NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|55925413|ref|NP_001007414|]
View 

serine/threonine-protein phosphatase CPPED1 [Danio rerio]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10164682)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 27-292 2.94e-176

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 487.60  E-value: 2.94e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  27 WSGPFYFIQAADPQLGLMKAWRIGdcdSGGDEWDEEVQLTKQAVQAINKLQPKPRFIVLCGDLVHAMPGSPFREQQIKDL 106
Cdd:cd07395   1 WKGPFYFIQGADPQLGLIKQNNIG---NGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 107 KDALRGTDPHIPLVFVSGNHDLGNAPTPDTVEQFCHEWGDDYFSFWVGGVLCLVLNSQFFFDSSGCPELMEAHEVWLENR 186
Cdd:cd07395  78 KDVLSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQ 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 187 LQMAVQTPSRHVLVFQHIPLFLRTPDEEDDYFNLQRGIREHLIQRFKRAGVKAVFSGHYHRNAGGCHDGLDMVVSSAVGC 266
Cdd:cd07395 158 LQIARESDAKHVVVFQHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGC 237

                       250       260
                ....*....|....*....|....*.
gi 55925413 267 QLGDDTHGVRVVVVTENNIIHRYHSL 292
Cdd:cd07395 238 QLGNDTSGLRVVVVTENKISHRYYSL 263
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 27-292 2.94e-176

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 487.60  E-value: 2.94e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  27 WSGPFYFIQAADPQLGLMKAWRIGdcdSGGDEWDEEVQLTKQAVQAINKLQPKPRFIVLCGDLVHAMPGSPFREQQIKDL 106
Cdd:cd07395   1 WKGPFYFIQGADPQLGLIKQNNIG---NGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 107 KDALRGTDPHIPLVFVSGNHDLGNAPTPDTVEQFCHEWGDDYFSFWVGGVLCLVLNSQFFFDSSGCPELMEAHEVWLENR 186
Cdd:cd07395  78 KDVLSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQ 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 187 LQMAVQTPSRHVLVFQHIPLFLRTPDEEDDYFNLQRGIREHLIQRFKRAGVKAVFSGHYHRNAGGCHDGLDMVVSSAVGC 266
Cdd:cd07395 158 LQIARESDAKHVVVFQHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGC 237

                       250       260
                ....*....|....*....|....*.
gi 55925413 267 QLGDDTHGVRVVVVTENNIIHRYHSL 292
Cdd:cd07395 238 QLGNDTSGLRVVVVTENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
31-293 3.94e-36

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 129.81  E-value: 3.94e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  31 FYFIQAADPQLGLmkawrigdcdsggDEWDEEVQLTKQAVQAINklQPKPRFIVLCGDLVHAMpgspfREQQIKDLKDAL 110
Cdd:COG1409   1 FRFAHISDLHLGA-------------PDGSDTAEVLAAALADIN--APRPDFVVVTGDLTDDG-----EPEEYAAAREIL 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 111 RGTDphIPLVFVSGNHDLGNAPTPDTVEQFCHEWGDD-YFSFWVGGVLCLVLNSQFFFDSSGcpELMEAHEVWLENRLQm 189
Cdd:COG1409  61 ARLG--VPVYVVPGNHDIRAAMAEAYREYFGDLPPGGlYYSFDYGGVRFIGLDSNVPGRSSG--ELGPEQLAWLEEELA- 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 190 avQTPSRHVLVFQHIPLFLRTPDEEDDYFnlqrGIREHLIQRFKRAGVKAVFSGHYHRNAGGCHDGLDMVVSSAVGCQLg 269
Cdd:COG1409 136 --AAPAKPVIVFLHHPPYSTGSGSDRIGL----RNAEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQV- 208

                       250       260
                ....*....|....*....|....
gi 55925413 270 DDTHGVRVVVVTENNIIHRYHSLD 293
Cdd:COG1409 209 RLPPGYRVIEVDGDGLTVEVRRVD 232
PLN02533 PLN02533
probable purple acid phosphatase
 53-246 2.24e-04

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 42.36  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413   53 DSGGDEWdeevqlTKQAVQAINKLQPKprFIVLCGDLVHAMPGSPfreqqikdLKDAL-RGTDP---HIPLVFVSGNHDL 128
Cdd:PLN02533 147 DLGTSEW------TKSTLEHVSKWDYD--VFILPGDLSYANFYQP--------LWDTFgRLVQPlasQRPWMVTHGNHEL 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  129 GNAPT--PDTVEQFCHEW----------GDDYFSFWVGGVLCLVLNSQFFFDSSGcpelmEAHEvWLENRLQMAVQTPSR 196
Cdd:PLN02533 211 EKIPIlhPEKFTAYNARWrmpfeesgstSNLYYSFNVYGVHIIMLGSYTDFEPGS-----EQYQ-WLENNLKKIDRKTTP 284

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55925413  197 HVLVFQHIPLF----LRTPDEEDDyfnlqrGIREHLIQRFKRAGVKAVFSGHYH 246
Cdd:PLN02533 285 WVVAVVHAPWYnsneAHQGEKESV------GMKESMETLLYKARVDLVFAGHVH 332
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 27-292 2.94e-176

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 487.60  E-value: 2.94e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  27 WSGPFYFIQAADPQLGLMKAWRIGdcdSGGDEWDEEVQLTKQAVQAINKLQPKPRFIVLCGDLVHAMPGSPFREQQIKDL 106
Cdd:cd07395   1 WKGPFYFIQGADPQLGLIKQNNIG---NGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 107 KDALRGTDPHIPLVFVSGNHDLGNAPTPDTVEQFCHEWGDDYFSFWVGGVLCLVLNSQFFFDSSGCPELMEAHEVWLENR 186
Cdd:cd07395  78 KDVLSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQ 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 187 LQMAVQTPSRHVLVFQHIPLFLRTPDEEDDYFNLQRGIREHLIQRFKRAGVKAVFSGHYHRNAGGCHDGLDMVVSSAVGC 266
Cdd:cd07395 158 LQIARESDAKHVVVFQHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGC 237

                       250       260
                ....*....|....*....|....*.
gi 55925413 267 QLGDDTHGVRVVVVTENNIIHRYHSL 292
Cdd:cd07395 238 QLGNDTSGLRVVVVTENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
31-293 3.94e-36

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 129.81  E-value: 3.94e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  31 FYFIQAADPQLGLmkawrigdcdsggDEWDEEVQLTKQAVQAINklQPKPRFIVLCGDLVHAMpgspfREQQIKDLKDAL 110
Cdd:COG1409   1 FRFAHISDLHLGA-------------PDGSDTAEVLAAALADIN--APRPDFVVVTGDLTDDG-----EPEEYAAAREIL 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 111 RGTDphIPLVFVSGNHDLGNAPTPDTVEQFCHEWGDD-YFSFWVGGVLCLVLNSQFFFDSSGcpELMEAHEVWLENRLQm 189
Cdd:COG1409  61 ARLG--VPVYVVPGNHDIRAAMAEAYREYFGDLPPGGlYYSFDYGGVRFIGLDSNVPGRSSG--ELGPEQLAWLEEELA- 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 190 avQTPSRHVLVFQHIPLFLRTPDEEDDYFnlqrGIREHLIQRFKRAGVKAVFSGHYHRNAGGCHDGLDMVVSSAVGCQLg 269
Cdd:COG1409 136 --AAPAKPVIVFLHHPPYSTGSGSDRIGL----RNAEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQV- 208

                       250       260
                ....*....|....*....|....
gi 55925413 270 DDTHGVRVVVVTENNIIHRYHSLD 293
Cdd:COG1409 209 RLPPGYRVIEVDGDGLTVEVRRVD 232
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 68-267 1.50e-15

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: 74.62  E-value: 1.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  68 QAVQAINKLQPKPRFIVLCGDLVHAmpGSPFREQQIKDLKDALRgtdphIPLVFVSGNHDLGNAPTPDTVEQFCHEWGDD 147
Cdd:cd07402  28 AAVAQVNALHPRPDLVVVTGDLSDD--GSPESYERLRELLAPLP-----APVYWIPGNHDDRAAMREALPEPPYDDNGPV 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 148 YFSFWVGGVLCLVLNSQFFFDSSGcpELMEAHEVWLENRLQMAvqtPSRHVLVFQH---IPLFLRTPDEeddyFNLQRGI 224
Cdd:cd07402 101 QYVVDFGGWRLILLDTSVPGVHHG--ELSDEQLDWLEAALAEA---PDRPTLIFLHhppFPLGIPWMDA----IRLRNSQ 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 55925413 225 R-EHLIQRFkrAGVKAVFSGHYHRNAGGCHDGLDMVVSSAVGCQ 267
Cdd:cd07402 172 AlFAVLARH--PQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQ 213
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 52-247 1.71e-08

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: 54.61  E-value: 1.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  52 CDSggdewdeEVQLTKQAVQAINKLQPKPRFIVLCGDLV-HAMPGSPFREQQ--IKDLKDALRGTDPHIPLVFVSGNHDL 128
Cdd:cd00842  49 CDS-------PWSLVESALEAIKKNHPKPDFILWTGDLVrHDVDEQTPEETVesESNLTNLLKKYFPNVPVYPALGNHDS 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 129 ---------GNAPTPDTvEQFCHEWGDD--------------YFSFWVGGVLCLVLNSQF-----FFDSSG----CPELm 176
Cdd:cd00842 122 ypvnqfpphSNSPSWLY-DALAELWKPWlpteaketfkkggyYSVDVKDGLRVISLNTNLyykknFWLYSNntdpCGQL- 199

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55925413 177 eaheVWLENRLQMAVQTpSRHVLVFQHIPlflrtP--DEEDDYFNLQRGireHLIQRFkRAGVKAVFSGHYHR 247
Cdd:cd00842 200 ----QWLEDELEDAEQK-GEKVWIIGHIP-----PglNSYDADWSERFY---QIINRY-SDTIAGQFFGHTHR 258
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 66-274 3.06e-08

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 53.84  E-value: 3.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  66 TKQAVQAINKLQPKPRFIVLCGDLVHAMpgspfreqqikDLKDALRGTD------P---HIPLVFVSGNHDLG------- 129
Cdd:cd00839  20 STNTLDHLEKELGNYDAIIHVGDIAYAD-----------GYNNGSRWDTfmrqiePlasYVPYMVAPGNHEADyngstsk 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 130 ---NAPTPDTVEQFCHEWGDDYFSFWVGGVLCLVLNSQFFFDSSGCPELMEAhevWLENRLQMAVQTPSRHVLVFQHIPL 206
Cdd:cd00839  89 ikfFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGDNISPQYD---WLEADLAKVDRSRTPWIIVMGHRPM 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 207 FLRTPDEEDDYFNLqrGIREHLIQRFKRAGVKAVFSGHYH---RNA----GGCHDGLDM----------VVSSAVGCQLG 269
Cdd:cd00839 166 YCSNDDDADCIEGE--KMREALEDLFYKYGVDLVLSGHVHayeRTCpvynNTVANSKDNiytnpkgpvhIVIGAAGNDEG 243


                ....*
gi 55925413 270 DDTHG 274
Cdd:cd00839 244 LDDAF 248
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 67-286 1.65e-06

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 48.48  E-value: 1.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  67 KQAVQAINKLQpKPRFIVLCGDLV-HAMPGSPFRE--QQIKDLKDALRGtdphiPLVFVSGNHDLGNAPTPDTVEQFCHE 143
Cdd:cd07396  35 ERAVEEWNRES-NLAFVVQLGDIIdGYNAKDRSKEalDAVLSILDRLKG-----PVHHVLGNHEFYNFPREYLNHLKTLN 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 144 wGDD--YFSFWVG-GVLCLVLNSQFFFDSSGCPELMeahevWLENRLQMAvQTPSRHVLVFQHIPLFlrtPDEEDDYFNL 220
Cdd:cd07396 109 -GEDayYYSFSPGpGFRFLVLDFVKFNGGIGEEQLA-----WLRNELTSA-DANGEKVIVLSHLPIY---PEAADPQCLL 178

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55925413 221 QrGIREHLIQRFKRAGVKAVFSGHYHRnaGG---CHDGLDMVVSSAVgCQLGDDTHGVRVVVVTENNII 286
Cdd:cd07396 179 W-NYEEVLAILESYPCVKACFSGHNHE--GGyeqDSHGVHHVTLEGV-LETPPDSQAFGTAYVYEDHMV 243
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
78-250 2.77e-05

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 44.24  E-value: 2.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  78 PKPRFIVLCGDLVHAMPgspfrEQQIKDLKDALRGTDphIPLVFVSGNHDlgnaptPDTVEQFCHEWG-----DDYFSFw 152
Cdd:COG2129  25 EDADLVILAGDLTDFGT-----AEEAREVLEELAALG--VPVLAVPGNHD------DPEVLDALEESGvhnlhGRVVEI- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 153 vGGVLclvlnsqFFFDSSGCP----ELMEAHEVWLENRLQMAVqTPSRHVLVFqHIPLFLRTPDEEDDYFNL-QRGIREh 227
Cdd:COG2129  91 -GGLR-------IAGLGGSRPtpfgTPYEYTEEEIEERLAKLR-EKDVDILLT-HAPPYGTTLDRVEDGPHVgSKALRE- 159

                       170       180
                ....*....|....*....|...
gi 55925413 228 LIQRFKragVKAVFSGHYHRNAG 250
Cdd:COG2129 160 LIEEFQ---PKLVLHGHIHESRG 179
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 70-128 8.12e-05

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: 41.87  E-value: 8.12e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 55925413  70 VQAINKLQPKPRFIVLCGDLVHAMPGSPFREQQIKDLKDAlrgtdpHIPLVFVSGNHDL 128
Cdd:cd00838  17 LEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLA------GIPVYVVPGNHDI 69
PLN02533 PLN02533
probable purple acid phosphatase
 53-246 2.24e-04

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 42.36  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413   53 DSGGDEWdeevqlTKQAVQAINKLQPKprFIVLCGDLVHAMPGSPfreqqikdLKDAL-RGTDP---HIPLVFVSGNHDL 128
Cdd:PLN02533 147 DLGTSEW------TKSTLEHVSKWDYD--VFILPGDLSYANFYQP--------LWDTFgRLVQPlasQRPWMVTHGNHEL 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  129 GNAPT--PDTVEQFCHEW----------GDDYFSFWVGGVLCLVLNSQFFFDSSGcpelmEAHEvWLENRLQMAVQTPSR 196
Cdd:PLN02533 211 EKIPIlhPEKFTAYNARWrmpfeesgstSNLYYSFNVYGVHIIMLGSYTDFEPGS-----EQYQ-WLENNLKKIDRKTTP 284

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55925413  197 HVLVFQHIPLF----LRTPDEEDDyfnlqrGIREHLIQRFKRAGVKAVFSGHYH 246
Cdd:PLN02533 285 WVVAVVHAPWYnsneAHQGEKESV------GMKESMETLLYKARVDLVFAGHVH 332
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 77-258 2.39e-04

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 41.51  E-value: 2.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  77 QPKPRFIVLCGDLVHAMPgsPFREQQIKDLKDALRGTDPH-IPLVFVSGNHDLGNAPTPDTVEqfchewgddyfsfwvgg 155
Cdd:cd07383  40 EEKPDLVVLTGDLITGEN--TADDNATSYLDKAVSPLVERgIPWAATFGNHDGYDWIDPSQVE----------------- 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 156 vlclvlnsqfffdssgcpelmeahevWLEN---RLQMAvQTPSRHVLVFQHIPL------FLRTP------DEEDDYFNL 220
Cdd:cd07383 101 --------------------------WFEStsaALKKK-YGKNIPSLAFFHIPLpeyrevWNEKGklgginREKVCCQKT 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 55925413 221 QRGIREHLIqrfKRAGVKAVFSGHYHRN--AGGCHDGLDM 258
Cdd:cd07383 154 NSGFFKALV---KRGDVKAVFCGHDHGNdfCGRWKNGIWL 190
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 60-246 3.90e-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: 41.20  E-value: 3.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413  60 DEEVQLTKQAVQAINKLQPKprFIVLCGDLVHA-----MPGSPFR-EQQIKDLKDAL--RGTDPHIpLVFVSGNHDLGNA 131
Cdd:cd07401  16 PNRIQDETFCSNFIDVIKPT--LVLITGDLTDNktgnkLPSYQYQeEWQWKYYNILKesSVINKEY-LFDIRGNHDLFGI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925413 132 PTPDTVE----QFCHEWGDDYFSF----WVGGVLCLVLNSQ--------FFFDSSGCPELMEAHEVWLENRLQmavqtpS 195
Cdd:cd07401  93 VSFDSQNnyyrKYSNTGRDHSHSFssttRFGNYSFIGFDPTifpgpkrpFNFFGSLDKKLLDRLEKELEKSKN------S 166

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 55925413 196 RHVLVFQHIPLFLRTPDEeddyfnlQRGIREHLIQRFKRAGVKAVFSGHYH 246
Cdd:cd07401 167 KYTIWFGHYPHSLIISPS-------AKSSSKTFKDLLKKYNVTAYLCGHLH 210
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
67-127 2.13e-03

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 39.01  E-value: 2.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55925413  67 KQAVQAINKLQPKprFIVLCGDLVHAmpgspfREQQIKDLKDALRGTDPHIPLVFVSGNHD 127
Cdd:COG1408  63 ERLVEKINALKPD--LVVLTGDLVDG------SVAELEALLELLKKLKAPLGVYAVLGNHD 115
 
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