLADLHYSRFVPlslisDAIALGIEQKPDLILLGGDYVLFdmplnfsafsNVLSPLAECAPTFACFGNHDRPVG 126
Cdd:pfam12850   2 RIGIISDTHDNLALP-----EAALERLKGVVDLIIHAGDIVAP----------EVLEELLELAPVLAVRGNNDAAAE 63
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 48-123 5.46e-03

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: 37.66  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510924913  48 PFKILFLADL----HYSRFVPLSLISDAialgieQKPDLILLGGDY---VLFDMPLNFSAFSNVLSPLAECAPTFACFGN 120
Cdd:cd00839    4 PLKFAVFGDMgqntNNSTNTLDHLEKEL------GNYDAIIHVGDIayaDGYNNGSRWDTFMRQIEPLASYVPYMVAPGN 77


                 ...
gi 510924913 121 HDR 123
Cdd:cd00839   78 HEA 80
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 51-123 6.82e-03

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the 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: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 36.12  E-value: 6.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510924913  51 ILFLADLHYSR-FVPLSLISDAIALGIEQKPDLILLGGDYVLFDMPLNFSAFSNVLSPLaECAPTFACFGNHDR 123
Cdd:cd07400    1 IAHISDLHFGEeRKPEVLELNLLDEINALKPDLVVVTGDLTQRARPAEFEEAREFLDAL-EPEPVVVVPGNHDA 73
 
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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