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Conserved domains on  [gi|1965571535|ref|XP_039074539|]
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GPI ethanolamine phosphate transferase 3 isoform X3 [Hyaena hyaena]

Protein Classification

GPI ethanolamine phosphate transferase 3( domain architecture ID 10887995)

GPI (glycosylphosphatidylinositol) ethanolamine phosphate transferase 3 catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of the GPI-anchor

EC:  2.-.-.-
Gene Ontology:  GO:0006506|GO:0016772

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 ...
 82-361 5.56e-175

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: 514.03  E-value: 5.56e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   82 SRFSRVVLVLIDALRFDFAQPQRSHGPGEPpvSLPFLGKLDSLQRILEIQPHHARLYQSKADPPTTTMQRLKALTTGSLP 161
Cdd:cd16023      2 PRFDKVVLLLIDALRYDFVLPDDENPPSEN--SLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  162 TFIDAGSNFASYAIVEDNLIKQFASAGRRVIFMGDDTWKDLFPGAFSQAFFFPSFNVRDLHTVDNGILEHLYPTMDSN-E 240
Cdd:cd16023     80 TFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEdD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  241 WDMLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVIGDHGMTMTGDHGGDSELEISAALFLYSP 320
Cdd:cd16023    160 WDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSK 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1965571535  321 MALFPS---------APPQEPEIVPQINLVPTLALLLGLPIPFGNIGEVM 361
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 ...
 82-361 5.56e-175

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: 514.03  E-value: 5.56e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   82 SRFSRVVLVLIDALRFDFAQPQRSHGPGEPpvSLPFLGKLDSLQRILEIQPHHARLYQSKADPPTTTMQRLKALTTGSLP 161
Cdd:cd16023      2 PRFDKVVLLLIDALRYDFVLPDDENPPSEN--SLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  162 TFIDAGSNFASYAIVEDNLIKQFASAGRRVIFMGDDTWKDLFPGAFSQAFFFPSFNVRDLHTVDNGILEHLYPTMDSN-E 240
Cdd:cd16023     80 TFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEdD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  241 WDMLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVIGDHGMTMTGDHGGDSELEISAALFLYSP 320
Cdd:cd16023    160 WDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSK 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1965571535  321 MALFPS---------APPQEPEIVPQINLVPTLALLLGLPIPFGNIGEVM 361
Cdd:cd16023    240 RPFNNSdepiesngpGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 86-298 1.30e-13

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 73.63  E-value: 1.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   86 RVVLVLIDALRFDFAQPQRshgpgeppvsLPFLgkldslQRILEiqpHHARLYQSKADPPTTTMQRLKALTTGSLPtfid 165
Cdd:COG1524     25 KVVLILVDGLRADLLERAH----------APNL------AALAA---RGVYARPLTSVFPSTTAPAHTTLLTGLYP---- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  166 AGSNFASYAIVEDNLIKQFASAGRRVIFMGDDTW---KDLFPGAFSQ-----AFFFPSFNVRDL------HTVDNGILEH 231
Cdd:COG1524     82 GEHGIVGNGWYDPELGRVVNSLSWVEDGFGSNSLlpvPTIFERARAAglttaAVFWPSFEGSGLidaarpYPYDGRKPLL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  232 LYPTMDS---NEW---------DMLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTLLVVIGD 294
Cdd:COG1524    162 GNPAADRwiaAAAlellregrpDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKarglyEGTLVIVTAD 241


                   ....
gi 1965571535  295 HGMT 298
Cdd:COG1524    242 HGMV 245
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 87-298 7.22e-13

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: 71.30  E-value: 7.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   87 VVLVLIDALRFDfaqpqrshgpgeppvslpflgkldsLQRILEIQPHHARLYQ--SKADP-----PTTTMQRLKALTTGS 159
Cdd:pfam01663    1 LLVISLDGFRAD-------------------------YLDRFELTPNLAALAKegVSAPNltpvfPTLTFPNHYTLVTGL 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  160 LP--------TFIDAGSNFASYAIVEDNLIKQF----------ASAGRRVI---FMGDD----TWKDLFPGAFSQAFFFP 214
Cdd:pfam01663   56 YPgshgivgnTFYDPKTGEYLVFVISDPEDPRWwqgepiwdtaAKAGVRAAalfWPGSEvdysTYYGTPPRYLKDDYNNS 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  215 -SFNVRDLHTVDNGILEHLYPTMDSNEWDMLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTL 288
Cdd:pfam01663  136 vPFEDRVDTAVLQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDerglfEDTN 215

                          250
                   ....*....|
gi 1965571535  289 LVVIGDHGMT 298
Cdd:pfam01663  216 VIVVSDHGMT 225
 
Name Accession Description Interval E-value
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 82-361 5.56e-175

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: 514.03  E-value: 5.56e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   82 SRFSRVVLVLIDALRFDFAQPQRSHGPGEPpvSLPFLGKLDSLQRILEIQPHHARLYQSKADPPTTTMQRLKALTTGSLP 161
Cdd:cd16023      2 PRFDKVVLLLIDALRYDFVLPDDENPPSEN--SLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  162 TFIDAGSNFASYAIVEDNLIKQFASAGRRVIFMGDDTWKDLFPGAFSQAFFFPSFNVRDLHTVDNGILEHLYPTMDSN-E 240
Cdd:cd16023     80 TFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEdD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  241 WDMLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVIGDHGMTMTGDHGGDSELEISAALFLYSP 320
Cdd:cd16023    160 WDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSK 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1965571535  321 MALFPS---------APPQEPEIVPQINLVPTLALLLGLPIPFGNIGEVM 361
Cdd:cd16023    240 RPFNNSdepiesngpGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 82-361 5.19e-114

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: 355.13  E-value: 5.19e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   82 SRFSRVVLVLIDALRFDFAQPQRSHGPgeppvslpflgKLDSLQRILEiQPHHARLYQSKADPPTTTMQRLKALTTGSLP 161
Cdd:cd16019      2 TKYDKVVLIVIDGLRYDLAVNVNKQSS-----------FFSFLQKLNE-QPNNSFLALSFADPPTVTGPRLKALTTGNPP 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  162 TFIDAGSNFASYAIVEDNLIKQFASAGRRVIFMGDDTWKDLFPGAFSQAFFFPSFNVRDLHTVDNGILEHLYPTMD---- 237
Cdd:cd16019     70 TFLDLISNFASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHINDNLDeniy 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  238 SNEWDMLIAHFLGVDHCGHKHG-PHHPEMAKKLSQMDQVIQGLVERLENDTLLVVIGDHGMTMTGDHGGDSELEISAALF 316
Cdd:cd16019    150 YDNWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDNDTLLVVVSDHGMNNDGNHGGSSTEETSSFFF 229

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1965571535  317 LYSPMALFPSAP------------------PQEPEIVPQINLVPTLALLLGLPIPFGNIGEVM 361
Cdd:cd16019    230 FISKKGFFKKRPidqiekikqnneqqkidpSEYIRIIYQIDILPTICYLLGIPIPFNNIGIII 292
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 82-358 1.61e-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 [Multi-domain]  Cd Length: 274  Bit Score: 315.66  E-value: 1.61e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   82 SRFSRVVLVLIDALRFDFAQpqrshgpgEPPVSLPFLGKLdslqrileIQPHHARLYQSKADPPTTTMQRLKALTTGSLP 161
Cdd:cd16024      2 PAFDKLVFMVIDALRADFVF--------GPDSNMPFTQSL--------INSGSALAFTAKAQPPTVTMPRIKALTTGSIP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  162 TFIDAGSNFASYAIVEDNLIKQFASAGRRVIFMGDDTWKDLFPGAFSQAFFFPSFNVRDLHTVDNGILEHLYPTMDSNEW 241
Cdd:cd16024     66 SFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDW 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  242 DMLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTLLVVIGDHGMTMTGDHGGDSELEISAALF 316
Cdd:cd16024    146 DVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEeqssnNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLL 225

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1965571535  317 LYSP----MALFPSAPPQEPEIVPQINLVPTLALLLGLPIPFGNIG 358
Cdd:cd16024    226 FISPkfssKPSNADGELSYYETVQQVDLAPTLALLLGLPIPKNSVG 271
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 86-348 5.32e-34

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: 131.00  E-value: 5.32e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   86 RVVLVLIDALRFDFAQPQRSHGPGEPpvslpflgkldslqRILEIQPHHARLYQSKADPPTTTMQRLKALTTGSLPTFID 165
Cdd:cd00016      2 HVVLIVLDGLGADDLGKAGNPAPTTP--------------NLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHG 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  166 AGSNFASY----------AIVEDNLIKQFASAGRRVIFMGddtwkdlfpgafsqafffpsfnvrdlhtvdngILEHLYPT 235
Cdd:cd00016     68 YTGNGSADpelpsraagkDEDGPTIPELLKQAGYRTGVIG--------------------------------LLKAIDET 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  236 MDSnEWDMLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERL-----ENDTLLVVIGDHGMTMTGDHG------ 304
Cdd:cd00016    116 SKE-KPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALkkagdADDTVIIVTADHGGIDKGHGGdpkadg 194

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1965571535  305 --GDSELEISAALFLYSPMAlfpSAPPQEPEIVPQINLVPTLALLL 348
Cdd:cd00016    195 kaDKSHTGMRVPFIAYGPGV---KKGGVKHELISQYDIAPTLADLL 237
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 242-349 8.03e-21

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: 93.42  E-value: 8.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  242 DMLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTLLVVIGDHGMTMTGDHGGDSELEISAALF 316
Cdd:cd16018    158 DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKergllDDTNIIVVSDHGMTDVGTHGYDNELPDMRAIF 237

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1965571535  317 LYSPMALFpsappqEPEIVPQINLV---PTLALLLG 349
Cdd:cd16018    238 IARGPAFK------KGKKLGPFRNVdiyPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 86-298 1.30e-13

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 73.63  E-value: 1.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   86 RVVLVLIDALRFDFAQPQRshgpgeppvsLPFLgkldslQRILEiqpHHARLYQSKADPPTTTMQRLKALTTGSLPtfid 165
Cdd:COG1524     25 KVVLILVDGLRADLLERAH----------APNL------AALAA---RGVYARPLTSVFPSTTAPAHTTLLTGLYP---- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  166 AGSNFASYAIVEDNLIKQFASAGRRVIFMGDDTW---KDLFPGAFSQ-----AFFFPSFNVRDL------HTVDNGILEH 231
Cdd:COG1524     82 GEHGIVGNGWYDPELGRVVNSLSWVEDGFGSNSLlpvPTIFERARAAglttaAVFWPSFEGSGLidaarpYPYDGRKPLL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  232 LYPTMDS---NEW---------DMLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTLLVVIGD 294
Cdd:COG1524    162 GNPAADRwiaAAAlellregrpDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKarglyEGTLVIVTAD 241


                   ....
gi 1965571535  295 HGMT 298
Cdd:COG1524    242 HGMV 245
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 247-360 2.27e-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: 71.85  E-value: 2.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  247 HFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE---ND--TLLVVIGDHGMTMTGDHGGDSELEISAALFLY--- 318
Cdd:cd16020    163 HLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEeyfNDgrTAYIFTSDHGMTDWGSHGDGSPDETETPFIAWgag 242

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1965571535  319 --SPMALFPSAPPQEPE-------IVPQINLVPTLALLLGLPIPFGNIGEV 360
Cdd:cd16020    243 ikHPTPGRGPSFSANWGglrlprhDLDQADLAPLMSALLGLPPPVNSVGIL 293
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 87-298 7.22e-13

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: 71.30  E-value: 7.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   87 VVLVLIDALRFDfaqpqrshgpgeppvslpflgkldsLQRILEIQPHHARLYQ--SKADP-----PTTTMQRLKALTTGS 159
Cdd:pfam01663    1 LLVISLDGFRAD-------------------------YLDRFELTPNLAALAKegVSAPNltpvfPTLTFPNHYTLVTGL 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  160 LP--------TFIDAGSNFASYAIVEDNLIKQF----------ASAGRRVI---FMGDD----TWKDLFPGAFSQAFFFP 214
Cdd:pfam01663   56 YPgshgivgnTFYDPKTGEYLVFVISDPEDPRWwqgepiwdtaAKAGVRAAalfWPGSEvdysTYYGTPPRYLKDDYNNS 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  215 -SFNVRDLHTVDNGILEHLYPTMDSNEWDMLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTL 288
Cdd:pfam01663  136 vPFEDRVDTAVLQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDerglfEDTN 215

                          250
                   ....*....|
gi 1965571535  289 LVVIGDHGMT 298
Cdd:pfam01663  216 VIVVSDHGMT 225
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 86-353 2.20e-06

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 [Multi-domain]  Cd Length: 271  Bit Score: 50.62  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   86 RVVLVLIDALRFDFAQPQrshgpGEPPVSLPFLgklDSL-QRILEIQPHHArlyqskADPPTttMQRLKALTTGSLPtfI 164
Cdd:cd16148      2 NVILIVIDSLRADHLGCY-----GYDRVTTPNL---DRLaAEGVVFDNHYS------GSNPT--LPSRFSLFTGLYP--F 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  165 DAGSNFASYAIVEDNLIKQFASAGRR-VIFmGDDTWKDLFPGaFSQAFFFPSFNVRDLHTVDNGILEHLYPTMDSnewdm 243
Cdd:cd16148     64 YHGVWGGPLEPDDPTLAEILRKAGYYtAAV-SSNPHLFGGPG-FDRGFDTFEDFRGQEGDPGEEGDERAERVTDR----- 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  244 lIAHFLGvDHCGHK------H--GPHHPEM-AKKLSQMDQVIQGLVERLEN-----DTLLVVIGDHGMTMtGDHGG---- 305
Cdd:cd16148    137 -ALEWLD-RNADDDpfflflHyfDPHEPYLyDAEVRYVDEQIGRLLDKLKElglleDTLVIVTSDHGEEF-GEHGLywgh 213

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1965571535  306 -----DSELEIsaALFLYspmalFPSAPPQE--PEIVPQINLVPTLALLLGLPIP 353
Cdd:cd16148    214 gsnlyDEQLHV--PLIIR-----WPGKEPGKrvDALVSHIDIAPTLLDLLGVEPP 261
Sulfatase pfam00884
Sulfatase;
87-350 4.48e-06

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 49.73  E-value: 4.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535   87 VVLVLIDALRFDFAQPQrshgpGEPPVSLPFLGKLdsLQRILEIQPHHArlyqskADPPTTTMqrLKALTTGSLPTFIDA 166
Cdd:pfam00884    3 VVLVLGESLRAPDLGLY-----GYPRPTTPFLDRL--AEEGLLFSNFYS------GGTLTAPS--RFALLTGLPPHNFGS 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  167 GSNFASY-AIVEDNLIKQFASAGRRVIFMG--DDTWKDLFPGA---FSQAFFFPSFNVRDLHTVDNGILEHLYPTMD--- 237
Cdd:pfam00884   68 YVSTPVGlPRTEPSLPDLLKRAGYNTGAIGkwHLGWYNNQSPCnlgFDKFFGRNTGSDLYADPPDVPYNCSGGGVSDeal 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  238 ---SNEWD-------MLIAHFLGVdHCGHKHGPHHPEMAKK------------------LSQMDQVIQGLVERLE----- 284
Cdd:pfam00884  148 ldeALEFLdnndkpfFLVLHTLGS-HGPPYYPDRYPEKYATfkpsscseeqllnsydntLLYTDDAIGRVLDKLEengll 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965571535  285 NDTLLVVIGDHG-MTMTGDHGGDSELEISAA-------LFLYSPmalfPSAPPQE--PEIVPQINLVPTLALLLGL 350
Cdd:pfam00884  227 DNTLVVYTSDHGeSLGEGGGYLHGGKYDNAPeggyrvpLLIWSP----GGKAKGQksEALVSHVDLFPTILDLAGI 298
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 272-353 1.17e-05

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 49.27  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  272 MDQVIQGLVERLEN-----DTLLVVIGDHGMTMTGDHGGDSELEISA-ALFLYSPMALfpsAPPQEPEIVPQINLVPTLA 345
Cdd:COG1368    426 ADQALGEFIEKLKKsgwydNTIFVIYGDHGPRSPGKTDYENPLERYRvPLLIYSPGLK---KPKVIDTVGSQIDIAPTLL 502


                   ....*...
gi 1965571535  346 LLLGLPIP 353
Cdd:COG1368    503 DLLGIDYP 510
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 264-349 3.25e-05

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 [Multi-domain]  Cd Length: 283  Bit Score: 46.91  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  264 EMAKKLSQMDQVIQGLVERLEN-----DTLLVVIGDHGMTMTGDHGGDSELEISAA---LFLYSPmalFPSAPPQEPEIV 335
Cdd:cd16015    193 NYLNAIHYTDKALGEFIEKLKKsglyeNTIIVIYGDHLPSLGSDYDETDEDPLDLYrtpLLIYSP---GLKKPKKIDRVG 269

                           90
                   ....*....|....
gi 1965571535  336 PQINLVPTLALLLG 349
Cdd:cd16015    270 SQIDIAPTLLDLLG 283
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 258-353 9.61e-03

sulfatase; 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: 293746 [Multi-domain]  Cd Length: 236  Bit Score: 38.96  E-value: 9.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965571535  258 HGPHHP-EMAKKLSQMD----QVIQGLVER-LENDTLLVVIGDHGMtMTGDHGGdseleISAALFLYS-----PMAL-FP 325
Cdd:cd16022    125 NAPHPPfAYYAMVSAIDdqigRILDALEELgLLDNTLIVFTSDHGD-MLGDHGL-----RGKKGSLYEggirvPFIVrWP 198

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1965571535  326 SAPPQ---EPEIVPQINLVPTLALLLGLPIP 353
Cdd:cd16022    199 GKIPAgqvSDALVSLLDLLPTLLDLAGIEPP 229
 
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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