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Conserved domains on  [gi|79365227|ref|NP_175775|]
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Calcineurin-like metallo-phosphoesterase superfamily protein [Arabidopsis thaliana]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10164614)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 55-319 2.18e-73

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. This group also contains Saccharomyces cerevisiae TED1 (Trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), which acts together with Emp24p and Erv25p in cargo exit from the ER, and human MPPE1. The human MPPE1 gene is a candidate susceptibility gene for bipolar disorder. These proteins 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: 277330 [Multi-domain]  Cd Length: 172  Bit Score: 230.31  E-value: 2.18e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  55 AIVTDPQLMDKTSFRLSSKTlALELAQFYTDINMRRSFFRSVLPFKPDVVLFLGDYFDGGPFLSEEEWQESLNRLKHVFG 134
Cdd:cd07384   1 LLIADPQILDETSYPPRPKP-ALRLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 135 LNSEGRVGDIPTFYIPGNHDIGYSRVASHKQgVIDRYEKVFgvrnrrfmignvefisidaqaidgnskkdlasevwkfvq 214
Cdd:cd07384  80 LKSPGSLGSIPVIFIPGNHDIGYGGEAVFPE-KVDRFEKYF--------------------------------------- 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 215 nvstdaqshprVLLTHIPLYRpdqtpcgphrgssvidqrfwrhsqdqeviyqnyitpesstkLLELIKPILVLSGHDHDQ 294
Cdd:cd07384 120 -----------ILLTHIPLYR-----------------------------------------LLDSIKPVLILSGHDHDY 147

                       250       260
                ....*....|....*....|....*
gi 79365227 295 CTVIHKSKAGSVTEHTLGTVSWQQG 319
Cdd:cd07384 148 CEVVHKSSPGSVKEITVKSFSWRMG 172
 
Name Accession Description Interval E-value
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 55-319 2.18e-73

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. This group also contains Saccharomyces cerevisiae TED1 (Trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), which acts together with Emp24p and Erv25p in cargo exit from the ER, and human MPPE1. The human MPPE1 gene is a candidate susceptibility gene for bipolar disorder. These proteins 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: 277330 [Multi-domain]  Cd Length: 172  Bit Score: 230.31  E-value: 2.18e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  55 AIVTDPQLMDKTSFRLSSKTlALELAQFYTDINMRRSFFRSVLPFKPDVVLFLGDYFDGGPFLSEEEWQESLNRLKHVFG 134
Cdd:cd07384   1 LLIADPQILDETSYPPRPKP-ALRLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 135 LNSEGRVGDIPTFYIPGNHDIGYSRVASHKQgVIDRYEKVFgvrnrrfmignvefisidaqaidgnskkdlasevwkfvq 214
Cdd:cd07384  80 LKSPGSLGSIPVIFIPGNHDIGYGGEAVFPE-KVDRFEKYF--------------------------------------- 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 215 nvstdaqshprVLLTHIPLYRpdqtpcgphrgssvidqrfwrhsqdqeviyqnyitpesstkLLELIKPILVLSGHDHDQ 294
Cdd:cd07384 120 -----------ILLTHIPLYR-----------------------------------------LLDSIKPVLILSGHDHDY 147

                       250       260
                ....*....|....*....|....*
gi 79365227 295 CTVIHKSKAGSVTEHTLGTVSWQQG 319
Cdd:cd07384 148 CEVVHKSSPGSVKEITVKSFSWRMG 172
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-330 2.11e-16

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 78.58  E-value: 2.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  52 TKVAIVTDPQLmdktSFRLSSKTLALeLAQFYTDINMRRsffrsvlpfkPDVVLFLGDYFDGGpflSEEEWQESLNRLKH 131
Cdd:COG1409   1 FRFAHISDLHL----GAPDGSDTAEV-LAAALADINAPR----------PDFVVVTGDLTDDG---EPEEYAAAREILAR 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 132 VfglnsegrvgDIPTFYIPGNHDIGYSRVashkqgviDRYEKVFGV-----RNRRFMIGNVEFISIDAqAIDGNSKKDLA 206
Cdd:COG1409  63 L----------GVPVYVVPGNHDIRAAMA--------EAYREYFGDlppggLYYSFDYGGVRFIGLDS-NVPGRSSGELG 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 207 SEVWKFVQNVSTDAQSHPRVLLTHIPLYrpdqtPCGPHRGSSVIDQRFwrhsqdqeviyqnyitpesstKLLELIKP--- 283
Cdd:COG1409 124 PEQLAWLEEELAAAPAKPVIVFLHHPPY-----STGSGSDRIGLRNAE---------------------ELLALLARygv 177

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 79365227 284 ILVLSGHDHDQCTVIHkskaGSVTEHTLGTVSWQQGNIhPSFMLLSV 330
Cdd:COG1409 178 DLVLSGHVHRYERTRR----DGVPYIVAGSTGGQVRLP-PGYRVIEV 219
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 100-182 2.57e-06

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: 46.44  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227   100 KPDVVLFLGDYFDGGPFlsEEEWQESLNRLkhvfglnsegrVGDIPTFYIPGNHDIGYSRvASHKQGVIDRYEKVFGVRN 179
Cdd:pfam00149  30 KPDLVLHAGDLVDRGPP--SEEVLELLERL-----------IKYVPVYLVRGNHDFDYGE-CLRLYPYLGLLARPWKRFL 95


                  ...
gi 79365227   180 RRF 182
Cdd:pfam00149  96 EVF 98
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 16-232 3.46e-03

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 39.45  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227   16 AATILYGEMFAF---WVPSLFTCSwpHHKSDGVESDGNFTKVAIVTDPQLMDKTSFRLSSKTLALELAQfytdinmrrsf 92
Cdd:PRK11340  13 AATIATSSGFGYmhyWEPGWFELI--RHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQ----------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227   93 frsvlpfKPDVVLFLGDYFDGGPFLSEEEWQESLNRLKHVfglnsegrvgdIPTFYIPGNHDigySRVASHKQGVIDRYE 172
Cdd:PRK11340  80 -------KPDLILLGGDYVLFDMPLNFSAFSDVLSPLAEC-----------APTFACFGNHD---RPVGTEKNHLIGETL 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  173 KVFGVrnrRFMIGNVEFISIDAQAIDGNSKKDLASEVWKFVQNVSTDAqshPRVLLTHIP 232
Cdd:PRK11340 139 KSAGI---TVLFNQATVIATPNRQFELVGTGDLWAGQCKPPPASEANL---PRLVLAHNP 192
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 100-154 4.98e-03

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 38.94  E-value: 4.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 79365227   100 KPDVVLFLGDYFDGG--PFLSEEEWQESLNRLKhvfglnsegRVGDIPTFYIPGNHD 154
Cdd:TIGR00619  39 QVDALLVAGDVFDTAnpPAEAQELFNAFFVNLS---------DTGIRPIVVISGNHD 86
 
Name Accession Description Interval E-value
MPP_Cdc1_like cd07384
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 55-319 2.18e-73

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. This group also contains Saccharomyces cerevisiae TED1 (Trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), which acts together with Emp24p and Erv25p in cargo exit from the ER, and human MPPE1. The human MPPE1 gene is a candidate susceptibility gene for bipolar disorder. These proteins 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: 277330 [Multi-domain]  Cd Length: 172  Bit Score: 230.31  E-value: 2.18e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  55 AIVTDPQLMDKTSFRLSSKTlALELAQFYTDINMRRSFFRSVLPFKPDVVLFLGDYFDGGPFLSEEEWQESLNRLKHVFG 134
Cdd:cd07384   1 LLIADPQILDETSYPPRPKP-ALRLTQFYTDLYMRRAFDRVQQLLKPDVVLFLGDLFDGGRILDSEEWKEYLHRFQKIFF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 135 LNSEGRVGDIPTFYIPGNHDIGYSRVASHKQgVIDRYEKVFgvrnrrfmignvefisidaqaidgnskkdlasevwkfvq 214
Cdd:cd07384  80 LKSPGSLGSIPVIFIPGNHDIGYGGEAVFPE-KVDRFEKYF--------------------------------------- 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 215 nvstdaqshprVLLTHIPLYRpdqtpcgphrgssvidqrfwrhsqdqeviyqnyitpesstkLLELIKPILVLSGHDHDQ 294
Cdd:cd07384 120 -----------ILLTHIPLYR-----------------------------------------LLDSIKPVLILSGHDHDY 147

                       250       260
                ....*....|....*....|....*
gi 79365227 295 CTVIHKSKAGSVTEHTLGTVSWQQG 319
Cdd:cd07384 148 CEVVHKSSPGSVKEITVKSFSWRMG 172
MPP_Cdc1 cd08163
Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also ...
 55-319 3.30e-49

Saccharomyces cerevisiae CDC1 and related proteins, metallophosphatase domain; Cdc1 (also known as XlCdc1 in Xenopus laevis) is an endoplasmic reticulum-localized transmembrane lipid phosphatase with a metallophosphatase domain facing the ER lumen. In budding yeast, the gene encoding CDC1 is essential while nonlethal mutations cause defects in Golgi inheritance and actin polarization. Cdc1 mutant cells accumulate an unidentified phospholipid, suggesting that Cdc1 is a lipid phosphatase. Cdc1 mutant cells also have highly elevated intracellular calcium levels suggesting a possible role for Cdc1 in calcium regulation. The 5' flanking region of Cdc1 is a regulatory region with conserved binding site motifs for AP1, AP2, Sp1, NF-1 and CREB. DNA polymerase delta consists of at least four subunits - Pol3, Cdc1, Cdc27, and Cdm1. Cdc1 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: 277370  Cd Length: 257  Bit Score: 170.28  E-value: 3.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  55 AIVTDPQLMDKTSFRLSSKTLaLELAQFYTDINMRRSFfRSVLP-FKPDVVLFLGDYFDGGPFLSEEEWQESLNRLKHVF 133
Cdd:cd08163   1 ALVADPQLVDDHTYPGRPWIL-NTLTEHFVDQYLRRNW-RYLQKqLKPDSTFFLGDLFDGGREWADEYWKKEYFRFNRIF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 134 GLNSEGRVgdipTFYIPGNHDIGYSRVASHKqgVIDRYEKVFGVRNRRFMIGNVEFISIDAQAIDGNSKKDLASEVWKFV 213
Cdd:cd08163  79 DPKPLRKM----IESLPGNHDIGFGNGVKLP--VRQRFESYFGPTSRVIDVGNHTFVIVDTISLSNNDNPQVYQPAREFL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 214 -QNVSTDAQSHPRVLLTHIPLYRPDQTPCGPHRGSSVIDQRFWRHSqdqeviYQNYITPESSTKLLELIKPILVLSGHDH 292
Cdd:cd08163 153 hSFEAMKVNSKPRILLTHVPLYRPPNTSCGPLREKKTPLPYGYGYQ------YQNVLEPSLSESILKAINPVAAFSGDDH 226

                       250       260       270
                ....*....|....*....|....*....|.
gi 79365227 293 DQCTVIH----KSKAGSVTEHTLGTVSWQQG 319
Cdd:cd08163 227 DYCEVVHeyqfDGKEGSAREITVKSISMAMG 257
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
52-330 2.11e-16

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 78.58  E-value: 2.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  52 TKVAIVTDPQLmdktSFRLSSKTLALeLAQFYTDINMRRsffrsvlpfkPDVVLFLGDYFDGGpflSEEEWQESLNRLKH 131
Cdd:COG1409   1 FRFAHISDLHL----GAPDGSDTAEV-LAAALADINAPR----------PDFVVVTGDLTDDG---EPEEYAAAREILAR 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 132 VfglnsegrvgDIPTFYIPGNHDIGYSRVashkqgviDRYEKVFGV-----RNRRFMIGNVEFISIDAqAIDGNSKKDLA 206
Cdd:COG1409  63 L----------GVPVYVVPGNHDIRAAMA--------EAYREYFGDlppggLYYSFDYGGVRFIGLDS-NVPGRSSGELG 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 207 SEVWKFVQNVSTDAQSHPRVLLTHIPLYrpdqtPCGPHRGSSVIDQRFwrhsqdqeviyqnyitpesstKLLELIKP--- 283
Cdd:COG1409 124 PEQLAWLEEELAAAPAKPVIVFLHHPPY-----STGSGSDRIGLRNAE---------------------ELLALLARygv 177

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 79365227 284 ILVLSGHDHDQCTVIHkskaGSVTEHTLGTVSWQQGNIhPSFMLLSV 330
Cdd:COG1409 178 DLVLSGHVHRYERTRR----DGVPYIVAGSTGGQVRLP-PGYRVIEV 219
MPP_MPPE1 cd08165
human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally ...
 79-317 3.16e-15

human MPPE1 and related proteins, metallophosphatase domain; MPPE1 is a functionally uncharacterized metallophosphatase domain-containing protein. The MPPE1 gene is located on chromosome 18 and is a candidate susceptibility gene for Bipolar disorder. MPPE1 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: 277372 [Multi-domain]  Cd Length: 156  Bit Score: 73.26  E-value: 3.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  79 LAQFYTDINMRRSFFRSVLPFKPDVVLFLGDYFDGGPFLSEEEWQESLNRLKHVFGLNSegrvgDIPTFYIPGNHDIGYS 158
Cdd:cd08165  17 LDKLRREWQMERAFQTALWLLQPDVVFILGDIFDEGKWSSPQAWADDVARFQKMFRHPS-----DTPLHVVAGNHDIGFH 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 159 rvASHKQGVIDRYEKVFgvrnrrfmignvefisidaqaidgnskkdlasevwkfvqnvstdaqshprVLLTHIPLYRpdq 238
Cdd:cd08165  92 --YEMTTYKVHRFEKVF--------------------------------------------------ILLQHYPLYR--- 116

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79365227 239 tpcgphrgssvidqrfwrhsqdqeviyqnyitpesstkLLELIKPILVLSGHDHDQCTVIHKskaGSVTEHTLGTVSWQ 317
Cdd:cd08165 117 --------------------------------------LLQWLKPRLVLSGHTHSACEVLHY---GGIPEISVPSFSWR 154
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
85-311 1.83e-12

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 66.58  E-value: 1.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  85 DINMRRSFFRSVLPFKPDVVLFLGDYFDGGPFLSEEEWQESLNRLkhvfglnsegrvgDIPTFYIPGNHDIGYsrvashk 164
Cdd:COG2129  11 NFDLLEKLLELARAEDADLVILAGDLTDFGTAEEAREVLEELAAL-------------GVPVLAVPGNHDDPE------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 165 qgVIDRYEKvFGVRN---RRFMIGNVEFISI-DAQAIDGNSKKDL-ASEVWKFVQNVSTDaqsHPRVLLTHIPLYRP--D 237
Cdd:COG2129  71 --VLDALEE-SGVHNlhgRVVEIGGLRIAGLgGSRPTPFGTPYEYtEEEIEERLAKLREK---DVDILLTHAPPYGTtlD 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79365227 238 QTPCGPHRGSSVIDqrfwrhsqdqeviyqnyitpesstKLLELIKPILVLSGHdhdqctvIHKSKAGSVTEHTL 311
Cdd:COG2129 145 RVEDGPHVGSKALR------------------------ELIEEFQPKLVLHGH-------IHESRGVDKIGGTR 187
MPP_Cdc1_like_1 cd08166
uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; ...
 56-223 1.36e-10

uncharacterized subgroup related to Saccharomyces cerevisiae CDC1, metallophosphatase domain; A functionally uncharacterized subgroup related to the metallophosphatase domain of Saccharomyces cerevisiae Cdc1, S. cerevisiae Ted1 and human MPPE1. Cdc1 is an endoplasmic reticulum-localized transmembrane lipid phosphatase and is a subunit of DNA polymerase delta. TED1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1), acts together with Emp24p and Erv25p in cargo exit from the ER. The MPPE1 gene is a candidate susceptibility gene for Bipolar disorder. Proteins in this uncharacterized subgroup 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: 277373  Cd Length: 195  Bit Score: 60.92  E-value: 1.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  56 IVTDPQLMDKTSFRLSSKtlalELAQFYTDINMRRSFFRSVLPFKPDVVLFLGDYFDGGPFLSEEEWQESLNRLKHVFGL 135
Cdd:cd08166   2 LVADPQILGYENEKFGLG----EISRWDSDRYLAKTYERALWYFKPDIVIFLGDLFDEGIIANDDEYYSYVQRFIGIFPL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 136 -NSEGRVgdiptfYIPGNHDIGysrvashkqGVIDRY-EKvfgvRNRRFmigNVEFISIdaqaidgnSKKDLASEVWKFV 213
Cdd:cd08166  78 kRGKNAI------YIPGDNDIG---------GESEIIiES----RVRRF---NNYFIML--------SHVPLLVEGYLLL 127

                       170
                ....*....|
gi 79365227 214 QNVSTDAQSH 223
Cdd:cd08166 128 KHVVVDLKPD 137
MPP_Ted1 cd08164
Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces ...
 56-311 3.45e-10

Saccharomyces cerevisiae Ted1 and related proteins, metallophosphatase domain; Saccharomyces cerevisiae Ted1 (trafficking of Emp24p/Erv25p-dependent cargo disrupted 1) is a metallophosphatase domain-containing protein which acts together with Emp24p and Erv25p in cargo exit from the ER. Ted1 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: 277371  Cd Length: 193  Bit Score: 59.42  E-value: 3.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  56 IVTDPQLmdKTSFRLSSKTLALELAQFYTDINMRRSFFRSVLPFKPDVVLFLGDYFdGGPFLSEEEWQESLNRLKHVFG- 134
Cdd:cd08164   2 ALGDPQI--EGDWPITNYGFKGRLDIFGNDYFLGHIYQMMQFRLKPTHVTVLGDLF-SSQWITDEEFEKRADRYKKRIFg 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 135 ----LNSEGRV-------GDIPTFYIPGNHDIGYSRVASHKQgvIDRYEKVFgvrnrrfmignvefisidaqaidgnskk 203
Cdd:cd08164  79 rsdwQVGNISLaartfenGDILLINIAGNHDVGYAGESTEAR--ISRFEQLF---------------------------- 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 204 dlasevwkfvqnvstdaqshprVLLTHIPLYrpdqtpcgphrgssvidqrfwrhsqdqeviyqnyitpesstKLLELIKP 283
Cdd:cd08164 129 ----------------------ILLTHVPLY-----------------------------------------KFFLEGKP 145

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 79365227 284 ILVLSGHDHDQCTVIHKSKAG------------SVTEHTL 311
Cdd:cd08164 146 GLILTGHDHEGCDYEYPSNPSvtwatsleesgnGVREYTV 185
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 77-292 1.78e-07

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 51.90  E-value: 1.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  77 LELAQFyTDI----NMRRSFF----RSVLPFKPDVVLFLGDYFDGGPFLSEEEwQESLNRLKHvfglnsegrvgDIPTFY 148
Cdd:cd07385   2 LRIVQL-SDIhlgpFVGRTRLqkvvRKVNELNPDLIVITGDLVDGDVSVLRLL-ASPLSKLKA-----------PLGVYF 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 149 IPGNHDIGYSRVASHKQgvidRYEK----VFGVRNRRFMIGNvEFISIDAQAIDGNSKKDLASEvwKFVQNVSTDaqsHP 224
Cdd:cd07385  69 VLGNHDYYSGDVEVWIA----ALEKagitVLRNESVELSRDG-ATIGLAGSGVDDIGGHGEDLE--KALKGLDEN---DP 138

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79365227 225 RVLLTHIPLYRpdqtpcgphrgssvidqrfwrhsqdqeviyqnyitpesstKLLELIKPILVLSGHDH 292
Cdd:cd07385 139 VILLAHNPDAA----------------------------------------EEAQRPGVDLVLSGHTH 166
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
100-232 3.20e-07

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 51.72  E-value: 3.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 100 KPDVVLFLGDYFDGGPFLsEEEWQESLNRLKHVFGlnsegrvgdipTFYIPGNHDIGysrvaSHKQGVIDRYEKVfGV-- 177
Cdd:COG1408  73 KPDLVVLTGDLVDGSVAE-LEALLELLKKLKAPLG-----------VYAVLGNHDYY-----AGLEELRAALEEA-GVrv 134

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79365227 178 -RNRRfmignvEFISIDAQAID--------GNSKKDLAsevwKFVQNVSTDAqshPRVLLTHIP 232
Cdd:COG1408 135 lRNEA------VTLERGGDRLNlagvddphAGRFPDLE----KALAGVPPDA---PRILLAHNP 185
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 100-239 1.71e-06

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: 49.63  E-value: 1.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 100 KPDVVLFLGDYFDGGPFLSEEEWQESlnRLKHVF-GLNSegrvgDIPTFYIPGNHDIGYSRVAShkqgVIDRYEKVFGVR 178
Cdd:cd07395  50 KPKFVVVCGDLVHAMPGEEFREQQVS--DLKDVLsKLDP-----DIPLVCVCGNHDVGNTPTPE----TIQRYRDDFGDD 118

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79365227 179 NRRFMIGNVEFISIDAQAIDGNSK-KDLASEVWKFVQNVSTDAQSHP---RVLLTHIP--LYRPDQT 239
Cdd:cd07395 119 YFSFWVGGVFFIVLNSQLFKDPSKvPELASAQDQWLEEQLQIARESDakhVVVFQHIPlfLEDPDEE 185
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 100-182 2.57e-06

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: 46.44  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227   100 KPDVVLFLGDYFDGGPFlsEEEWQESLNRLkhvfglnsegrVGDIPTFYIPGNHDIGYSRvASHKQGVIDRYEKVFGVRN 179
Cdd:pfam00149  30 KPDLVLHAGDLVDRGPP--SEEVLELLERL-----------IKYVPVYLVRGNHDFDYGE-CLRLYPYLGLLARPWKRFL 95


                  ...
gi 79365227   180 RRF 182
Cdd:pfam00149  96 EVF 98
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 100-163 4.71e-06

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: 46.11  E-value: 4.71e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79365227 100 KPDVVLFLGDYFDGGPFLSEEEWQESLNRLKhvfglnsegrvgDIPTFYIPGNHDIgysrVASH 163
Cdd:cd00838  26 KPDLVICLGDLVDYGPDPEEVELKALRLLLA------------GIPVYVVPGNHDI----LVTH 73
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
100-154 4.67e-04

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 41.82  E-value: 4.67e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 79365227 100 KPDVVLFLGDYFDGG--PFLSEEEWQESLNRLKHvfglnsegrvGDIPTFYIPGNHD 154
Cdd:COG0420  39 KVDAVLIAGDLFDSAnpSPEAVRLLAEALRRLSE----------AGIPVVLIAGNHD 85
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 16-232 3.46e-03

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 39.45  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227   16 AATILYGEMFAF---WVPSLFTCSwpHHKSDGVESDGNFTKVAIVTDPQLMDKTSFRLSSKTLALELAQfytdinmrrsf 92
Cdd:PRK11340  13 AATIATSSGFGYmhyWEPGWFELI--RHRLAFFKDNAAPFKILFLADLHYSRFVPLSLISDAIALGIEQ----------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227   93 frsvlpfKPDVVLFLGDYFDGGPFLSEEEWQESLNRLKHVfglnsegrvgdIPTFYIPGNHDigySRVASHKQGVIDRYE 172
Cdd:PRK11340  80 -------KPDLILLGGDYVLFDMPLNFSAFSDVLSPLAEC-----------APTFACFGNHD---RPVGTEKNHLIGETL 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  173 KVFGVrnrRFMIGNVEFISIDAQAIDGNSKKDLASEVWKFVQNVSTDAqshPRVLLTHIP 232
Cdd:PRK11340 139 KSAGI---TVLFNQATVIATPNRQFELVGTGDLWAGQCKPPPASEANL---PRLVLAHNP 192
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 100-154 4.98e-03

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 38.94  E-value: 4.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 79365227   100 KPDVVLFLGDYFDGG--PFLSEEEWQESLNRLKhvfglnsegRVGDIPTFYIPGNHD 154
Cdd:TIGR00619  39 QVDALLVAGDVFDTAnpPAEAQELFNAFFVNLS---------DTGIRPIVVISGNHD 86
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 99-292 5.73e-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: 38.85  E-value: 5.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227  99 FKPDVVLFLGD--YFDGGPFLSEEEWQESLnrlKHVFGLNSEgrvgDIPTFYIPGNHDIGYSR---VASHKQGVIDR--- 170
Cdd:cd07378  35 LGIDFILSLGDnfYDDGVKDVDDPRFQETF---EDVYSAPSL----QVPWYLVLGNHDHRGNVsaqIAYTQRPNSKRwnf 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79365227 171 ----YEKV--FGVRNRrfmigNVEFISIDAQAIDGNSKKD------------LASEVWKFVQNVSTDAQSHPRVLLTHIP 232
Cdd:cd07378 108 pnyyYDISfkFPSSDV-----TVAFIMIDTVLLCGNTDDEasgqprgppnkkLAETQLAWLEKQLAASKADYKIVVGHYP 182

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79365227 233 LYRpdqtpCGPHRGssvidqrfwrhsqDQEVIYQnyitpesstkLLELIKPI---LVLSGHDH 292
Cdd:cd07378 183 IYS-----SGEHGP-------------TKCLVDI----------LLPLLKKYkvdAYLSGHDH 217
 
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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