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Conserved domains on  [gi|573459752|ref|NP_001275980|]
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GPI ethanolamine phosphate transferase 2 isoform 3 [Homo sapiens]

Protein Classification

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 5.31e-148

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: 437.38  E-value: 5.31e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752   1 MPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKL 80
Cdd:cd16024   27 MPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  81 FPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTS 160
Cdd:cd16024  107 FPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYES 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 161 LQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP----GDIRHPKHVQQTDVAATLAIALGLP 236
Cdd:cd16024  187 LE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPsnadGELSYYETVQQVDLAPTLALLLGLP 264

                        250
                 ....*....|
gi 573459752 237 IPKDSVGSLL 246
Cdd:cd16024  265 IPKNSVGVLI 274
PIGO_PIGG super family cl44747
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ...
 714-876 2.07e-19

GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the transmembrane region of the GPI ethanolamine phosphate transferase enzymes. The family includes the PIGO and PIGG proteins from human. These proteins are involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis.


The actual alignment was detected with superfamily member pfam19316:

Pssm-ID: 437148  Cd Length: 423  Bit Score: 91.88  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  714 LLAALLF---RPHNLPVLAFSLLIQTLMTkfiwkPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYv 790
Cdd:pfam19316 242 LLTLFLItqsRATNIPLFLLFRLQLEFLS-----SLDLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGY- 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  791 EIPAV-LLTAFGTYAGPVLWASHLVHFLSSETRSGSAlSHACFCYALICSipVFTYIVLV------TSLRYHLFIWSVFS 863
Cdd:pfam19316 316 NVVAVgVLTFVSNWAGPIWWTSATNLLLLRKRRRGEG-RGVFFQHLALLT--LFVAASLVsvmaacTALRTHLFIWTVFS 392

                         170
                  ....*....|....*...
gi 573459752  864 PKLLYE-----GMHLLIT 876
Cdd:pfam19316 393 PKYLYTmawslGQHLLVN 410
 
Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 1-246 5.31e-148

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: 437.38  E-value: 5.31e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752   1 MPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKL 80
Cdd:cd16024   27 MPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  81 FPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTS 160
Cdd:cd16024  107 FPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYES 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 161 LQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP----GDIRHPKHVQQTDVAATLAIALGLP 236
Cdd:cd16024  187 LE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPsnadGELSYYETVQQVDLAPTLALLLGLP 264

                        250
                 ....*....|
gi 573459752 237 IPKDSVGSLL 246
Cdd:cd16024  265 IPKNSVGVLI 274
PIGO_PIGG pfam19316
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ...
 714-876 2.07e-19

GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the transmembrane region of the GPI ethanolamine phosphate transferase enzymes. The family includes the PIGO and PIGG proteins from human. These proteins are involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis.


Pssm-ID: 437148  Cd Length: 423  Bit Score: 91.88  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  714 LLAALLF---RPHNLPVLAFSLLIQTLMTkfiwkPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYv 790
Cdd:pfam19316 242 LLTLFLItqsRATNIPLFLLFRLQLEFLS-----SLDLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGY- 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  791 EIPAV-LLTAFGTYAGPVLWASHLVHFLSSETRSGSAlSHACFCYALICSipVFTYIVLV------TSLRYHLFIWSVFS 863
Cdd:pfam19316 316 NVVAVgVLTFVSNWAGPIWWTSATNLLLLRKRRRGEG-RGVFFQHLALLT--LFVAASLVsvmaacTALRTHLFIWTVFS 392

                         170
                  ....*....|....*...
gi 573459752  864 PKLLYE-----GMHLLIT 876
Cdd:pfam19316 393 PKYLYTmawslGQHLLVN 410
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 1-236 1.11e-11

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 67.47  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752   1 MPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG----------FVDVIRNLNSPALLED-----------S 57
Cdd:COG1524   44 APNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGLYPGehgivgngwyDPELGRVVNSLSWVEDgfgsnsllpvpT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  58 VIRQAKAAGKRIVFYGdetWVKLFPKHFVEY------DGTTSFFVSDYTevDNNVTRHLDKVLKRGDWDILILHYLGLDH 131
Cdd:COG1524  121 IFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLLGNPAA--DRWIAAAALELLREGRPDLLLVYLPDLDY 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 132 IGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSET-------------------------- 185
Cdd:COG1524  196 AGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDVppdidlnrlrlagllavragesahly 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 186 -----------------------------------------------------GSHGASSTEEVNTPLILISSAFerkpg 212
Cdd:COG1524  274 lkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkGSHGGLPDEEMRVPLLASGPGF----- 348

                        330       340
                 ....*....|....*....|....
gi 573459752 213 dirhPKHVQQTDVAATLAIALGLP 236
Cdd:COG1524  349 ----RPGVRNVDVAPTIARLLGLP 368
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 1-190 9.26e-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: 55.12  E-value: 9.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752    1 MPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------FVD---------VIRNLNSPALLEDSVIRQ 61
Cdd:pfam01663  20 TPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktgeylvfVISDPEDPRWWQGEPIWD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752   62 -AKAAGKRIVFYGdetWVKLFPKHFVEYDGTTSFFVSDYT-------EVDNNVTR----HLDKVLKRGDWDILILHYLGL 129
Cdd:pfam01663  97 tAAKAGVRAAALF---WPGSEVDYSTYYGTPPRYLKDDYNnsvpfedRVDTAVLQtwldLPFADVAAERPDLLLVYLEEP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 573459752  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 5.31e-148

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: 437.38  E-value: 5.31e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752   1 MPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKL 80
Cdd:cd16024   27 MPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  81 FPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTS 160
Cdd:cd16024  107 FPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYES 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 161 LQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP----GDIRHPKHVQQTDVAATLAIALGLP 236
Cdd:cd16024  187 LE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPsnadGELSYYETVQQVDLAPTLALLLGLP 264

                        250
                 ....*....|
gi 573459752 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 1.57e-84

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: 272.51  E-value: 1.57e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752   1 MPYTTYLVEKGASHS----FVAEakPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDET 76
Cdd:cd16023   39 LPVLEELLKSQPNNSrlfkFIAD--PPTTTLQRLKGLTTGSLPTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDT 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  77 WVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRG-DWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLM 155
Cdd:cd16023  117 WTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEdDWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIR 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 156 KIHTSLQSKereTplpnLLVLCGDHGMSETGSHGASSTEEVNTPLILIS---------SAFERKPGDIRHPKHVQQTDVA 226
Cdd:cd16023  197 DIIERLDDD---T----LLLVFGDHGMTETGDHGGDSDEEVDAALFAYSkrpfnnsdePIESNGPGDPSKVRSVPQIDLV 269

                        250
                 ....*....|....*....
gi 573459752 227 ATLAIALGLPIPKDSVGSL 245
Cdd:cd16023  270 PTLSLLLGLPIPFSNLGTV 288
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 16-243 6.09e-66

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: 222.62  E-value: 6.09e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  16 FVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFF 95
Cdd:cd16019   46 ALSFADPPTVTGPRLKALTTGNPPTFLDLISNFASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFN 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  96 VSDYTEVDNNVTRHL----DKVLKRGDWDILILHYLGLDHIGHISG-PNSPLIGQKLSEMDSVLMKIHTSLQSKeretpl 170
Cdd:cd16019  126 IRDMHDVDPIFYNHIndnlDENIYYDNWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDND------ 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 171 pNLLVLCGDHGMSETGSHGASSTEEVNTPLILIS-SAFERKPGDIRHPKHVQ-----------------QTDVAATLAIA 232
Cdd:cd16019  200 -TLLVVVSDHGMNNDGNHGGSSTEETSSFFFFISkKGFFKKRPIDQIEKIKQnneqqkidpseyiriiyQIDILPTICYL 278

                        250
                 ....*....|.
gi 573459752 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 5.10e-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: 91.50  E-value: 5.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  56 DSVIRQAKAAgkriVFYGDETWVKLFPK------HFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWD--------- 120
Cdd:cd16020   82 DSVFNRSRRS----WAWGSPDILPMFPKgatggkVLTYIYPEEDFDSTDASELDEWVFDKVEEFLANASSNktellnqdg 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 121 -ILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQS--KERETPLpnllVLCGDHGMSETGSHGASSTEEVN 197
Cdd:cd16020  158 lVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEyfNDGRTAY----IFTSDHGMTDWGSHGDGSPDETE 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 198 TPLIL-----------ISSAFERKPGDIRHPKH-VQQTDVAATLAIALGLPIPKDSVGSL 245
Cdd:cd16020  234 TPFIAwgagikhptpgRGPSFSANWGGLRLPRHdLDQADLAPLMSALLGLPPPVNSVGIL 293
PIGO_PIGG pfam19316
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ...
 714-876 2.07e-19

GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the transmembrane region of the GPI ethanolamine phosphate transferase enzymes. The family includes the PIGO and PIGG proteins from human. These proteins are involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis.


Pssm-ID: 437148  Cd Length: 423  Bit Score: 91.88  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  714 LLAALLF---RPHNLPVLAFSLLIQTLMTkfiwkPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYv 790
Cdd:pfam19316 242 LLTLFLItqsRATNIPLFLLFRLQLEFLS-----SLDLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGY- 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  791 EIPAV-LLTAFGTYAGPVLWASHLVHFLSSETRSGSAlSHACFCYALICSipVFTYIVLV------TSLRYHLFIWSVFS 863
Cdd:pfam19316 316 NVVAVgVLTFVSNWAGPIWWTSATNLLLLRKRRRGEG-RGVFFQHLALLT--LFVAASLVsvmaacTALRTHLFIWTVFS 392

                         170
                  ....*....|....*...
gi 573459752  864 PKLLYE-----GMHLLIT 876
Cdd:pfam19316 393 PKYLYTmawslGQHLLVN 410
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 120-234 2.17e-12

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: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 120 DILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKERETPLpNLLVLcGDHGMSETGSHGASSTE-EVNT 198
Cdd:cd16018  158 DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDT-NIIVV-SDHGMTDVGTHGYDNELpDMRA 235

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 573459752 199 PLILissafeRKPgDIRHPKHV---QQTDVAATLAIALG 234
Cdd:cd16018  236 IFIA------RGP-AFKKGKKLgpfRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 1-236 1.11e-11

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 67.47  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752   1 MPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG----------FVDVIRNLNSPALLED-----------S 57
Cdd:COG1524   44 APNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGLYPGehgivgngwyDPELGRVVNSLSWVEDgfgsnsllpvpT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  58 VIRQAKAAGKRIVFYGdetWVKLFPKHFVEY------DGTTSFFVSDYTevDNNVTRHLDKVLKRGDWDILILHYLGLDH 131
Cdd:COG1524  121 IFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLLGNPAA--DRWIAAAALELLREGRPDLLLVYLPDLDY 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 132 IGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSET-------------------------- 185
Cdd:COG1524  196 AGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDVppdidlnrlrlagllavragesahly 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 186 -----------------------------------------------------GSHGASSTEEVNTPLILISSAFerkpg 212
Cdd:COG1524  274 lkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkGSHGGLPDEEMRVPLLASGPGF----- 348

                        330       340
                 ....*....|....*....|....
gi 573459752 213 dirhPKHVQQTDVAATLAIALGLP 236
Cdd:COG1524  349 ----RPGVRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 22-230 1.13e-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: 62.82  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  22 PPTVTMPRIKALMTGSLPGFVDVIRNL----------NSPALLEDSVIRQAKAAGKRIVFYGdetwvklFPKHFVEydgt 91
Cdd:cd00016   46 PPTSSAPNHAALLTGAYPTLHGYTGNGsadpelpsraAGKDEDGPTIPELLKQAGYRTGVIG-------LLKAIDE---- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752  92 tsffvsdytevdnnvtrhldkvLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSK--ERETp 169
Cdd:cd00016  115 ----------------------TSKEKPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAgdADDT- 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 573459752 170 lpnLLVLCGDHGMSETGSHGA--------SSTEEVNTPLILISSAFeRKPGDIRHPkhVQQTDVAATLA 230
Cdd:cd00016  172 ---VIIVTADHGGIDKGHGGDpkadgkadKSHTGMRVPFIAYGPGV-KKGGVKHEL--ISQYDIAPTLA 234
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 1-190 9.26e-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: 55.12  E-value: 9.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752    1 MPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------FVD---------VIRNLNSPALLEDSVIRQ 61
Cdd:pfam01663  20 TPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktgeylvfVISDPEDPRWWQGEPIWD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752   62 -AKAAGKRIVFYGdetWVKLFPKHFVEYDGTTSFFVSDYT-------EVDNNVTR----HLDKVLKRGDWDILILHYLGL 129
Cdd:pfam01663  97 tAAKAGVRAAALF---WPGSEVDYSTYYGTPPRYLKDDYNnsvpfedRVDTAVLQtwldLPFADVAAERPDLLLVYLEEP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 573459752  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 4.03e-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: 52.55  E-value: 4.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 173 LLVLCGDHGMS-----ETGSHGASSTEE-VNTPLILissAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 246
Cdd:cd16148  193 LVIVTSDHGEEfgehgLYWGHGSNLYDEqLHVPLII---RWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSL 269


                 ..
gi 573459752 247 FP 248
Cdd:cd16148  270 LP 271
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 173-237 9.54e-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: 9.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 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 1.03e-03

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: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 173 LLVLCGDHGMSeTGSHG-----ASSTEE-VNTPLIlISSAFERKPGDIRHpKHVQQTDVAATLAIALGLPIPKDSVG-SL 245
Cdd:COG3119  230 IVVFTSDNGPS-LGEHGlrggkGTLYEGgIRVPLI-VRWPGKIKAGSVSD-ALVSLIDLLPTLLDLAGVPIPEDLDGrSL 306


                 ....*....
gi 573459752 246 LfPVVEGRP 254
Cdd:COG3119  307 L-PLLTGEK 314
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 170-257 1.51e-03

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: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 170 LPNLLVL-CGDHGMSeTGSH-----GASSTEEV-NTPLILISSAFERKPGDIRHPkhVQQTDVAATLAIALGLPIPKDSV 242
Cdd:cd16156  265 AEDAWVIyTSDHGDM-LGAHklwakGPAVYDEItNIPLIIRGKGGEKAGTVTDTP--VSHIDLAPTILDYAGIPQPKVLE 341

                         90
                 ....*....|....*
gi 573459752 243 GSLLFPVVEGRPMRE 257
Cdd:cd16156  342 GESILATIEDPEIPE 356
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 173-268 6.40e-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: 6.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573459752 173 LLVLCGDHGMSeTGSHG---ASSTEE--VNTPLILISsaferkPG-----DIRHPkhVQQTDVAATLAIALGLPIPKDSV 242
Cdd:cd16155  222 IIVFTSDHGLA-VGSHGlmgKQNLYEhsMRVPLIISG------PGipkgkRRDAL--VYLQDVFPTLCELAGIEIPESVE 292

                         90       100
                 ....*....|....*....|....*...
gi 573459752 243 GSLLFPVVEG--RPMREQLrFLHLNTVQ 268
Cdd:cd16155  293 GKSLLPVIRGekKAVRDTL-YGAYRDGQ 319
 
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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