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Conserved domains on  [gi|2118037379|ref|XP_044312377|]
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ectonucleotide pyrophosphatase/phosphodiesterase family member 7 [Varanus komodoensis]

Protein Classification

ectonucleotide pyrophosphatase/phosphodiesterase( domain architecture ID 10887878)

ectonucleotide pyrophosphatase/phosphodiesterase (ENPPs) hydrolyzes 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 28-389 6.25e-104

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: 311.83  E-value: 6.25e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  28 KLLLVSFDGFRWNY-DQDVDTPNLDTMASEGVKARYMTPAFVTQTSPCHFTLLTGRYIENHGVIHNMWFNTSSGRKYSYY 106
Cdd:cd16018     2 PLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSDS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 107 DTQQksDWWDNGSLPIWISAQRQGLKAASLFFPGGNAIYQGEEVQVKKVEKKWHKYDNETEWRQNVDTVMEWFTKDDLDF 186
Cdd:cd16018    82 DWVW--DPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWLDLERPDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 187 VALYFGEPDSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINETGLVSRLNLIITSDHGMETVikeneihlatvanfsfqd 266
Cdd:cd16018   160 ILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------------ 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 267 lqfelldygphalllprpgkleqvyqalhkahpklhvykkeafptrfhyannsrvtslvlygdpgyvihgrfkvqfnkGE 346
Cdd:cd16018   222 ------------------------------------------------------------------------------GT 223

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2118037379 347 HGFDNMAMNMKTIFRAVGPAFRKGLEVDPFESVNVYALLCDLL 389
Cdd:cd16018   224 HGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLL 266
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 28-389 6.25e-104

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: 311.83  E-value: 6.25e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  28 KLLLVSFDGFRWNY-DQDVDTPNLDTMASEGVKARYMTPAFVTQTSPCHFTLLTGRYIENHGVIHNMWFNTSSGRKYSYY 106
Cdd:cd16018     2 PLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSDS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 107 DTQQksDWWDNGSLPIWISAQRQGLKAASLFFPGGNAIYQGEEVQVKKVEKKWHKYDNETEWRQNVDTVMEWFTKDDLDF 186
Cdd:cd16018    82 DWVW--DPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWLDLERPDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 187 VALYFGEPDSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINETGLVSRLNLIITSDHGMETVikeneihlatvanfsfqd 266
Cdd:cd16018   160 ILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------------ 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 267 lqfelldygphalllprpgkleqvyqalhkahpklhvykkeafptrfhyannsrvtslvlygdpgyvihgrfkvqfnkGE 346
Cdd:cd16018   222 ------------------------------------------------------------------------------GT 223

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2118037379 347 HGFDNMAMNMKTIFRAVGPAFRKGLEVDPFESVNVYALLCDLL 389
Cdd:cd16018   224 HGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLL 266
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 29-350 5.93e-90

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: 278.92  E-value: 5.93e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  29 LLLVSFDGFRWNY-DQDVDTPNLDTMASEGVKARYMTPAFVTQTSPCHFTLLTGRYIENHGVIHNMWFNTSSGRKYSYYD 107
Cdd:pfam01663   1 LLVISLDGFRADYlDRFELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 108 TQQKS-DWWDNGslPIWISAQRQGLKAASLFFPGGNAIYQGEEVQVKKVEKKwhKYDNETEWRQNVDTVM--EWFTKDDL 184
Cdd:pfam01663  81 SDPEDpRWWQGE--PIWDTAAKAGVRAAALFWPGSEVDYSTYYGTPPRYLKD--DYNNSVPFEDRVDTAVlqTWLDLPFA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 185 -------DFVALYFGEPDSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINETGLVSRLNLIITSDHGMETVIKENEIHLA 257
Cdd:pfam01663 157 dvaaerpDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLN 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 258 TVANFSfqdLQFELLDYGPHALLLPR--------PGKLEQVYQALHKA--------HPKLHVYKKEAFPTRFHYanNSRV 321
Cdd:pfam01663 237 DYLREK---GLLHLVDGGPVVAIYPKarelghvpPGEVEEVYAELKEKllglriqdGEHLAVYLKEEIPGRLHY--NPRI 311

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2118037379 322 TSLVLYGDPGYVIHGRFKVQFN---KGEHGFD 350
Cdd:pfam01663 312 PDLVLVADPGWYITGKDGGDKEaaiHGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 1-391 2.00e-67

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 221.16  E-value: 2.00e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379   1 MLSLLGLaatVLALGACAPLQEARNRTKLLLVSFDGFRWNYDQDVDTPNLDTMASEGVKARYMTPAFVTQTSPCHFTLLT 80
Cdd:COG1524     1 MKRGLSL---LLASLLAAAAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  81 GRYIENHGVIHNMWFNTSSGRKYSYYDTQQKSDWWDN--GSLPIWISAQRQGLKAASLFFPG--GNAIYQGEEVQVKKVE 156
Cdd:COG1524    78 GLYPGEHGIVGNGWYDPELGRVVNSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVFWPSfeGSGLIDAARPYPYDGR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 157 KKWHKYDNETEWRqnVDTVMEWFTKDDLDFVALYFGEPDSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINETGLVSRLN 236
Cdd:COG1524   158 KPLLGNPAADRWI--AAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 237 LIITSDHGMETVikENEIHLATvanfsFQDLQFELLDYGPHALLLPRPGKLEQVYQALhkaHPKLHVYKKEAFpTRFHYa 316
Cdd:COG1524   236 VIVTADHGMVDV--PPDIDLNR-----LRLAGLLAVRAGESAHLYLKDGADAEVRALL---GLPARVLTREEL-AAGHF- 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118037379 317 NNSRVTSLVLYGDPGYVIHGRFkvqfnKGEHGFDNmAMNMKTIFRAVGPAFRKGlevdpFESVNVYALLCDLLEI 391
Cdd:COG1524   304 GPHRIGDLVLVAKPGWALDAPL-----KGSHGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 28-389 6.25e-104

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: 311.83  E-value: 6.25e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  28 KLLLVSFDGFRWNY-DQDVDTPNLDTMASEGVKARYMTPAFVTQTSPCHFTLLTGRYIENHGVIHNMWFNTSSGRKYSYY 106
Cdd:cd16018     2 PLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSDS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 107 DTQQksDWWDNGSLPIWISAQRQGLKAASLFFPGGNAIYQGEEVQVKKVEKKWHKYDNETEWRQNVDTVMEWFTKDDLDF 186
Cdd:cd16018    82 DWVW--DPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWLDLERPDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 187 VALYFGEPDSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINETGLVSRLNLIITSDHGMETVikeneihlatvanfsfqd 266
Cdd:cd16018   160 ILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDV------------------ 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 267 lqfelldygphalllprpgkleqvyqalhkahpklhvykkeafptrfhyannsrvtslvlygdpgyvihgrfkvqfnkGE 346
Cdd:cd16018   222 ------------------------------------------------------------------------------GT 223

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2118037379 347 HGFDNMAMNMKTIFRAVGPAFRKGLEVDPFESVNVYALLCDLL 389
Cdd:cd16018   224 HGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLL 266
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 29-350 5.93e-90

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: 278.92  E-value: 5.93e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  29 LLLVSFDGFRWNY-DQDVDTPNLDTMASEGVKARYMTPAFVTQTSPCHFTLLTGRYIENHGVIHNMWFNTSSGRKYSYYD 107
Cdd:pfam01663   1 LLVISLDGFRADYlDRFELTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEYLVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 108 TQQKS-DWWDNGslPIWISAQRQGLKAASLFFPGGNAIYQGEEVQVKKVEKKwhKYDNETEWRQNVDTVM--EWFTKDDL 184
Cdd:pfam01663  81 SDPEDpRWWQGE--PIWDTAAKAGVRAAALFWPGSEVDYSTYYGTPPRYLKD--DYNNSVPFEDRVDTAVlqTWLDLPFA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 185 -------DFVALYFGEPDSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINETGLVSRLNLIITSDHGMETVIKENEIHLA 257
Cdd:pfam01663 157 dvaaerpDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLN 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 258 TVANFSfqdLQFELLDYGPHALLLPR--------PGKLEQVYQALHKA--------HPKLHVYKKEAFPTRFHYanNSRV 321
Cdd:pfam01663 237 DYLREK---GLLHLVDGGPVVAIYPKarelghvpPGEVEEVYAELKEKllglriqdGEHLAVYLKEEIPGRLHY--NPRI 311

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2118037379 322 TSLVLYGDPGYVIHGRFKVQFN---KGEHGFD 350
Cdd:pfam01663 312 PDLVLVADPGWYITGKDGGDKEaaiHGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 1-391 2.00e-67

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 221.16  E-value: 2.00e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379   1 MLSLLGLaatVLALGACAPLQEARNRTKLLLVSFDGFRWNYDQDVDTPNLDTMASEGVKARYMTPAFVTQTSPCHFTLLT 80
Cdd:COG1524     1 MKRGLSL---LLASLLAAAAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  81 GRYIENHGVIHNMWFNTSSGRKYSYYDTQQKSDWWDN--GSLPIWISAQRQGLKAASLFFPG--GNAIYQGEEVQVKKVE 156
Cdd:COG1524    78 GLYPGEHGIVGNGWYDPELGRVVNSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVFWPSfeGSGLIDAARPYPYDGR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 157 KKWHKYDNETEWRqnVDTVMEWFTKDDLDFVALYFGEPDSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINETGLVSRLN 236
Cdd:COG1524   158 KPLLGNPAADRWI--AAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 237 LIITSDHGMETVikENEIHLATvanfsFQDLQFELLDYGPHALLLPRPGKLEQVYQALhkaHPKLHVYKKEAFpTRFHYa 316
Cdd:COG1524   236 VIVTADHGMVDV--PPDIDLNR-----LRLAGLLAVRAGESAHLYLKDGADAEVRALL---GLPARVLTREEL-AAGHF- 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118037379 317 NNSRVTSLVLYGDPGYVIHGRFkvqfnKGEHGFDNmAMNMKTIFRAVGPAFRKGlevdpFESVNVYALLCDLLEI 391
Cdd:COG1524   304 GPHRIGDLVLVAKPGWALDAPL-----KGSHGGLP-DEEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGL 367
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 29-292 7.65e-20

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 88.63  E-value: 7.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  29 LLLVSFDGFRWNYDQD-----VDTPNLDTMASEGVKARYMTPAFVTQTSPCHFTLLTGRYIENHGVIHNMWFNTSsgrky 103
Cdd:cd00016     3 VVLIVLDGLGADDLGKagnpaPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPE----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 104 syydTQQKSDWWDNGSLPIWISAQRQGLKAASLFFpggnaiyqgeevqvkkvekkwhkydnetewrqnvDTVMEWFTKDD 183
Cdd:cd00016    78 ----LPSRAAGKDEDGPTIPELLKQAGYRTGVIGL----------------------------------LKAIDETSKEK 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 184 LDFVALYFGEPDSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINETGLVSRLNLIITSDHGMETVIKENEIHLATVANFS 263
Cdd:cd00016   120 PFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADGKADKS 199

                         250       260
                  ....*....|....*....|....*....
gi 2118037379 264 FQDLQFELLDYGPHAlllPRPGKLEQVYQ 292
Cdd:cd00016   200 HTGMRVPFIAYGPGV---KKGGVKHELIS 225
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 41-245 4.65e-09

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: 58.29  E-value: 4.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  41 YDQDVDTPNLDTMASEGVkaRYmTPAFVTQT--SPCHFTLLTGRYIENHGVIHNMWfntssgRKYSYYDTQQksdwwdng 118
Cdd:cd16027    19 GGNVVKTPNLDRLAAEGV--RF-TNAFTTAPvcSPSRSALLTGLYPHQNGAHGLRS------RGFPLPDGVK-------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 119 SLPIWisaqrqgLKAAslffpG---GNA---IYQGEEVqVKKVEKKWHKYDNETEWRQNVDTVMEWFTKDDLD--FVALY 190
Cdd:cd16027    82 TLPEL-------LREA-----GyytGLIgktHYNPDAV-FPFDDEMRGPDDGGRNAWDYASNAADFLNRAKKGqpFFLWF 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 191 --------FGEPDSTGHKYGPES-----------QQRKDM------VKQVDRTVGYLRQRINETGL-----VsrlnlIIT 240
Cdd:cd16027   149 gfhdphrpYPPGDGEEPGYDPEKvkvppylpdtpEVREDLadyydeIERLDQQVGEILDELEEDGLldntiV-----IFT 223


                  ....*
gi 2118037379 241 SDHGM 245
Cdd:cd16027   224 SDHGM 228
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
11-244 4.44e-07

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 52.19  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  11 VLALGACAPLQEARNRTKLLLVSFDGFRWNY-----DQDVDTPNLDTMASEGVKaryMTPAFVTQ--TSPCHFTLLTGRY 83
Cdd:COG3119     8 LLALLAAAAAAAAAKRPNILFILADDLGYGDlgcygNPLIKTPNIDRLAAEGVR---FTNAYVTSpvCSPSRASLLTGRY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  84 IENHGVIHNMWFNTSSGRKysyydtqqksdwwDNGSLPiwisaqrQGLKAAslffpGgnaiYQ----GeevqvkkvekKW 159
Cdd:COG3119    85 PHRTGVTDNGEGYNGGLPP-------------DEPTLA-------ELLKEA-----G----YRtalfG----------KW 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 160 HKYdnETEWrqNVDTVMEWF---TKDD-------------------LDFVALYFGEPDSTGHKYGPESQQRK-------- 209
Cdd:COG3119   126 HLY--LTDL--LTDKAIDFLerqADKDkpfflylafnaphapyqapEEYLDKYDGKDIPLPPNLAPRDLTEEelrraraa 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2118037379 210 --DMVKQVDRTVGYLRQRINETGL-----VsrlnlIITSDHG 244
Cdd:COG3119   202 yaAMIEEVDDQVGRLLDALEELGLadntiV-----VFTSDNG 238
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 29-92 5.85e-07

Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.


Pssm-ID: 293752 [Multi-domain]  Cd Length: 449  Bit Score: 51.88  E-value: 5.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118037379  29 LLLVSFDGFRWNY-----DQDVDTPNLDTMASEGVkarymtpAF---VTQTSPC---HFTLLTGRYIENHGVIHN 92
Cdd:cd16028     3 VLFITADQWRADClsclgHPLVKTPNLDRLAAEGV-------RFrnhYTQAAPCgpsRASLYTGRYLMNHRSVWN 70
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 44-244 1.12e-06

sulfatase; 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: 293746 [Multi-domain]  Cd Length: 236  Bit Score: 49.74  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  44 DVDTPNLDTMASEGVKaryMTPAFVTQT--SPCHFTLLTGRYIENHGVIHNMwfntssgrkysyydtqqksdwWDNGSLP 121
Cdd:cd16022    23 DIKTPNLDRLAAEGVR---FTNAYVASPvcSPSRASLLTGRYPHRHGVRGNV---------------------GNGGGLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 122 IWIS--AQRqgLKAAslffpGgnaiYQ----GeevqvkkvekKWHkydnetewrqnvDTVMEWFTKDDLD---FVALYFG 192
Cdd:cd16022    79 PDEPtlAEL--LKEA-----G----YRtaliG----------KWH------------DEAIDFIERRDKDkpfFLYVSFN 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2118037379 193 EPDSTGHKYGpesqqrkdMVKQVDRTVGYLRQRINETGLvsrLN--LII-TSDHG 244
Cdd:cd16022   126 APHPPFAYYA--------MVSAIDDQIGRILDALEELGL---LDntLIVfTSDHG 169
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 42-244 1.49e-06

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: 50.26  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  42 DQDVDTPNLDTMASEGVkarYMTPAFVTQ--TSPCHFTLLTGRYIENHGVIHNMW------------FNtSSGRKYSY-- 105
Cdd:cd16034    22 DDPVKTPNLDRLAKEGV---VFTNAVSNYpvCSPYRASLLTGQYPLTNGVFGNDVplppdaptiadvLK-DAGYRTGYig 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 106 ----YDTQQKSDWWDNgslPIWISAQRQG---LKAASLFFPGGNAIYQGEEvQVKKVEKKW------------------- 159
Cdd:cd16034    98 kwhlDGPERNDGRADD---YTPPPERRHGfdyWKGYECNHDHNNPHYYDDD-GKRIYIKGYspdaetdlaieylenqadk 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 160 -------------H--------KYDN-----ETEWRQNVDTVMEWfTKDDLDFVALYFGepdstghkygpesqqrkdMVK 213
Cdd:cd16034   174 dkpfalvlswnppHdpyttapeEYLDmydpkKLLLRPNVPEDKKE-EAGLREDLRGYYA------------------MIT 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2118037379 214 QVDRTVGYLRQRINETGLVSRLNLIITSDHG 244
Cdd:cd16034   235 ALDDNIGRLLDALKELGLLENTIVVFTSDHG 265
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 28-246 2.57e-06

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: 49.08  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  28 KLLLVSFDGFRW------NYDQDVdTPNLDTMASEGVK-ARYMTPAFVTQTSpcHFTLLTGRYIENHGVIHnmwfntssg 100
Cdd:cd16148     2 NVILIVIDSLRAdhlgcyGYDRVT-TPNLDRLAAEGVVfDNHYSGSNPTLPS--RFSLFTGLYPFYHGVWG--------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 101 rkysyydtqqksdWWDNGSLPIWISA-QRQGLKAASL----FFPGGNAIYQGEEVQVKKVEKKWHKYDNETE-WRQNVDT 174
Cdd:cd16148    70 -------------GPLEPDDPTLAEIlRKAGYYTAAVssnpHLFGGPGFDRGFDTFEDFRGQEGDPGEEGDErAERVTDR 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118037379 175 VMEWFTKDDLD---FVALYFGEPdstgH---KYGPEsqqrkdmVKQVDRTVGYLRQRINETGLVSRLNLIITSDHGME 246
Cdd:cd16148   137 ALEWLDRNADDdpfFLFLHYFDP----HepyLYDAE-------VRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEE 203
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 42-244 3.13e-05

unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.


Pssm-ID: 293755 [Multi-domain]  Cd Length: 429  Bit Score: 46.37  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  42 DQDVDTPNLDTMASEGVkarYMTPAFVTqTSPC---HFTLLTGRYIENHGVIhnmwFNTSSGRKY---SYYDTQQKSDW- 114
Cdd:cd16031    23 NPIVKTPNIDRLAKEGV---RFDNAFVT-TSICapsRASILTGQYSHRHGVT----DNNGPLFDAsqpTYPKLLRKAGYq 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 115 ------W---DNGSLPI-----WISAQRQGlkaasLFFPGGNaIYQGEEVQ----------------VKKVEKK------ 158
Cdd:cd16031    95 tafigkWhlgSGGDLPPpgfdyWVSFPGQG-----SYYDPEF-IENGKRVGqkgyvtdiitdkaldfLKERDKDkpfcls 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 159 -WHK---------------YDN------ETEWRQNVDTVMEWFtKDDLDFVALYFGEPDSTGHKYgpesqQR--KD---M 211
Cdd:cd16031   169 lSFKaphrpftpaprhrglYEDvtipepETFDDDDYAGRPEWA-REQRNRIRGVLDGRFDTPEKY-----QRymKDylrT 242

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2118037379 212 VKQVDRTVGYLRQRINETGLVSrlNLII--TSDHG 244
Cdd:cd16031   243 VTGVDDNVGRILDYLEEQGLAD--NTIIiyTSDNG 275
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 26-244 5.64e-05

SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.


Pssm-ID: 293740 [Multi-domain]  Cd Length: 457  Bit Score: 45.60  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  26 RTKLLL-VSFDGFRWNYdqdvdtpnLD------------TMASEGV---KARYMTPAfvTQTSPCHFTLLTGRYIENHGV 89
Cdd:cd16016     1 RPKLVVgIVVDQMRADY--------LYryrdrfgeggfkRLLNEGFvfeNAHYNYAP--TDTAPGHATIYTGTTPAIHGI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  90 IHNMWFNTSSGRK-YSYYDTQQK---------------------SDW----WDNGSLPIWISaqrqgLKAASLFFPGG-- 141
Cdd:cd16016    71 IGNDWYDRETGREvYCVEDSTVTtvggnstagkmsprnllvttiGDElklaTNGRSKVIGVA-----LKDRAAILPAGha 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 142 -NAIYqgeevqvkkvekkWhkYDNET--------------EWRQN--------VDTVMEWFTK-----------DDLDFV 187
Cdd:cd16016   146 aDAAY-------------W--FDDETgkfitstyymkelpAWVEKfnakklpfGNTLTLDFAKaaleneklgkdDVTDLL 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118037379 188 ALYFGEPDSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINET-GLVSRLnLIITSDHG 244
Cdd:cd16016   211 AVSFSATDYIGHAFGPNSVEMEDTYLRLDRDLARLLDALDKKvGKGNYL-VFLTADHG 267
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 43-249 5.82e-05

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 45.28  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  43 QDVDTPNLDTMASEGVKAR--YMTPafvtQTSPCHFTLLTGRYIENHGVIHNMWF--NTSSGR--KYSYYDTQQKSDWWD 116
Cdd:cd16151    22 ESYKTPNIDALAAEGVRFNnaYAQP----LCTPSRVQLMTGKYNFRNYVVFGYLDpkQKTFGHllKDAGYATAIAGKWQL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 117 NGSLPIWISAQRQGLKAASLFfpggnaiyqgeevQVKKVEKKWHKYDNETEWRQN---VDTVMEWFTKDD-----LDFVA 188
Cdd:cd16151    98 GGGRGDGDYPHEFGFDEYCLW-------------QLTETGEKYSRPATPTFNIRNgklLETTEGDYGPDLfadflIDFIE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 189 --------LYF----------GEPDSTGHKYGPESQQR-----KDMVKQVDRTVGYLRQRINETGLvsRLNLII--TSDH 243
Cdd:cd16151   165 rnkdqpffAYYpmvlvhdpfvPTPDSPDWDPDDKRKKDdpeyfPDMVAYMDKLVGKLVDKLEELGL--RENTIIifTGDN 242


                  ....*.
gi 2118037379 244 GMETVI 249
Cdd:cd16151   243 GTHRPI 248
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 35-92 7.11e-05

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 44.91  E-value: 7.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118037379  35 DGFRWN----YDQDVD-TPNLDTMASEGVKARYmtpAFVTQ--TSPCHFTLLTGRYIENHGVIHN 92
Cdd:cd16152    10 DQQRWDtlgcYGQPLDlTPNLDALAEEGVLFEN---AFTPQpvCGPARACLQTGLYPTETGCFRN 71
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 180-245 1.73e-04

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: 43.50  E-value: 1.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118037379 180 TKDDLDFVALYFGEPDSTGHKYG-PESQQRKDMVKQVDRTVGYLRQRINETGLvsrlnLIITSDHGM 245
Cdd:cd16019   149 YYDNWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDNDTL-----LVVVSDHGM 210
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 44-89 2.27e-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: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 43.00  E-value: 2.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2118037379  44 DVDTPNLDTMASEGVKaryMTPAFVTQ--TSPCHFTLLTGRYIENHGV 89
Cdd:cd16149    23 EAVTPNLDRLAAEGVR---FENFFCTSpvCSPARASLLTGRMPSQHGI 67
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 45-93 2.63e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 43.36  E-value: 2.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2118037379  45 VDTPNLDTMASEGVK-ARYMTPAFVTqtSPCHFTLLTGRYIENHGVIHNM 93
Cdd:cd16033    24 VKTPNIDRLAAEGVRfTNAYTPSPVC--CPARASLLTGLYPHEHGVLNNV 71
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 45-99 2.92e-04

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 42.75  E-value: 2.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118037379  45 VDTPNLDTMASEGVkarYMTPAFvTQT---SPCHFTLLTGRYIENHGVIHNMWFNTSS 99
Cdd:cd16153    35 VESPNIDALAAEGV---LFTNAY-CNSpvcVPSRTSMLTGRYPHRTGVYGFEAAHPAL 88
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 42-130 2.14e-03

glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).


Pssm-ID: 293766 [Multi-domain]  Cd Length: 396  Bit Score: 40.61  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379  42 DQDVDTPNLDTM-------ASEGVkarYMTPAFVTqTSPC---HFTLLTGRYIENHGVIHNmwfntssGRKYSYYDTqqk 111
Cdd:cd16147    11 DQDVELGSMDPMpktkkllADQGT---TFTNAFVT-TPLCcpsRASILTGQYAHNHGVTNN-------SPPGGGYPK--- 76

                          90       100
                  ....*....|....*....|...
gi 2118037379 112 sdWWDNG----SLPIWIsaQRQG 130
Cdd:cd16147    77 --FWQNGlersTLPVWL--QEAG 95
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 181-244 2.65e-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: 40.08  E-value: 2.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037379 181 KDDLDFVALYFGEPDSTGHkygpesqqRKDM------VKQVDRTVGYLRQRINETGLVsrlnLIITSDHG 244
Cdd:pfam01676 297 KEKYDFVFVNFANTDMVGH--------TGDVegkvkaIEAVDERLGELLDALEEDDGL----LIITADHG 354
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
 45-101 3.14e-03

uncharacterized arylsulfatase; 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: 293765 [Multi-domain]  Cd Length: 409  Bit Score: 39.84  E-value: 3.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118037379  45 VDTPNLDTMASEGVkarYMTPAFVTQT-SPCHFTLLTGRYIENHGVIHnmwfnTSSGR 101
Cdd:cd16146    24 LKTPNLDRLAAESV---RFTNFHVSPVcAPTRAALLTGRYPFRTGVWH-----TILGR 73
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 43-83 3.78e-03

galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.


Pssm-ID: 293750 [Multi-domain]  Cd Length: 399  Bit Score: 39.47  E-value: 3.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2118037379  43 QDVDTPNLDTMASEGVKAR-YMTPAFVtqTSPCHFTLLTGRY 83
Cdd:cd16026    23 PLIKTPNIDRLAAEGVRFTdFYAAAPV--CSPSRAALLTGRY 62
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 195-245 4.58e-03

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: 39.08  E-value: 4.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2118037379 195 DSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINETGLvsrlnLIITSDHGM 245
Cdd:cd16023   171 DHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTL-----LLVFGDHGM 216
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 195-245 7.83e-03

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: 38.34  E-value: 7.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2118037379 195 DSTGHKYGPESQQRKDMVKQVDRTVGYLRQRINETGLVSRLNLIITSDHGM 245
Cdd:cd16020   168 DTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGM 218
 
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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