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Conserved domains on  [gi|71996034|ref|NP_001022356|]
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Calcineurin-like phosphoesterase domain-containing protein [Caenorhabditis elegans]

Protein Classification

metallophosphoesterase( domain architecture ID 10164616)

metallophosphoesterase contains an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to Bacillus subtilis YkuE, which is specifically targeted by the Tat pathway to the cell wall

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 216-443 9.99e-78

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: 241.03  E-value: 9.99e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 216 LKLAVISDLHAGASVYSEQINQVVEKVLENPVDAILIVGDMVDAPVAEIEDRVRPILQLPAHAPTYFVTGNHEYYYGDVQ 295
Cdd:cd07385   2 LRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGDVE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 296 EWIRFYKNGRINVLENESTMLKGVCLAGVNDIsSPKSGILNTKMDLPKAIHRCPSNTSQIVMAHNPASIREFivdhpkEL 375
Cdd:cd07385  82 VWIAALEKAGITVLRNESVELSRDGATIGLAG-SGVDDIGGHGEDLEKALKGLDENDPVILLAHNPDAAEEA------QR 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 376 SEIDIVLSGHTHAGQFY--VVIPVVYWLLPYFYGLYEIPFGGQLMVMAGSLYQGPPMKMIGMSEVWVLEL 443
Cdd:cd07385 155 PGVDLVLSGHTHGGQIFppNYGVLSKLGFPYDSGLYQIGGTTYLYVSRGLGTWGPPIRLGCPPEITLITL 224
 
Name Accession Description Interval E-value
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 216-443 9.99e-78

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: 241.03  E-value: 9.99e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 216 LKLAVISDLHAGASVYSEQINQVVEKVLENPVDAILIVGDMVDAPVAEIEDRVRPILQLPAHAPTYFVTGNHEYYYGDVQ 295
Cdd:cd07385   2 LRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGDVE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 296 EWIRFYKNGRINVLENESTMLKGVCLAGVNDIsSPKSGILNTKMDLPKAIHRCPSNTSQIVMAHNPASIREFivdhpkEL 375
Cdd:cd07385  82 VWIAALEKAGITVLRNESVELSRDGATIGLAG-SGVDDIGGHGEDLEKALKGLDENDPVILLAHNPDAAEEA------QR 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 376 SEIDIVLSGHTHAGQFY--VVIPVVYWLLPYFYGLYEIPFGGQLMVMAGSLYQGPPMKMIGMSEVWVLEL 443
Cdd:cd07385 155 PGVDLVLSGHTHGGQIFppNYGVLSKLGFPYDSGLYQIGGTTYLYVSRGLGTWGPPIRLGCPPEITLITL 224
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
180-443 2.25e-55

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 184.61  E-value: 2.25e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 180 MIITLLLSVSMFISRDWIVVKEKTIKIKNFTADGNRLKLAVISDLHAGASVYSEQINQVVEKVLENPVDAILIVGDMVDA 259
Cdd:COG1408   7 ALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGDLVDG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 260 PVAEIEDRVRPILQLPAHAPTYFVTGNHEYYYGdVQEWIRFYKNGRINVLENESTMLK----GVCLAGVNDISSPKSGil 335
Cdd:COG1408  87 SVAELEALLELLKKLKAPLGVYAVLGNHDYYAG-LEELRAALEEAGVRVLRNEAVTLErggdRLNLAGVDDPHAGRFP-- 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 336 ntkmDLPKAIHRCPSNTSQIVMAHNPASIREFIVDHpkelseIDIVLSGHTHAGQFYV-----VIPVVYWLLPYFYGLYE 410
Cdd:COG1408 164 ----DLEKALAGVPPDAPRILLAHNPDVFDEAAAAG------VDLQLSGHTHGGQIRLpgigaLLTPVRLGRKYVAGLYR 233

                       250       260       270
                ....*....|....*....|....*....|....
gi 71996034 411 IPfGGQLMVMAGSLYQGPPMKmIGM-SEVWVLEL 443
Cdd:COG1408 234 EG-GTQLYVSRGLGTSGPPVR-FGCpPEITLITL 265
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 203-443 1.76e-15

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 76.43  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034  203 TIKIKNFTADGNRLKLAVISDLHAGASVYSEQINQVVEKVLENPVDAILIVGDMVDAPVAEIEDRVRPILQ-LPAHAPTY 281
Cdd:PRK11340  37 RHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDYVLFDMPLNFSAFSDVLSpLAECAPTF 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034  282 FVTGNHEYYYGDVQEWI--RFYKNGRINVLENESTML----KGVCLAGVNDISSpksgilnTKMDLPKAIHrcpSNTSQI 355
Cdd:PRK11340 117 ACFGNHDRPVGTEKNHLigETLKSAGITVLFNQATVIatpnRQFELVGTGDLWA-------GQCKPPPASE---ANLPRL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034  356 VMAHNPASiREFIVDHPkelseIDIVLSGHTHAGQfyVVIPVVYW-LLP-----YFYGLYeiPFGG-QLMVM--AGSLYq 426
Cdd:PRK11340 187 VLAHNPDS-KEVMRDEP-----WDLMLCGHTHGGQ--LRVPLVGEpFAPvedkrYVAGLN--AFGErQIYTTrgVGSLY- 255

                        250
                 ....*....|....*..
gi 71996034  427 gpPMKMIGMSEVWVLEL 443
Cdd:PRK11340 256 --GLRLNCRPEVTMLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 216-303 1.31e-09

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: 55.68  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034   216 LKLAVISDLHAGASVYSeqINQVVEKVLENP-VDAILIVGDMVDaPVAEIEDRVRPILQLPAHAPTYFVTGNHEYYYGDV 294
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD--LLELLKKLLEEGkPDLVLHAGDLVD-RGPPSEEVLELLERLIKYVPVYLVRGNHDFDYGEC 77


                  ....*....
gi 71996034   295 QEWIRFYKN 303
Cdd:pfam00149  78 LRLYPYLGL 86
 
Name Accession Description Interval E-value
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 216-443 9.99e-78

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: 241.03  E-value: 9.99e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 216 LKLAVISDLHAGASVYSEQINQVVEKVLENPVDAILIVGDMVDAPVAEIEDRVRPILQLPAHAPTYFVTGNHEYYYGDVQ 295
Cdd:cd07385   2 LRIVQLSDIHLGPFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYSGDVE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 296 EWIRFYKNGRINVLENESTMLKGVCLAGVNDIsSPKSGILNTKMDLPKAIHRCPSNTSQIVMAHNPASIREFivdhpkEL 375
Cdd:cd07385  82 VWIAALEKAGITVLRNESVELSRDGATIGLAG-SGVDDIGGHGEDLEKALKGLDENDPVILLAHNPDAAEEA------QR 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 376 SEIDIVLSGHTHAGQFY--VVIPVVYWLLPYFYGLYEIPFGGQLMVMAGSLYQGPPMKMIGMSEVWVLEL 443
Cdd:cd07385 155 PGVDLVLSGHTHGGQIFppNYGVLSKLGFPYDSGLYQIGGTTYLYVSRGLGTWGPPIRLGCPPEITLITL 224
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
180-443 2.25e-55

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 184.61  E-value: 2.25e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 180 MIITLLLSVSMFISRDWIVVKEKTIKIKNFTADGNRLKLAVISDLHAGASVYSEQINQVVEKVLENPVDAILIVGDMVDA 259
Cdd:COG1408   7 ALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFIGGERLERLVEKINALKPDLVVLTGDLVDG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 260 PVAEIEDRVRPILQLPAHAPTYFVTGNHEYYYGdVQEWIRFYKNGRINVLENESTMLK----GVCLAGVNDISSPKSGil 335
Cdd:COG1408  87 SVAELEALLELLKKLKAPLGVYAVLGNHDYYAG-LEELRAALEEAGVRVLRNEAVTLErggdRLNLAGVDDPHAGRFP-- 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 336 ntkmDLPKAIHRCPSNTSQIVMAHNPASIREFIVDHpkelseIDIVLSGHTHAGQFYV-----VIPVVYWLLPYFYGLYE 410
Cdd:COG1408 164 ----DLEKALAGVPPDAPRILLAHNPDVFDEAAAAG------VDLQLSGHTHGGQIRLpgigaLLTPVRLGRKYVAGLYR 233

                       250       260       270
                ....*....|....*....|....*....|....
gi 71996034 411 IPfGGQLMVMAGSLYQGPPMKmIGM-SEVWVLEL 443
Cdd:COG1408 234 EG-GTQLYVSRGLGTSGPPVR-FGCpPEITLITL 265
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
216-411 2.04e-18

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 83.97  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 216 LKLAVISDLHAGA---SVYSEQINQVVEKVLENPVDAILIVGDMV-DAPVAEIEdRVRPILQlPAHAPTYFVTGNHEYYY 291
Cdd:COG1409   1 FRFAHISDLHLGApdgSDTAEVLAAALADINAPRPDFVVVTGDLTdDGEPEEYA-AAREILA-RLGVPVYVVPGNHDIRA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 292 GDVQEWIRFYKNGRINVLeNESTMLKGVCLAGVN--DISSPKSGILNTKMD-LPKAIHRCPSNTSqIVMAHNP-----AS 363
Cdd:COG1409  79 AMAEAYREYFGDLPPGGL-YYSFDYGGVRFIGLDsnVPGRSSGELGPEQLAwLEEELAAAPAKPV-IVFLHHPpystgSG 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71996034 364 IREFIVDHPKELSEI------DIVLSGHTH-------AGQFYVVIP--VVYWLLPYFYGLYEI 411
Cdd:COG1409 157 SDRIGLRNAEELLALlarygvDLVLSGHVHryertrrDGVPYIVAGstGGQVRLPPGYRVIEV 219
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
217-395 2.29e-17

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 80.44  E-value: 2.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 217 KLAVISDLHAGASVYSEqinqVVEKVLENPVDAILIVGDMVD-APVAEIEDRVRPILQLPAhaPTYFVTGNHEYYygdvq 295
Cdd:COG2129   1 KILAVSDLHGNFDLLEK----LLELARAEDADLVILAGDLTDfGTAEEAREVLEELAALGV--PVLAVPGNHDDP----- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 296 EWIRFYKNGRINVLENESTMLKGVCLAGV-----NDISSPksgILNTKMDLPKAIHRCPSNTSQIVMAHNP--------- 361
Cdd:COG2129  70 EVLDALEESGVHNLHGRVVEIGGLRIAGLggsrpTPFGTP---YEYTEEEIEERLAKLREKDVDILLTHAPpygttldrv 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 71996034 362 --------ASIREFIVDHpkelsEIDIVLSGHTHAGQFYVVI 395
Cdd:COG2129 147 edgphvgsKALRELIEEF-----QPKLVLHGHIHESRGVDKI 183
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 203-443 1.76e-15

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 76.43  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034  203 TIKIKNFTADGNRLKLAVISDLHAGASVYSEQINQVVEKVLENPVDAILIVGDMVDAPVAEIEDRVRPILQ-LPAHAPTY 281
Cdd:PRK11340  37 RHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQKPDLILLGGDYVLFDMPLNFSAFSDVLSpLAECAPTF 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034  282 FVTGNHEYYYGDVQEWI--RFYKNGRINVLENESTML----KGVCLAGVNDISSpksgilnTKMDLPKAIHrcpSNTSQI 355
Cdd:PRK11340 117 ACFGNHDRPVGTEKNHLigETLKSAGITVLFNQATVIatpnRQFELVGTGDLWA-------GQCKPPPASE---ANLPRL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034  356 VMAHNPASiREFIVDHPkelseIDIVLSGHTHAGQfyVVIPVVYW-LLP-----YFYGLYeiPFGG-QLMVM--AGSLYq 426
Cdd:PRK11340 187 VLAHNPDS-KEVMRDEP-----WDLMLCGHTHGGQ--LRVPLVGEpFAPvedkrYVAGLN--AFGErQIYTTrgVGSLY- 255

                        250
                 ....*....|....*..
gi 71996034  427 gpPMKMIGMSEVWVLEL 443
Cdd:PRK11340 256 --GLRLNCRPEVTMLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 216-303 1.31e-09

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: 55.68  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034   216 LKLAVISDLHAGASVYSeqINQVVEKVLENP-VDAILIVGDMVDaPVAEIEDRVRPILQLPAHAPTYFVTGNHEYYYGDV 294
Cdd:pfam00149   1 MRILVIGDLHLPGQLDD--LLELLKKLLEEGkPDLVLHAGDLVD-RGPPSEEVLELLERLIKYVPVYLVRGNHDFDYGEC 77


                  ....*....
gi 71996034   295 QEWIRFYKN 303
Cdd:pfam00149  78 LRLYPYLGL 86
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
217-399 2.29e-08

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 54.92  E-value: 2.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 217 KLAVISDLHAGASVYSEQ--------INQVVEKVLENPVDAILIVGDMVDAPVAEIEDRVRPILQL----PAHAPTYFVT 284
Cdd:COG0420   2 RFLHTADWHLGKPLHGASrredqlaaLDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALrrlsEAGIPVVLIA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 285 GNHEyYYGDVQEWIRFYKNGRINVL---ENESTMLK---GVCLAGVNDISspKSGILNTKMDLPKAIHRCPSNTSQIVMA 358
Cdd:COG0420  82 GNHD-SPSRLSAGSPLLENLGVHVFgsvEPEPVELEdglGVAVYGLPYLR--PSDEEALRDLLERLPRALDPGGPNILLL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 71996034 359 H---NPASIREFIVDHPKELSE-----IDIVLSGHTHagQFYVVI---PVVY 399
Cdd:COG0420 159 HgfvAGASGSRDIYVAPVPLSAlpaagFDYVALGHIH--RPQVLGgdpRIRY 208
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 219-288 4.22e-06

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 46.11  E-value: 4.22e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 219 AVISDLHAGasVYSEQINQVVEKVLENPVDAILIVGDMVDAPVAEIEDRVRPILQLPAHAPTYFVTGNHE 288
Cdd:cd00838   1 LVISDIHGN--LEALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHD 68
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 218-402 1.42e-05

Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized Microscilla protein with a metallophosphatase domain. Microscilla proteins MS152, and MS153 are also included in this family. 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: 277349 [Multi-domain]  Cd Length: 201  Bit Score: 45.79  E-value: 1.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 218 LAVISDLHAgaSVYsEQINQVVEKVLENPVDAILIVGDMVDAPVAEIEDrVRPILQLPAHAPTYFVTGNHEYY---YGDV 294
Cdd:cd07404   1 LQIASDLHL--EVE-QNLAKLKFFPKVPDADILILAGDIGRLTDAEAWD-NFLDLQSFQFEPVYYVPGNHEFYggsLDIT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 295 QEWIRFYKNGRINV--LENESTMLKGVCLAGV---NDISSPKSGILNTKM-DLPKAIhrcpsntsqIVMAHNPASIREFI 368
Cdd:cd07404  77 LDALRMAAQDLSNVhyLNNQEVVLDDVRILGCtlwSDFDPDGEDIVQRKLnDFRGAT---------VVVTHHAPSPRSTS 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 71996034 369 VDHPK----------------ELSEIDIVLSGHTHAGQFYVVIPVvyWLL 402
Cdd:cd07404 148 DNYADglpknaafhvdlkdliLAPPIDLWIHGHTHFNTDYSVGGT--RVV 195
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
217-290 1.97e-04

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 42.21  E-value: 1.97e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71996034 217 KLAVISDLHAgasvYSEQINQVVEKVLENPVDAILIVGDMVDAPVAEIE--DRVRpilQLPAHAptyfVTGNHEYY 290
Cdd:COG0622   1 KIAVISDTHG----NLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEvlDLLR---ELPIVA----VRGNHDGA 65
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 218-287 2.81e-04

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: 42.26  E-value: 2.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 218 LAVISDLHAGAS-------VYSEQINQ-VVEKV--LENPVDAILIVGDMVDAPVAEIEDRVRPILQlPAHAPTYFVTGNH 287
Cdd:cd07402   1 IAQISDTHLFAPgegallgVDTAARLAaAVAQVnaLHPRPDLVVVTGDLSDDGSPESYERLRELLA-PLPAPVYWIPGNH 79
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 217-387 5.61e-04

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: 40.33  E-value: 5.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 217 KLAVISDLHAgasvYSEQINQVVEKvLENPVDAILIVGDMVDAPVaeiedrVRPILQLPahAPTYFVTGNHEYYYGDVQE 296
Cdd:cd00841   1 KIGVISDTHG----NLEAIEKALEL-FEDGVDAVIHAGDFVSPFV------LNALLELK--APLIAVRGNNDGEVDQLLG 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 297 WIRFyknGRINVLEnestmlkgvcLAGVndisspksgilntkmdlpkaihrcpsntsQIVMAHNPASIREFIVDHPKELs 376
Cdd:cd00841  68 RPIL---PEFLTLE----------IGGL-----------------------------RILLTHGHLFGVLEALYLAKEG- 104

                       170
                ....*....|.
gi 71996034 377 EIDIVLSGHTH 387
Cdd:cd00841 105 GADVVVFGHTH 115
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 218-287 6.21e-04

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: 39.97  E-value: 6.21e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71996034 218 LAVISDLHAGASVYSEQI-NQVVEKVLENPVDAILIVGDMVD-APVAEIEDRVRPILQLPAHaPTYFVTGNH 287
Cdd:cd07400   1 IAHISDLHFGEERKPEVLeLNLLDEINALKPDLVVVTGDLTQrARPAEFEEAREFLDALEPE-PVVVVPGNH 71
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 217-301 1.27e-03

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: 39.56  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034 217 KLAVISDLHAGASVYS------EQIN---QVVEKVLENPVDAILIVGDMVDAPVAEIEDRVRPILQL----PAHAPTYFV 283
Cdd:cd00840   1 RFLHTADWHLGYPLYGlsrreeDFFKafeEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLrrlcEAGIPVFVI 80

                        90
                ....*....|....*...
gi 71996034 284 TGNHEYYYGdvqewIRFY 301
Cdd:cd00840  81 AGNHDSPAR-----VAIY 93
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 217-296 9.36e-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: 36.52  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996034   217 KLAVISDLHAGAsvysEQINQVVEkVLENPVDAILIVGDMVDAPVAEIEDRVRPIlqlpahaptYFVTGNHEYYYGDVQE 296
Cdd:pfam12850   2 RIGIISDTHDNL----ALPEAALE-RLKGVVDLIIHAGDIVAPEVLEELLELAPV---------LAVRGNNDAAAEFATD 67
 
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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