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Conserved domains on  [gi|71981013|ref|NP_491750|]
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GPI ethanolamine phosphate transferase 3 [Caenorhabditis elegans]

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 ...
52-319 1.77e-139

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: 415.81  E-value: 1.77e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013  52 KQQYQRVILILVDALRYDFLIPIDENTKkSKEEWYYRGQMKNIEKLVKS--GNVSIGTLLADPPTTTLQRLKALTTGTLP 129
Cdd:cd16023   1 PPRFDKVVLLLIDALRYDFVLPDDENPP-SENSLYYHNKLPVLEELLKSqpNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 130 TFIDAGDNFSPDAvISEDSFVYQAAQLGKNVTLLGDDTWLSLFPNQFSKTAAYDSFDINDLNTVDDKIAPILQDEMLNSN 209
Cdd:cd16023  80 TFIDAGSNFASSA-IVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSED 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 210 S-SIIIAHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQTIETMKSD-------DHGMTSTGDHGGESENEIRAGILVHS 281
Cdd:cd16023 159 DwDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDtlllvfgDHGMTETGDHGGDSDEEVDAALFAYS 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 71981013 282 KKHQIILPE-------------RPIHQIDIVPTISLLMGLPIPFSNLGTVI 319
Cdd:cd16023 239 KRPFNNSDEpiesngpgdpskvRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
 
Name Accession Description Interval E-value
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
52-319 1.77e-139

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: 415.81  E-value: 1.77e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013  52 KQQYQRVILILVDALRYDFLIPIDENTKkSKEEWYYRGQMKNIEKLVKS--GNVSIGTLLADPPTTTLQRLKALTTGTLP 129
Cdd:cd16023   1 PPRFDKVVLLLIDALRYDFVLPDDENPP-SENSLYYHNKLPVLEELLKSqpNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 130 TFIDAGDNFSPDAvISEDSFVYQAAQLGKNVTLLGDDTWLSLFPNQFSKTAAYDSFDINDLNTVDDKIAPILQDEMLNSN 209
Cdd:cd16023  80 TFIDAGSNFASSA-IVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSED 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 210 S-SIIIAHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQTIETMKSD-------DHGMTSTGDHGGESENEIRAGILVHS 281
Cdd:cd16023 159 DwDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDtlllvfgDHGMTETGDHGGDSDEEVDAALFAYS 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 71981013 282 KKHQIILPE-------------RPIHQIDIVPTISLLMGLPIPFSNLGTVI 319
Cdd:cd16023 239 KRPFNNSDEpiesngpgdpskvRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
53-265 1.85e-13

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 72.86  E-value: 1.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013  53 QQYQRVILILVDALRYDFLipidentkkskeewyYRGQMKNIEKLVKSGnVSIGTLLADPPTTTlqrlkA-----LTTGT 127
Cdd:COG1524  21 PPAKKVVLILVDGLRADLL---------------ERAHAPNLAALAARG-VYARPLTSVFPSTT-----ApahttLLTGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 128 LP--------TFIDAGDnfspDAVISEDSFVYQAAQLGKNVTLlgdDTWLSLFPNQFSKTAAYDSFDINDLNTV------ 193
Cdd:COG1524  80 YPgehgivgnGWYDPEL----GRVVNSLSWVEDGFGSNSLLPV---PTIFERARAAGLTTAAVFWPSFEGSGLIdaarpy 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 194 --------------DDKIAPILQDEMLNSNSSIIIAHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQTIETMKSD---- 255
Cdd:COG1524 153 pydgrkpllgnpaaDRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARglye 232
                       250
                ....*....|....*...
gi 71981013 256 --------DHGMTSTGDH 265
Cdd:COG1524 233 gtlvivtaDHGMVDVPPD 250
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
58-273 4.36e-12

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: 68.60  E-value: 4.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013    58 VILILVDALRYDFLipidentkkskeewYYRGQMKNIEKLVKSGnVSIGTLLADPPTTTLQRLKALTTGTLP-------- 129
Cdd:pfam01663   1 LLVISLDGFRADYL--------------DRFELTPNLAALAKEG-VSAPNLTPVFPTLTFPNHYTLVTGLYPgshgivgn 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013   130 TFIDAGDNfspdaviseDSFVYQAAQLGKNVTLLGDDTWLSL------------------FPNQFSKTAAYDSFDINDLN 191
Cdd:pfam01663  66 TFYDPKTG---------EYLVFVISDPEDPRWWQGEPIWDTAakagvraaalfwpgsevdYSTYYGTPPRYLKDDYNNSV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013   192 TVDDKIAPILQDEMLNSNS--------SIIIAHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQTIETMKSD-------- 255
Cdd:pfam01663 137 PFEDRVDTAVLQTWLDLPFadvaaerpDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERglfedtnv 216
                         250       260
                  ....*....|....*....|..
gi 71981013   256 ----DHGMTSTGDHGGESENEI 273
Cdd:pfam01663 217 ivvsDHGMTPVSDDKVIFLNDY 238
 
Name Accession Description Interval E-value
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
52-319 1.77e-139

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: 415.81  E-value: 1.77e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013  52 KQQYQRVILILVDALRYDFLIPIDENTKkSKEEWYYRGQMKNIEKLVKS--GNVSIGTLLADPPTTTLQRLKALTTGTLP 129
Cdd:cd16023   1 PPRFDKVVLLLIDALRYDFVLPDDENPP-SENSLYYHNKLPVLEELLKSqpNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 130 TFIDAGDNFSPDAvISEDSFVYQAAQLGKNVTLLGDDTWLSLFPNQFSKTAAYDSFDINDLNTVDDKIAPILQDEMLNSN 209
Cdd:cd16023  80 TFIDAGSNFASSA-IVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSED 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 210 S-SIIIAHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQTIETMKSD-------DHGMTSTGDHGGESENEIRAGILVHS 281
Cdd:cd16023 159 DwDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDtlllvfgDHGMTETGDHGGDSDEEVDAALFAYS 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 71981013 282 KKHQIILPE-------------RPIHQIDIVPTISLLMGLPIPFSNLGTVI 319
Cdd:cd16023 239 KRPFNNSDEpiesngpgdpskvRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
52-319 1.04e-74

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: 245.55  E-value: 1.04e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013  52 KQQYQRVILILVDALRYDFLIPIDENtkkskeewyyrgqMKNIEKLVKSGNVSIGTLLADPPTTTLQRLKALTTGTLPTF 131
Cdd:cd16024   1 KPAFDKLVFMVIDALRADFVFGPDSN-------------MPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSF 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 132 IDAGDNFSpDAVISEDSFVYQAAQLGKNVTLLGDDTWLSLFPNQFSKTAAYDSFDINDLNTVDDKIAPILQDEMLNSNSS 211
Cdd:cd16024  68 LDVVLNFA-SSLLEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 212 IIIAHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQTIETMKSD------------DHGMTSTGDHGGESENEIRAGILV 279
Cdd:cd16024 147 VLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQssnnptllvvcgDHGMTDAGNHGGSSPGETSVPLLF 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 71981013 280 HSKKHQI--------ILPERPIHQIDIVPTISLLMGLPIPFSNLGTVI 319
Cdd:cd16024 227 ISPKFSSkpsnadgeLSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
52-319 6.05e-69

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: 230.71  E-value: 6.05e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013  52 KQQYQRVILILVDALRYDFLIPIDENTKKskeewyyrgqMKNIEKLVKSGNVSIGTL-LADPPTTTLQRLKALTTGTLPT 130
Cdd:cd16019   1 PTKYDKVVLIVIDGLRYDLAVNVNKQSSF----------FSFLQKLNEQPNNSFLALsFADPPTVTGPRLKALTTGNPPT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 131 FIDAGDNFSPDAvISEDSFVYQAAQLGKNVTLLGDDTWLSLFPNQFSKTAAYDSFDINDLNTVD----DKIAPILQDEML 206
Cdd:cd16019  71 FLDLISNFASSE-IKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDpifyNHINDNLDENIY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 207 NSNSSIIIAHFLGVDHCGHKFG-PSHPVMADTLRKMDRIIGQTIETMKSD-------DHGMTSTGDHGGESENEIRAGIL 278
Cdd:cd16019 150 YDNWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDNDtllvvvsDHGMNNDGNHGGSSTEETSSFFF 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71981013 279 VHSKKHQII----------------------LPERPIHQIDIVPTISLLMGLPIPFSNLGTVI 319
Cdd:cd16019 230 FISKKGFFKkrpidqiekikqnneqqkidpsEYIRIIYQIDILPTICYLLGIPIPFNNIGIII 292
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
57-306 2.26e-19

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: 88.25  E-value: 2.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013  57 RVILILVDALRYDFLipidentkkskEEWYYRGQMKNIEKLVKSGNVSIGTLLADPPTTTLQRLKALTTGTLPTFIDAGD 136
Cdd:cd00016   2 HVVLIVLDGLGADDL-----------GKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 137 NFSPDAVISEdsfvyqaaqlgknvtllGDDTWLSLFPNQFS--KTAAYDSFDINdlntVDDKIapilqDEMLNSNSSIII 214
Cdd:cd00016  71 NGSADPELPS-----------------RAAGKDEDGPTIPEllKQAGYRTGVIG----LLKAI-----DETSKEKPFVLF 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 215 AHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQTIETMKSD------------DHGMTSTGDHG--------GESENEIR 274
Cdd:cd00016 125 LHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAgdaddtviivtaDHGGIDKGHGGdpkadgkaDKSHTGMR 204
                       250       260       270
                ....*....|....*....|....*....|....
gi 71981013 275 AGILVHSK--KHQIILPErPIHQIDIVPTISLLM 306
Cdd:cd00016 205 VPFIAYGPgvKKGGVKHE-LISQYDIAPTLADLL 237
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
56-307 5.79e-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 [Multi-domain]  Cd Length: 267  Bit Score: 87.64  E-value: 5.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013  56 QRVILILVDALRYDFLipidentkkskeewYYRGQMKNIEKLVKSGNVSIGtllADP--PTTTLQRLKALTTGTLP---- 129
Cdd:cd16018   1 PPLIVISIDGFRWDYL--------------DRAGLTPNLKRLAEEGVRAKY---VKPvfPTLTFPNHYSIVTGLYPeshg 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 130 ----TFIDAGDNFSPDAVISEDSF-------VYQAAQL-----------GKNVTLLGDdtWLSLFPNQFSKTAAYDSFdi 187
Cdd:cd16018  64 ivgnYFYDPKTNEEFSDSDWVWDPwwiggepIWVTAEKaglktasyfwpGSEVAIIGY--NPTPIPLGGYWQPYNDSF-- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 188 ndlnTVDDKIAPILQdEMLNSNSSIIIAHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQTIETMKSD------------ 255
Cdd:cd16018 140 ----PFEERVDTILE-WLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERgllddtniivvs 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71981013 256 DHGMTSTGDHGGESEN-EIRAGILVH--SKKHQIILPerPIHQIDIVPTISLLMG 307
Cdd:cd16018 215 DHGMTDVGTHGYDNELpDMRAIFIARgpAFKKGKKLG--PFRNVDIYPLMCNLLG 267
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
202-318 2.71e-15

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: 77.24  E-value: 2.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 202 QDEMLNSNSSIIIAHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQT---IETMKSD---------DHGMTSTGDHGGES 269
Cdd:cd16020 149 KTELLNQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTyplIEEYFNDgrtayiftsDHGMTDWGSHGDGS 228
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71981013 270 ENEIR-------AGI--------LVHSKKHQI-ILPERPIHQIDIVPTISLLMGLPIPFSNLGTV 318
Cdd:cd16020 229 PDETEtpfiawgAGIkhptpgrgPSFSANWGGlRLPRHDLDQADLAPLMSALLGLPPPVNSVGIL 293
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
53-265 1.85e-13

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 72.86  E-value: 1.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013  53 QQYQRVILILVDALRYDFLipidentkkskeewyYRGQMKNIEKLVKSGnVSIGTLLADPPTTTlqrlkA-----LTTGT 127
Cdd:COG1524  21 PPAKKVVLILVDGLRADLL---------------ERAHAPNLAALAARG-VYARPLTSVFPSTT-----ApahttLLTGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 128 LP--------TFIDAGDnfspDAVISEDSFVYQAAQLGKNVTLlgdDTWLSLFPNQFSKTAAYDSFDINDLNTV------ 193
Cdd:COG1524  80 YPgehgivgnGWYDPEL----GRVVNSLSWVEDGFGSNSLLPV---PTIFERARAAGLTTAAVFWPSFEGSGLIdaarpy 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 194 --------------DDKIAPILQDEMLNSNSSIIIAHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQTIETMKSD---- 255
Cdd:COG1524 153 pydgrkpllgnpaaDRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARglye 232
                       250
                ....*....|....*...
gi 71981013 256 --------DHGMTSTGDH 265
Cdd:COG1524 233 gtlvivtaDHGMVDVPPD 250
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
58-273 4.36e-12

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: 68.60  E-value: 4.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013    58 VILILVDALRYDFLipidentkkskeewYYRGQMKNIEKLVKSGnVSIGTLLADPPTTTLQRLKALTTGTLP-------- 129
Cdd:pfam01663   1 LLVISLDGFRADYL--------------DRFELTPNLAALAKEG-VSAPNLTPVFPTLTFPNHYTLVTGLYPgshgivgn 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013   130 TFIDAGDNfspdaviseDSFVYQAAQLGKNVTLLGDDTWLSL------------------FPNQFSKTAAYDSFDINDLN 191
Cdd:pfam01663  66 TFYDPKTG---------EYLVFVISDPEDPRWWQGEPIWDTAakagvraaalfwpgsevdYSTYYGTPPRYLKDDYNNSV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013   192 TVDDKIAPILQDEMLNSNS--------SIIIAHFLGVDHCGHKFGPSHPVMADTLRKMDRIIGQTIETMKSD-------- 255
Cdd:pfam01663 137 PFEDRVDTAVLQTWLDLPFadvaaerpDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERglfedtnv 216
                         250       260
                  ....*....|....*....|..
gi 71981013   256 ----DHGMTSTGDHGGESENEI 273
Cdd:pfam01663 217 ivvsDHGMTPVSDDKVIFLNDY 238
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
57-311 8.41e-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 [Multi-domain]  Cd Length: 271  Bit Score: 45.23  E-value: 8.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013  57 RVILILVDALRYDFLipidentkksKEEWYYRGQMKNIEKLVKSGNV-------SIGTLLADPptttlqrlkALTTGTLP 129
Cdd:cd16148   2 NVILIVIDSLRADHL----------GCYGYDRVTTPNLDRLAAEGVVfdnhysgSNPTLPSRF---------SLFTGLYP 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 130 TFIDAGDNFSPDaviSEDSFVYQAAQLGKNVTLLGDDTWLSLFPNqFSKTaaYDSFDINDLNTVDDKIAPILQDEMLNSn 209
Cdd:cd16148  63 FYHGVWGGPLEP---DDPTLAEILRKAGYYTAAVSSNPHLFGGPG-FDRG--FDTFEDFRGQEGDPGEEGDERAERVTD- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013 210 ssiIIAHFLGvDHCGHK--------FGPSHPVMADT-LRKMDRIIGQTIETMKsdDHGM---TS---TGDHGGE-SENEI 273
Cdd:cd16148 136 ---RALEWLD-RNADDDpfflflhyFDPHEPYLYDAeVRYVDEQIGRLLDKLK--ELGLledTLvivTSDHGEEfGEHGL 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71981013 274 RAG--------------ILVHSKKHQIILPERPIHQIDIVPTISLLMGLPIP 311
Cdd:cd16148 210 YWGhgsnlydeqlhvplIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPP 261
Sulfatase pfam00884
Sulfatase;
58-308 6.45e-03

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 39.71  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013    58 VILILVDALRYDFLIPIDentkkskeewYYRGQMKNIEKLVKSGNVSIGTLLADPPTT-TLQrlkALTTGTLPTFIDAGD 136
Cdd:pfam00884   3 VVLVLGESLRAPDLGLYG----------YPRPTTPFLDRLAEEGLLFSNFYSGGTLTApSRF---ALLTGLPPHNFGSYV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013   137 NFSPDAVISEDSFVYQAAQLG----------------KNVTLLGDDTWLSLFPNQFSKTAAYDSFDINDLNTVDDKI--A 198
Cdd:pfam00884  70 STPVGLPRTEPSLPDLLKRAGyntgaigkwhlgwynnQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVSDEAllD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981013   199 PILQDEMLNSNSSIIIAHFLGVdHCGHKFGPSHPVM------------------ADTLRKMDRIIGQTIETMKSD----- 255
Cdd:pfam00884 150 EALEFLDNNDKPFFLVLHTLGS-HGPPYYPDRYPEKyatfkpsscseeqllnsyDNTLLYTDDAIGRVLDKLEENglldn 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71981013   256 -------DHG----MTSTGDHGGESENEIRAGILV--------HSKKHQIIlpERPIHQIDIVPTISLLMGL 308
Cdd:pfam00884 229 tlvvytsDHGeslgEGGGYLHGGKYDNAPEGGYRVplliwspgGKAKGQKS--EALVSHVDLFPTILDLAGI 298
 
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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