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Conserved domains on  [gi|1220191544|ref|XP_021786408|]
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tartrate-resistant acid phosphatase type 5 [Papio anubis]

Protein Classification

tartrate-resistant acid phosphatase type 5 family protein( domain architecture ID 10164501)

tartrate-resistant acid phosphatase type 5 family protein which is a metallophosphatase; similar to human tartrate-resistant acid phosphatase type 5 (ACP5) which is involved in osteopontin/bone sialoprotein dephosphorylation in bone matrix, and to Arabidopsis thaliana purple acid phosphatase 17 (PAP17) which is involved in phosphate metabolism and has a peroxidase activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 26-311 5.91e-165

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: 460.64  E-value: 5.91e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  26 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDVNDKRFQETFEDVFSDRSLrNVPWY 105
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 106 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPFYRLRFKIPRTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLART 183
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 184 QLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYRVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1220191544 264 MDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASG 311
Cdd:cd07378   239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 26-311 5.91e-165

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: 460.64  E-value: 5.91e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  26 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDVNDKRFQETFEDVFSDRSLrNVPWY 105
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 106 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPFYRLRFKIPRTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLART 183
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 184 QLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYRVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1220191544 264 MDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASG 311
Cdd:cd07378   239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
26-286 2.54e-26

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 104.00  E-value: 2.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  26 LRFVAVGDWGGVPNAPFHTAREMANAkeiARTVQILGADFILSLGDNfyftgVQDVNDKRFQEtFEDVFSDRslrNVPWY 105
Cdd:COG1409     1 FRFAHISDLHLGAPDGSDTAEVLAAA---LADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILARL---GVPVY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 106 VLAGNHDHLGNVSAqiAYSKISKRWNFPSPFYRLRFKiprtnvSVAIFMLDTVTLCGNSDDflsqqperprdvkLARTQL 185
Cdd:COG1409    69 VVPGNHDIRAAMAE--AYREYFGDLPPGGLYYSFDYG------GVRFIGLDSNVPGRSSGE-------------LGPEQL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 186 SWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLV--KQLRPLLATYRVTAYLCGHDHNlQYLQDENGVGYVLSGAGNf 263
Cdd:COG1409   128 AWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPYIVAGSTG- 205

                         250       260
                  ....*....|....*....|...
gi 1220191544 264 mdpskrHQRKVPNGYLRFHYGTE 286
Cdd:COG1409   206 ------GQVRLPPGYRVIEVDGD 222
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 26-325 2.74e-18

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 84.49  E-value: 2.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  26 LRFVAVGDWGGVPNApfhtarEMANAKEIARTVQILGADFILSLGDNFyFTGVQDVNDKRFQETFEDVFSDRS-LRNVPW 104
Cdd:PTZ00422   27 LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 105 YVLAGNHDHLGNVSAQ----------------IAYSKISK---RWNFPSPFYRL-----------RFKIPRTNVSVAIFM 154
Cdd:PTZ00422  100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYfthftdtsgpsLLKSGHKDMSVAFIF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 155 LDTVTLCGNSDDflsqqperpRDVklarTQLSW--LKKQLAAARE--DYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLAT 230
Cdd:PTZ00422  180 IDTWILSSSFPY---------KKV----SERAWqdLKATLEYAPKiaDYIIVVGDKPIYSSGSSKGDSYLSYYLLPLLKD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 231 YRVTAYLCGHDHNLqYLQDENGVGYVLSGAGNfmdpskRHQRKVPNGYLRFHYGTEDSlgGFAYVEISSKEMTVTYIEA- 309
Cdd:PTZ00422  247 AQVDLYISGYDRNM-EVLTDEGTAHINCGSGG------NSGRKSIMKNSKSLFYSEDI--GFCIHELNAEGMVTKFVSGn 317

                         330
                  ....*....|....*.
gi 1220191544 310 SGKSLFKTSLPRRARP 325
Cdd:PTZ00422  318 TGEVLYTHKQPLKKRK 333
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 26-137 3.25e-05

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 42.59  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  26 LRFVAVGDWGGVPNAPfhtaremANAKEIARTVQILGADFILSLGDNfyftgvqdVNDKRFQETFEDVFsDRSLRNVPWY 105
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDL--------VDRGPPSEEVLELL-ERLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1220191544 106 VLAGNHD--HLGNVSAQIAYSKISKRWNFPSPFY 137
Cdd:pfam00149  65 LVRGNHDfdYGECLRLYPYLGLLARPWKRFLEVF 98
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 26-311 5.91e-165

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: 460.64  E-value: 5.91e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  26 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDVNDKRFQETFEDVFSDRSLrNVPWY 105
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 106 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPFYRLRFKIPRTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLART 183
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 184 QLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYRVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1220191544 264 MDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASG 311
Cdd:cd07378   239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
26-286 2.54e-26

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 104.00  E-value: 2.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  26 LRFVAVGDWGGVPNAPFHTAREMANAkeiARTVQILGADFILSLGDNfyftgVQDVNDKRFQEtFEDVFSDRslrNVPWY 105
Cdd:COG1409     1 FRFAHISDLHLGAPDGSDTAEVLAAA---LADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILARL---GVPVY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 106 VLAGNHDHLGNVSAqiAYSKISKRWNFPSPFYRLRFKiprtnvSVAIFMLDTVTLCGNSDDflsqqperprdvkLARTQL 185
Cdd:COG1409    69 VVPGNHDIRAAMAE--AYREYFGDLPPGGLYYSFDYG------GVRFIGLDSNVPGRSSGE-------------LGPEQL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 186 SWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLV--KQLRPLLATYRVTAYLCGHDHNlQYLQDENGVGYVLSGAGNf 263
Cdd:COG1409   128 AWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPYIVAGSTG- 205

                         250       260
                  ....*....|....*....|...
gi 1220191544 264 mdpskrHQRKVPNGYLRFHYGTE 286
Cdd:COG1409   206 ------GQVRLPPGYRVIEVDGD 222
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 26-325 2.74e-18

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 84.49  E-value: 2.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  26 LRFVAVGDWGGVPNApfhtarEMANAKEIARTVQILGADFILSLGDNFyFTGVQDVNDKRFQETFEDVFSDRS-LRNVPW 104
Cdd:PTZ00422   27 LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 105 YVLAGNHDHLGNVSAQ----------------IAYSKISK---RWNFPSPFYRL-----------RFKIPRTNVSVAIFM 154
Cdd:PTZ00422  100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYfthftdtsgpsLLKSGHKDMSVAFIF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 155 LDTVTLCGNSDDflsqqperpRDVklarTQLSW--LKKQLAAARE--DYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLAT 230
Cdd:PTZ00422  180 IDTWILSSSFPY---------KKV----SERAWqdLKATLEYAPKiaDYIIVVGDKPIYSSGSSKGDSYLSYYLLPLLKD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 231 YRVTAYLCGHDHNLqYLQDENGVGYVLSGAGNfmdpskRHQRKVPNGYLRFHYGTEDSlgGFAYVEISSKEMTVTYIEA- 309
Cdd:PTZ00422  247 AQVDLYISGYDRNM-EVLTDEGTAHINCGSGG------NSGRKSIMKNSKSLFYSEDI--GFCIHELNAEGMVTKFVSGn 317

                         330
                  ....*....|....*.
gi 1220191544 310 SGKSLFKTSLPRRARP 325
Cdd:PTZ00422  318 TGEVLYTHKQPLKKRK 333
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 26-243 3.79e-10

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: 60.00  E-value: 3.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  26 LRFVAVGDWGGVPNAPFHTAREMANAKEiartvqilGADFILSLGDNFYFTGvqDVNDKR---FQETFEDVFSdrslrNV 102
Cdd:cd00839     5 LKFAVFGDMGQNTNNSTNTLDHLEKELG--------NYDAIIHVGDIAYADG--YNNGSRwdtFMRQIEPLAS-----YV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 103 PWYVLAGNHDhlgnvsaqiayskiskrWNFPSPFYRLRFKIPRTNV-------------SVAIFMLDTVTLCGNSDDFLS 169
Cdd:cd00839    70 PYMVAPGNHE-----------------ADYNGSTSKIKFFMPGRGMppspsgstenlwySFDVGPVHFISLSTETDFLKG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 170 QQPERprdvklartQLSWLKKQLAAA---REDYVLVAGHYPvWSIAEHGPTHCLVK-----QLRPLLATYRVTAYLCGHD 241
Cdd:cd00839   133 DNISP---------QYDWLEADLAKVdrsRTPWIIVMGHRP-MYCSNDDDADCIEGekmreALEDLFYKYGVDLVLSGHV 202


                  ..
gi 1220191544 242 HN 243
Cdd:cd00839   203 HA 204
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 63-256 5.83e-09

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: 55.80  E-value: 5.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  63 ADFILSLGD--NFYFTgvqdvnDKRFQETFEDVFSDRSLRNVPWYVLAGNHDHLGNVSAQIAYSKISKRWNFP----SPF 136
Cdd:cd07396    47 LAFVVQLGDiiDGYNA------KDRSKEALDAVLSILDRLKGPVHHVLGNHEFYNFPREYLNHLKTLNGEDAYyysfSPG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 137 YRLRFkiprtnvsvaiFMLDTVTLCGNsddflsqqperprdvkLARTQLSWLKKQL--AAAREDYVLVAGHYPVWSIAEH 214
Cdd:cd07396   121 PGFRF-----------LVLDFVKFNGG----------------IGEEQLAWLRNELtsADANGEKVIVLSHLPIYPEAAD 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1220191544 215 GptHCLVKQLRPLLATYR----VTAYLCGHDHNLQYLQDENGVGYV 256
Cdd:cd07396   174 P--QCLLWNYEEVLAILEsypcVKACFSGHNHEGGYEQDSHGVHHV 217
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 39-242 2.15e-06

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: 48.45  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  39 NAPFHTARE-MANAKEIArtvqiLGADFILSLGDNfyftgVQDVNDKRFQETFEDVFS------DRSLRNVPWYVLAGNH 111
Cdd:cd00842    50 DSPWSLVESaLEAIKKNH-----PKPDFILWTGDL-----VRHDVDEQTPEETVESESnltnllKKYFPNVPVYPALGNH 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 112 DhlGNVSAQIAYSKISKRWNFPSpFYRL-----------RFK-------IPRTNVSVaIFmLDTVtLCGNSDDFLSQQPE 173
Cdd:cd00842   120 D--SYPVNQFPPHSNSPSWLYDA-LAELwkpwlpteakeTFKkggyysvDVKDGLRV-IS-LNTN-LYYKKNFWLYSNNT 193

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1220191544 174 RPRDvklartQLSWLKKQLAAARE--DYVLVAGH-YPVWSIAEHGPTHCLVKqlrpLLATYR--VTAYLCGHDH 242
Cdd:cd00842   194 DPCG------QLQWLEDELEDAEQkgEKVWIIGHiPPGLNSYDADWSERFYQ----IINRYSdtIAGQFFGHTH 257
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 104-245 6.17e-06

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: 46.97  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 104 WYVLAGNHDHLGNVSAQIA---YSKISKRwnFPSPFYRLRFKIPRTNVSVAIFmldtvtlcgnsDDFLSQQPERPRDV-- 178
Cdd:cd07401    80 LFDIRGNHDLFGIVSFDSQnnyYRKYSNT--GRDHSHSFSSTTRFGNYSFIGF-----------DPTIFPGPKRPFNFfg 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1220191544 179 KLARTQLSWLKKQLAAA-REDYVLVAGHYPVWSIAEHGPTHCLvKQLRPLLATYRVTAYLCGHDHNLQ 245
Cdd:cd07401   147 SLDKKLLDRLEKELEKSkNSKYTIWFGHYPHSLIISPSAKSSS-KTFKDLLKKYNVTAYLCGHLHPLG 213
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 101-243 8.27e-06

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: 46.12  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 101 NVPWYVLAGNHDHlgnvsaQIAYSKIskrwnFPSPFYRLRFKIPRTnVSVA---IFMLDTVTlCGNSDDFLSQQperprd 177
Cdd:cd07402    69 PAPVYWIPGNHDD------RAAMREA-----LPEPPYDDNGPVQYV-VDFGgwrLILLDTSV-PGVHHGELSDE------ 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 178 vklartQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGP-THCLVKQ--LRPLLATY-RVTAYLCGHDHN 243
Cdd:cd07402   130 ------QLDWLEAALAEAPDRPTLIFLHHPPFPLGIPWMdAIRLRNSqaLFAVLARHpQVKAILCGHIHR 193
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 26-137 3.25e-05

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 42.59  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  26 LRFVAVGDWGGVPNAPfhtaremANAKEIARTVQILGADFILSLGDNfyftgvqdVNDKRFQETFEDVFsDRSLRNVPWY 105
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDL--------VDRGPPSEEVLELL-ERLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1220191544 106 VLAGNHD--HLGNVSAQIAYSKISKRWNFPSPFY 137
Cdd:pfam00149  65 LVRGNHDfdYGECLRLYPYLGLLARPWKRFLEVF 98
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 200-259 4.01e-05

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the 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: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 42.67  E-value: 4.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1220191544 200 VLVAGHYPVWSIAEHG---PTHCLVKQLRPLLATYRVTAYLCGHDH--NLQYLQDENGVGYVLSG 259
Cdd:cd07400    73 AIVALHHPLLPPPDTGrerNVLLDAGDALKLLKELGVDLVLHGHKHvpAVWNLGLLNGIVVVNAG 137
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
27-259 4.60e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 44.13  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  27 RFVAVGDW--GgvpnAPFHtAREMANA-----KEIARTVQILGADFILSLGDNFyftgvqDVN--DKRFQETFEDVFSDR 97
Cdd:COG0420     2 RFLHTADWhlG----KPLH-GASRREDqlaalDRLVDLAIEEKVDAVLIAGDLF------DSAnpSPEAVRLLAEALRRL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  98 SLRNVPWYVLAGNHDHLGnvsaqiayskiskRWNFPSPFYRlrfkipRTNVSV-AIFMLDTVTLCGNSD------DFLsq 170
Cdd:COG0420    71 SEAGIPVVLIAGNHDSPS-------------RLSAGSPLLE------NLGVHVfGSVEPEPVELEDGLGvavyglPYL-- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 171 qpeRPRDVKLARTQLSWLKKQLAAARedYVLVAGHYPVWSIAEHGPTHclVKQLRP-LLATYRVTAYLCGHDHNLQYLQD 249
Cdd:COG0420   130 ---RPSDEEALRDLLERLPRALDPGG--PNILLLHGFVAGASGSRDIY--VAPVPLsALPAAGFDYVALGHIHRPQVLGG 202

                         250
                  ....*....|
gi 1220191544 250 ENGVGYvlSG 259
Cdd:COG0420   203 DPRIRY--SG 210
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 187-257 6.95e-05

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 41.87  E-value: 6.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 187 WLKKQLAAAREDYVLVAG-------HYPVWSIAEHG--PTHCLVKQLRPLLATYRVTAYLCGHDHNLQYLQDENGVGYVL 257
Cdd:cd00838    48 LKALRLLLAGIPVYVVPGnhdilvtHGPPYDPLDEGspGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLVV 127
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
27-243 1.18e-04

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 42.69  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  27 RFVAVGDWGGvpnapfhtarEMANAKEIARTVQILGADFILSLGDnfyftgvqdVNDKRFQETFEDVFSDRSLRNVPWYV 106
Cdd:COG2129     1 KILAVSDLHG----------NFDLLEKLLELARAEDADLVILAGD---------LTDFGTAEEAREVLEELAALGVPVLA 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 107 LAGNHDHlgnvsaqiayskiskrwnfpspfYRLRFKIPRTNVSVA---IFMLDTVTLCGnsddfLSQQPERPRDVKLART 183
Cdd:COG2129    62 VPGNHDD-----------------------PEVLDALEESGVHNLhgrVVEIGGLRIAG-----LGGSRPTPFGTPYEYT 113

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1220191544 184 QlSWLKKQLAAAREDY--VLVAgHYPVWSIA---EHGPTHCLVKQLRPLLATYRVTAYLCGHDHN 243
Cdd:COG2129   114 E-EEIEERLAKLREKDvdILLT-HAPPYGTTldrVEDGPHVGSKALRELIEEFQPKLVLHGHIHE 176
PhoD COG3540
Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism];
19-196 1.95e-04

Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism];


Pssm-ID: 442761 [Multi-domain]  Cd Length: 482  Bit Score: 42.99  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  19 ADGATPALRFVAVGDWGGvPNAPFHTAREMANAKeiartvqilgADFILSLGDNFYFTGVQDVNDKRFQ--------ETF 90
Cdd:COG3540   128 APGAPDRLRFAFASCQNY-EGGYFTAYRAMAEED----------PDFVLHLGDYIYEDGPGPYGLPGLWrpepskeaETL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  91 ED-------VFSDRSLR----NVPWYVLAGNHDHLGNvsaqiAYSKISKRWNFPSPFYRLRFK-----------IPRTNV 148
Cdd:COG3540   197 ADyrgryaqYRSDPDLQalhaAVPWIATWDDHEVANN-----WAGGGAEHDRYTEGDFAARRAaalqafyeympIRRPGP 271

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1220191544 149 S---------------VAIFMLDTVTLCGNSDDFLSQQPERPRDVKLARTQLSWLKKQLAAAR 196
Cdd:COG3540   272 DgddgriyrrfrygdlADLFMLDTRSYRDPQPCLQCPEADDPDRTLLGAEQLAWLKDGLAAST 334
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 64-242 2.32e-04

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 42.23  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  64 DFILSLGDNfyftgVQDVNDKRFQETFEDVfsdRSLrNVPWYVLAGNHD---HLGNV--SAQIAYSK---ISKRWNfpsp 135
Cdd:PRK11148   57 DLIVATGDL-----AQDHSSEAYQHFAEGI---APL-RKPCVWLPGNHDfqpAMYSAlqDAGISPAKhvlIGEHWQ---- 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544 136 fyrlrfkiprtnvsvaIFMLDTvTLCGNSDDFLSQQperprdvklartQLSWLKKQLAAAREDYVLVA-GHYPVwsiaeh 214
Cdd:PRK11148  124 ----------------ILLLDS-QVFGVPHGELSEY------------QLEWLERKLADAPERHTLVLlHHHPL------ 168

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1220191544 215 gPTHCL---------VKQLRPLLATY-RVTAYLCGHDH 242
Cdd:PRK11148  169 -PAGCAwldqhslrnAHELAEVLAKFpNVKAILCGHIH 205
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 43-114 2.75e-04

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 40.33  E-value: 2.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1220191544  43 HTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDVNDKRFQEtfedvfsdRSLRNVPWYVLAGNHDHL 114
Cdd:cd00838     7 HGNLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALR--------LLLAGIPVYVVPGNHDIL 70
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 27-155 2.31e-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: 38.40  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220191544  27 RFVAVGDW--GgvpnAPFHTAREMANA-----KEIARTVQILGADFILSLGDNFyftgvqDVNDKRF--QETFEDVFSDR 97
Cdd:cd00840     1 RFLHTADWhlG----YPLYGLSRREEDffkafEEIVDLAIEEKVDFVLIAGDLF------DSNNPSPeaLKLAIEGLRRL 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1220191544  98 SLRNVPWYVLAGNHDHLGnvSAQI-AYSKISKRWNFPSPFYRLRFKIPRTNVSVAIFML 155
Cdd:cd00840    71 CEAGIPVFVIAGNHDSPA--RVAIyGLPYLRDERLERLFEDLELRPRLLKPDWFNILLL 127
 
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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