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Conserved domains on  [gi|1081357648|gb|OFU95536|]
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nucleotide pyrophosphatase [Morganella sp. HMSC11D09]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 11445914)

alkaline phosphatase family protein catalyzes the hydrolysis of phosphate monoesters or diesters, similar to ectonucleotide pyrophosphatases/phosphodiesterases (ENPPs), which hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates

CATH:  3.40.720.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
3-257 7.51e-43

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


:

Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 149.90  E-value: 7.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648   3 NPVILVVLDGLNYRTAHD-CMGFMQGLAESGdATLYRLSCELPSLSRPLYECILTGVRPVDSGVVHNQVVRLSHNDSIFS 81
Cdd:COG1524    24 KKVVLILVDGLRADLLERaHAPNLAALAARG-VYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVVNS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648  82 LAQKAGKTTAAAayHWISE-LYNRA-----------PFDAVRDRFTHDDSLAIQHGCFYQADHYPDD-HLFLDAEYLRRQ 148
Cdd:COG1524   103 LSWVEDGFGSNS--LLPVPtIFERAraaglttaavfWPSFEGSGLIDAARPYPYDGRKPLLGNPAADrWIAAAALELLRE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 149 YHPDFLLIHPMNIDDAGHKSGGDSQQYRNSARRADGLLSAYLPAW----LEAGYQVLVTSDHGMNNDR------------ 212
Cdd:COG1524   181 GRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALkargLYEGTLVIVTADHGMVDVPpdidlnrlrlag 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 213 -------------------------------------------------------------------SHGGILDEERAVP 225
Cdd:COG1524   261 llavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkgSHGGLPDEEMRVP 340
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1081357648 226 LFVTGDAFSHEadlpVQQTQLCGTICRLLGLS 257
Cdd:COG1524   341 LLASGPGFRPG----VRNVDVAPTIARLLGLP 368
 
Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
3-257 7.51e-43

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 149.90  E-value: 7.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648   3 NPVILVVLDGLNYRTAHD-CMGFMQGLAESGdATLYRLSCELPSLSRPLYECILTGVRPVDSGVVHNQVVRLSHNDSIFS 81
Cdd:COG1524    24 KKVVLILVDGLRADLLERaHAPNLAALAARG-VYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVVNS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648  82 LAQKAGKTTAAAayHWISE-LYNRA-----------PFDAVRDRFTHDDSLAIQHGCFYQADHYPDD-HLFLDAEYLRRQ 148
Cdd:COG1524   103 LSWVEDGFGSNS--LLPVPtIFERAraaglttaavfWPSFEGSGLIDAARPYPYDGRKPLLGNPAADrWIAAAALELLRE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 149 YHPDFLLIHPMNIDDAGHKSGGDSQQYRNSARRADGLLSAYLPAW----LEAGYQVLVTSDHGMNNDR------------ 212
Cdd:COG1524   181 GRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALkargLYEGTLVIVTADHGMVDVPpdidlnrlrlag 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 213 -------------------------------------------------------------------SHGGILDEERAVP 225
Cdd:COG1524   261 llavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkgSHGGLPDEEMRVP 340
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1081357648 226 LFVTGDAFSHEadlpVQQTQLCGTICRLLGLS 257
Cdd:COG1524   341 LLASGPGFRPG----VRNVDVAPTIARLLGLP 368
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
3-255 2.17e-13

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 68.38  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648   3 NPVILVVLDGL--NYRTAHDCMGFMQGLAESGDATLYrLSCELPSLSRPLYECILTGVRPVDSGVVHNQVvrlshndsIF 80
Cdd:cd16018     1 PPLIVISIDGFrwDYLDRAGLTPNLKRLAEEGVRAKY-VKPVFPTLTFPNHYSIVTGLYPESHGIVGNYF--------YD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648  81 SLAQKAGKTTAAAAYHWiselYNRAP--FDAVR--------------DRFTHDDSLAiqhGCFYQADHYPDDHLFLDAEY 144
Cdd:cd16018    72 PKTNEEFSDSDWVWDPW----WIGGEpiWVTAEkaglktasyfwpgsEVAIIGYNPT---PIPLGGYWQPYNDSFPFEER 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 145 L------RRQYHPDFLLIHPMNIDDAGHKSGGDSQQYRNSARRADG----LLSAYLPAWLEAGYQVLVTSDHGMNNDRSH 214
Cdd:cd16018   145 VdtilewLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRrlgyLIEALKERGLLDDTNIIVVSDHGMTDVGTH 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1081357648 215 GGILDEERAVPLFV-TGDAFSHEADL-PVQQTQLCGTICRLLG 255
Cdd:cd16018   225 GYDNELPDMRAIFIaRGPAFKKGKKLgPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
5-208 1.06e-10

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 61.28  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648   5 VILVVLDGL--NYRTAHDCMGFMQGLAESGDATLYrLSCELPSLSRPLYECILTGVRPVDSGVVHNQVV-RLSHNDSIFS 81
Cdd:pfam01663   1 LLVISLDGFraDYLDRFELTPNLAALAKEGVSAPN-LTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYdPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648  82 LAQkagkttaaaayHWISELYNRAP--FDAVRDRFT-------------HDDSLAIQHGC---FYQADHYPDDH------ 137
Cdd:pfam01663  80 ISD-----------PEDPRWWQGEPiwDTAAKAGVRaaalfwpgsevdySTYYGTPPRYLkddYNNSVPFEDRVdtavlq 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081357648 138 -LFLDAEYLRRQYHPDFLLIHPMNIDDAGHKSGGDSQQYRNSARRADGLLsAYLPAWLE-----AGYQVLVTSDHGM 208
Cdd:pfam01663 149 tWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAI-GDLLEALDerglfEDTNVIVVSDHGM 224
 
Name Accession Description Interval E-value
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
3-257 7.51e-43

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 149.90  E-value: 7.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648   3 NPVILVVLDGLNYRTAHD-CMGFMQGLAESGdATLYRLSCELPSLSRPLYECILTGVRPVDSGVVHNQVVRLSHNDSIFS 81
Cdd:COG1524    24 KKVVLILVDGLRADLLERaHAPNLAALAARG-VYARPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVVNS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648  82 LAQKAGKTTAAAayHWISE-LYNRA-----------PFDAVRDRFTHDDSLAIQHGCFYQADHYPDD-HLFLDAEYLRRQ 148
Cdd:COG1524   103 LSWVEDGFGSNS--LLPVPtIFERAraaglttaavfWPSFEGSGLIDAARPYPYDGRKPLLGNPAADrWIAAAALELLRE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 149 YHPDFLLIHPMNIDDAGHKSGGDSQQYRNSARRADGLLSAYLPAW----LEAGYQVLVTSDHGMNNDR------------ 212
Cdd:COG1524   181 GRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALkargLYEGTLVIVTADHGMVDVPpdidlnrlrlag 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 213 -------------------------------------------------------------------SHGGILDEERAVP 225
Cdd:COG1524   261 llavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkgSHGGLPDEEMRVP 340
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1081357648 226 LFVTGDAFSHEadlpVQQTQLCGTICRLLGLS 257
Cdd:COG1524   341 LLASGPGFRPG----VRNVDVAPTIARLLGLP 368
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
3-255 2.17e-13

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 68.38  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648   3 NPVILVVLDGL--NYRTAHDCMGFMQGLAESGDATLYrLSCELPSLSRPLYECILTGVRPVDSGVVHNQVvrlshndsIF 80
Cdd:cd16018     1 PPLIVISIDGFrwDYLDRAGLTPNLKRLAEEGVRAKY-VKPVFPTLTFPNHYSIVTGLYPESHGIVGNYF--------YD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648  81 SLAQKAGKTTAAAAYHWiselYNRAP--FDAVR--------------DRFTHDDSLAiqhGCFYQADHYPDDHLFLDAEY 144
Cdd:cd16018    72 PKTNEEFSDSDWVWDPW----WIGGEpiWVTAEkaglktasyfwpgsEVAIIGYNPT---PIPLGGYWQPYNDSFPFEER 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 145 L------RRQYHPDFLLIHPMNIDDAGHKSGGDSQQYRNSARRADG----LLSAYLPAWLEAGYQVLVTSDHGMNNDRSH 214
Cdd:cd16018   145 VdtilewLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRrlgyLIEALKERGLLDDTNIIVVSDHGMTDVGTH 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1081357648 215 GGILDEERAVPLFV-TGDAFSHEADL-PVQQTQLCGTICRLLG 255
Cdd:cd16018   225 GYDNELPDMRAIFIaRGPAFKKGKKLgPFRNVDIYPLMCNLLG 267
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
5-257 7.01e-11

GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 61.04  E-value: 7.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648   5 VILVVLDGLnyRT-----AHDCMGFMQGLAESGDATLYRLSCELPSLSRPLYECILTGVRPVDSGVVHNQVVRLSHNDSI 79
Cdd:cd16024     7 LVFMVIDAL--RAdfvfgPDSNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLEEDNW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648  80 fsLAQKAGKTTAAAAY---HWISeLynrapFDAVRDRFTHDDSlaiqhgcFYQADHYPDD-----HLflDAEYLRRQYhp 151
Cdd:cd16024    85 --LSQLKAAGKKIVFYgddTWLK-L-----FPGSFTRSDGTTS-------FFVSDFTEVDnnvtrHL--DSELSRDDW-- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 152 DFLLIHPMNIDDAGHKSGGDSQQYRNSARRADGLLSAYLPAWLEAGYQ----VLVTSDHGMNNDRSHGGILDEERAVPLF 227
Cdd:cd16024   146 DVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQSSNnptlLVVCGDHGMTDAGNHGGSSPGETSVPLL 225
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1081357648 228 VTGDAFSHEADLP---------VQQTQLCGTICRLLGLS 257
Cdd:cd16024   226 FISPKFSSKPSNAdgelsyyetVQQVDLAPTLALLLGLP 264
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
3-229 7.53e-11

GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293743 [Multi-domain]  Cd Length: 292  Bit Score: 61.22  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648   3 NPVILVVLDGLNYRTAHD------CMGFMQGLAE-SGDATLYRLSCELPSLSRPLYECILTGVRPVDSGVVHNQVVRLSH 75
Cdd:cd16019     5 DKVVLIVIDGLRYDLAVNvnkqssFFSFLQKLNEqPNNSFLALSFADPPTVTGPRLKALTTGNPPTFLDLISNFASSEIK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648  76 NDSIFS-LAQKAGKTTAAAAYHWIS----ELYNRAPFDAVRDRFTHDDSLAIQHGCFYQADHYP--DDHlfldaeylrrq 148
Cdd:cd16019    85 EDNIIRqLKKNGKKILFYGDDTWLDlfpeIFTYKFTITSFNIRDMHDVDPIFYNHINDNLDENIyyDNW----------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 149 yhpDFLLIHPMNIDDAGHKSGGD-SQQYRNSARRADGLLSAYLPAwLEAGYQVLVTSDHGMNNDRSHGGILDEERAVPLF 227
Cdd:cd16019   154 ---DFIILHFLGLDHLGHKHNTTsSPELEKKLDQMDNLIRDIYDR-MDNDTLLVVVSDHGMNNDGNHGGSSTEETSSFFF 229

                  ..
gi 1081357648 228 VT 229
Cdd:cd16019   230 FI 231
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
4-254 9.18e-11

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 60.51  E-value: 9.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648   4 PVILVVLDGL------NYRTAHDCMGFMQGLAESGdATLYRLSCELPSLSRPLYECILTGVRPVDSGVVHNQVVRLSHND 77
Cdd:cd00016     2 HVVLIVLDGLgaddlgKAGNPAPTTPNLKRLASEG-ATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648  78 SIFSLAqkagkttaaaaYHWIS--ELYNRApfdavrdrfthddslAIQHGCFYqadhypddhlFLDAEYLRRQYHPDFLL 155
Cdd:cd00016    81 RAAGKD-----------EDGPTipELLKQA---------------GYRTGVIG----------LLKAIDETSKEKPFVLF 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 156 IHPMNIDDAGHKSGGDSQQYRNSARRAD----GLLSAYLPAWLEAGYQVLVTSDHGMnNDRSHGGI----------LDEE 221
Cdd:cd00016   125 LHFDGPDGPGHAYGPNTPEYYDAVEEIDerigKVLDALKKAGDADDTVIIVTADHGG-IDKGHGGDpkadgkadksHTGM 203
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1081357648 222 RaVPLFVTGD--AFSHEADLPVQQTQLCGTICRLL 254
Cdd:cd00016   204 R-VPFIAYGPgvKKGGVKHELISQYDIAPTLADLL 237
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
5-208 1.06e-10

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 61.28  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648   5 VILVVLDGL--NYRTAHDCMGFMQGLAESGDATLYrLSCELPSLSRPLYECILTGVRPVDSGVVHNQVV-RLSHNDSIFS 81
Cdd:pfam01663   1 LLVISLDGFraDYLDRFELTPNLAALAKEGVSAPN-LTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYdPKTGEYLVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648  82 LAQkagkttaaaayHWISELYNRAP--FDAVRDRFT-------------HDDSLAIQHGC---FYQADHYPDDH------ 137
Cdd:pfam01663  80 ISD-----------PEDPRWWQGEPiwDTAAKAGVRaaalfwpgsevdySTYYGTPPRYLkddYNNSVPFEDRVdtavlq 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081357648 138 -LFLDAEYLRRQYHPDFLLIHPMNIDDAGHKSGGDSQQYRNSARRADGLLsAYLPAWLE-----AGYQVLVTSDHGM 208
Cdd:pfam01663 149 tWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAI-GDLLEALDerglfEDTNVIVVSDHGM 224
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
153-256 9.71e-08

GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293744  Cd Length: 294  Bit Score: 52.21  E-value: 9.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 153 FLLIHPMNIDDAGHKSGGDSQQYRNSARRAD-------GLLSAYLP----AWLeagyqvlVTSDHGMNNDRSHGGILDEE 221
Cdd:cd16020   159 VFFLHLLGLDTNGHAHKPYSKEYLENIRYVDkgiektyPLIEEYFNdgrtAYI-------FTSDHGMTDWGSHGDGSPDE 231
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1081357648 222 RAVPLFVTGDAFSHEADLP-----------------VQQTQLCGTICRLLGL 256
Cdd:cd16020   232 TETPFIAWGAGIKHPTPGRgpsfsanwgglrlprhdLDQADLAPLMSALLGL 283
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
131-256 1.50e-04

GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293747  Cd Length: 289  Bit Score: 42.16  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081357648 131 DHYPDDHLFldaEYLRRQYHPDFLLIHPMNIDDAGHKSGGDSQQYRNSARRADGLLSAYLpawlEAGYQ---VLVTSDHG 207
Cdd:cd16023   143 DNGVLKHLF---PELQSEDDWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDII----ERLDDdtlLLVFGDHG 215
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081357648 208 MNNDRSHGGILDEERAVPLFV--------------TGDAFSHEADLPVQQTQLCGTICRLLGL 256
Cdd:cd16023   216 MTETGDHGGDSDEEVDAALFAyskrpfnnsdepieSNGPGDPSKVRSVPQIDLVPTLSLLLGL 278
 
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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