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Conserved domains on  [gi|573459748|ref|NP_001275984|]
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GPI ethanolamine phosphate transferase 2 isoform 6 [Homo sapiens]

Protein Classification

GPI ethanolamine phosphate transferase 2( domain architecture ID 10888022)

GPI (glycosylphosphatidylinositol) ethanolamine phosphate transferase 2 catalyzes the transfer of ethanolamine phosphate to the second mannose of the GPI-anchor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 1-213 7.73e-132

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: 376.91  E-value: 7.73e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748   1 MTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKV 80
Cdd:cd16024   60 TTGSIPSFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSE 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  81 LKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQskERETPLPNLLVLCGDHGMSETGSHGASST 160
Cdd:cd16024  140 LSRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSP 217

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 573459748 161 EEVNTPLILISSAFERKP----GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 213
Cdd:cd16024  218 GETSVPLLFISPKFSSKPsnadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
 
Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 1-213 7.73e-132

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: 376.91  E-value: 7.73e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748   1 MTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKV 80
Cdd:cd16024   60 TTGSIPSFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSE 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  81 LKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQskERETPLPNLLVLCGDHGMSETGSHGASST 160
Cdd:cd16024  140 LSRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSP 217

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 573459748 161 EEVNTPLILISSAFERKP----GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 213
Cdd:cd16024  218 GETSVPLLFISPKFSSKPsnadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 13-203 1.31e-11

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 64.77  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  13 RNLNSPALLEdsvirQAKAAGKRIVFYGdetWVKLFPKHFVEY------DGTTSFFVSDYTevDNNVTRHLDKVLKRGDW 86
Cdd:COG1524  114 SLLPVPTIFE-----RARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLLGNPAA--DRWIAAAALELLREGRP 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  87 DILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSET-------------- 152
Cdd:COG1524  184 DLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDVppdidlnrlrlagl 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748 153 -----------------------------------------------------------------GSHGASSTEEVNTPL 167
Cdd:COG1524  262 lavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkGSHGGLPDEEMRVPL 341

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 573459748 168 ILISSAFerkpgdirhPKHVQQTDVAATLAIALGLP 203
Cdd:COG1524  342 LASGPGF---------RPGVRNVDVAPTIARLLGLP 368
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 54-157 1.99e-06

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: 48.96  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748   54 EYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKER 133
Cdd:pfam01663 131 DYNNSVPFEDRVDTAVLQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DER 208

                          90       100
                  ....*....|....*....|....
gi 573459748  134 ETPLPNLLVLCGDHGMSETGSHGA 157
Cdd:pfam01663 209 GLFEDTNVIVVSDHGMTPVSDDKV 232
 
Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 1-213 7.73e-132

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: 376.91  E-value: 7.73e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748   1 MTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKV 80
Cdd:cd16024   60 TTGSIPSFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSE 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  81 LKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQskERETPLPNLLVLCGDHGMSETGSHGASST 160
Cdd:cd16024  140 LSRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSP 217

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 573459748 161 EEVNTPLILISSAFERKP----GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 213
Cdd:cd16024  218 GETSVPLLFISPKFSSKPsnadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 1-212 4.84e-77

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: 237.84  E-value: 4.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748   1 MTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKV 80
Cdd:cd16023   74 TTGSLPTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPE 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  81 LKRG-DWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKereTplpnLLVLCGDHGMSETGSHGASS 159
Cdd:cd16023  154 LQSEdDWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDD---T----LLLVFGDHGMTETGDHGGDS 226

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 573459748 160 TEEVNTPLILIS---------SAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSL 212
Cdd:cd16023  227 DEEVDAALFAYSkrpfnnsdePIESNGPGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTV 288
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 1-210 3.16e-59

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: 192.58  E-value: 3.16e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748   1 MTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHL--- 77
Cdd:cd16019   64 TTGNPPTFLDLISNFASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHIndn 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  78 -DKVLKRGDWDILILHYLGLDHIGHISG-PNSPLIGQKLSEMDSVLMKIHTSLQSKeretplpNLLVLCGDHGMSETGSH 155
Cdd:cd16019  144 lDENIYYDNWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDND-------TLLVVVSDHGMNNDGNH 216

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 573459748 156 GASSTEEVNTPLILIS-SAFERKPGDIRHPKHVQ-----------------QTDVAATLAIALGLPIPKDSVG 210
Cdd:cd16019  217 GGSSTEETSSFFFFISkKGFFKKRPIDQIEKIKQnneqqkidpseyiriiyQIDILPTICYLLGIPIPFNNIG 289
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 23-212 1.07e-20

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: 90.34  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  23 DSVIRQAKAAgkriVFYGDETWVKLFPK------HFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWD--------- 87
Cdd:cd16020   82 DSVFNRSRRS----WAWGSPDILPMFPKgatggkVLTYIYPEEDFDSTDASELDEWVFDKVEEFLANASSNktellnqdg 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  88 -ILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQS--KERETPLpnllVLCGDHGMSETGSHGASSTEEVN 164
Cdd:cd16020  158 lVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEyfNDGRTAY----IFTSDHGMTDWGSHGDGSPDETE 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748 165 TPLIL-----------ISSAFERKPGDIRHPKH-VQQTDVAATLAIALGLPIPKDSVGSL 212
Cdd:cd16020  234 TPFIAwgagikhptpgRGPSFSANWGGLRLPRHdLDQADLAPLMSALLGLPPPVNSVGIL 293
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 87-201 3.82e-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: 3.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  87 DILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKERETPLpNLLVLcGDHGMSETGSHGASSTE-EVNT 165
Cdd:cd16018  158 DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDT-NIIVV-SDHGMTDVGTHGYDNELpDMRA 235

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 573459748 166 PLILissafeRKPgDIRHPKHV---QQTDVAATLAIALG 201
Cdd:cd16018  236 IFIA------RGP-AFKKGKKLgpfRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 13-203 1.31e-11

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 64.77  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  13 RNLNSPALLEdsvirQAKAAGKRIVFYGdetWVKLFPKHFVEY------DGTTSFFVSDYTevDNNVTRHLDKVLKRGDW 86
Cdd:COG1524  114 SLLPVPTIFE-----RARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLLGNPAA--DRWIAAAALELLREGRP 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  87 DILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSET-------------- 152
Cdd:COG1524  184 DLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDVppdidlnrlrlagl 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748 153 -----------------------------------------------------------------GSHGASSTEEVNTPL 167
Cdd:COG1524  262 lavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkGSHGGLPDEEMRVPL 341

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 573459748 168 ILISSAFerkpgdirhPKHVQQTDVAATLAIALGLP 203
Cdd:COG1524  342 LASGPGF---------RPGVRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 76-197 4.02e-10

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: 59.36  E-value: 4.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748  76 HLDKVLKR---GDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSK--ERETplpnLLVLCGDHGMS 150
Cdd:cd00016  107 GLLKAIDEtskEKPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAgdADDT----VIIVTADHGGI 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 573459748 151 ETGSHGA--------SSTEEVNTPLILISSAFeRKPGDIRHPkhVQQTDVAATLA 197
Cdd:cd00016  183 DKGHGGDpkadgkadKSHTGMRVPFIAYGPGV-KKGGVKHEL--ISQYDIAPTLA 234
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 140-215 1.13e-07

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: 52.17  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748 140 LLVLCGDHGMS-----ETGSHGASSTEE-VNTPLILissAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 213
Cdd:cd16148  193 LVIVTSDHGEEfgehgLYWGHGSNLYDEqLHVPLII---RWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSL 269


                 ..
gi 573459748 214 FP 215
Cdd:cd16148  270 LP 271
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 54-157 1.99e-06

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: 48.96  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748   54 EYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKER 133
Cdd:pfam01663 131 DYNNSVPFEDRVDTAVLQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DER 208

                          90       100
                  ....*....|....*....|....
gi 573459748  134 ETPLPNLLVLCGDHGMSETGSHGA 157
Cdd:pfam01663 209 GLFEDTNVIVVSDHGMTPVSDDKV 232
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 140-204 2.44e-04

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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 42.36  E-value: 2.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748 140 LLVLCGDHGmSETGSHGASST-----EEVNTPLILISSAFERKPGDIRHPKHVQQTDVAATLAIALGLPI 204
Cdd:cd16153  201 IVYVTGDHG-WHLGEQGILAKftfwpQSHRVPLIVVSSDKLKAPAGKVRHDFVEFVDLAPTLLAAAGVDV 269
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
140-221 2.66e-04

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 42.56  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748 140 LLVLCGDHGMSeTGSHG-----ASSTEE-VNTPLIlISSAFERKPGDIRHpKHVQQTDVAATLAIALGLPIPKDSVG-SL 212
Cdd:COG3119  230 IVVFTSDNGPS-LGEHGlrggkGTLYEGgIRVPLI-VRWPGKIKAGSVSD-ALVSLIDLLPTLLDLAGVPIPEDLDGrSL 306


                 ....*....
gi 573459748 213 LfPVVEGRP 221
Cdd:COG3119  307 L-PLLTGEK 314
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 137-224 3.87e-04

uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; 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: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 41.98  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748 137 LPNLLVL-CGDHGMSeTGSH-----GASSTEEV-NTPLILISSAFERKPGDIRHPkhVQQTDVAATLAIALGLPIPKDSV 209
Cdd:cd16156  265 AEDAWVIyTSDHGDM-LGAHklwakGPAVYDEItNIPLIIRGKGGEKAGTVTDTP--VSHIDLAPTILDYAGIPQPKVLE 341

                         90
                 ....*....|....*
gi 573459748 210 GSLLFPVVEGRPMRE 224
Cdd:cd16156  342 GESILATIEDPEIPE 356
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 140-235 1.72e-03

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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 39.86  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748 140 LLVLCGDHGMSeTGSHG---ASSTEE--VNTPLILISsaferkPG-----DIRHPkhVQQTDVAATLAIALGLPIPKDSV 209
Cdd:cd16155  222 IIVFTSDHGLA-VGSHGlmgKQNLYEhsMRVPLIISG------PGipkgkRRDAL--VYLQDVFPTLCELAGIEIPESVE 292

                         90       100
                 ....*....|....*....|....*...
gi 573459748 210 GSLLFPVVEG--RPMREQLrFLHLNTVQ 235
Cdd:cd16155  293 GKSLLPVIRGekKAVRDTL-YGAYRDGQ 319
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 140-219 6.64e-03

N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.


Pssm-ID: 293751 [Multi-domain]  Cd Length: 373  Bit Score: 37.87  E-value: 6.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748 140 LLVLCGDHGMS---------ETGSHgassteevnTPLILissafeRKPGDIRHPKH----VQQTDVAATLAIALGLPIPK 206
Cdd:cd16027  219 IVIFTSDHGMPfprakgtlyDSGLR---------VPLIV------RWPGKIKPGSVsdalVSFIDLAPTLLDLAGIEPPE 283

                         90
                 ....*....|...
gi 573459748 207 DSVGSLLFPVVEG 219
Cdd:cd16027  284 YLQGRSFLPLLKG 296
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 141-213 9.83e-03

2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.


Pssm-ID: 293734  Cd Length: 503  Bit Score: 37.78  E-value: 9.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459748 141 LVLCGDHG----M--SETGS-HGASSTEEVntPLILISSAFE---RKPGDIrhpkhvqqTDVAATLAIALGLPIPKDSVG 210
Cdd:cd16010  430 LLITADHGnaeeMidPETGGpHTAHTTNPV--PFIIVDPGLKrklLKDGGL--------ADVAPTILDLLGIEKPKEMTG 499


                 ...
gi 573459748 211 SLL 213
Cdd:cd16010  500 KSL 502
 
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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