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Conserved domains on  [gi|928529884|ref|XP_014083739|]
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uncharacterized protein COCC4DRAFT_185242 [Bipolaris maydis ATCC 48331]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10164588)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc); similar to Kluyveromyces lactis protein SIA1 that may be involved in the activation of the plasma membrane proton-ATPase by glucose; may be inactive

CATH:  3.60.21.10
Gene Ontology:  GO:0046872
PubMed:  25837850|8003970
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 216-485 6.84e-60

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: 197.13  E-value: 6.84e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 216 GKFKIMQISDLHLSTGLGKCRdeepkgangGHCDADPRTIEFVERVLDDEKPDMVVLSGDQINGDTAPD--VQSAMFKIV 293
Cdd:cd07383    1 GKFKILQFADLHFGEGEWTCW---------EGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 294 DPLAERKIPYAAIFGNHDdegtlsrhaqmdlydslpysvsepgtntidgvgnyfveiqahsskhsaltlwfldthsyspd 373
Cdd:cd07383   72 SPLVERGIPWAATFGNHD-------------------------------------------------------------- 89

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 374 ethyrGYDWIKPNQIEWFKTTAESLKEAhrhYTHKHLDMAFIHIPLPEY---GDRDNDRVGNWTEPITAPAFNTHFKDAL 450
Cdd:cd07383   90 -----GYDWIDPSQVEWFESTSAALKKK---YGKNIPSLAFFHIPLPEYrevWNEKGKLGGINREKVCCQKTNSGFFKAL 161

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 928529884 451 VEF-NIKSVSCGHDHVNDYCSLAKDpttgepQIWMC 485
Cdd:cd07383  162 VKRgDVKAVFCGHDHGNDFCGRWKN------GIWLC 191
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 216-485 6.84e-60

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: 197.13  E-value: 6.84e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 216 GKFKIMQISDLHLSTGLGKCRdeepkgangGHCDADPRTIEFVERVLDDEKPDMVVLSGDQINGDTAPD--VQSAMFKIV 293
Cdd:cd07383    1 GKFKILQFADLHFGEGEWTCW---------EGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 294 DPLAERKIPYAAIFGNHDdegtlsrhaqmdlydslpysvsepgtntidgvgnyfveiqahsskhsaltlwfldthsyspd 373
Cdd:cd07383   72 SPLVERGIPWAATFGNHD-------------------------------------------------------------- 89

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 374 ethyrGYDWIKPNQIEWFKTTAESLKEAhrhYTHKHLDMAFIHIPLPEY---GDRDNDRVGNWTEPITAPAFNTHFKDAL 450
Cdd:cd07383   90 -----GYDWIDPSQVEWFESTSAALKKK---YGKNIPSLAFFHIPLPEYrevWNEKGKLGGINREKVCCQKTNSGFFKAL 161

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 928529884 451 VEF-NIKSVSCGHDHVNDYCSLAKDpttgepQIWMC 485
Cdd:cd07383  162 VKRgDVKAVFCGHDHGNDFCGRWKN------GIWLC 191
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
218-468 3.53e-19

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 86.67  E-value: 3.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 218 FKIMQISDLHLSTGLGKcrdeepkgangghcdadpRTIEFVERVLDD---EKPDMVVLSGDQINGDTAPDVQSAmfkiVD 294
Cdd:COG1409    1 FRFAHISDLHLGAPDGS------------------DTAEVLAAALADinaPRPDFVVVTGDLTDDGEPEEYAAA----RE 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 295 PLAERKIPYAAIFGNHDDEGTLS----RHAQMDLYDSLPYSVSEPGtntidgvgnyfveiqahsskhsaLTLWFLDTHSY 370
Cdd:COG1409   59 ILARLGVPVYVVPGNHDIRAAMAeayrEYFGDLPPGGLYYSFDYGG-----------------------VRFIGLDSNVP 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 371 SpdethyRGYDWIKPNQIEWFKTTAESLKEAHRhythkhldMAFIHIPL-PEYGDRDNDRVGNWTEpitapafnthFKDA 449
Cdd:COG1409  116 G------RSSGELGPEQLAWLEEELAAAPAKPV--------IVFLHHPPySTGSGSDRIGLRNAEE----------LLAL 171

                        250
                 ....*....|....*....
gi 928529884 450 LVEFNIKSVSCGHDHVNDY 468
Cdd:COG1409  172 LARYGVDLVLSGHVHRYER 190
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 218-312 1.93e-05

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 44.13  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884  218 FKIMQISDLHLSTGLgkcrdeepkgangghcdadPRTIEFVERVLDDEKPDMVVLSGDQINGDTAPDVQSAMFKivdpLA 297
Cdd:pfam00149   1 MRILVIGDLHLPGQL-------------------DDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLE----RL 57

                          90
                  ....*....|....*
gi 928529884  298 ERKIPYAAIFGNHDD 312
Cdd:pfam00149  58 IKYVPVYLVRGNHDF 72
 
Name Accession Description Interval E-value
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 216-485 6.84e-60

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: 197.13  E-value: 6.84e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 216 GKFKIMQISDLHLSTGLGKCRdeepkgangGHCDADPRTIEFVERVLDDEKPDMVVLSGDQINGDTAPD--VQSAMFKIV 293
Cdd:cd07383    1 GKFKILQFADLHFGEGEWTCW---------EGCEADLKTVEFIESVLDEEKPDLVVLTGDLITGENTADdnATSYLDKAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 294 DPLAERKIPYAAIFGNHDdegtlsrhaqmdlydslpysvsepgtntidgvgnyfveiqahsskhsaltlwfldthsyspd 373
Cdd:cd07383   72 SPLVERGIPWAATFGNHD-------------------------------------------------------------- 89

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 374 ethyrGYDWIKPNQIEWFKTTAESLKEAhrhYTHKHLDMAFIHIPLPEY---GDRDNDRVGNWTEPITAPAFNTHFKDAL 450
Cdd:cd07383   90 -----GYDWIDPSQVEWFESTSAALKKK---YGKNIPSLAFFHIPLPEYrevWNEKGKLGGINREKVCCQKTNSGFFKAL 161

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 928529884 451 VEF-NIKSVSCGHDHVNDYCSLAKDpttgepQIWMC 485
Cdd:cd07383  162 VKRgDVKAVFCGHDHGNDFCGRWKN------GIWLC 191
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
218-468 3.53e-19

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 86.67  E-value: 3.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 218 FKIMQISDLHLSTGLGKcrdeepkgangghcdadpRTIEFVERVLDD---EKPDMVVLSGDQINGDTAPDVQSAmfkiVD 294
Cdd:COG1409    1 FRFAHISDLHLGAPDGS------------------DTAEVLAAALADinaPRPDFVVVTGDLTDDGEPEEYAAA----RE 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 295 PLAERKIPYAAIFGNHDDEGTLS----RHAQMDLYDSLPYSVSEPGtntidgvgnyfveiqahsskhsaLTLWFLDTHSY 370
Cdd:COG1409   59 ILARLGVPVYVVPGNHDIRAAMAeayrEYFGDLPPGGLYYSFDYGG-----------------------VRFIGLDSNVP 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 371 SpdethyRGYDWIKPNQIEWFKTTAESLKEAHRhythkhldMAFIHIPL-PEYGDRDNDRVGNWTEpitapafnthFKDA 449
Cdd:COG1409  116 G------RSSGELGPEQLAWLEEELAAAPAKPV--------IVFLHHPPySTGSGSDRIGLRNAEE----------LLAL 171

                        250
                 ....*....|....*....
gi 928529884 450 LVEFNIKSVSCGHDHVNDY 468
Cdd:COG1409  172 LARYGVDLVLSGHVHRYER 190
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
194-311 4.45e-10

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 60.58  E-value: 4.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 194 RLTIRRgraVKLekPIPKIRKDGK-FKIMQISDLHLSTGLGKcrdeepkgangghcdadprtiEFVERVLD---DEKPDM 269
Cdd:COG1408   23 RLRVRR---YTV--PIPKLPPAFDgLRIVQLSDLHLGPFIGG---------------------ERLERLVEkinALKPDL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 928529884 270 VVLSGDQINGDTAPdvqsaMFKIVDPLAE--RKIPYAAIFGNHD 311
Cdd:COG1408   77 VVLTGDLVDGSVAE-----LEALLELLKKlkAPLGVYAVLGNHD 115
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
218-323 2.83e-06

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 48.76  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 218 FKIMQISDLHL-STGLGKCRDEEpkgangghcdadprTIEFVERVLD---DEKPDMVVLSGDqI--NGDTAPDVQSAMFK 291
Cdd:COG0420    1 MRFLHTADWHLgKPLHGASRRED--------------QLAALDRLVDlaiEEKVDAVLIAGD-LfdSANPSPEAVRLLAE 65

                         90       100       110
                 ....*....|....*....|....*....|..
gi 928529884 292 IVDPLAERKIPYAAIFGNHDDEGTLSRHAQMD 323
Cdd:COG0420   66 ALRRLSEAGIPVVLIAGNHDSPSRLSAGSPLL 97
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 218-311 5.70e-06

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: 47.66  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 218 FKIMQISDLHLstglgkcrdeepkGANGGhcdaDPRTIEFVERVLdDEKPDMVVLSGDQINGDTaPDVQSAmfkiVDPLA 297
Cdd:cd07385    2 LRIVQLSDIHL-------------GPFVG----RTRLQKVVRKVN-ELNPDLIVITGDLVDGDV-SVLRLL----ASPLS 58

                         90
                 ....*....|....*.
gi 928529884 298 ERKIPYAAIF--GNHD 311
Cdd:cd07385   59 KLKAPLGVYFvlGNHD 74
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 218-312 1.93e-05

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 44.13  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884  218 FKIMQISDLHLSTGLgkcrdeepkgangghcdadPRTIEFVERVLDDEKPDMVVLSGDQINGDTAPDVQSAMFKivdpLA 297
Cdd:pfam00149   1 MRILVIGDLHLPGQL-------------------DDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLE----RL 57

                          90
                  ....*....|....*
gi 928529884  298 ERKIPYAAIFGNHDD 312
Cdd:pfam00149  58 IKYVPVYLVRGNHDF 72
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
219-318 1.00e-04

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 43.85  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 219 KIMQISDLHLSTGLgkcrdeepkgangghcdadprtIEFVERVLDDEKPDMVVLSGDQINGDTAPDVQsamfKIVDPLAE 298
Cdd:COG2129    1 KILAVSDLHGNFDL----------------------LEKLLELARAEDADLVILAGDLTDFGTAEEAR----EVLEELAA 54

                         90       100
                 ....*....|....*....|
gi 928529884 299 RKIPYAAIFGNHDDEGTLSR 318
Cdd:COG2129   55 LGVPVLAVPGNHDDPEVLDA 74
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 219-312 1.03e-04

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: 43.41  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 219 KIMQISDLHLstglgkcrdeepkGAN-GGHCDADPRTIEFVERVLD---DEKPDMVVLSGDQINGDT-APDVQSAMFKIV 293
Cdd:cd00840    1 RFLHTADWHL-------------GYPlYGLSRREEDFFKAFEEIVDlaiEEKVDFVLIAGDLFDSNNpSPEALKLAIEGL 67

                         90
                 ....*....|....*....
gi 928529884 294 DPLAERKIPYAAIFGNHDD 312
Cdd:cd00840   68 RRLCEAGIPVFVIAGNHDS 86
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 220-465 1.62e-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: 43.42  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 220 IMQISDLHLSTglgkcrdeEPKGANGGHcdaDPRtiEFVERVLD-----DEKPDMVVLSGDQINGDTAPDVQsamfKIVD 294
Cdd:cd07402    1 IAQISDTHLFA--------PGEGALLGV---DTA--ARLAAAVAqvnalHPRPDLVVVTGDLSDDGSPESYE----RLRE 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 295 PLAERKIPYAAIFGNHDDEGTlsrhaqmdLYDSLPysvsEPGTNTIDGVgnYFVEIQAHsskhsaLTLWFLDTHsySPDE 374
Cdd:cd07402   64 LLAPLPAPVYWIPGNHDDRAA--------MREALP----EPPYDDNGPV--QYVVDFGG------WRLILLDTS--VPGV 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 375 THYrgydWIKPNQIEWFkttAESLKEAhrhyTHKHLDMAFIHIPLPEyGDRDNDRVGnwtepitapAFNTHFKDALVE-- 452
Cdd:cd07402  122 HHG----ELSDEQLDWL---EAALAEA----PDRPTLIFLHHPPFPL-GIPWMDAIR---------LRNSQALFAVLArh 180

                        250
                 ....*....|...
gi 928529884 453 FNIKSVSCGHDHV 465
Cdd:cd07402  181 PQVKAILCGHIHR 193
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 247-311 3.42e-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: 40.71  E-value: 3.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928529884 247 HCDADPRTIEFVERVLDDEKPDMVVLSGDQINGDTAPDVQSAMFKIvdpLAERKIPYAAIFGNHD 311
Cdd:cd00838    7 HGNLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALR---LLLAGIPVYVVPGNHD 68
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 220-464 5.17e-03

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: 38.89  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 220 IMQISDLHLStglgKCRDEEPKgangghcdadpRTIEFVERVLDDEKPDMVVLSGDQINGDTAPDVQSAMFKIVDP---L 296
Cdd:cd07401    2 FVHLTDIHVS----SFHDPNRI-----------QDETFCSNFIDVIKPTLVLITGDLTDNKTGNKLPSYQYQEEWQwkyY 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 297 AERKIPYAA-------IFGNHDDEGTLSRHAQMDLYdsLPYSVSEPgtntidgvgnyfveiqahSSKHSALTLWFLDTHS 369
Cdd:cd07401   67 NILKESSVInkeylfdIRGNHDLFGIVSFDSQNNYY--RKYSNTGR------------------DHSHSFSSTTRFGNYS 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 370 YSP-DETHYRG----YDWI---KPNQIEWFKTTAESLKEAHR-----HYTHKHLDmafihiplpeygdrdndrvgnwteP 436
Cdd:cd07401  127 FIGfDPTIFPGpkrpFNFFgslDKKLLDRLEKELEKSKNSKYtiwfgHYPHSLII------------------------S 182

                        250       260
                 ....*....|....*....|....*...
gi 928529884 437 ITAPAFNTHFKDALVEFNIKSVSCGHDH 464
Cdd:cd07401  183 PSAKSSSKTFKDLLKKYNVTAYLCGHLH 210
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 220-311 5.36e-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: 39.20  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 220 IMQISDLHLS------------TGLGKCRDEEPKGANGG--------HCDADPRTIE----FVERVLDdeKPDMVVLSGD 275
Cdd:cd00842    1 FLHISDIHYDplykvgseyancRSPLCCRDESGPGDVKPpagywgtyGCDSPWSLVEsaleAIKKNHP--KPDFILWTGD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 928529884 276 QINGD----TAPDVQSAMFKIVDPLAER--KIPYAAIFGNHD 311
Cdd:cd00842   79 LVRHDvdeqTPEETVESESNLTNLLKKYfpNVPVYPALGNHD 120
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
219-313 7.83e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 37.59  E-value: 7.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928529884 219 KIMQISDLHlstglgkcrdeepkgangGHCDAdprtIEFVERVLDDEKPDMVVLSGDQINGDTAPDvqsamfKIVDPLAE 298
Cdd:COG0622    1 KIAVISDTH------------------GNLPA----LEAVLEDLEREGVDLIVHLGDLVGYGPDPP------EVLDLLRE 52

                         90
                 ....*....|....*
gi 928529884 299 RKIPyaAIFGNHDDE 313
Cdd:COG0622   53 LPIV--AVRGNHDGA 65
MPP_NostocDevT-like cd07397
Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative ...
 259-311 8.61e-03

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: 38.04  E-value: 8.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 928529884 259 ERVLDDEKPDMVVLSGDQINGDTapdvqsamfKIVDPLAERKIPYAAIFGNHD 311
Cdd:cd07397   18 ERALRLLQPDLVLFVGDFGNENV---------QLVRRIASLDLPKAVILGNHD 61
 
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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