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Conserved domains on  [gi|31981882|ref|NP_666179|]
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serine/threonine-protein phosphatase CPPED1 isoform 1 [Mus musculus]

Protein Classification

MPP_CSTP1 domain-containing protein( domain architecture ID 10164682)

MPP_CSTP1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 29-294 1.11e-171

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: 476.04  E-value: 1.11e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  29 WKGPFYFVQGADTQFGLMKAWSTGNcdaGGDEWGQEIRLTEQAVEAINKLNPKPKFFVLCGDLVHAMPGTPWRQEQTRDL 108
Cdd:cd07395   1 WKGPFYFIQGADPQLGLIKQNNIGN---GGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 109 QRVLKAVDQDIPLVMVSGNHDLGNAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFLYDASRCPALKQAQDHWLDQQ 188
Cdd:cd07395  78 KDVLSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQ 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 189 LNIAEQKQCQHAIVFQHIPLFLQSIDEDDDYFNLTKTVRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGC 268
Cdd:cd07395 158 LQIARESDAKHVVVFQHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGC 237

                       250       260
                ....*....|....*....|....*.
gi 31981882 269 QLGKDTHGLRVVAITAEKIVHRYYSL 294
Cdd:cd07395 238 QLGNDTSGLRVVVVTENKISHRYYSL 263
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 29-294 1.11e-171

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: 476.04  E-value: 1.11e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  29 WKGPFYFVQGADTQFGLMKAWSTGNcdaGGDEWGQEIRLTEQAVEAINKLNPKPKFFVLCGDLVHAMPGTPWRQEQTRDL 108
Cdd:cd07395   1 WKGPFYFIQGADPQLGLIKQNNIGN---GGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 109 QRVLKAVDQDIPLVMVSGNHDLGNAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFLYDASRCPALKQAQDHWLDQQ 188
Cdd:cd07395  78 KDVLSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQ 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 189 LNIAEQKQCQHAIVFQHIPLFLQSIDEDDDYFNLTKTVRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGC 268
Cdd:cd07395 158 LQIARESDAKHVVVFQHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGC 237

                       250       260
                ....*....|....*....|....*.
gi 31981882 269 QLGKDTHGLRVVAITAEKIVHRYYSL 294
Cdd:cd07395 238 QLGNDTSGLRVVVVTENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
33-296 3.60e-33

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 122.11  E-value: 3.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  33 FYFVQGADTQFGLMKAWSTgncdaggdewgqeIRLTEQAVEAINKlnPKPKFFVLCGDLVHAmpGTPwrqEQTRDLQRVL 112
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDT-------------AEVLAAALADINA--PRPDFVVVTGDLTDD--GEP---EEYAAAREIL 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 113 KAVDqdIPLVMVSGNHDLGNAPTAETVEEFCQTWGDD-YFSFWVGGVLFLVLNSQFLYDASRcpALKQAQDHWLDQQLni 191
Cdd:COG1409  61 ARLG--VPVYVVPGNHDIRAAMAEAYREYFGDLPPGGlYYSFDYGGVRFIGLDSNVPGRSSG--ELGPEQLAWLEEEL-- 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 192 aEQKQCQHAIVFQHIPLFLQSIDEDDDYFNLtktvRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQLg 271
Cdd:COG1409 135 -AAAPAKPVIVFLHHPPYSTGSGSDRIGLRN----AEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQV- 208

                       250       260
                ....*....|....*....|....*
gi 31981882 272 KDTHGLRVVAITAEKIVHRYYSLDE 296
Cdd:COG1409 209 RLPPGYRVIEVDGDGLTVEVRRVDG 233
PLN02533 PLN02533
probable purple acid phosphatase
 55-248 1.72e-06

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 49.30  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882   55 DAGGDEWgqeirlTEQAVEAINKLNPKpkFFVLCGDLVHAMPGTP-WRQeqtrdLQRVLKAVDQDIPLVMVSGNHDLGNA 133
Cdd:PLN02533 147 DLGTSEW------TKSTLEHVSKWDYD--VFILPGDLSYANFYQPlWDT-----FGRLVQPLASQRPWMVTHGNHELEKI 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  134 PT--AETVEEFCQTW----------GDDYFSFWVGGVLFLVLNSQFLYDasrcPALKQAQdhWLDQQLNIAEQKQCQHAI 201
Cdd:PLN02533 214 PIlhPEKFTAYNARWrmpfeesgstSNLYYSFNVYGVHIIMLGSYTDFE----PGSEQYQ--WLENNLKKIDRKTTPWVV 287

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 31981882  202 VFQHIPLF-----LQSIDEDDDyfnltktVRKELAEKLTRAGIRAVFSGHYH 248
Cdd:PLN02533 288 AVVHAPWYnsneaHQGEKESVG-------MKESMETLLYKARVDLVFAGHVH 332
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 68-130 4.23e-04

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: 39.50  E-value: 4.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31981882    68 TEQAVEAINKlNPKPKFFVLCGDLVHampGTPWRQEQTRDLQRVLKAvdqdIPLVMVSGNHDL 130
Cdd:pfam00149  18 LLELLKKLLE-EGKPDLVLHAGDLVD---RGPPSEEVLELLERLIKY----VPVYLVRGNHDF 72
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 29-294 1.11e-171

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: 476.04  E-value: 1.11e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  29 WKGPFYFVQGADTQFGLMKAWSTGNcdaGGDEWGQEIRLTEQAVEAINKLNPKPKFFVLCGDLVHAMPGTPWRQEQTRDL 108
Cdd:cd07395   1 WKGPFYFIQGADPQLGLIKQNNIGN---GGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 109 QRVLKAVDQDIPLVMVSGNHDLGNAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFLYDASRCPALKQAQDHWLDQQ 188
Cdd:cd07395  78 KDVLSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQ 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 189 LNIAEQKQCQHAIVFQHIPLFLQSIDEDDDYFNLTKTVRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGC 268
Cdd:cd07395 158 LQIARESDAKHVVVFQHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGC 237

                       250       260
                ....*....|....*....|....*.
gi 31981882 269 QLGKDTHGLRVVAITAEKIVHRYYSL 294
Cdd:cd07395 238 QLGNDTSGLRVVVVTENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
33-296 3.60e-33

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 122.11  E-value: 3.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  33 FYFVQGADTQFGLMKAWSTgncdaggdewgqeIRLTEQAVEAINKlnPKPKFFVLCGDLVHAmpGTPwrqEQTRDLQRVL 112
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDT-------------AEVLAAALADINA--PRPDFVVVTGDLTDD--GEP---EEYAAAREIL 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 113 KAVDqdIPLVMVSGNHDLGNAPTAETVEEFCQTWGDD-YFSFWVGGVLFLVLNSQFLYDASRcpALKQAQDHWLDQQLni 191
Cdd:COG1409  61 ARLG--VPVYVVPGNHDIRAAMAEAYREYFGDLPPGGlYYSFDYGGVRFIGLDSNVPGRSSG--ELGPEQLAWLEEEL-- 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 192 aEQKQCQHAIVFQHIPLFLQSIDEDDDYFNLtktvRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQLg 271
Cdd:COG1409 135 -AAAPAKPVIVFLHHPPYSTGSGSDRIGLRN----AEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQV- 208

                       250       260
                ....*....|....*....|....*
gi 31981882 272 KDTHGLRVVAITAEKIVHRYYSLDE 296
Cdd:COG1409 209 RLPPGYRVIEVDGDGLTVEVRRVDG 233
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 69-269 3.43e-13

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: 67.69  E-value: 3.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  69 EQAVEAINKLNPKPKFFVLCGDLVHAmpGTPwrqEQTRDLQRVLKAVdqDIPLVMVSGNHDLGNAPTAETVEEFCQTWGD 148
Cdd:cd07402  27 AAAVAQVNALHPRPDLVVVTGDLSDD--GSP---ESYERLRELLAPL--PAPVYWIPGNHDDRAAMREALPEPPYDDNGP 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 149 DYFSFWVGGVLFLVLNSQFlyDASRCPALKQAQDHWLDQQLNIAEQKqcqHAIVFQHIPLFLQSIDEDDDYfNLTKTvrK 228
Cdd:cd07402 100 VQYVVDFGGWRLILLDTSV--PGVHHGELSDEQLDWLEAALAEAPDR---PTLIFLHHPPFPLGIPWMDAI-RLRNS--Q 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 31981882 229 ELAEKLTR-AGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQ 269
Cdd:cd07402 172 ALFAVLARhPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQ 213
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 49-249 9.61e-12

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: 64.24  E-value: 9.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  49 WSTGNCDAggdewgqEIRLTEQAVEAINKLNPKPKFFVLCGDLVhamPGTPWRQ------EQTRDLQRVLKAVDQDIPLV 122
Cdd:cd00842  44 WGTYGCDS-------PWSLVESALEAIKKNHPKPDFILWTGDLV---RHDVDEQtpeetvESESNLTNLLKKYFPNVPVY 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 123 MVSGNHDL----GNAPTAETV----EEFCQTWGDD--------------YFSFWVGGVLFLVLNSQFLYDASRcPALKQA 180
Cdd:cd00842 114 PALGNHDSypvnQFPPHSNSPswlyDALAELWKPWlpteaketfkkggyYSVDVKDGLRVISLNTNLYYKKNF-WLYSNN 192

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31981882 181 QD-----HWLDQQLNIAEQKQcQHAIVFQHIPLflqSIDEDDDYFN--LTKTVRKelaeklTRAGIRAVFSGHYHR 249
Cdd:cd00842 193 TDpcgqlQWLEDELEDAEQKG-EKVWIIGHIPP---GLNSYDADWSerFYQIINR------YSDTIAGQFFGHTHR 258
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 69-255 1.68e-10

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: 60.04  E-value: 1.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  69 EQAVEAINKlNPKPKFFVLCGDLV-HAMPgtpwRQEQTRDLQRVLKAVDQ-DIPLVMVSGNHDLGNAPTAETVEEFCQTw 146
Cdd:cd07396  35 ERAVEEWNR-ESNLAFVVQLGDIIdGYNA----KDRSKEALDAVLSILDRlKGPVHHVLGNHEFYNFPREYLNHLKTLN- 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 147 GDD--YFSFWVG-GVLFLVLNSQFLydasrCPALKQAQDHWLDQQLNIAEQKQcQHAIVFQHIPLflQSIDEDD-----D 218
Cdd:cd07396 109 GEDayYYSFSPGpGFRFLVLDFVKF-----NGGIGEEQLAWLRNELTSADANG-EKVIVLSHLPI--YPEAADPqcllwN 180

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 31981882 219 YFNLTKTVRKelaekltRAGIRAVFSGHYHRnagGTY 255
Cdd:cd07396 181 YEEVLAILES-------YPCVKACFSGHNHE---GGY 207
PLN02533 PLN02533
probable purple acid phosphatase
 55-248 1.72e-06

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 49.30  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882   55 DAGGDEWgqeirlTEQAVEAINKLNPKpkFFVLCGDLVHAMPGTP-WRQeqtrdLQRVLKAVDQDIPLVMVSGNHDLGNA 133
Cdd:PLN02533 147 DLGTSEW------TKSTLEHVSKWDYD--VFILPGDLSYANFYQPlWDT-----FGRLVQPLASQRPWMVTHGNHELEKI 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  134 PT--AETVEEFCQTW----------GDDYFSFWVGGVLFLVLNSQFLYDasrcPALKQAQdhWLDQQLNIAEQKQCQHAI 201
Cdd:PLN02533 214 PIlhPEKFTAYNARWrmpfeesgstSNLYYSFNVYGVHIIMLGSYTDFE----PGSEQYQ--WLENNLKKIDRKTTPWVV 287

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 31981882  202 VFQHIPLF-----LQSIDEDDDyfnltktVRKELAEKLTRAGIRAVFSGHYH 248
Cdd:PLN02533 288 AVVHAPWYnsneaHQGEKESVG-------MKESMETLLYKARVDLVFAGHVH 332
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 31-250 2.26e-06

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: 47.29  E-value: 2.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  31 GPFYFVQGADTQFGlmkawstgNCDAGGDEWGQEIRLTEQAVEAINKlNPKPKFFVLCGDLVHampGTPWRQEqtrDLQR 110
Cdd:cd07383   1 GKFKILQFADLHFG--------EGEWTCWEGCEADLKTVEFIESVLD-EEKPDLVVLTGDLIT---GENTADD---NATS 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 111 VLK-----AVDQDIPLVMVSGNHDLGNAPTAETVEEFCQTwgddyfsfwvggvlflvlnSQflydasrcpALKQAQDHwl 185
Cdd:cd07383  66 YLDkavspLVERGIPWAATFGNHDGYDWIDPSQVEWFEST-------------------SA---------ALKKKYGK-- 115

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31981882 186 dqqlNIaeqkqcqHAIVFQHIPlfLQSIDEDDDYFNLTKTVRKE-----------LAEKLTRAGIRAVFSGHYHRN 250
Cdd:cd07383 116 ----NI-------PSLAFFHIP--LPEYREVWNEKGKLGGINREkvccqktnsgfFKALVKRGDVKAVFCGHDHGN 178
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 119-276 4.87e-06

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: 47.29  E-value: 4.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 119 IPLVMVSGNHDLG----------NAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFLYDASRcpaLKQAQDHWLDQQ 188
Cdd:cd00839  69 VPYMVAPGNHEADyngstskikfFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEAD 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 189 LNIAEQKQCQHAIVFQHIPLFlQSIDEDDDYFNLTKtVRKELAEKLTRAGIRAVFSGHYH------RNAGGTYQNLDM-- 260
Cdd:cd00839 146 LAKVDRSRTPWIIVMGHRPMY-CSNDDDADCIEGEK-MREALEDLFYKYGVDLVLSGHVHayertcPVYNNTVANSKDni 223

                       170       180
                ....*....|....*....|....*
gi 31981882 261 ---------VVSSAIGCQLGKDTHG 276
Cdd:cd00839 224 ytnpkgpvhIVIGAAGNDEGLDDAF 248
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 65-248 1.80e-05

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: 45.43  E-value: 1.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  65 IRLTEQAVEAINKLnpKPKFFVLCGDLVHA-----MPGTPWRQEQTRDLQRVLK--AVDQDIPLVMVSGNHDLGNAPTAE 137
Cdd:cd07401  19 IQDETFCSNFIDVI--KPTLVLITGDLTDNktgnkLPSYQYQEEWQWKYYNILKesSVINKEYLFDIRGNHDLFGIVSFD 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 138 TVEE----FCQTWGDDYFSF----WVGGVLFLVLNSQ--------FLYDASRCPALkqaqdhwLDQQLNIAEQ-KQCQHA 200
Cdd:cd07401  97 SQNNyyrkYSNTGRDHSHSFssttRFGNYSFIGFDPTifpgpkrpFNFFGSLDKKL-------LDRLEKELEKsKNSKYT 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 31981882 201 IVFQHIPlfLQSIDEDDdyfnlTKTVRKELAEKLTRAGIRAVFSGHYH 248
Cdd:cd07401 170 IWFGHYP--HSLIISPS-----AKSSSKTFKDLLKKYNVTAYLCGHLH 210
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 69-254 2.72e-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: 43.02  E-value: 2.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882  69 EQAVEAINKLNPKPKFFVLCGDLVHAMPGTPWRQEQtrdlqrVLKAVDQDIPLVMVSGNHDlgnaptaetveefcqtwgd 148
Cdd:cd00838  14 EAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELK------ALRLLLAGIPVYVVPGNHD------------------- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 149 dyfsfwvggvlflvlnsqflydasrcpalkqaqdhwldqqlniaeqkqcqhaIVFQHIPLFlqsiDEDDDYFNLTKTVRK 228
Cdd:cd00838  69 ----------------------------------------------------ILVTHGPPY----DPLDEGSPGEDPGSE 92

                       170       180
                ....*....|....*....|....*.
gi 31981882 229 ELAEKLTRAGIRAVFSGHYHRNAGGT 254
Cdd:cd00838  93 ALLELLDKYGPDLVLSGHTHVPGRRE 118
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 68-130 4.23e-04

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: 39.50  E-value: 4.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31981882    68 TEQAVEAINKlNPKPKFFVLCGDLVHampGTPWRQEQTRDLQRVLKAvdqdIPLVMVSGNHDL 130
Cdd:pfam00149  18 LLELLKKLLE-EGKPDLVLHAGDLVD---RGPPSEEVLELLERLIKY----VPVYLVRGNHDF 72
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 62-129 4.69e-04

Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277337  Cd Length: 175  Bit Score: 40.37  E-value: 4.69e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31981882  62 GQEIRLTEQAVEAINKLNPKpKFFVLcGDLVHAMPGTPWrqeQTRDLQRVLKAVDQDIPLVMVSGNHD 129
Cdd:cd07391  24 RQKERLLERLDRLLEELGPD-RLVIL-GDLKHSFGRVSR---QERREVPFFRLLAKDVDVILIRGNHD 86
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
57-129 2.05e-03

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 39.13  E-value: 2.05e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31981882  57 GGDEWGQEIRLT-EQAVEAINKLnpKPKFFVLCGDLVHampgTPWRQEQTRDL--QRVLKAVDQDIPLVMVSGNHD 129
Cdd:COG0420  16 HGASRREDQLAAlDRLVDLAIEE--KVDAVLIAGDLFD----SANPSPEAVRLlaEALRRLSEAGIPVVLIAGNHD 85
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 117-293 3.05e-03

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 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: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 38.46  E-value: 3.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 117 QDIPLVMVSGNHD-LGNApTAE---TVEEFCQTWG------DDYFSFWVGGVL--FLVLNSQFL-----------YDASR 173
Cdd:cd07378  73 LQVPWYLVLGNHDhRGNV-SAQiayTQRPNSKRWNfpnyyyDISFKFPSSDVTvaFIMIDTVLLcgntddeasgqPRGPP 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981882 174 CPALKQAQDHWLDQQLNIAEQkqcQHAIVFQHIPLFlqSIDEDDDyfnlTKTVRKELAEKLTRAGIRAVFSGHYH----- 248
Cdd:cd07378 152 NKKLAETQLAWLEKQLAASKA---DYKIVVGHYPIY--SSGEHGP----TKCLVDILLPLLKKYKVDAYLSGHDHnlqhi 222

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31981882 249 RNAGGTYqnldMVVSSAIGCQLGKDTH--------------------GLRVVAITAEKIVHRYYS 293
Cdd:cd07378 223 VDESGTY----YVISGAGSKADPSDIHrdkvpqgyllffsgfyssggGFAYLEITSSELVIRFVD 283
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 69-129 3.05e-03

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 38.02  E-value: 3.05e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31981882  69 EQAVEAINKlnPKPKFFVLCGDLVH-AMPGtpwRQEQTRDLQRVLKAVDQDIPLVMVSGNHD 129
Cdd:cd00840  29 EEIVDLAIE--EKVDFVLIAGDLFDsNNPS---PEALKLAIEGLRRLCEAGIPVFVIAGNHD 85
 
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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