NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|198429005|ref|XP_002123287|]
View 

serine/threonine-protein phosphatase CPPED1-like [Ciona intestinalis]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10164682)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

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 ...
 22-289 2.23e-161

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: 449.46  E-value: 2.23e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005  22 WHDDHFFVFLADPQPGLIDK-VNGGNGSTWDVEIKRTHDAVEAINKMRPKPKFVCIGGDLIDAFPGESLRDPQVSDLKSA 100
Cdd:cd07395    1 WKGPFYFIQGADPQLGLIKQnNIGNGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDLKDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 101 FADLDQTIPIVVVSGNHDVGNVPTMKTMSMYNNDFGEDYYSFWVEGVFYIVVNSQYMYNDSETREQSSNQDSWLRAQLEI 180
Cdd:cd07395   81 LSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQLQI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 181 ARLSSCQHVVVFMHIPLFLQDPDEEDSYFAIPGAKRMDLLTRYSDAGIKIVFSGHYHRNAGGFWRnergdkQVEVVVSSA 260
Cdd:cd07395  161 ARESDAKHVVVFQHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYR------DLEMVVTSA 234

                        250       260
                 ....*....|....*....|....*....
gi 198429005 261 IGAQLGNDVAGLRVVKVTADDITHTYYPL 289
Cdd:cd07395  235 VGCQLGNDTSGLRVVVVTENKISHRYYSL 263
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 22-289 2.23e-161

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: 449.46  E-value: 2.23e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005  22 WHDDHFFVFLADPQPGLIDK-VNGGNGSTWDVEIKRTHDAVEAINKMRPKPKFVCIGGDLIDAFPGESLRDPQVSDLKSA 100
Cdd:cd07395    1 WKGPFYFIQGADPQLGLIKQnNIGNGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDLKDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 101 FADLDQTIPIVVVSGNHDVGNVPTMKTMSMYNNDFGEDYYSFWVEGVFYIVVNSQYMYNDSETREQSSNQDSWLRAQLEI 180
Cdd:cd07395   81 LSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQLQI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 181 ARLSSCQHVVVFMHIPLFLQDPDEEDSYFAIPGAKRMDLLTRYSDAGIKIVFSGHYHRNAGGFWRnergdkQVEVVVSSA 260
Cdd:cd07395  161 ARESDAKHVVVFQHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYR------DLEMVVTSA 234

                        250       260
                 ....*....|....*....|....*....
gi 198429005 261 IGAQLGNDVAGLRVVKVTADDITHTYYPL 289
Cdd:cd07395  235 VGCQLGNDTSGLRVVVVTENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
28-291 2.24e-28

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 109.01  E-value: 2.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005  28 FVFLADPQPGLIDKVNggngstwdvEIKRTHDAVEAINkmRPKPKFVCIGGDLIDAFpgeslRDPQVSDLKSAFADLDqt 107
Cdd:COG1409    3 FAHISDLHLGAPDGSD---------TAEVLAAALADIN--APRPDFVVVTGDLTDDG-----EPEEYAAAREILARLG-- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 108 IPIVVVSGNHDVGNVPTMKTMSMYNN-DFGEDYYSFWVEGVFYIVVNSQYMYNDSetREQSSNQDSWLRAQLEiarLSSC 186
Cdd:COG1409   65 VPVYVVPGNHDIRAAMAEAYREYFGDlPPGGLYYSFDYGGVRFIGLDSNVPGRSS--GELGPEQLAWLEEELA---AAPA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 187 QHVVVFMHIPLFLQDPDEEDSYFAIPGAkrmdLLTRYSDAGIKIVFSGHYHRNAGGFWRNergdkqVEVVVSSAIGAQLG 266
Cdd:COG1409  140 KPVIVFLHHPPYSTGSGSDRIGLRNAEE----LLALLARYGVDLVLSGHVHRYERTRRDG------VPYIVAGSTGGQVR 209

                        250       260
                 ....*....|....*....|....*
gi 198429005 267 NdVAGLRVVKVTADDITHTYYPLDG 291
Cdd:COG1409  210 L-PPGYRVIEVDGDGLTVEVRRVDG 233
PLN02533 PLN02533
probable purple acid phosphatase
 109-237 1.08e-06

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 49.68  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 109 PIVVVSGNHDVGNVPTM--KTMSMYNN----DFGED------YYSFWVEGVFYIVVNSqymYNDSETreqSSNQDSWLRA 176
Cdd:PLN02533 200 PWMVTHGNHELEKIPILhpEKFTAYNArwrmPFEESgstsnlYYSFNVYGVHIIMLGS---YTDFEP---GSEQYQWLEN 273

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 198429005 177 QLEIARLSSCQHVVVFMHIPLFLQDPDEEDSYFAIPGAKRMDLLtrYSDAGIKIVFSGHYH 237
Cdd:PLN02533 274 NLKKIDRKTTPWVVAVVHAPWYNSNEAHQGEKESVGMKESMETL--LYKARVDLVFAGHVH 332
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 22-289 2.23e-161

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: 449.46  E-value: 2.23e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005  22 WHDDHFFVFLADPQPGLIDK-VNGGNGSTWDVEIKRTHDAVEAINKMRPKPKFVCIGGDLIDAFPGESLRDPQVSDLKSA 100
Cdd:cd07395    1 WKGPFYFIQGADPQLGLIKQnNIGNGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDLKDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 101 FADLDQTIPIVVVSGNHDVGNVPTMKTMSMYNNDFGEDYYSFWVEGVFYIVVNSQYMYNDSETREQSSNQDSWLRAQLEI 180
Cdd:cd07395   81 LSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQLQI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 181 ARLSSCQHVVVFMHIPLFLQDPDEEDSYFAIPGAKRMDLLTRYSDAGIKIVFSGHYHRNAGGFWRnergdkQVEVVVSSA 260
Cdd:cd07395  161 ARESDAKHVVVFQHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYR------DLEMVVTSA 234

                        250       260
                 ....*....|....*....|....*....
gi 198429005 261 IGAQLGNDVAGLRVVKVTADDITHTYYPL 289
Cdd:cd07395  235 VGCQLGNDTSGLRVVVVTENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
28-291 2.24e-28

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 109.01  E-value: 2.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005  28 FVFLADPQPGLIDKVNggngstwdvEIKRTHDAVEAINkmRPKPKFVCIGGDLIDAFpgeslRDPQVSDLKSAFADLDqt 107
Cdd:COG1409    3 FAHISDLHLGAPDGSD---------TAEVLAAALADIN--APRPDFVVVTGDLTDDG-----EPEEYAAAREILARLG-- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 108 IPIVVVSGNHDVGNVPTMKTMSMYNN-DFGEDYYSFWVEGVFYIVVNSQYMYNDSetREQSSNQDSWLRAQLEiarLSSC 186
Cdd:COG1409   65 VPVYVVPGNHDIRAAMAEAYREYFGDlPPGGLYYSFDYGGVRFIGLDSNVPGRSS--GELGPEQLAWLEEELA---AAPA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 187 QHVVVFMHIPLFLQDPDEEDSYFAIPGAkrmdLLTRYSDAGIKIVFSGHYHRNAGGFWRNergdkqVEVVVSSAIGAQLG 266
Cdd:COG1409  140 KPVIVFLHHPPYSTGSGSDRIGLRNAEE----LLALLARYGVDLVLSGHVHRYERTRRDG------VPYIVAGSTGGQVR 209

                        250       260
                 ....*....|....*....|....*
gi 198429005 267 NdVAGLRVVKVTADDITHTYYPLDG 291
Cdd:COG1409  210 L-PPGYRVIEVDGDGLTVEVRRVDG 233
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 28-249 7.56e-12

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: 63.89  E-value: 7.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005  28 FVFLADPQpgLIDKVNGGNGSTWD----VEIKRTHDAVEAINKMRpKPKFVCIGGDLIDafpGESLRDPQVSDLKSAFAD 103
Cdd:cd07396    3 FGIIADIQ--YADIDDGKNLGTRRryyrNSLGVLERAVEEWNRES-NLAFVVQLGDIID---GYNAKDRSKEALDAVLSI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 104 LDQ-TIPIVVVSGNHDVGNVPTMKTMSMYN-NDFGEDYYSFWVEGVFYIVVNSQYMYNDSETREQSSnqdsWLRAQLEIA 181
Cdd:cd07396   77 LDRlKGPVHHVLGNHEFYNFPREYLNHLKTlNGEDAYYYSFSPGPGFRFLVLDFVKFNGGIGEEQLA----WLRNELTSA 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 198429005 182 rLSSCQHVVVFMHIPLflqDPDEEDSYFAIPGAKR-MDLLTRYSDagIKIVFSGHYHRnaGGFWRNERG 249
Cdd:cd07396  153 -DANGEKVIVLSHLPI---YPEAADPQCLLWNYEEvLAILESYPC--VKACFSGHNHE--GGYEQDSHG 213
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 60-238 8.24e-11

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: 61.55  E-value: 8.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005  60 AVEAINKMRPKPKFVCIGGDLIDAFPGESLRDPQVSDLKSAFADLDQ---TIPIVVVSGNHD---VGNVPTMKTMSMYNN 133
Cdd:cd00842   59 ALEAIKKNHPKPDFILWTGDLVRHDVDEQTPEETVESESNLTNLLKKyfpNVPVYPALGNHDsypVNQFPPHSNSPSWLY 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 134 DFgedYYSFWVE------------GVFY----------IVVNSQYMYND----SETREQSSNQDSWLRAQLEIARLSScQ 187
Cdd:cd00842  139 DA---LAELWKPwlpteaketfkkGGYYsvdvkdglrvISLNTNLYYKKnfwlYSNNTDPCGQLQWLEDELEDAEQKG-E 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 198429005 188 HVVVFMHIP--LFLQDPDEEDSYFAIpgakrmdlLTRYSD--AGIkivFSGHYHR 238
Cdd:cd00842  215 KVWIIGHIPpgLNSYDADWSERFYQI--------INRYSDtiAGQ---FFGHTHR 258
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 60-245 7.42e-08

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: 52.28  E-value: 7.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005  60 AVEAINKMRPKPKFVCIGGDLID-AFPGESLRdpqvsdLKSAFADLDqtIPIVVVSGNHDVGNV--PTMKTMSMYNNDFG 136
Cdd:cd07402   29 AVAQVNALHPRPDLVVVTGDLSDdGSPESYER------LRELLAPLP--APVYWIPGNHDDRAAmrEALPEPPYDDNGPV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 137 EDYYSFwvEGVFYIVVNSQymYNDSETREQSSNQDSWLRAQLEIARLSscqHVVVFMHIPLF-----------LQDPDEE 205
Cdd:cd07402  101 QYVVDF--GGWRLILLDTS--VPGVHHGELSDEQLDWLEAALAEAPDR---PTLIFLHHPPFplgipwmdairLRNSQAL 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 198429005 206 dsyfaipgakrMDLLTRYSDagIKIVFSGHYHRNAGGFWR 245
Cdd:cd07402  174 -----------FAVLARHPQ--VKAILCGHIHRPISGSFR 200
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 107-237 3.48e-07

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: 50.76  E-value: 3.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 107 TIPIVVVSGNHDVG----------NVPTMKTMSMYNNDFGEDYYSFWVEGVFYIVVNSQYMYNDSetrEQSSNQDSWLRA 176
Cdd:cd00839   68 YVPYMVAPGNHEADyngstskikfFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKG---DNISPQYDWLEA 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 198429005 177 QLEIARLSSCQHVVVFMHIPLFLQDPDEEDSYFAipGAKRM---DLLTRYsdaGIKIVFSGHYH 237
Cdd:cd00839  145 DLAKVDRSRTPWIIVMGHRPMYCSNDDDADCIEG--EKMREaleDLFYKY---GVDLVLSGHVH 203
PLN02533 PLN02533
probable purple acid phosphatase
 109-237 1.08e-06

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 49.68  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198429005 109 PIVVVSGNHDVGNVPTM--KTMSMYNN----DFGED------YYSFWVEGVFYIVVNSqymYNDSETreqSSNQDSWLRA 176
Cdd:PLN02533 200 PWMVTHGNHELEKIPILhpEKFTAYNArwrmPFEESgstsnlYYSFNVYGVHIIMLGS---YTDFEP---GSEQYQWLEN 273

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 198429005 177 QLEIARLSSCQHVVVFMHIPLFLQDPDEEDSYFAIPGAKRMDLLtrYSDAGIKIVFSGHYH 237
Cdd:PLN02533 274 NLKKIDRKTTPWVVAVVHAPWYNSNEAHQGEKESVGMKESMETL--LYKARVDLVFAGHVH 332
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
55-118 5.83e-05

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 43.63  E-value: 5.83e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 198429005  55 KRTHDAVEAINKMrpKPKFVCIGGDLIDAFPGEslrdpqVSDLKSAFADLDQTIPIVVVSGNHD 118
Cdd:COG1408   60 ERLERLVEKINAL--KPDLVVLTGDLVDGSVAE------LEALLELLKKLKAPLGVYAVLGNHD 115
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 61-119 2.92e-03

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: 37.25  E-value: 2.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 198429005  61 VEAINKMRPKPKFVCIGGDLIDAFPGESLRDPQVSDLKSAFadldqtIPIVVVSGNHDV 119
Cdd:cd00838   17 LEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAG------IPVYVVPGNHDI 69
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 55-126 3.28e-03

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: 38.03  E-value: 3.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 198429005  55 KRTHDAVEAINKMrpKPKFVCIGGDLIDAfpgeslRDPQVSDLKSAFADLDQTIPIVVVSGNHD--VGNVPTMK 126
Cdd:cd07385   19 TRLQKVVRKVNEL--NPDLIVITGDLVDG------DVSVLRLLASPLSKLKAPLGVYFVLGNHDyySGDVEVWI 84
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 188-241 5.00e-03

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: 36.48  E-value: 5.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 198429005 188 HVVVFMHIPLFlqDPDEEDSYFAIPGAKRMDLLTRysDAGIKIVFSGHYHRNAG 241
Cdd:cd00838   67 HDILVTHGPPY--DPLDEGSPGEDPGSEALLELLD--KYGPDLVLSGHTHVPGR 116
 
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