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Conserved domains on  [gi|1800043704|ref|XP_031996636|]
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bis(5'-adenosyl)-triphosphatase ENPP4 [Hylobates moloch]

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 ...
 29-382 2.66e-108

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: 321.07  E-value: 2.66e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  29 PKLLLVSFDGFRADYL-KNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKKHFSD 107
Cdd:cd16018     1 PPLIVISIDGFRWDYLdRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 108 SNDKDPFWWNEAVPIWVTNQLQeNRSSAAAMWPGTDVPIHNT------ISSYFMNYNSSVSFEERLNNITIWLNNSNPpv 181
Cdd:cd16018    81 SDWVWDPWWIGGEPIWVTAEKA-GLKTASYFWPGSEVAIIGYnptpipLGGYWQPYNDSFPFEERVDTILEWLDLERP-- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 182 TFAALYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQKLKMLGLWENLNVIITSDHGMTQcsqdrlinldfcidhs 261
Cdd:cd16018   158 DLILLYFEEPDSAGHKYGPDSPE-VNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTD---------------- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 262 yytlidlspvaailpkinrtevynklkncsphmnvylkedipnrfyyqhndriqpiilvadegwaivlnessqkLGDHGY 341
Cdd:cd16018   221 --------------------------------------------------------------------------VGTHGY 226

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1800043704 342 DNSLPSMHPFLAAHGPAFHRGYKHSTINIVDIYPMMCHILG 382
Cdd:cd16018   227 DNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 29-382 2.66e-108

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: 321.07  E-value: 2.66e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  29 PKLLLVSFDGFRADYL-KNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKKHFSD 107
Cdd:cd16018     1 PPLIVISIDGFRWDYLdRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 108 SNDKDPFWWNEAVPIWVTNQLQeNRSSAAAMWPGTDVPIHNT------ISSYFMNYNSSVSFEERLNNITIWLNNSNPpv 181
Cdd:cd16018    81 SDWVWDPWWIGGEPIWVTAEKA-GLKTASYFWPGSEVAIIGYnptpipLGGYWQPYNDSFPFEERVDTILEWLDLERP-- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 182 TFAALYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQKLKMLGLWENLNVIITSDHGMTQcsqdrlinldfcidhs 261
Cdd:cd16018   158 DLILLYFEEPDSAGHKYGPDSPE-VNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTD---------------- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 262 yytlidlspvaailpkinrtevynklkncsphmnvylkedipnrfyyqhndriqpiilvadegwaivlnessqkLGDHGY 341
Cdd:cd16018   221 --------------------------------------------------------------------------VGTHGY 226

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1800043704 342 DNSLPSMHPFLAAHGPAFHRGYKHSTINIVDIYPMMCHILG 382
Cdd:cd16018   227 DNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 31-342 3.85e-103

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: 310.89  E-value: 3.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  31 LLLVSFDGFRADYLKNYE-FPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKK--HFSD 107
Cdd:pfam01663   1 LLVISLDGFRADYLDRFElTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEylVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 108 SNDKDPFWWNEAvPIWVTNQLQeNRSSAAAMWPGTDVPIHNTISS----YFMNYNSSVSFEERLNNITI--WLNNSNP-- 179
Cdd:pfam01663  81 SDPEDPRWWQGE-PIWDTAAKA-GVRAAALFWPGSEVDYSTYYGTppryLKDDYNNSVPFEDRVDTAVLqtWLDLPFAdv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 180 ---PVTFAALYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQKLKMLGLWENLNVIITSDHGMTQCSQDRLINLDF 256
Cdd:pfam01663 159 aaeRPDLLLVYLEEPDYAGHRYGPDSPE-VEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLND 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 257 CIDHS-YYTLIDLSPVAAILPK---------INRTEVYNKLKNCS--------PHMNVYLKEDIPNRFYYqhNDRIQPII 318
Cdd:pfam01663 238 YLREKgLLHLVDGGPVVAIYPKarelghvppGEVEEVYAELKEKLlglriqdgEHLAVYLKEEIPGRLHY--NPRIPDLV 315

                         330       340
                  ....*....|....*....|....*...
gi 1800043704 319 LVADEGWAIVLNESSQKL----GDHGYD 342
Cdd:pfam01663 316 LVADPGWYITGKDGGDKEaaihGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 4-384 1.18e-71

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 230.79  E-value: 1.18e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704   4 MKLLVILLFSGLITGCRSDSSSslPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTG 83
Cdd:COG1524     1 MKRGLSLLLASLLAAAAAAAPP--AKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  84 LYEESHGIVANSMYDAVTKKH-FSDSNDKDPFWWNEAV---PIWVTnqLQEN-RSSAAAMWPGTDVpihntisSYFMNYN 158
Cdd:COG1524    79 LYPGEHGIVGNGWYDPELGRVvNSLSWVEDGFGSNSLLpvpTIFER--ARAAgLTTAAVFWPSFEG-------SGLIDAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 159 SSVSFEERLN------------NITIWLNNSNPPvTFAALYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQKLKM 226
Cdd:COG1524   150 RPYPYDGRKPllgnpaadrwiaAAALELLREGRP-DLLLVYLPDLDYAGHRYGPDSPE-YRAALREVDAALGRLLDALKA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 227 LGLWENLNVIITSDHGMTQCSQDRLINLdfcIDHSYYTLIDLSPVAAILPKINRTE-VYNKLKNcspHMNVYLKEDIpNR 305
Cdd:COG1524   228 RGLYEGTLVIVTADHGMVDVPPDIDLNR---LRLAGLLAVRAGESAHLYLKDGADAeVRALLGL---PARVLTREEL-AA 300

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800043704 306 FYYQHNdRIQPIILVADEGWAIvlneSSQKLGDHGYDNSlPSMHPFLAAHGPAFHRGykhstINIVDIYPMMCHILGLK 384
Cdd:COG1524   301 GHFGPH-RIGDLVLVAKPGWAL----DAPLKGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 29-382 2.66e-108

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: 321.07  E-value: 2.66e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  29 PKLLLVSFDGFRADYL-KNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKKHFSD 107
Cdd:cd16018     1 PPLIVISIDGFRWDYLdRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 108 SNDKDPFWWNEAVPIWVTNQLQeNRSSAAAMWPGTDVPIHNT------ISSYFMNYNSSVSFEERLNNITIWLNNSNPpv 181
Cdd:cd16018    81 SDWVWDPWWIGGEPIWVTAEKA-GLKTASYFWPGSEVAIIGYnptpipLGGYWQPYNDSFPFEERVDTILEWLDLERP-- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 182 TFAALYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQKLKMLGLWENLNVIITSDHGMTQcsqdrlinldfcidhs 261
Cdd:cd16018   158 DLILLYFEEPDSAGHKYGPDSPE-VNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTD---------------- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 262 yytlidlspvaailpkinrtevynklkncsphmnvylkedipnrfyyqhndriqpiilvadegwaivlnessqkLGDHGY 341
Cdd:cd16018   221 --------------------------------------------------------------------------VGTHGY 226

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1800043704 342 DNSLPSMHPFLAAHGPAFHRGYKHSTINIVDIYPMMCHILG 382
Cdd:cd16018   227 DNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 31-342 3.85e-103

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: 310.89  E-value: 3.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  31 LLLVSFDGFRADYLKNYE-FPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKK--HFSD 107
Cdd:pfam01663   1 LLVISLDGFRADYLDRFElTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEylVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 108 SNDKDPFWWNEAvPIWVTNQLQeNRSSAAAMWPGTDVPIHNTISS----YFMNYNSSVSFEERLNNITI--WLNNSNP-- 179
Cdd:pfam01663  81 SDPEDPRWWQGE-PIWDTAAKA-GVRAAALFWPGSEVDYSTYYGTppryLKDDYNNSVPFEDRVDTAVLqtWLDLPFAdv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 180 ---PVTFAALYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQKLKMLGLWENLNVIITSDHGMTQCSQDRLINLDF 256
Cdd:pfam01663 159 aaeRPDLLLVYLEEPDYAGHRYGPDSPE-VEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLND 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 257 CIDHS-YYTLIDLSPVAAILPK---------INRTEVYNKLKNCS--------PHMNVYLKEDIPNRFYYqhNDRIQPII 318
Cdd:pfam01663 238 YLREKgLLHLVDGGPVVAIYPKarelghvppGEVEEVYAELKEKLlglriqdgEHLAVYLKEEIPGRLHY--NPRIPDLV 315

                         330       340
                  ....*....|....*....|....*...
gi 1800043704 319 LVADEGWAIVLNESSQKL----GDHGYD 342
Cdd:pfam01663 316 LVADPGWYITGKDGGDKEaaihGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 4-384 1.18e-71

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 230.79  E-value: 1.18e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704   4 MKLLVILLFSGLITGCRSDSSSslPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTG 83
Cdd:COG1524     1 MKRGLSLLLASLLAAAAAAAPP--AKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  84 LYEESHGIVANSMYDAVTKKH-FSDSNDKDPFWWNEAV---PIWVTnqLQEN-RSSAAAMWPGTDVpihntisSYFMNYN 158
Cdd:COG1524    79 LYPGEHGIVGNGWYDPELGRVvNSLSWVEDGFGSNSLLpvpTIFER--ARAAgLTTAAVFWPSFEG-------SGLIDAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 159 SSVSFEERLN------------NITIWLNNSNPPvTFAALYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQKLKM 226
Cdd:COG1524   150 RPYPYDGRKPllgnpaadrwiaAAALELLREGRP-DLLLVYLPDLDYAGHRYGPDSPE-YRAALREVDAALGRLLDALKA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 227 LGLWENLNVIITSDHGMTQCSQDRLINLdfcIDHSYYTLIDLSPVAAILPKINRTE-VYNKLKNcspHMNVYLKEDIpNR 305
Cdd:COG1524   228 RGLYEGTLVIVTADHGMVDVPPDIDLNR---LRLAGLLAVRAGESAHLYLKDGADAeVRALLGL---PARVLTREEL-AA 300

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1800043704 306 FYYQHNdRIQPIILVADEGWAIvlneSSQKLGDHGYDNSlPSMHPFLAAHGPAFHRGykhstINIVDIYPMMCHILGLK 384
Cdd:COG1524   301 GHFGPH-RIGDLVLVAKPGWAL----DAPLKGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 29-244 7.54e-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: 88.25  E-value: 7.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  29 PKLLLVSFDGFRADYL-KNYEFPHLQNFIK----EGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKK 103
Cdd:cd00016     1 KHVVLIVLDGLGADDLgKAGNPAPTTPNLKrlasEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 104 HFSDSNDKDPFWWNeavpiwvtnQLQENRSSAAAMwpgtdvpihntissyfmnynssvSFEERLNNITiwlnNSNPpvTF 183
Cdd:cd00016    81 RAAGKDEDGPTIPE---------LLKQAGYRTGVI-----------------------GLLKAIDETS----KEKP--FV 122

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800043704 184 AALYWEEPDASGHKYGPeDKENMSRVLKKIDDLIGDLVQKLKMLGLWENLNVIITSDHGMT 244
Cdd:cd00016   123 LFLHFDGPDGPGHAYGP-NTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGI 182
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 29-242 1.79e-10

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: 61.41  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  29 PKLLLVSFDGFRADYLKNYEF-----PHLQNFIKEGVLVEhvkNVFITK--TFPNHYSIVTGLYEESHGIVANSMydavt 101
Cdd:cd16148     1 MNVILIVIDSLRADHLGCYGYdrvttPNLDRLAAEGVVFD---NHYSGSnpTLPSRFSLFTGLYPFYHGVWGGPL----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 102 kkhfsdsndkdpfwwnEAVPIWVTNQLQEN------RSSAAAMWPGTdvPIHNTISSYFMNY-------NSSVSFEERLN 168
Cdd:cd16148    73 ----------------EPDDPTLAEILRKAgyytaaVSSNPHLFGGP--GFDRGFDTFEDFRgqegdpgEEGDERAERVT 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 169 NITI-WL--NNSNPPVtFAAL-YWE--EP---DASghkygpedkenmsrvLKKIDDLIGDLVQKLKMLGLWENLNVIITS 239
Cdd:cd16148   135 DRALeWLdrNADDDPF-FLFLhYFDphEPylyDAE---------------VRYVDEQIGRLLDKLKELGLLEDTLVIVTS 198


                  ...
gi 1800043704 240 DHG 242
Cdd:cd16148   199 DHG 201
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 28-388 5.88e-08

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: 54.85  E-value: 5.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  28 PPKLLL-VSFDGFRADYLknYEF-PHLQN-----FIKEGVlveHVKNVFI----TKTFPNHYSIVTGLYEESHGIVANSM 96
Cdd:cd16016     1 RPKLVVgIVVDQMRADYL--YRYrDRFGEggfkrLLNEGF---VFENAHYnyapTDTAPGHATIYTGTTPAIHGIIGNDW 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  97 YDAVTKKhfSDSNDKDPfwwneAVPIWVTNQLQENRS-------------------------------SA---------A 136
Cdd:cd16016    76 YDRETGR--EVYCVEDS-----TVTTVGGNSTAGKMSprnllvttigdelklatngrskvigvalkdrAAilpaghaadA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 137 AMWPGTDVPihNTISS-YFM--------NYNSS---------VSF------EERL--NNITIWLNnsnppVTFAAlywee 190
Cdd:cd16016   149 AYWFDDETG--KFITStYYMkelpawveKFNAKklpfgntltLDFakaaleNEKLgkDDVTDLLA-----VSFSA----- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 191 PDASGHKYGPEDKENMSRVLkKIDDLIGDLVQKL-KMLGLwENLNVIITSDHG--------------MTQCSQDRLI--- 252
Cdd:cd16016   217 TDYIGHAFGPNSVEMEDTYL-RLDRDLARLLDALdKKVGK-GNYLVFLTADHGaadnpeflkdhkipAGRFDPKRLKall 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 253 --------NLDFCIDHSYYTLIDLSPVAAILPKINRTEVYNKLKNC-----------------SPHMNVYLKEDIPNRFY 307
Cdd:cd16016   295 naylmakyGLGKWVLGYSNGQVYLNHKLIEEKGLDLAEVQAAAAEFllqmpgvaaaytadellAGPEPTGIRERLRNGYN 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 308 YQHN-DriqpIILVADEGWaiVLNESSQKLGDHG----YDNSLPSMhpFLAAHGPAFHRgykHSTINIVDIYPMMCHILG 382
Cdd:cd16016   375 PKRSgD----LIVVLKPGW--IEGDGSGKGTTHGspydYDTHVPLL--FYGWGIKPGEI---PRPVEITDIAPTLAALLG 443


                  ....*.
gi 1800043704 383 LKPhPN 388
Cdd:cd16016   444 IQP-PN 448
Sulfatase pfam00884
Sulfatase;
29-242 3.21e-06

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 48.57  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  29 PKLLLVSFDGFRADYLKNY-----EFPHLQNFIKEGVLvehvknvfitktFPNHYS-----------IVTGLYEESHGIV 92
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYgyprpTTPFLDRLAEEGLL------------FSNFYSggtltapsrfaLLTGLPPHNFGSY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  93 ANSM------------------YD--AVTKKHFSdsndkdpFWWNEAVPIWVTNQLQENRSSAAAMWPGTDVPIHNTISS 152
Cdd:pfam00884  69 VSTPvglprtepslpdllkragYNtgAIGKWHLG-------WYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 153 YFMN--YNSSVSFEERLNN---ITIWLNNSNPPVTFAALYwEEPDASGHKYGPEDKENMS---RVLKKIDDLIGDLVQKL 224
Cdd:pfam00884 142 VSDEalLDEALEFLDNNDKpffLVLHTLGSHGPPYYPDRY-PEKYATFKPSSCSEEQLLNsydNTLLYTDDAIGRVLDKL 220

                         250
                  ....*....|....*...
gi 1800043704 225 KMLGLWENLNVIITSDHG 242
Cdd:pfam00884 221 EENGLLDNTLVVYTSDHG 238
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
4-242 5.35e-06

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 48.34  E-value: 5.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704   4 MKLLVILLFSGLITGCRSDSSSslPPKLLLVSFDGFRADYL-----KNYEFPHLQNFIKEGVlvehvknvfitkTFPNHY 78
Cdd:COG3119     1 MKRLLLLLLALLAAAAAAAAAK--RPNILFILADDLGYGDLgcygnPLIKTPNIDRLAAEGV------------RFTNAY 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  79 -----------SIVTGLYEESHGIVANSmydavtkkhfsdsnDKDPFWWNEAVPIWVtNQLQEN--RSSAAAMWpgtdvp 145
Cdd:COG3119    67 vtspvcspsraSLLTGRYPHRTGVTDNG--------------EGYNGGLPPDEPTLA-ELLKEAgyRTALFGKW------ 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 146 iHNTISSYFMNYnsSVSF-EERLNN-----ITIWLNN----SNPPVTFAALYWEE---------PDASGHKYGPEDKENM 206
Cdd:COG3119   126 -HLYLTDLLTDK--AIDFlERQADKdkpffLYLAFNAphapYQAPEEYLDKYDGKdiplppnlaPRDLTEEELRRARAAY 202

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1800043704 207 SRVLKKIDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:COG3119   203 AAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG 238
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 213-251 8.73e-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: 47.95  E-value: 8.73e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1800043704 213 IDDLIGDLVQKLKMLGLWENLNVIITSDHGMTQCSQDRL 251
Cdd:cd16034   236 LDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM 274
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 30-245 2.26e-05

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: 46.20  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  30 KLLLVSFDGFRADYLKN-YEFPHLQNFIKEgvLVEHVKNVFI--------TKTFPNHYSIVTGlyeeshgIVANSMyDAv 100
Cdd:cd16019     6 KVVLIVIDGLRYDLAVNvNKQSSFFSFLQK--LNEQPNNSFLalsfadppTVTGPRLKALTTG-------NPPTFL-DL- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 101 tKKHFSDSNDKDPFWwneavpiwvTNQLQENRSSAAAMwpGTDV-----PIHNTISSYFMNYNSSVSFEERL---NNITI 172
Cdd:cd16019    75 -ISNFASSEIKEDNI---------IRQLKKNGKKILFY--GDDTwldlfPEIFTYKFTITSFNIRDMHDVDPifyNHIND 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1800043704 173 WL--NNSNPPVTFAALYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQKLKmlglwENLNVIITSDHGMTQ 245
Cdd:cd16019   143 NLdeNIYYDNWDFIILHFLGLDHLGHKHNTTSSPELEKKLDQMDNLIRDIYDRMD-----NDTLLVVVSDHGMNN 212
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 213-242 3.42e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 46.06  E-value: 3.42e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1800043704 213 IDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:cd16033   226 IDDAIGRILDALEELGLADDTLVIFTSDHG 255
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 50-243 5.83e-05

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: 45.19  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  50 PHLQNFIKEGVLvehvknvfitktFPNHY-----------SIVTGLYEESHGIVAN-----SMYDAVT------------ 101
Cdd:cd16027    26 PNLDRLAAEGVR------------FTNAFttapvcspsrsALLTGLYPHQNGAHGLrsrgfPLPDGVKtlpellreagyy 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 102 -----KKHFSDsnDKDPFWWNEAVPIWVTNQLQENRSSAAAMW---PGTDVPihntissYFMNYNSSVSFEERLNNITIW 173
Cdd:cd16027    94 tgligKTHYNP--DAVFPFDDEMRGPDDGGRNAWDYASNAADFlnrAKKGQP-------FFLWFGFHDPHRPYPPGDGEE 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1800043704 174 LNNSNPPVTFAAlYWeePDasghkyGPEDKENMSRVLKKI---DDLIGDLVQKLKMLGLWENLNVIITSDHGM 243
Cdd:cd16027   165 PGYDPEKVKVPP-YL--PD------TPEVREDLADYYDEIerlDQQVGEILDELEEDGLLDNTIVIFTSDHGM 228
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 195-244 6.44e-05

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: 44.47  E-value: 6.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1800043704 195 GHKYGPEDKEnMSRVLKKIDDLIGDLVQKLKMLGLwenlnVIITSDHGMT 244
Cdd:cd16023   174 GHRYGPNHPE-MARKLTQMDQFIRDIIERLDDDTL-----LLVFGDHGMT 217
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
 154-243 6.59e-05

Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 442317 [Multi-domain]  Cd Length: 603  Bit Score: 45.28  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704 154 FMNYNSSVSFEERlnnitiwlnNSNPPVTFAALYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQKLKMLGLWENL 233
Cdd:COG3083   386 YLFLDAPHAYSFP---------ADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENT 456

                          90
                  ....*....|
gi 1800043704 234 NVIITSDHGM 243
Cdd:COG3083   457 IVIITADHGE 466
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 191-253 1.01e-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: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 44.51  E-value: 1.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800043704 191 PDASGHKYGPEDKENMSRVLKK----IDDLIGDLVQKLKMLGLWENLNVIITSDHG----MTQCSQDRLIN 253
Cdd:cd16151   188 PDSPDWDPDDKRKKDDPEYFPDmvayMDKLVGKLVDKLEELGLRENTIIIFTGDNGthrpITSRTNGREVR 258
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 213-243 3.19e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 42.94  E-value: 3.19e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1800043704 213 IDDLIGDLVQKLKMLGLWENLNVIITSDHGM 243
Cdd:cd16155   201 LDAQIGRILDALEASGELDNTIIVFTSDHGL 231
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 208-242 3.45e-04

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: 42.54  E-value: 3.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1800043704 208 RVLKKIDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:cd16147   246 RTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNG 280
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 213-242 3.78e-04

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: 42.04  E-value: 3.78e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1800043704 213 IDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:cd16022   140 IDDQIGRILDALEELGLLDNTLIVFTSDHG 169
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 213-242 3.99e-04

iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.


Pssm-ID: 293754 [Multi-domain]  Cd Length: 435  Bit Score: 42.56  E-value: 3.99e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1800043704 213 IDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:cd16030   270 VDAQVGRVLDALEELGLADNTIVVLWSDHG 299
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 213-242 7.41e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 41.37  E-value: 7.41e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1800043704 213 IDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:cd16037   171 LDENIGRVLDALEELGLLDNTLIIYTSDHG 200
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 213-243 1.05e-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: 40.69  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1800043704 213 IDDLIGDLVQKLKMLGLWENLNVIITSDHGM 243
Cdd:cd16149   151 VDRNVGRLLDELEELGLTENTLVIFTSDNGF 181
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 29-94 1.20e-03

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: 41.09  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800043704  29 PKLLLVSFDGFRADYLKNY-----EFPHLQNFIKEGVlvehvknvfitkTFPNHY-----------SIVTGLYEESHGIV 92
Cdd:cd16028     1 RNVLFITADQWRADCLSCLghplvKTPNLDRLAAEGV------------RFRNHYtqaapcgpsraSLYTGRYLMNHRSV 68


                  ..
gi 1800043704  93 AN 94
Cdd:cd16028    69 WN 70
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 188-242 1.26e-03

uncharacterized arylsulfatase 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: 293764 [Multi-domain]  Cd Length: 415  Bit Score: 41.04  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1800043704 188 WEEPDASGHKYGPEDKE-----NMSRVLKK-------IDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:cd16145   203 LQVPDDGPYKYKPKDPGiyaylPWPQPEKAyaamvtrLDRDVGRILALLKELGIDENTLVVFTSDNG 269
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 213-242 2.39e-03

uncharacterized arylsulfatase 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: 293762 [Multi-domain]  Cd Length: 395  Bit Score: 39.88  E-value: 2.39e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1800043704 213 IDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:cd16143   210 LDWVVGRILDALKELGLAENTLVIFTSDNG 239
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 213-242 3.36e-03

choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.


Pssm-ID: 293756 [Multi-domain]  Cd Length: 327  Bit Score: 39.48  E-value: 3.36e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1800043704 213 IDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:cd16032   173 VDDKVGQLLDTLERTGLADDTIVIFTSDHG 202
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
 198-242 5.65e-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: 38.70  E-value: 5.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1800043704 198 YGPEDKENMSR------VLKKIDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:cd16026   199 FASEKFKGRSGaglygdVVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 213-242 6.48e-03

uncharacterized arylsulfatase 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: 293763 [Multi-domain]  Cd Length: 421  Bit Score: 38.68  E-value: 6.48e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1800043704 213 IDDLIGDLVQKLKMLGLWENLNVIITSDHG 242
Cdd:cd16144   232 LDESVGRILDALEELGLADNTLVIFTSDNG 261
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 183-243 6.78e-03

Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.


Pssm-ID: 293739 [Multi-domain]  Cd Length: 283  Bit Score: 38.43  E-value: 6.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1800043704 183 FAALYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQKLKMLGLWENLNVIITSDHGM 243
Cdd:cd16015   171 YDLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLP 231
 
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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