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Conserved domains on  [gi|23397648|ref|NP_116023.2|]
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GPI ethanolamine phosphate transferase 3 isoform 1 [Homo sapiens]

Protein Classification

GPI_EPT_3 domain-containing protein (domain architecture ID 10887995)

GPI_EPT_3 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
65-344 3.69e-174

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: 515.57  E-value: 3.69e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648   65 SRFSRVVLVLIDALRFDFAQPQHSHVPREPpvSLPFLGKLSSLQRILEIQPHHARLYRSQVDPPTTTMQRLKALTTGSLP 144
Cdd:cd16023    2 PRFDKVVLLLIDALRYDFVLPDDENPPSEN--SLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  145 TFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSG-E 223
Cdd:cd16023   80 TFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEdD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  224 WDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALFLYSP 303
Cdd:cd16023  160 WDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 23397648  304 TAVFPST---------PPEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVM 344
Cdd:cd16023  240 RPFNNSDepiesngpgDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
 
Name Accession Description Interval E-value
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
65-344 3.69e-174

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: 515.57  E-value: 3.69e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648   65 SRFSRVVLVLIDALRFDFAQPQHSHVPREPpvSLPFLGKLSSLQRILEIQPHHARLYRSQVDPPTTTMQRLKALTTGSLP 144
Cdd:cd16023    2 PRFDKVVLLLIDALRYDFVLPDDENPPSEN--SLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  145 TFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSG-E 223
Cdd:cd16023   80 TFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEdD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  224 WDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALFLYSP 303
Cdd:cd16023  160 WDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 23397648  304 TAVFPST---------PPEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVM 344
Cdd:cd16023  240 RPFNNSDepiesngpgDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
Npp1 COG1524
Predicted pyrophosphatase or phosphodiesterase, AlkP superfamily [General function prediction ...
42-299 1.18e-25

Predicted pyrophosphatase or phosphodiesterase, AlkP superfamily [General function prediction only];


Pssm-ID: 224441  Cd Length: 450  Bit Score: 111.50  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648   42 QEPPGPGSLPWGSQgkPGACWMASRFSRVVLVLIDALRFDFAQPQHSHvpreppvsLPFLGKLSSlqRILEIQPHHARLy 121
Cdd:COG1524   15 LDLFFAADVPILSQ--SYQAATPAPKKKLVLISIDGLRADVLDRKAGI--------LPFLSSLAE--NGVHVAELISVF- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  122 rsqvdpPTTTMQRLKALTTGSLPTFIDAGSNFASHAIVEDNLiKQLTSAGRRVVFMGDD--TWKDLFPGAFSKAF----- 194
Cdd:COG1524   82 ------PTTTRPRHTTLITGSYPDEHGIVGNILYDPETGDSV-LQFLLDNPTILFPGDDeaGMDVAAPFESLTVSdklrv 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  195 ----------------FFPSFNVRDLDTVD-NGILEHLYPTMDSGEWDV-----------------LIAHFLGVDHCGHK 240
Cdd:COG1524  155 avdlvwdvpilhylhiGGPDHITMRRFLIDeDDNIKPGYDYISEHFLDSllfldsvllldradpdlLLVYLPNIDAIGHK 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397648  241 HGPHHPEMAKKLSQMDQVIQGLVERLEN-----DTLLVVAGDHGMTTNGDHGG--DSELEVSAALF 299
Cdd:COG1524  235 YGPDSPEYAEAVREVDSLLGELLELLKKrglyeEYLVIITSDHGMSPLGVHGIiyLNELLEEKGIF 300
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
70-287 6.90e-15

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, tumor 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: 307681  Cd Length: 346  Bit Score: 77.09  E-value: 6.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648     70 VVLVLIDALRFDFaqpqhshvpreppvsLPFLGKLSSLQRILEiQPHHARLYRSQVdpPTTTMQRLKALTTGSLPtfida 149
Cdd:pfam01663    1 LLVISLDGFRADY---------------LDRLGLTPNLAALAK-EGVSAPNLTPVF--PTLTFPNHYTLVTGLYP----- 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648    150 gsnfASHAIVEDNLIKQLTsaGRRVVFMGDDTWKDLF----P--------GAFSKAFFFP--SFNVRDL----------- 204
Cdd:pfam01663   58 ----GSHGIVGNTFYDPKT--GEYLVFVISDPEDPRWwqgePiwvtaakaGVRAAALFWPgsEVDYSTYdrgtpprylkd 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648    205 ---------DTVDNGIL-----EHLYPTMDSGEWDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE--- 267
Cdd:pfam01663  132 dynnsvpfeDRVDTAVLptwldLPFADLAQDERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDerg 211
                          250       260
                   ....*....|....*....|..
gi 23397648    268 --NDTLLVVAGDHGMTTNGDHG 287
Cdd:pfam01663  212 lfEDTNVIVVSDHGMTPVSDDK 233
 
Name Accession Description Interval E-value
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
65-344 3.69e-174

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: 515.57  E-value: 3.69e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648   65 SRFSRVVLVLIDALRFDFAQPQHSHVPREPpvSLPFLGKLSSLQRILEIQPHHARLYRSQVDPPTTTMQRLKALTTGSLP 144
Cdd:cd16023    2 PRFDKVVLLLIDALRYDFVLPDDENPPSEN--SLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  145 TFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSG-E 223
Cdd:cd16023   80 TFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEdD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  224 WDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALFLYSP 303
Cdd:cd16023  160 WDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 23397648  304 TAVFPST---------PPEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVM 344
Cdd:cd16023  240 RPFNNSDepiesngpgDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
65-344 2.98e-113

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  Cd Length: 292  Bit Score: 356.29  E-value: 2.98e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648   65 SRFSRVVLVLIDALRFDFAQPQHSHVPreppvslpflgKLSSLQRILEiQPHHARLYRSQVDPPTTTMQRLKALTTGSLP 144
Cdd:cd16019    2 TKYDKVVLIVIDGLRYDLAVNVNKQSS-----------FFSFLQKLNE-QPNNSFLALSFADPPTVTGPRLKALTTGNPP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  145 TFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSGE- 223
Cdd:cd16019   70 TFLDLISNFASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHINDNLDENIy 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  224 ---WDVLIAHFLGVDHCGHKHG-PHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALF 299
Cdd:cd16019  150 ydnWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDNDTLLVVVSDHGMNNDGNHGGSSTEETSSFFF 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397648  300 LYSPTAVFPSTP------------------PEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVM 344
Cdd:cd16019  230 FISKKGFFKKRPidqiekikqnneqqkidpSEYIRIIYQIDILPTICYLLGIPIPFNNIGIII 292
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
65-341 8.46e-99

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  Cd Length: 274  Bit Score: 316.43  E-value: 8.46e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648   65 SRFSRVVLVLIDALRFDFAQPQHSHvpreppvsLPFLGKLsslqrileIQPHHARLYRSQVDPPTTTMQRLKALTTGSLP 144
Cdd:cd16024    2 PAFDKLVFMVIDALRADFVFGPDSN--------MPFTQSL--------INSGSALAFTAKAQPPTVTMPRIKALTTGSIP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  145 TFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSGEW 224
Cdd:cd16024   66 SFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDW 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  225 DVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTLLVVAGDHGMTTNGDHGGDSELEVSAALF 299
Cdd:cd16024  146 DVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEeqssnNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLL 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 23397648  300 LYSP----TAVFPSTPPEEPEVIPQVSLVPTLALLLGLPIPFGNIG 341
Cdd:cd16024  226 FISPkfssKPSNADGELSYYETVQQVDLAPTLALLLGLPIPKNSVG 271
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
69-331 1.81e-38

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  Cd Length: 237  Bit Score: 146.03  E-value: 1.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648   69 RVVLVLIDALRFDFAQPQHSHVPREPpvslpflgklsslqRILEIQPHHARLYRSQVDPPTTTMQRLKALTTGSLPTFID 148
Cdd:cd00016    2 HVVLIVLDGLGADDLGKAGNPAPTTP--------------NLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  149 AGSN----------FASHAIVEDNLIKQLTSAGRRVVFMGddtwkdlfpgafskafffpsfnvrdldtvdngILEHLYPT 218
Cdd:cd00016   68 YTGNgsadpelpsrAAGKDEDGPTIPELLKQAGYRTGVIG--------------------------------LLKAIDET 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  219 MDSgEWDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERL-----ENDTLLVVAGDHGMTTNGDHG------ 287
Cdd:cd00016  116 SKE-KPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALkkagdADDTVIIVTADHGGIDKGHGGdpkadg 194
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 23397648  288 --GDSELEVSAALFLYSPTAvfpSTPPEEPEVIPQVSLVPTLALLL 331
Cdd:cd00016  195 kaDKSHTGMRVPFIAYGPGV---KKGGVKHELISQYDIAPTLADLL 237
Npp1 COG1524
Predicted pyrophosphatase or phosphodiesterase, AlkP superfamily [General function prediction ...
42-299 1.18e-25

Predicted pyrophosphatase or phosphodiesterase, AlkP superfamily [General function prediction only];


Pssm-ID: 224441  Cd Length: 450  Bit Score: 111.50  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648   42 QEPPGPGSLPWGSQgkPGACWMASRFSRVVLVLIDALRFDFAQPQHSHvpreppvsLPFLGKLSSlqRILEIQPHHARLy 121
Cdd:COG1524   15 LDLFFAADVPILSQ--SYQAATPAPKKKLVLISIDGLRADVLDRKAGI--------LPFLSSLAE--NGVHVAELISVF- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  122 rsqvdpPTTTMQRLKALTTGSLPTFIDAGSNFASHAIVEDNLiKQLTSAGRRVVFMGDD--TWKDLFPGAFSKAF----- 194
Cdd:COG1524   82 ------PTTTRPRHTTLITGSYPDEHGIVGNILYDPETGDSV-LQFLLDNPTILFPGDDeaGMDVAAPFESLTVSdklrv 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  195 ----------------FFPSFNVRDLDTVD-NGILEHLYPTMDSGEWDV-----------------LIAHFLGVDHCGHK 240
Cdd:COG1524  155 avdlvwdvpilhylhiGGPDHITMRRFLIDeDDNIKPGYDYISEHFLDSllfldsvllldradpdlLLVYLPNIDAIGHK 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397648  241 HGPHHPEMAKKLSQMDQVIQGLVERLEN-----DTLLVVAGDHGMTTNGDHGG--DSELEVSAALF 299
Cdd:COG1524  235 YGPDSPEYAEAVREVDSLLGELLELLKKrglyeEYLVIITSDHGMSPLGVHGIiyLNELLEEKGIF 300
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
225-332 4.87e-19

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  Cd Length: 267  Bit Score: 89.18  E-value: 4.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  225 DVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTLLVVAGDHGMTTNGDHGGDSELEVSAALF 299
Cdd:cd16018  158 DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKergllDDTNIIVVSDHGMTDVGTHGYDNELPDMRAIF 237
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 23397648  300 LYSPTAVFpstppeEPEVIPQVSLV---PTLALLLG 332
Cdd:cd16018  238 IARGPAFK------KGKKLGPFRNVdiyPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
70-287 6.90e-15

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, tumor 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: 307681  Cd Length: 346  Bit Score: 77.09  E-value: 6.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648     70 VVLVLIDALRFDFaqpqhshvpreppvsLPFLGKLSSLQRILEiQPHHARLYRSQVdpPTTTMQRLKALTTGSLPtfida 149
Cdd:pfam01663    1 LLVISLDGFRADY---------------LDRLGLTPNLAALAK-EGVSAPNLTPVF--PTLTFPNHYTLVTGLYP----- 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648    150 gsnfASHAIVEDNLIKQLTsaGRRVVFMGDDTWKDLF----P--------GAFSKAFFFP--SFNVRDL----------- 204
Cdd:pfam01663   58 ----GSHGIVGNTFYDPKT--GEYLVFVISDPEDPRWwqgePiwvtaakaGVRAAALFWPgsEVDYSTYdrgtpprylkd 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648    205 ---------DTVDNGIL-----EHLYPTMDSGEWDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE--- 267
Cdd:pfam01663  132 dynnsvpfeDRVDTAVLptwldLPFADLAQDERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDerg 211
                          250       260
                   ....*....|....*....|..
gi 23397648    268 --NDTLLVVAGDHGMTTNGDHG 287
Cdd:pfam01663  212 lfEDTNVIVVSDHGMTPVSDDK 233
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
226-343 2.60e-13

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: 71.47  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  226 VLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE---ND--TLLVVAGDHGMTTNGDHGGDSELEVSAALFL 300
Cdd:cd16020  159 VFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEeyfNDgrTAYIFTSDHGMTDWGSHGDGSPDETETPFIA 238
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 23397648  301 Y-----SPTAVFPSTPPEEPE-------VIPQVSLVPTLALLLGLPIPFGNIGEV 343
Cdd:cd16020  239 WgagikHPTPGRGPSFSANWGglrlprhDLDQADLAPLMSALLGLPPPVNSVGIL 293
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
69-336 2.92e-05

uncharacterized sulfatase subfamily; 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. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293767  Cd Length: 271  Bit Score: 46.77  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648   69 RVVLVLIDALRFDFAQPQHSHvprepPVSLPFLGKLSSlqrileiqphharlyRSQV-------DPPTttMQRLKALTTG 141
Cdd:cd16148    2 NVILIVIDSLRADHLGCYGYD-----RVTTPNLDRLAA---------------EGVVfdnhysgSNPT--LPSRFSLFTG 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  142 SLPtfIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGaFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDS 221
Cdd:cd16148   60 LYP--FYHGVWGGPLEPDDPTLAEILRKAGYYTAAVSSNPHLFGGPG-FDRGFDTFEDFRGQEGDPGEEGDERAERVTDR 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  222 GewdvliAHFLGvDHCGHK------H--GPHHPEM-AKKLSQMDQVIQGLVERLEN-----DTLLVVAGDHGMtTNGDHG 287
Cdd:cd16148  137 A------LEWLD-RNADDDpfflflHyfDPHEPYLyDAEVRYVDEQIGRLLDKLKElglleDTLVIVTSDHGE-EFGEHG 208
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397648  288 G---------DSELEVsaALFLYSPTAvfpstppEEPEVIP-QVS---LVPTLALLLGLPIP 336
Cdd:cd16148  209 LywghgsnlyDEQLHV--PLIIRWPGK-------EPGKRVDaLVShidIAPTLLDLLGVEPP 261
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
247-332 2.07e-04

Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.


Pssm-ID: 293739  Cd Length: 283  Bit Score: 44.21  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648  247 EMAKKLSQMDQVIQGLVERLEN-----DTLLVVAGDHGMTTNGDHGGDSELEVSAA---LFLYSPtavFPSTPPEEPEVI 318
Cdd:cd16015  193 NYLNAIHYTDKALGEFIEKLKKsglyeNTIIVIYGDHLPSLGSDYDETDEDPLDLYrtpLLIYSP---GLKKPKKIDRVG 269
                         90
                 ....*....|....
gi 23397648  319 PQVSLVPTLALLLG 332
Cdd:cd16015  270 SQIDIAPTLLDLLG 283
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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