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Conserved domains on  [gi|19112330|ref|NP_595538|]
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putative pig-O family ethanolamine phosphate transferase [Schizosaccharomyces pombe]

Protein Classification

GPI ethanolamine phosphate transferase 3( domain architecture ID 10887995)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 78-353 2.92e-147

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: 436.99  E-value: 2.92e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330  78 PKIFERAVIVIIDALRYDFLIPYNDSN------YYHNAFTTPYETSVLHPENSYLTQFIADAPTTTSQRLKGLTTGSLPT 151
Cdd:cd16023   1 PPRFDKVVLLLIDALRYDFVLPDDENPpsenslYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLPT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 152 FIDLGSNFAGTNIDEDNLLLQWKSLDKQIVLLGDDTWDVLFHDYLNETLsqPAFSFNVPDLHGVDNKVNQYVFDYI-KDA 230
Cdd:cd16023  81 FIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSY--PFPSFNVKDLDTVDNGVLKHLFPELqSED 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 231 NFDVLIAHYLGVDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLLDDSTLLIVMGDHGMDNKGNHGGDSFDEINSVLWMYS 310
Cdd:cd16023 159 DWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYS 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 19112330 311 KKPTFGYLK--------QPGKVLSANQVDLVPTLSLLLGNPIPYGNLGTLI 353
Cdd:cd16023 239 KRPFNNSDEpiesngpgDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
 
Name Accession Description Interval E-value
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 78-353 2.92e-147

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: 436.99  E-value: 2.92e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330  78 PKIFERAVIVIIDALRYDFLIPYNDSN------YYHNAFTTPYETSVLHPENSYLTQFIADAPTTTSQRLKGLTTGSLPT 151
Cdd:cd16023   1 PPRFDKVVLLLIDALRYDFVLPDDENPpsenslYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLPT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 152 FIDLGSNFAGTNIDEDNLLLQWKSLDKQIVLLGDDTWDVLFHDYLNETLsqPAFSFNVPDLHGVDNKVNQYVFDYI-KDA 230
Cdd:cd16023  81 FIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSY--PFPSFNVKDLDTVDNGVLKHLFPELqSED 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 231 NFDVLIAHYLGVDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLLDDSTLLIVMGDHGMDNKGNHGGDSFDEINSVLWMYS 310
Cdd:cd16023 159 DWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYS 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 19112330 311 KKPTFGYLK--------QPGKVLSANQVDLVPTLSLLLGNPIPYGNLGTLI 353
Cdd:cd16023 239 KRPFNNSDEpiesngpgDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 83-290 2.52e-14

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 75.55  E-value: 2.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330  83 RAVIVIIDALRYDFLipyndsnyyhNAFTTPYETSVLHpENSYLTQFIADAPTTT-----SqrlkgLTTGSLPtfiD--- 154
Cdd:COG1524  25 KVVLILVDGLRADLL----------ERAHAPNLAALAA-RGVYARPLTSVFPSTTapahtT-----LLTGLYP---Gehg 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 155 -LGSNFAGTNIDEDNLLLQWKSLDKQIV--LLGDDTWDVL-------------------FHDYLNETLSQPAFSFNVP-- 210
Cdd:COG1524  86 iVGNGWYDPELGRVVNSLSWVEDGFGSNslLPVPTIFERAraaglttaavfwpsfegsgLIDAARPYPYDGRKPLLGNpa 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 211 -DLHGVDNkvnqyVFDYIKDANFDVLIAHYLGVDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLLD-----DSTLLIVMG 284
Cdd:COG1524 166 aDRWIAAA-----ALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKarglyEGTLVIVTA 240


                ....*.
gi 19112330 285 DHGMDN 290
Cdd:COG1524 241 DHGMVD 246
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 188-302 4.17e-11

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: 65.52  E-value: 4.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330   188 WDVLFHDYLNETLSQPAFSFNVPDLHGVDNKVNQYVFDYIKDANF----DVLIAHYLGVDHVGHRLGPDHPTMRDKLNQM 263
Cdd:pfam01663 115 VDYSTYYGTPPRYLKDDYNNSVPFEDRVDTAVLQTWLDLPFADVAaerpDLLLVYLEEPDYAGHRYGPDSPEVEDALRRV 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 19112330   264 DRCVKEMMDLLDD-----STLLIVMGDHGMDNKGNHGGDSFDEI 302
Cdd:pfam01663 195 DRAIGDLLEALDErglfeDTNVIVVSDHGMTPVSDDKVIFLNDY 238
 
Name Accession Description Interval E-value
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 78-353 2.92e-147

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: 436.99  E-value: 2.92e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330  78 PKIFERAVIVIIDALRYDFLIPYNDSN------YYHNAFTTPYETSVLHPENSYLTQFIADAPTTTSQRLKGLTTGSLPT 151
Cdd:cd16023   1 PPRFDKVVLLLIDALRYDFVLPDDENPpsenslYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLPT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 152 FIDLGSNFAGTNIDEDNLLLQWKSLDKQIVLLGDDTWDVLFHDYLNETLsqPAFSFNVPDLHGVDNKVNQYVFDYI-KDA 230
Cdd:cd16023  81 FIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSY--PFPSFNVKDLDTVDNGVLKHLFPELqSED 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 231 NFDVLIAHYLGVDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLLDDSTLLIVMGDHGMDNKGNHGGDSFDEINSVLWMYS 310
Cdd:cd16023 159 DWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYS 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 19112330 311 KKPTFGYLK--------QPGKVLSANQVDLVPTLSLLLGNPIPYGNLGTLI 353
Cdd:cd16023 239 KRPFNNSDEpiesngpgDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 81-353 1.17e-72

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: 240.54  E-value: 1.17e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330  81 FERAVIVIIDALRYDFLIPyNDSNyyhnaftTPYETSVLHPENSYLTQFIADAPTTTSQRLKGLTTGSLPTFIDLGSNFA 160
Cdd:cd16024   4 FDKLVFMVIDALRADFVFG-PDSN-------MPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 161 GTNIDEDNLLLQWKSLDKQIVLLGDDTWDVLF-HDYLNetlSQPAFSFNVPDLHGVDNKVNQYVFDYIKDANFDVLIAHY 239
Cdd:cd16024  76 SSLLEEDNWLSQLKAAGKKIVFYGDDTWLKLFpGSFTR---SDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 240 LGVDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLL-----DDSTLLIVMGDHGMDNKGNHGGDSFDEINSVLWMYSKK-- 312
Cdd:cd16024 153 LGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLeeqssNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKfs 232

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 19112330 313 ----PTFGYLKQPGKVlsaNQVDLVPTLSLLLGNPIPYGNLGTLI 353
Cdd:cd16024 233 skpsNADGELSYYETV---QQVDLAPTLALLLGLPIPKNSVGVLI 274
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 78-353 7.68e-69

GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293743 [Multi-domain]  Cd Length: 292  Bit Score: 230.71  E-value: 7.68e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330  78 PKIFERAVIVIIDALRYDFLIPyNDSNYYHNAFttpYETSVLHPENSYLTQFIADAPTTTSQRLKGLTTGSLPTFIDLGS 157
Cdd:cd16019   1 PTKYDKVVLIVIDGLRYDLAVN-VNKQSSFFSF---LQKLNEQPNNSFLALSFADPPTVTGPRLKALTTGNPPTFLDLIS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 158 NFAGTNIDEDNLLLQWKSLDKQIVLLGDDTWDVLFHDYLneTLSQPAFSFNVPDLHGVDNKVN---QYVFD-YIKDANFD 233
Cdd:cd16019  77 NFASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIF--TYKFTITSFNIRDMHDVDPIFYnhiNDNLDeNIYYDNWD 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 234 VLIAHYLGVDHVGHRLG-PDHPTMRDKLNQMDRCVKEMMDLLDDSTLLIVMGDHGMDNKGNHGGDSFDEINSVLWMYSKK 312
Cdd:cd16019 155 FIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDNDTLLVVVSDHGMNNDGNHGGSSTEETSSFFFFISKK 234

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19112330 313 PTF--GYLKQPGKVLSAN---------------QVDLVPTLSLLLGNPIPYGNLGTLI 353
Cdd:cd16019 235 GFFkkRPIDQIEKIKQNNeqqkidpseyiriiyQIDILPTICYLLGIPIPFNNIGIII 292
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 85-340 1.08e-22

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: 97.88  E-value: 1.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330  85 VIVIIDALRYDFLipyndSNYYHNAFTTPYeTSVLHPENSYLTQFIADAPTTTSQRLKGLTTGSLPTFIDLGSNFAGTni 164
Cdd:cd00016   4 VLIVLDGLGADDL-----GKAGNPAPTTPN-LKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSAD-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 165 dednlllqwkSLDKQIVLLGDDTWDVLFHDYLNETLSQPAFsfnvpdlhgvdnkvnqYVFDYIK---DANFDVLIAHYLG 241
Cdd:cd00016  76 ----------PELPSRAAGKDEDGPTIPELLKQAGYRTGVI----------------GLLKAIDetsKEKPFVLFLHFDG 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 242 VDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLLD-----DSTLLIVMGDHGMDNKGNHG--------GDSFDEINSVLWM 308
Cdd:cd00016 130 PDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKkagdaDDTVIIVTADHGGIDKGHGGdpkadgkaDKSHTGMRVPFIA 209

                       250       260       270
                ....*....|....*....|....*....|..
gi 19112330 309 YSKkptfGYLKQPGKVLSANQVDLVPTLSLLL 340
Cdd:cd00016 210 YGP----GVKKGGVKHELISQYDIAPTLADLL 237
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 233-341 1.28e-17

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: 83.79  E-value: 1.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 233 DVLIAHYLGVDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLLD-----DSTLLIVMGDHGMDNKGNHGGD-SFDEINSVL 306
Cdd:cd16018 158 DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKergllDDTNIIVVSDHGMTDVGTHGYDnELPDMRAIF 237

                        90       100       110
                ....*....|....*....|....*....|....*
gi 19112330 307 wmYSKKPTFgylKQPGKVLSANQVDLVPTLSLLLG 341
Cdd:cd16018 238 --IARGPAF---KKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 83-290 2.52e-14

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 75.55  E-value: 2.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330  83 RAVIVIIDALRYDFLipyndsnyyhNAFTTPYETSVLHpENSYLTQFIADAPTTT-----SqrlkgLTTGSLPtfiD--- 154
Cdd:COG1524  25 KVVLILVDGLRADLL----------ERAHAPNLAALAA-RGVYARPLTSVFPSTTapahtT-----LLTGLYP---Gehg 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 155 -LGSNFAGTNIDEDNLLLQWKSLDKQIV--LLGDDTWDVL-------------------FHDYLNETLSQPAFSFNVP-- 210
Cdd:COG1524  86 iVGNGWYDPELGRVVNSLSWVEDGFGSNslLPVPTIFERAraaglttaavfwpsfegsgLIDAARPYPYDGRKPLLGNpa 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 211 -DLHGVDNkvnqyVFDYIKDANFDVLIAHYLGVDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLLD-----DSTLLIVMG 284
Cdd:COG1524 166 aDRWIAAA-----ALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKarglyEGTLVIVTA 240


                ....*.
gi 19112330 285 DHGMDN 290
Cdd:COG1524 241 DHGMVD 246
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 234-352 4.84e-13

GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293744  Cd Length: 294  Bit Score: 70.70  E-value: 4.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 234 VLIAHYLGVDHVGHRLGPDHPTMRDKLNQMDRCVKEMMDLL-----DDSTLLIVMGDHGMDNKGNHGGDSFDEINS--VL 306
Cdd:cd16020 159 VFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIeeyfnDGRTAYIFTSDHGMTDWGSHGDGSPDETETpfIA 238

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112330 307 W-------MYSKKPTFGYL--KQPGKVLSANQVDLVPTLSLLLGNPIPYGNLGTL 352
Cdd:cd16020 239 WgagikhpTPGRGPSFSANwgGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGIL 293
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 188-302 4.17e-11

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: 65.52  E-value: 4.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330   188 WDVLFHDYLNETLSQPAFSFNVPDLHGVDNKVNQYVFDYIKDANF----DVLIAHYLGVDHVGHRLGPDHPTMRDKLNQM 263
Cdd:pfam01663 115 VDYSTYYGTPPRYLKDDYNNSVPFEDRVDTAVLQTWLDLPFADVAaerpDLLLVYLEEPDYAGHRYGPDSPEVEDALRRV 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 19112330   264 DRCVKEMMDLLDD-----STLLIVMGDHGMDNKGNHGGDSFDEI 302
Cdd:pfam01663 195 DRAIGDLLEALDErglfeDTNVIVVSDHGMTPVSDDKVIFLNDY 238
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 251-345 3.91e-06

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: 50.20  E-value: 3.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 251 PDHPTMR-------DKLNQMDRCVKEMMDLLDDS-----TLLIVMGDHGMDN---KGNhggdSFDEINSVLWMYSkkptF 315
Cdd:cd16027 179 PDTPEVRedladyyDEIERLDQQVGEILDELEEDglldnTIVIFTSDHGMPFpraKGT----LYDSGLRVPLIVR----W 250

                        90       100       110
                ....*....|....*....|....*....|..
gi 19112330 316 GYLKQPGKVLSA--NQVDLVPTLSLLLGNPIP 345
Cdd:cd16027 251 PGKIKPGSVSDAlvSFIDLAPTLLDLAGIEPP 282
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
262-345 7.36e-05

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 46.02  E-value: 7.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 262 QMDRCVKEMMDLLDDS-----TLLIVMGDHGmDNKGNHG-----GDSFDEINSV--LWMYSKKptfgylKQPGKVLSA-- 327
Cdd:COG3119 208 EVDDQVGRLLDALEELgladnTIVVFTSDNG-PSLGEHGlrggkGTLYEGGIRVplIVRWPGK------IKAGSVSDAlv 280

                        90
                ....*....|....*...
gi 19112330 328 NQVDLVPTLSLLLGNPIP 345
Cdd:COG3119 281 SLIDLLPTLLDLAGVPIP 298
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 246-289 2.83e-04

Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.


Pssm-ID: 293733  Cd Length: 382  Bit Score: 44.36  E-value: 2.83e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19112330 246 GHRLGPDhpTMRDKLNQMDRCVKEMMDLLDDSTLLIVMGDHGMD 289
Cdd:cd16009 286 GHRRDPE--GYAEALEEFDRRLPELLAKLKEDDLLIITADHGND 327
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 262-350 5.31e-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: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 42.92  E-value: 5.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 262 QMDRCVKEMMDLLD-----DSTLLIVMGDHG---MDNKGNHGGDS--FDEINSV-LWMYSKKptfgylKQPGKVLSA--N 328
Cdd:cd16148 171 YVDEQIGRLLDKLKelgllEDTLVIVTSDHGeefGEHGLYWGHGSnlYDEQLHVpLIIRWPG------KEPGKRVDAlvS 244

                        90       100
                ....*....|....*....|..
gi 19112330 329 QVDLVPTLSLLLGNPIPYGNLG 350
Cdd:cd16148 245 HIDIAPTLLDLLGVEPPDYSDG 266
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 223-287 3.37e-03

Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.


Pssm-ID: 396305  Cd Length: 410  Bit Score: 40.85  E-value: 3.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112330   223 VFDYIKDA---NFDVLIAHYLGVDHVGHRlgpdhptmRD------KLNQMDRCVKEMMDLLDDS-TLLIVMGDHG 287
Cdd:pfam01676 288 ITDKLLEAlkeKYDFVFVNFANTDMVGHT--------GDvegkvkAIEAVDERLGELLDALEEDdGLLIITADHG 354
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 264-345 4.87e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 40.24  E-value: 4.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 264 DRCVKEMMDLLDDS-----TLLIV-------MGDHGMDNKGNHggdsFDE-INSVLWMYSKKPtfgyLKQPGKV-LSANQ 329
Cdd:cd16034 237 DDNIGRLLDALKELgllenTIVVFtsdhgdmLGSHGLMNKQVP----YEEsIRVPFIIRYPGK----IKAGRVVdLLINT 308

                        90
                ....*....|....*.
gi 19112330 330 VDLVPTLSLLLGNPIP 345
Cdd:cd16034 309 VDIMPTLLGLCGLPIP 324
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 263-345 6.89e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 39.14  E-value: 6.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112330 263 MDRCVKEMMDLLD-----DSTLLIVMGDHGMdNKGNHG----GDSFDEINsvLWMYS-KKPTFgyLKQPGKVL------- 325
Cdd:cd16149 151 VDRNVGRLLDELEelgltENTLVIFTSDNGF-NMGHHGiwgkGNGTFPLN--MYDNSvKVPFI--IRWPGVVPagrvvds 225

                        90       100
                ....*....|....*....|
gi 19112330 326 SANQVDLVPTLSLLLGNPIP 345
Cdd:cd16149 226 LVSAYDFFPTLLELAGVDPP 245
 
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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