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Conserved domains on  [gi|153251270|ref|NP_060810|]
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serine/threonine-protein phosphatase CPPED1 isoform a [Homo sapiens]

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 ...
 29-295 2.07e-178

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: 493.38  E-value: 2.07e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  29 WKGPFYFILGADPQFGLIKAWSTGdcdNGGDEWEQEIRLTEQAVQAINKLNPKPKFFVLCGDLIHAMPGKPWRTEQTEDL 108
Cdd:cd07395    1 WKGPFYFIQGADPQLGLIKQNNIG---NGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 109 KRVLRAVDRAIPLVLVSGNHDIGNTPTAETVEEFCRTWGDDYFSFWVGGVLFLVLNSQFYENPSKCPSLKQAQDQWLDEQ 188
Cdd:cd07395   78 KDVLSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 189 LSIARQRHCQHAIVFQHIPLFLESIDEDDDyYFNLSKSTRKKLADKFIHAGVKVVFSGHYHRNAGGTYQNLDMVVSSAIG 268
Cdd:cd07395  158 LQIARESDAKHVVVFQHIPLFLEDPDEEDD-YFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVG 236

                        250       260
                 ....*....|....*....|....*..
gi 153251270 269 CQLGRDPHGLRVVVVTAEKIVHRYYSL 295
Cdd:cd07395  237 CQLGNDTSGLRVVVVTENKISHRYYSL 263
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 29-295 2.07e-178

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: 493.38  E-value: 2.07e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  29 WKGPFYFILGADPQFGLIKAWSTGdcdNGGDEWEQEIRLTEQAVQAINKLNPKPKFFVLCGDLIHAMPGKPWRTEQTEDL 108
Cdd:cd07395    1 WKGPFYFIQGADPQLGLIKQNNIG---NGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 109 KRVLRAVDRAIPLVLVSGNHDIGNTPTAETVEEFCRTWGDDYFSFWVGGVLFLVLNSQFYENPSKCPSLKQAQDQWLDEQ 188
Cdd:cd07395   78 KDVLSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 189 LSIARQRHCQHAIVFQHIPLFLESIDEDDDyYFNLSKSTRKKLADKFIHAGVKVVFSGHYHRNAGGTYQNLDMVVSSAIG 268
Cdd:cd07395  158 LQIARESDAKHVVVFQHIPLFLEDPDEEDD-YFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVG 236

                        250       260
                 ....*....|....*....|....*..
gi 153251270 269 CQLGRDPHGLRVVVVTAEKIVHRYYSL 295
Cdd:cd07395  237 CQLGNDTSGLRVVVVTENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-297 1.39e-34

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 125.96  E-value: 1.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  52 GDCDNGGDEWEQEIRLTEQAVQAINKlnPKPKFFVLCGDLIHAmpgkpWRTEQTEDLKRVLRAVDraIPLVLVSGNHDIG 131
Cdd:COG1409    7 SDLHLGAPDGSDTAEVLAAALADINA--PRPDFVVVTGDLTDD-----GEPEEYAAAREILARLG--VPVYVVPGNHDIR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 132 NTPTAETVEEFCRTWGDD-YFSFWVGGVLFLVLNSQFYENPSKCPSLKQAQdqWLDEQLSIARQRHcqhAIVFQHIPLFL 210
Cdd:COG1409   78 AAMAEAYREYFGDLPPGGlYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLA--WLEEELAAAPAKP---VIVFLHHPPYS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 211 ESIDEDDDYYFNlskstRKKLADKFIHAGVKVVFSGHYHRNAGGTYQNLDMVVSSAIGCQLgRDPHGLRVVVVTAEKIVH 290
Cdd:COG1409  153 TGSGSDRIGLRN-----AEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQV-RLPPGYRVIEVDGDGLTV 226


                 ....*..
gi 153251270 291 RYYSLDE 297
Cdd:COG1409  227 EVRRVDG 233
PLN02533 PLN02533
probable purple acid phosphatase
 55-249 1.31e-04

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 43.13  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  55 DNGGDEWeqeirlTEQAVQAINKLNPKpkFFVLCGDLIHAMPGKP-WRTeqtedLKRVLRAVDRAIPLVLVSGNHDIGNT 133
Cdd:PLN02533 147 DLGTSEW------TKSTLEHVSKWDYD--VFILPGDLSYANFYQPlWDT-----FGRLVQPLASQRPWMVTHGNHELEKI 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 134 PT--AETVEEFCRTW----------GDDYFSFWVGGVLFLVLNSQFYENPSkcpslkQAQDQWLDEQLSIARQRHCQHAI 201
Cdd:PLN02533 214 PIlhPEKFTAYNARWrmpfeesgstSNLYYSFNVYGVHIIMLGSYTDFEPG------SEQYQWLENNLKKIDRKTTPWVV 287

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153251270 202 VFQHIPLFLESIDEDDDyyfNLSKSTRKKLADKFIHAGVKVVFSGHYH 249
Cdd:PLN02533 288 AVVHAPWYNSNEAHQGE---KESVGMKESMETLLYKARVDLVFAGHVH 332
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 68-130 1.12e-03

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: 37.96  E-value: 1.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153251270   68 TEQAVQAINKlNPKPKFFVLCGDLIHampgkpwRTEQTEDLKRVLRAVDRAIPLVLVSGNHDI 130
Cdd:pfam00149  18 LLELLKKLLE-EGKPDLVLHAGDLVD-------RGPPSEEVLELLERLIKYVPVYLVRGNHDF 72
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 29-295 2.07e-178

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: 493.38  E-value: 2.07e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  29 WKGPFYFILGADPQFGLIKAWSTGdcdNGGDEWEQEIRLTEQAVQAINKLNPKPKFFVLCGDLIHAMPGKPWRTEQTEDL 108
Cdd:cd07395    1 WKGPFYFIQGADPQLGLIKQNNIG---NGGDEWDKEIELTEQAVQAINKLNPKPKFVVVCGDLVHAMPGEEFREQQVSDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 109 KRVLRAVDRAIPLVLVSGNHDIGNTPTAETVEEFCRTWGDDYFSFWVGGVLFLVLNSQFYENPSKCPSLKQAQDQWLDEQ 188
Cdd:cd07395   78 KDVLSKLDPDIPLVCVCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 189 LSIARQRHCQHAIVFQHIPLFLESIDEDDDyYFNLSKSTRKKLADKFIHAGVKVVFSGHYHRNAGGTYQNLDMVVSSAIG 268
Cdd:cd07395  158 LQIARESDAKHVVVFQHIPLFLEDPDEEDD-YFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVG 236

                        250       260
                 ....*....|....*....|....*..
gi 153251270 269 CQLGRDPHGLRVVVVTAEKIVHRYYSL 295
Cdd:cd07395  237 CQLGNDTSGLRVVVVTENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-297 1.39e-34

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 125.96  E-value: 1.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  52 GDCDNGGDEWEQEIRLTEQAVQAINKlnPKPKFFVLCGDLIHAmpgkpWRTEQTEDLKRVLRAVDraIPLVLVSGNHDIG 131
Cdd:COG1409    7 SDLHLGAPDGSDTAEVLAAALADINA--PRPDFVVVTGDLTDD-----GEPEEYAAAREILARLG--VPVYVVPGNHDIR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 132 NTPTAETVEEFCRTWGDD-YFSFWVGGVLFLVLNSQFYENPSKCPSLKQAQdqWLDEQLSIARQRHcqhAIVFQHIPLFL 210
Cdd:COG1409   78 AAMAEAYREYFGDLPPGGlYYSFDYGGVRFIGLDSNVPGRSSGELGPEQLA--WLEEELAAAPAKP---VIVFLHHPPYS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 211 ESIDEDDDYYFNlskstRKKLADKFIHAGVKVVFSGHYHRNAGGTYQNLDMVVSSAIGCQLgRDPHGLRVVVVTAEKIVH 290
Cdd:COG1409  153 TGSGSDRIGLRN-----AEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQV-RLPPGYRVIEVDGDGLTV 226


                 ....*..
gi 153251270 291 RYYSLDE 297
Cdd:COG1409  227 EVRRVDG 233
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 33-256 1.09e-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: 66.59  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  33 FYFILGADPQFGlikawstgDCDNG--GDEWEQEIRLTEQAVQ-AINKLNP--KPKFFVLCGDLIHampGKPWRTEQTED 107
Cdd:cd07396    1 FSFGIIADIQYA--------DIDDGknLGTRRRYYRNSLGVLErAVEEWNResNLAFVVQLGDIID---GYNAKDRSKEA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 108 LKRVLRAVDRA-IPLVLVSGNHDIGNTPTAETVEEFCRTwGDD--YFSFWVG-GVLFLVLNSQFYenpskCPSLKQAQDQ 183
Cdd:cd07396   70 LDAVLSILDRLkGPVHHVLGNHEFYNFPREYLNHLKTLN-GEDayYYSFSPGpGFRFLVLDFVKF-----NGGIGEEQLA 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153251270 184 WLDEQLSIARQRHcQHAIVFQHIPLFLESIDE-----DDDYYFNLSKStrkkladkfiHAGVKVVFSGHYHRnagGTY 256
Cdd:cd07396  144 WLRNELTSADANG-EKVIVLSHLPIYPEAADPqcllwNYEEVLAILES----------YPCVKACFSGHNHE---GGY 207
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 69-270 1.26e-12

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: 66.15  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  69 EQAVQAINKLNPKPKFFVLCGDLIHampgkpW-RTEQTEDLKRVLRAVDraIPLVLVSGNHDIGNTPTAETVEEFCRTWG 147
Cdd:cd07402   27 AAAVAQVNALHPRPDLVVVTGDLSD------DgSPESYERLRELLAPLP--APVYWIPGNHDDRAAMREALPEPPYDDNG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 148 DDYFSFWVGGVLFLVLNSQFYENPSKCpsLKQAQDQWLDEQLSIARQRHcqhAIVFQHIPLFLESIDEDDDYyfNLSKST 227
Cdd:cd07402   99 PVQYVVDFGGWRLILLDTSVPGVHHGE--LSDEQLDWLEAALAEAPDRP---TLIFLHHPPFPLGIPWMDAI--RLRNSQ 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153251270 228 RkkLADK-FIHAGVKVVFSGHYHRNAGGTYQNLDMVVSSAIGCQ 270
Cdd:cd07402  172 A--LFAVlARHPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQ 213
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 66-250 3.80e-10

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: 59.62  E-value: 3.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  66 RLTEQAVQAINKLNPKPKFFVLCGDLIHAMPGKPWRTEQTEDLKRVLRAVDRAIPLVLVS---GNHDI----GNTPTAET 138
Cdd:cd00842   54 SLVESALEAIKKNHPKPDFILWTGDLVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYpalGNHDSypvnQFPPHSNS 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 139 V----EEFCRTWGDD--------------YFSFWVGGVLFLVLNSQFY--ENPskcPSLKQAQD-----QWLDEQLSIAR 193
Cdd:cd00842  134 PswlyDALAELWKPWlpteaketfkkggyYSVDVKDGLRVISLNTNLYykKNF---WLYSNNTDpcgqlQWLEDELEDAE 210

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153251270 194 QRHcQHAIVFQHIPLfleSIDEDDDYYFNLSkstrKKLADKFIHAgVKVVFSGHYHR 250
Cdd:cd00842  211 QKG-EKVWIIGHIPP---GLNSYDADWSERF----YQIINRYSDT-IAGQFFGHTHR 258
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 119-277 1.36e-09

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: 58.08  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 119 IPLVLVSGNHDIG----------NTPTAETVEEFCRTWGDDYFSFWVGGVLFLVLNSQFYENPSKcpsLKQAQDQWLDEQ 188
Cdd:cd00839   69 VPYMVAPGNHEADyngstskikfFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEAD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 189 LSIARQRHCQHAIVFQHIPLFlESIDEDDDYYFNLSKstRKKLADKFIHAGVKVVFSGHYH------RNAGGTYQNLDM- 261
Cdd:cd00839  146 LAKVDRSRTPWIIVMGHRPMY-CSNDDDADCIEGEKM--REALEDLFYKYGVDLVLSGHVHayertcPVYNNTVANSKDn 222

                        170       180
                 ....*....|....*....|....*.
gi 153251270 262 ----------VVSSAIGCQLGRDPHG 277
Cdd:cd00839  223 iytnpkgpvhIVIGAAGNDEGLDDAF 248
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 52-251 9.67e-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: 45.75  E-value: 9.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  52 GDCDNGGDEWEQEIRLTEQAVQAINKlNPKPKFFVLCGDLIHampGKPWRTEQ-TEDLKRVLR-AVDRAIPLVLVSGNHD 129
Cdd:cd07383   14 GEGEWTCWEGCEADLKTVEFIESVLD-EEKPDLVVLTGDLIT---GENTADDNaTSYLDKAVSpLVERGIPWAATFGNHD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 130 IGNTPTAETVEEFCRTwgddyfsfwvggvlflvlNSQFYENPSKCPslkqaqdqwldeqlsiarqrhcqHAIVFQHIPL- 208
Cdd:cd07383   90 GYDWIDPSQVEWFEST------------------SAALKKKYGKNI-----------------------PSLAFFHIPLp 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153251270 209 -FLE---------SIDEDDDYYFNLSKSTRKKLADKfihAGVKVVFSGHYHRN 251
Cdd:cd07383  129 eYREvwnekgklgGINREKVCCQKTNSGFFKALVKR---GDVKAVFCGHDHGN 178
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 69-130 2.79e-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: 2.79e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153251270  69 EQAVQAINKLNPKPKFFVLCGDLIHAMPGKPWrteqteDLKRVLRAVDRAIPLVLVSGNHDI 130
Cdd:cd00838   14 EAVLEAALAKAEKPDLVICLGDLVDYGPDPEE------VELKALRLLLAGIPVYVVPGNHDI 69
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
80-253 5.91e-05

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 43.46  E-value: 5.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  80 PKPKFFVLCGDLIHAMPgkpwrteqTEDLKRVLRAVDR-AIPLVLVSGNHDigntpTAETVEEFCR---TWGDDYFSFwV 155
Cdd:COG2129   25 EDADLVILAGDLTDFGT--------AEEAREVLEELAAlGVPVLAVPGNHD-----DPEVLDALEEsgvHNLHGRVVE-I 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 156 GGVLFLVLNsqfYENPSKCPSLKQAQDQWLDEQLsiARQRHCQHAIVFQHIPLFLESIDEDDDYYFNLSKSTRkKLADKF 235
Cdd:COG2129   91 GGLRIAGLG---GSRPTPFGTPYEYTEEEIEERL--AKLREKDVDILLTHAPPYGTTLDRVEDGPHVGSKALR-ELIEEF 164

                        170
                 ....*....|....*...
gi 153251270 236 ihaGVKVVFSGHYHRNAG 253
Cdd:COG2129  165 ---QPKLVLHGHIHESRG 179
PLN02533 PLN02533
probable purple acid phosphatase
 55-249 1.31e-04

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 43.13  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270  55 DNGGDEWeqeirlTEQAVQAINKLNPKpkFFVLCGDLIHAMPGKP-WRTeqtedLKRVLRAVDRAIPLVLVSGNHDIGNT 133
Cdd:PLN02533 147 DLGTSEW------TKSTLEHVSKWDYD--VFILPGDLSYANFYQPlWDT-----FGRLVQPLASQRPWMVTHGNHELEKI 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153251270 134 PT--AETVEEFCRTW----------GDDYFSFWVGGVLFLVLNSQFYENPSkcpslkQAQDQWLDEQLSIARQRHCQHAI 201
Cdd:PLN02533 214 PIlhPEKFTAYNARWrmpfeesgstSNLYYSFNVYGVHIIMLGSYTDFEPG------SEQYQWLENNLKKIDRKTTPWVV 287

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153251270 202 VFQHIPLFLESIDEDDDyyfNLSKSTRKKLADKFIHAGVKVVFSGHYH 249
Cdd:PLN02533 288 AVVHAPWYNSNEAHQGE---KESVGMKESMETLLYKARVDLVFAGHVH 332
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 81-131 2.98e-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: 40.76  E-value: 2.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153251270  81 KPKFFVLCGDLIHAMPGKPWrteQTEDLKRVLRAVDRAIPLVLVSGNHDIG 131
Cdd:cd07391   41 GPDRLVILGDLKHSFGRVSR---QERREVPFFRLLAKDVDVILIRGNHDGG 88
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 68-130 1.12e-03

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: 37.96  E-value: 1.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153251270   68 TEQAVQAINKlNPKPKFFVLCGDLIHampgkpwRTEQTEDLKRVLRAVDRAIPLVLVSGNHDI 130
Cdd:pfam00149  18 LLELLKKLLE-EGKPDLVLHAGDLVD-------RGPPSEEVLELLERLIKYVPVYLVRGNHDF 72
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
57-129 2.04e-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: 2.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153251270  57 GGDEWEQEIRLT-EQAVQAINKLnpKPKFFVLCGDLIHampgKPWRTEQTEDL--KRVLRAVDRAIPLVLVSGNHD 129
Cdd:COG0420   16 HGASRREDQLAAlDRLVDLAIEE--KVDAVLIAGDLFD----SANPSPEAVRLlaEALRRLSEAGIPVVLIAGNHD 85
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 56-130 7.58e-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: 36.86  E-value: 7.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153251270  56 NGGDEWEQEIRLT-EQAVQAINKlnPKPKFFVLCGDLIHamPGKPWRTEQTEDLKRVLRAVDRAIPLVLVSGNHDI 130
Cdd:cd00840   15 YGLSRREEDFFKAfEEIVDLAIE--EKVDFVLIAGDLFD--SNNPSPEALKLAIEGLRRLCEAGIPVFVIAGNHDS 86
 
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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