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Conserved domains on  [gi|573459701|ref|NP_001275986|]
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GPI ethanolamine phosphate transferase 2 isoform 7 [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 ...
 1-246 1.17e-154

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: 432.76  E-value: 1.17e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701   1 MPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKL 80
Cdd:cd16024   27 MPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  81 FPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTS 160
Cdd:cd16024  107 FPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYES 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 161 LQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP----GDIRHPKHVQQTDVAATLAIALGLP 236
Cdd:cd16024  187 LE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPsnadGELSYYETVQQVDLAPTLALLLGLP 264

                        250
                 ....*....|
gi 573459701 237 IPKDSVGSLL 246
Cdd:cd16024  265 IPKNSVGVLI 274
 
Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 1-246 1.17e-154

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: 432.76  E-value: 1.17e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701   1 MPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKL 80
Cdd:cd16024   27 MPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  81 FPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTS 160
Cdd:cd16024  107 FPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYES 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 161 LQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP----GDIRHPKHVQQTDVAATLAIALGLP 236
Cdd:cd16024  187 LE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPsnadGELSYYETVQQVDLAPTLALLLGLP 264

                        250
                 ....*....|
gi 573459701 237 IPKDSVGSLL 246
Cdd:cd16024  265 IPKNSVGVLI 274
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 1-236 8.50e-13

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 67.85  E-value: 8.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701   1 MPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG----------FVDVIRNLNSPALLED-----------S 57
Cdd:COG1524   44 APNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGLYPGehgivgngwyDPELGRVVNSLSWVEDgfgsnsllpvpT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  58 VIRQAKAAGKRIVFYGdetWVKLFPKHFVEY------DGTTSFFVSDYTevDNNVTRHLDKVLKRGDWDILILHYLGLDH 131
Cdd:COG1524  121 IFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLLGNPAA--DRWIAAAALELLREGRPDLLLVYLPDLDY 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 132 IGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSET-------------------------- 185
Cdd:COG1524  196 AGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDVppdidlnrlrlagllavragesahly 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 186 -----------------------------------------------------GSHGASSTEEVNTPLILISSAFerkpg 212
Cdd:COG1524  274 lkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkGSHGGLPDEEMRVPLLASGPGF----- 348

                        330       340
                 ....*....|....*....|....
gi 573459701 213 dirhPKHVQQTDVAATLAIALGLP 236
Cdd:COG1524  349 ----RPGVRNVDVAPTIARLLGLP 368
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 1-190 2.93e-08

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: 53.96  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701    1 MPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------FVD---------VIRNLNSPALLEDSVIRQ 61
Cdd:pfam01663  20 TPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktgeylvfVISDPEDPRWWQGEPIWD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701   62 -AKAAGKRIVFYGdetWVKLFPKHFVEYDGTTSFFVSDYT-------EVDNNVTR----HLDKVLKRGDWDILILHYLGL 129
Cdd:pfam01663  97 tAAKAGVRAAALF---WPGSEVDYSTYYGTPPRYLKDDYNnsvpfedRVDTAVLQtwldLPFADVAAERPDLLLVYLEEP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 573459701  130 DHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSETGSHGA 190
Cdd:pfam01663 174 DYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMTPVSDDKV 232
 
Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 1-246 1.17e-154

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: 432.76  E-value: 1.17e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701   1 MPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKL 80
Cdd:cd16024   27 MPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  81 FPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTS 160
Cdd:cd16024  107 FPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYES 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 161 LQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP----GDIRHPKHVQQTDVAATLAIALGLP 236
Cdd:cd16024  187 LE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPsnadGELSYYETVQQVDLAPTLALLLGLP 264

                        250
                 ....*....|
gi 573459701 237 IPKDSVGSLL 246
Cdd:cd16024  265 IPKNSVGVLI 274
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 1-245 6.41e-89

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: 266.73  E-value: 6.41e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701   1 MPYTTYLVEKGASHS----FVAEakPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDET 76
Cdd:cd16023   39 LPVLEELLKSQPNNSrlfkFIAD--PPTTTLQRLKGLTTGSLPTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDT 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  77 WVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRG-DWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLM 155
Cdd:cd16023  117 WTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEdDWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIR 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 156 KIHTSLQSKeretplpNLLVLCGDHGMSETGSHGASSTEEVNTPLILIS---------SAFERKPGDIRHPKHVQQTDVA 226
Cdd:cd16023  197 DIIERLDDD-------TLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSkrpfnnsdePIESNGPGDPSKVRSVPQIDLV 269

                        250
                 ....*....|....*....
gi 573459701 227 ATLAIALGLPIPKDSVGSL 245
Cdd:cd16023  270 PTLSLLLGLPIPFSNLGTV 288
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 16-243 3.12e-70

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: 219.15  E-value: 3.12e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  16 FVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFF 95
Cdd:cd16019   46 ALSFADPPTVTGPRLKALTTGNPPTFLDLISNFASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFN 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  96 VSDYTEVDNNVTRHL----DKVLKRGDWDILILHYLGLDHIGHISG-PNSPLIGQKLSEMDSVLMKIHTSLQSKeretpl 170
Cdd:cd16019  126 IRDMHDVDPIFYNHIndnlDENIYYDNWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDND------ 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 171 pNLLVLCGDHGMSETGSHGASSTEEVNTPLILIS-SAFERKPGDIRHPKHVQ-----------------QTDVAATLAIA 232
Cdd:cd16019  200 -TLLVVVSDHGMNNDGNHGGSSTEETSSFFFFISkKGFFKKRPIDQIEKIKQnneqqkidpseyiriiyQIDILPTICYL 278

                        250
                 ....*....|.
gi 573459701 233 LGLPIPKDSVG 243
Cdd:cd16019  279 LGIPIPFNNIG 289
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 56-245 6.08e-21

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: 6.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  56 DSVIRQAKAAgkriVFYGDETWVKLFPK------HFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWD--------- 120
Cdd:cd16020   82 DSVFNRSRRS----WAWGSPDILPMFPKgatggkVLTYIYPEEDFDSTDASELDEWVFDKVEEFLANASSNktellnqdg 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 121 -ILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQS--KERETPLpnllVLCGDHGMSETGSHGASSTEEVN 197
Cdd:cd16020  158 lVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEyfNDGRTAY----IFTSDHGMTDWGSHGDGSPDETE 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 198 TPLIL-----------ISSAFERKPGDIRHPKH-VQQTDVAATLAIALGLPIPKDSVGSL 245
Cdd:cd16020  234 TPFIAwgagikhptpgRGPSFSANWGGLRLPRHdLDQADLAPLMSALLGLPPPVNSVGIL 293
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 120-234 5.20e-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: 67.61  E-value: 5.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 120 DILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKERETPLpNLLVLcGDHGMSETGSHGASSTEEVNTP 199
Cdd:cd16018  158 DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDT-NIIVV-SDHGMTDVGTHGYDNELPDMRA 235

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 573459701 200 LILISSAFERKPGDIrhpKHVQQTDVAATLAIALG 234
Cdd:cd16018  236 IFIARGPAFKKGKKL---GPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 1-236 8.50e-13

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 67.85  E-value: 8.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701   1 MPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG----------FVDVIRNLNSPALLED-----------S 57
Cdd:COG1524   44 APNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGLYPGehgivgngwyDPELGRVVNSLSWVEDgfgsnsllpvpT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  58 VIRQAKAAGKRIVFYGdetWVKLFPKHFVEY------DGTTSFFVSDYTevDNNVTRHLDKVLKRGDWDILILHYLGLDH 131
Cdd:COG1524  121 IFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLLGNPAA--DRWIAAAALELLREGRPDLLLVYLPDLDY 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 132 IGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSET-------------------------- 185
Cdd:COG1524  196 AGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDVppdidlnrlrlagllavragesahly 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 186 -----------------------------------------------------GSHGASSTEEVNTPLILISSAFerkpg 212
Cdd:COG1524  274 lkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkGSHGGLPDEEMRVPLLASGPGF----- 348

                        330       340
                 ....*....|....*....|....
gi 573459701 213 dirhPKHVQQTDVAATLAIALGLP 236
Cdd:COG1524  349 ----RPGVRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 22-230 1.37e-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: 60.13  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  22 PPTVTMPRIKALMTGSLPGFVDVIRNL----------NSPALLEDSVIRQAKAAGKRIVFYGdetwvklFPKHFVEydgt 91
Cdd:cd00016   46 PPTSSAPNHAALLTGAYPTLHGYTGNGsadpelpsraAGKDEDGPTIPELLKQAGYRTGVIG-------LLKAIDE---- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701  92 tsffvsdytevdnnvtrhldkvLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSK--ERETp 169
Cdd:cd00016  115 ----------------------TSKEKPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAgdADDT- 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 573459701 170 lpnLLVLCGDHGMSETGSHGA--------SSTEEVNTPLILISSAFeRKPGDIRHPkhVQQTDVAATLA 230
Cdd:cd00016  172 ---VIIVTADHGGIDKGHGGDpkadgkadKSHTGMRVPFIAYGPGV-KKGGVKHEL--ISQYDIAPTLA 234
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 1-190 2.93e-08

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: 53.96  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701    1 MPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------FVD---------VIRNLNSPALLEDSVIRQ 61
Cdd:pfam01663  20 TPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktgeylvfVISDPEDPRWWQGEPIWD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701   62 -AKAAGKRIVFYGdetWVKLFPKHFVEYDGTTSFFVSDYT-------EVDNNVTR----HLDKVLKRGDWDILILHYLGL 129
Cdd:pfam01663  97 tAAKAGVRAAALF---WPGSEVDYSTYYGTPPRYLKDDYNnsvpfedRVDTAVLQtwldLPFADVAAERPDLLLVYLEEP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 573459701  130 DHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSETGSHGA 190
Cdd:pfam01663 174 DYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMTPVSDDKV 232
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 173-248 7.28e-08

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: 52.55  E-value: 7.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 173 LLVLCGDHGMS-----ETGSHGASSTEE-VNTPLILissAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 246
Cdd:cd16148  193 LVIVTSDHGEEfgehgLYWGHGSNLYDEqLHVPLII---RWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSL 269


                 ..
gi 573459701 247 FP 248
Cdd:cd16148  270 LP 271
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 173-237 2.45e-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: 41.98  E-value: 2.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 173 LLVLCGDHGmSETGSHGASST-----EEVNTPLILISSAFERKPGDIRHPKHVQQTDVAATLAIALGLPI 237
Cdd:cd16153  201 IVYVTGDHG-WHLGEQGILAKftfwpQSHRVPLIVVSSDKLKAPAGKVRHDFVEFVDLAPTLLAAAGVDV 269
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
173-254 2.64e-04

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 42.17  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 173 LLVLCGDHGMSeTGSHG-----ASSTEE-VNTPLIlISSAFERKPGDIRHpKHVQQTDVAATLAIALGLPIPKDSVG-SL 245
Cdd:COG3119  230 IVVFTSDNGPS-LGEHGlrggkGTLYEGgIRVPLI-VRWPGKIKAGSVSD-ALVSLIDLLPTLLDLAGVPIPEDLDGrSL 306


                 ....*....
gi 573459701 246 LfPVVEGRP 254
Cdd:COG3119  307 L-PLLTGEK 314
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 170-257 3.02e-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: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 170 LPNLLVL-CGDHGMSeTGSH-----GASSTEEV-NTPLILISSAFERKPGDIRHPkhVQQTDVAATLAIALGLPIPKDSV 242
Cdd:cd16156  265 AEDAWVIyTSDHGDM-LGAHklwakGPAVYDEItNIPLIIRGKGGEKAGTVTDTP--VSHIDLAPTILDYAGIPQPKVLE 341

                         90
                 ....*....|....*
gi 573459701 243 GSLLFPVVEGRPMRE 257
Cdd:cd16156  342 GESILATIEDPEIPE 356
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 173-268 2.57e-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: 39.08  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 173 LLVLCGDHGMSeTGSHG---ASSTEE--VNTPLILISsaferkPG-----DIRHPkhVQQTDVAATLAIALGLPIPKDSV 242
Cdd:cd16155  222 IIVFTSDHGLA-VGSHGlmgKQNLYEhsMRVPLIISG------PGipkgkRRDAL--VYLQDVFPTLCELAGIEIPESVE 292

                         90       100
                 ....*....|....*....|....*...
gi 573459701 243 GSLLFPVVEG--RPMREQLrFLHLNTVQ 268
Cdd:cd16155  293 GKSLLPVIRGekKAVRDTL-YGAYRDGQ 319
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 173-252 6.88e-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: 37.49  E-value: 6.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 173 LLVLCGDHGMS---------ETGSHgassteevnTPLILissafeRKPGDIRHPKH----VQQTDVAATLAIALGLPIPK 239
Cdd:cd16027  219 IVIFTSDHGMPfprakgtlyDSGLR---------VPLIV------RWPGKIKPGSVsdalVSFIDLAPTLLDLAGIEPPE 283

                         90
                 ....*....|...
gi 573459701 240 DSVGSLLFPVVEG 252
Cdd:cd16027  284 YLQGRSFLPLLKG 296
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 174-246 9.36e-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: 37.39  E-value: 9.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459701 174 LVLCGDHG----M--SETGS-HGASSTEEVntPLILISSAFE---RKPGDIrhpkhvqqTDVAATLAIALGLPIPKDSVG 243
Cdd:cd16010  430 LLITADHGnaeeMidPETGGpHTAHTTNPV--PFIIVDPGLKrklLKDGGL--------ADVAPTILDLLGIEKPKEMTG 499


                 ...
gi 573459701 244 SLL 246
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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