NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2507793320|ref|WP_283139942|]
View 

metallophosphoesterase [Bacteroides congonensis]

Protein Classification

metallophosphoesterase( domain architecture ID 10003658)

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

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0042578|GO:0016311
PubMed:  25837850|8003970

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
108-387 4.55e-98

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


:

Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 292.47  E-value: 4.55e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 108 TGLTLAVLCIIMILYGSFIGRSQFEVKEVTYSSPRLPQAFDGYRIVQLSDLHIGSWIgNAPDIERMVNLVNAQQPDLIVF 187
Cdd:COG1408     1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFI-GGERLERLVEKINALKPDLVVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 188 TGDLVNHRAKELDGFQEILVRLKAKDGVYSILGNHDYGpyfrwkskqeqdDNLIDLEQRQAAMGWKLLNNSHSILIQGND 267
Cdd:COG1408    80 TGDLVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYY------------AGLEELRAALEEAGVRVLRNEAVTLERGGD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 268 SIALIGVENegePPFSQHGDLAGAKAGTD-GMFQILLSHNPTHWRRevLPKSDVDLMLAGHTHAMQLQF----GSYSPSV 342
Cdd:COG1408   148 RLNLAGVDD---PHAGRFPDLEKALAGVPpDAPRILLAHNPDVFDE--AAAAGVDLQLSGHTHGGQIRLpgigALLTPVR 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2507793320 343 YVYPEWGGMYLEGTRGLYVNVGIGYVGLPFRFGAWPEITVLTLRR 387
Cdd:COG1408   223 LGRKYVAGLYREGGTQLYVSRGLGTSGPPVRFGCPPEITLITLKS 267
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
108-387 4.55e-98

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 292.47  E-value: 4.55e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 108 TGLTLAVLCIIMILYGSFIGRSQFEVKEVTYSSPRLPQAFDGYRIVQLSDLHIGSWIgNAPDIERMVNLVNAQQPDLIVF 187
Cdd:COG1408     1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFI-GGERLERLVEKINALKPDLVVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 188 TGDLVNHRAKELDGFQEILVRLKAKDGVYSILGNHDYGpyfrwkskqeqdDNLIDLEQRQAAMGWKLLNNSHSILIQGND 267
Cdd:COG1408    80 TGDLVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYY------------AGLEELRAALEEAGVRVLRNEAVTLERGGD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 268 SIALIGVENegePPFSQHGDLAGAKAGTD-GMFQILLSHNPTHWRRevLPKSDVDLMLAGHTHAMQLQF----GSYSPSV 342
Cdd:COG1408   148 RLNLAGVDD---PHAGRFPDLEKALAGVPpDAPRILLAHNPDVFDE--AAAAGVDLQLSGHTHGGQIRLpgigALLTPVR 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2507793320 343 YVYPEWGGMYLEGTRGLYVNVGIGYVGLPFRFGAWPEITVLTLRR 387
Cdd:COG1408   223 LGRKYVAGLYREGGTQLYVSRGLGTSGPPVRFGCPPEITLITLKS 267
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 149-385 3.64e-60

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: 194.04  E-value: 3.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 149 GYRIVQLSDLHIGSWIGnAPDIERMVNLVNAQQPDLIVFTGDLVNHRAKELDGFQEILVRLKAKDGVYSILGNHDYGPyf 228
Cdd:cd07385     1 GLRIVQLSDIHLGPFVG-RTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYS-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 229 rwkskqeqdDNLIDLEQRQAAMGWKLLNNSHSILIQGNDSIALIGVENEGEPPFSQHGDLAGaKAGTDGMFQILLSHNPT 308
Cdd:cd07385    78 ---------GDVEVWIAALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGGHGEDLEKAL-KGLDENDPVILLAHNPD 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2507793320 309 HWRRevLPKSDVDLMLAGHTHAMQLQFGSYSPSVYVYPEWG-GMY-LEGTRGLYVNVGIGYVGLPFRFGAWPEITVLTL 385
Cdd:cd07385   148 AAEE--AQRPGVDLVLSGHTHGGQIFPPNYGVLSKLGFPYDsGLYqIGGTTYLYVSRGLGTWGPPIRLGCPPEITLITL 224
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 150-385 8.54e-20

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 88.37  E-value: 8.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 150 YRIVQLSDLHIGSWIgNAPDIERMVNLVNAQQPDLIVFTGDLVNH-RAKELDGFQEILVRLKAKDGVYSILGNHDYgPYf 228
Cdd:PRK11340   50 FKILFLADLHYSRFV-PLSLISDAIALGIEQKPDLILLGGDYVLFdMPLNFSAFSDVLSPLAECAPTFACFGNHDR-PV- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 229 rwkskqeQDDNLIDLEQRQAAMGWKLLNNSHSILIQGNDSIALIGV----ENEGEPPfsqhgdlagaKAGTDGMFQILLS 304
Cdd:PRK11340  127 -------GTEKNHLIGETLKSAGITVLFNQATVIATPNRQFELVGTgdlwAGQCKPP----------PASEANLPRLVLA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 305 HNPThwRREVLPKSDVDLMLAGHTHAMQLQFGSYS-PSVYVYPE--WGGMYLEGTRGLYVNVGIGYVGlPFRFGAWPEIT 381
Cdd:PRK11340  190 HNPD--SKEVMRDEPWDLMLCGHTHGGQLRVPLVGePFAPVEDKryVAGLNAFGERQIYTTRGVGSLY-GLRLNCRPEVT 266


                  ....
gi 2507793320 382 VLTL 385
Cdd:PRK11340  267 MLEL 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 150-224 2.96e-11

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: 59.92  E-value: 2.96e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2507793320 150 YRIVQLSDLHIGswiGNAPDIERMVN-LVNAQQPDLIVFTGDLVnHRAKELDGFQEILVRLKAKDGVYSILGNHDY 224
Cdd:pfam00149   1 MRILVIGDLHLP---GQLDDLLELLKkLLEEGKPDLVLHAGDLV-DRGPPSEEVLELLERLIKYVPVYLVRGNHDF 72
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 150-223 2.70e-03

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 38.94  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 150 YRIVQLSDLHIGSWIGNAPDIERMVNLVN-------AQQPDLIVFTGDL---VNHRAKELDGFQEILVRLKAKD--GVYS 217
Cdd:TIGR00619   1 MRILHTSDWHLGKTLEGVSRLAEQKAFLDdllefakAEQVDALLVAGDVfdtANPPAEAQELFNAFFVNLSDTGirPIVV 80


                  ....*.
gi 2507793320 218 ILGNHD 223
Cdd:TIGR00619  81 ISGNHD 86
 
Name Accession Description Interval E-value
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
108-387 4.55e-98

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 292.47  E-value: 4.55e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 108 TGLTLAVLCIIMILYGSFIGRSQFEVKEVTYSSPRLPQAFDGYRIVQLSDLHIGSWIgNAPDIERMVNLVNAQQPDLIVF 187
Cdd:COG1408     1 LALALLALGLALLAYGLYIEPRRLRVRRYTVPIPKLPPAFDGLRIVQLSDLHLGPFI-GGERLERLVEKINALKPDLVVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 188 TGDLVNHRAKELDGFQEILVRLKAKDGVYSILGNHDYGpyfrwkskqeqdDNLIDLEQRQAAMGWKLLNNSHSILIQGND 267
Cdd:COG1408    80 TGDLVDGSVAELEALLELLKKLKAPLGVYAVLGNHDYY------------AGLEELRAALEEAGVRVLRNEAVTLERGGD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 268 SIALIGVENegePPFSQHGDLAGAKAGTD-GMFQILLSHNPTHWRRevLPKSDVDLMLAGHTHAMQLQF----GSYSPSV 342
Cdd:COG1408   148 RLNLAGVDD---PHAGRFPDLEKALAGVPpDAPRILLAHNPDVFDE--AAAAGVDLQLSGHTHGGQIRLpgigALLTPVR 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2507793320 343 YVYPEWGGMYLEGTRGLYVNVGIGYVGLPFRFGAWPEITVLTLRR 387
Cdd:COG1408   223 LGRKYVAGLYREGGTQLYVSRGLGTSGPPVRFGCPPEITLITLKS 267
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 149-385 3.64e-60

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: 194.04  E-value: 3.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 149 GYRIVQLSDLHIGSWIGnAPDIERMVNLVNAQQPDLIVFTGDLVNHRAKELDGFQEILVRLKAKDGVYSILGNHDYGPyf 228
Cdd:cd07385     1 GLRIVQLSDIHLGPFVG-RTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLKAPLGVYFVLGNHDYYS-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 229 rwkskqeqdDNLIDLEQRQAAMGWKLLNNSHSILIQGNDSIALIGVENEGEPPFSQHGDLAGaKAGTDGMFQILLSHNPT 308
Cdd:cd07385    78 ---------GDVEVWIAALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGGHGEDLEKAL-KGLDENDPVILLAHNPD 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2507793320 309 HWRRevLPKSDVDLMLAGHTHAMQLQFGSYSPSVYVYPEWG-GMY-LEGTRGLYVNVGIGYVGLPFRFGAWPEITVLTL 385
Cdd:cd07385   148 AAEE--AQRPGVDLVLSGHTHGGQIFPPNYGVLSKLGFPYDsGLYqIGGTTYLYVSRGLGTWGPPIRLGCPPEITLITL 224
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
150-367 1.87e-20

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 89.37  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 150 YRIVQLSDLHIGSWIGN--APDIERMVNLVNAQQPDLIVFTGDLVNH-RAKELDGFQEILVRLKAKdgVYSILGNHDYGP 226
Cdd:COG1409     1 FRFAHISDLHLGAPDGSdtAEVLAAALADINAPRPDFVVVTGDLTDDgEPEEYAAAREILARLGVP--VYVVPGNHDIRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 227 YFrwkskqeqddnlidLEQRQAAMGWKLLNNSHSILIQGNdsIALIGV------ENEGEPPFSQ----HGDLAGAKAGtd 296
Cdd:COG1409    79 AM--------------AEAYREYFGDLPPGGLYYSFDYGG--VRFIGLdsnvpgRSSGELGPEQlawlEEELAAAPAK-- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 297 gmFQILLSHNP------------THWRREVLP---KSDVDLMLAGHTHamqlqfgsyspsVYVYPEWGGMYLEGTRGLYV 361
Cdd:COG1409   141 --PVIVFLHHPpystgsgsdrigLRNAEELLAllaRYGVDLVLSGHVH------------RYERTRRDGVPYIVAGSTGG 206


                  ....*.
gi 2507793320 362 NVGIGY 367
Cdd:COG1409   207 QVRLPP 212
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 150-385 8.54e-20

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 88.37  E-value: 8.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 150 YRIVQLSDLHIGSWIgNAPDIERMVNLVNAQQPDLIVFTGDLVNH-RAKELDGFQEILVRLKAKDGVYSILGNHDYgPYf 228
Cdd:PRK11340   50 FKILFLADLHYSRFV-PLSLISDAIALGIEQKPDLILLGGDYVLFdMPLNFSAFSDVLSPLAECAPTFACFGNHDR-PV- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 229 rwkskqeQDDNLIDLEQRQAAMGWKLLNNSHSILIQGNDSIALIGV----ENEGEPPfsqhgdlagaKAGTDGMFQILLS 304
Cdd:PRK11340  127 -------GTEKNHLIGETLKSAGITVLFNQATVIATPNRQFELVGTgdlwAGQCKPP----------PASEANLPRLVLA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 305 HNPThwRREVLPKSDVDLMLAGHTHAMQLQFGSYS-PSVYVYPE--WGGMYLEGTRGLYVNVGIGYVGlPFRFGAWPEIT 381
Cdd:PRK11340  190 HNPD--SKEVMRDEPWDLMLCGHTHGGQLRVPLVGePFAPVEDKryVAGLNAFGERQIYTTRGVGSLY-GLRLNCRPEVT 266


                  ....
gi 2507793320 382 VLTL 385
Cdd:PRK11340  267 MLEL 270
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 152-336 1.76e-11

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: 63.45  E-value: 1.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 152 IVQLSDLHI-----GSWIGNAPDI--ERMVNLVNA--QQPDLIVFTGDLVNH-RAKELDGFQEILVRLKAKdgVYSILGN 221
Cdd:cd07402     1 IAQISDTHLfapgeGALLGVDTAArlAAAVAQVNAlhPRPDLVVVTGDLSDDgSPESYERLRELLAPLPAP--VYWIPGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 222 HDYGPYFRWKSKQEQDDNLIDLEQRQAAMGWKLLnnSHSILIQGndsialigvENEGEPPFSQHGDLAGAKAGTDGMFQI 301
Cdd:cd07402    79 HDDRAAMREALPEPPYDDNGPVQYVVDFGGWRLI--LLDTSVPG---------VHHGELSDEQLDWLEAALAEAPDRPTL 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2507793320 302 LLSHNP----------------THWRREVL-PKSDVDLMLAGHTH-AMQLQFG 336
Cdd:cd07402   148 IFLHHPpfplgipwmdairlrnSQALFAVLaRHPQVKAILCGHIHrPISGSFR 200
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 150-224 2.96e-11

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: 59.92  E-value: 2.96e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2507793320 150 YRIVQLSDLHIGswiGNAPDIERMVN-LVNAQQPDLIVFTGDLVnHRAKELDGFQEILVRLKAKDGVYSILGNHDY 224
Cdd:pfam00149   1 MRILVIGDLHLP---GQLDDLLELLKkLLEEGKPDLVLHAGDLV-DRGPPSEEVLELLERLIKYVPVYLVRGNHDF 72
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 152-224 8.74e-11

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: 59.23  E-value: 8.74e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2507793320 152 IVQLSDLHIGSwIGNAPDIER-MVNLVNAQQPDLIVFTGDLVNhRAK--ELDGFQEILVRLKAKDgVYSILGNHDY 224
Cdd:cd07400     1 IAHISDLHFGE-ERKPEVLELnLLDEINALKPDLVVVTGDLTQ-RARpaEFEEAREFLDALEPEP-VVVVPGNHDA 73
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
151-329 2.07e-10

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: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 151 RIVQLSDLHigswiGNAPDIERMVNLVNAQQPDLIVFTGDLVNHR-AKELDGFQEILVRLKAKdgVYSILGNHDYgpyfr 229
Cdd:COG2129     1 KILAVSDLH-----GNFDLLEKLLELARAEDADLVILAGDLTDFGtAEEAREVLEELAALGVP--VLAVPGNHDD----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 230 wkskqeqddnlIDLEQRQAAMGWKLLNNShSILIQGndsIALIGVENEGEPPFSQHGDL----------AGAKAGTDgmf 299
Cdd:COG2129    69 -----------PEVLDALEESGVHNLHGR-VVEIGG---LRIAGLGGSRPTPFGTPYEYteeeieerlaKLREKDVD--- 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2507793320 300 qILLSHNPTHWR----------------REVLPKSDVDLMLAGHTH 329
Cdd:COG2129   131 -ILLTHAPPYGTtldrvedgphvgskalRELIEEFQPKLVLHGHIH 175
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
151-329 3.85e-10

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 58.77  E-value: 3.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 151 RIVQLSDLHigswiGNAPDIERMVNLVNAQQPDLIVFTGDLVNHRAKELdgfqEILVRLKAKdGVYSILGNHDYgpyfrw 230
Cdd:COG0622     1 KIAVISDTH-----GNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPP----EVLDLLREL-PIVAVRGNHDG------ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 231 kskqEQDDNLIDLEQRQaamgwkllnnshsILIQGNDSIALIgvenegeppfsqHGdlagakagtdGMFQILLSHNPTHW 310
Cdd:COG0622    65 ----AVLRGLRSLPETL-------------RLELEGVRILLV------------HG----------SPNEYLLPDTPAER 105

                         170
                  ....*....|....*....
gi 2507793320 311 RREVLPKSDVDLMLAGHTH 329
Cdd:COG0622   106 LRALAAEGDADVVVCGHTH 124
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
151-332 6.78e-10

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 59.16  E-value: 6.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 151 RIVQLSDLHIGSWIGNA---PD----IERMVNLVNAQQPDLIVFTGDLVNHR---AKELDGFQEILVRLKAKDG-VYSIL 219
Cdd:COG0420     2 RFLHTADWHLGKPLHGAsrrEDqlaaLDRLVDLAIEEKVDAVLIAGDLFDSAnpsPEAVRLLAEALRRLSEAGIpVVLIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 220 GNHDYgPYFRWKSKQEQDDNLIDLEQRQAAmgwkllnnsHSILIQGNDSIALIGVenegepPFSQHGDLAG--------A 291
Cdd:COG0420    82 GNHDS-PSRLSAGSPLLENLGVHVFGSVEP---------EPVELEDGLGVAVYGL------PYLRPSDEEAlrdllerlP 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2507793320 292 KAGTDGMFQILLSH-----NPTHWRR-------EVLPKSDVDLMLAGHTHAMQ 332
Cdd:COG0420   146 RALDPGGPNILLLHgfvagASGSRDIyvapvplSALPAAGFDYVALGHIHRPQ 198
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 153-223 1.34e-09

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: 55.74  E-value: 1.34e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2507793320 153 VQLSDLHIGSWignAPDIERMVNLVNAQQPDLIVFTGDLVNHRAKELDGFQEILVRLKAKDGVYSILGNHD 223
Cdd:cd00838     1 LVISDIHGNLE---ALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHD 68
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 151-343 9.78e-08

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: 51.50  E-value: 9.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 151 RIVQLSDLHIGSWIGNAPDI--------ERMVNLVNAQQPDLIVFTGDLVNHR---AKELDGFQEILVRLKAKDG-VYSI 218
Cdd:cd00840     1 RFLHTADWHLGYPLYGLSRReedffkafEEIVDLAIEEKVDFVLIAGDLFDSNnpsPEALKLAIEGLRRLCEAGIpVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 219 LGNHDYGPYFRwkskqeqddnlidleqrqaamgwkllnnshsiliqgndsIALIGVENEGEPPFSQHGDLAGAKAGTDGM 298
Cdd:cd00840    81 AGNHDSPARVA---------------------------------------IYGLPYLRDERLERLFEDLELRPRLLKPDW 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2507793320 299 FQILLSH------NPTHWRREVLPKSD----VDLMLAGHTHAMQLQFGSYSPSVY 343
Cdd:cd00840   122 FNILLLHqgvdgaGPSDSERPIVPEDLlpdgFDYVALGHIHKPQIIEGGGPPIVY 176
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 150-224 2.39e-07

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: 50.75  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 150 YRIVQLSDLHIGS-----WIGNAPD---IERMVNLVNAQQPDLIVFTGDLVNHRA-------KELDGFQEILVRLK---A 211
Cdd:cd07383     3 FKILQFADLHFGEgewtcWEGCEADlktVEFIESVLDEEKPDLVVLTGDLITGENtaddnatSYLDKAVSPLVERGipwA 82

                          90
                  ....*....|...
gi 2507793320 212 kdgvySILGNHDY 224
Cdd:cd07383    83 -----ATFGNHDG 90
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 152-223 3.01e-04

Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) is an uncharacterized Homo sapiens transmembrane protein with an N-terminal metallophosphatase domain. TMEM62 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277346 [Multi-domain]  Cd Length: 254  Bit Score: 41.97  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 152 IVQLSDLHIGSWI--GNAPDIERMVNLVNAQQPDLIVFTGDLV-NHRAKELDGFQE-------ILVRLKAKDGV-----Y 216
Cdd:cd07401     2 FVHLTDIHVSSFHdpNRIQDETFCSNFIDVIKPTLVLITGDLTdNKTGNKLPSYQYqeewqwkYYNILKESSVInkeylF 81


                  ....*..
gi 2507793320 217 SILGNHD 223
Cdd:cd07401    82 DIRGNHD 88
MPP_NostocDevT-like cd07397
Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative ...
 150-255 3.85e-04

Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative protein phosphatase from Nostoc PCC 7120 (Anabaena PCC 7120). DevT mutants form mature heterocysts, but they are unable to fix N(2) and must be supplied with a source of combined nitrogen in order to survive. Anabaena DevT shows homology to phosphatases of the PPP family and displays a Mn(2+)-dependent phosphatase activity. DevT is constitutively expressed in both vegetative cells and heterocysts, and is not regulated by NtcA. The heterocyst regulator HetR may exert a certain inhibition on the expression of devT. Under diazotrophic growth conditions, DevT protein accumulates specifically in mature heterocysts. The role that DevT plays in a late essential step of heterocyst differentiation is still unknown. 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: 277342 [Multi-domain]  Cd Length: 245  Bit Score: 41.51  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 150 YRIVQLSDLHiGSWigNAPDIErmvnLVNAQQPDLIVFTGDLVNHRAKeldgfqeiLVRLKAK--DGVYSILGNHDygpy 227
Cdd:cd07397     1 VRIAIVGDVH-GQW--DAEDER----ALRLLQPDLVLFVGDFGNENVQ--------LVRRIASldLPKAVILGNHD---- 61

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2507793320 228 fRWKSKQ-----EQDDNLIDLEQRQAAM------GWKLL 255
Cdd:cd07397    62 -AWYTATrwgrcPYDRSKGDRVQQQLEIlgdehvGYGRL 99
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 178-226 1.19e-03

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase 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: 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: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 40.36  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2507793320 178 NAQQPDLIVFTGDLVNH-----RAKELDGFQEILVRLKAKDG----VYSILGNHDYGP 226
Cdd:cd00842    66 NHPKPDFILWTGDLVRHdvdeqTPEETVESESNLTNLLKKYFpnvpVYPALGNHDSYP 123
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 150-223 2.70e-03

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 38.94  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 150 YRIVQLSDLHIGSWIGNAPDIERMVNLVN-------AQQPDLIVFTGDL---VNHRAKELDGFQEILVRLKAKD--GVYS 217
Cdd:TIGR00619   1 MRILHTSDWHLGKTLEGVSRLAEQKAFLDdllefakAEQVDALLVAGDVfdtANPPAEAQELFNAFFVNLSDTGirPIVV 80


                  ....*.
gi 2507793320 218 ILGNHD 223
Cdd:TIGR00619  81 ISGNHD 86
Metallophos_3 pfam14582
Metallophosphoesterase, calcineurin superfamily; Members of this family are part of the ...
 151-198 5.68e-03

Metallophosphoesterase, calcineurin superfamily; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 405297 [Multi-domain]  Cd Length: 259  Bit Score: 38.34  E-value: 5.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2507793320 151 RIVQLSDLHigswiGNAPDIERMVNLVNAQQPDLIVFTGDLVNHRAKE 198
Cdd:pfam14582   7 KVLAISDFH-----GETELLERLVGKIEDKSPDALVLVGDLVKGQARA 49
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 151-226 6.75e-03

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 37.99  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507793320 151 RIVQLSDLHI-----GSWIG-NAPD-IERMVNLVNAQQP--DLIVFTGDLV-NHRAKELDGFQEILVRLKAKdgVYSILG 220
Cdd:PRK11148   16 RILQITDTHLfadehETLLGvNTWEsYQAVLEAIRAQQHefDLIVATGDLAqDHSSEAYQHFAEGIAPLRKP--CVWLPG 93


                  ....*.
gi 2507793320 221 NHDYGP 226
Cdd:PRK11148   94 NHDFQP 99
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH