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Conserved domains on  [gi|7662358|ref|NP_055751|]
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bis(5'-adenosyl)-triphosphatase ENPP4 precursor [Homo sapiens]

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 ...
 26-379 2.74e-109

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: 323.77  E-value: 2.74e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   26 PKLLLVSFDGFRADYL-KNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKKHFSD 104
Cdd:cd16018   1 PPLIVISIDGFRWDYLdRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  105 SNDKDPFWWNEAVPIWVTNQLQeNRSSAAAMWPGTDVPIHDT------ISSYFMNYNSSVSFEERLNNITMWLNNSNPpv 178
Cdd:cd16018  81 SDWVWDPWWIGGEPIWVTAEKA-GLKTASYFWPGSEVAIIGYnptpipLGGYWQPYNDSFPFEERVDTILEWLDLERP-- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  179 TFATLYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQcsqdrlinldscidhs 258
Cdd:cd16018 158 DLILLYFEEPDSAGHKYGPDSPE-VNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTD---------------- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  259 yytlidlspvaailpkinrtevynklkncsphmnvylkedipnrfyyqhndriqpiilvadegwtivlnessqkLGDHGY 338
Cdd:cd16018 221 --------------------------------------------------------------------------VGTHGY 226

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 7662358  339 DNSLPSMHPFLAAHGPAFHKGYKHSTINIVDIYPMMCHILG 379
Cdd:cd16018 227 DNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 26-379 2.74e-109

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: 323.77  E-value: 2.74e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   26 PKLLLVSFDGFRADYL-KNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKKHFSD 104
Cdd:cd16018   1 PPLIVISIDGFRWDYLdRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  105 SNDKDPFWWNEAVPIWVTNQLQeNRSSAAAMWPGTDVPIHDT------ISSYFMNYNSSVSFEERLNNITMWLNNSNPpv 178
Cdd:cd16018  81 SDWVWDPWWIGGEPIWVTAEKA-GLKTASYFWPGSEVAIIGYnptpipLGGYWQPYNDSFPFEERVDTILEWLDLERP-- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  179 TFATLYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQcsqdrlinldscidhs 258
Cdd:cd16018 158 DLILLYFEEPDSAGHKYGPDSPE-VNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTD---------------- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  259 yytlidlspvaailpkinrtevynklkncsphmnvylkedipnrfyyqhndriqpiilvadegwtivlnessqkLGDHGY 338
Cdd:cd16018 221 --------------------------------------------------------------------------VGTHGY 226

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 7662358  339 DNSLPSMHPFLAAHGPAFHKGYKHSTINIVDIYPMMCHILG 379
Cdd:cd16018 227 DNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 28-339 5.72e-104

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: 312.82  E-value: 5.72e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358     28 LLLVSFDGFRADYLKNYE-FPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKK--HFSD 104
Cdd:pfam01663   1 LLVISLDGFRADYLDRFElTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEylVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358    105 SNDKDPFWWNEAvPIWVTNQLQeNRSSAAAMWPGTDVPIHDTISS----YFMNYNSSVSFEERLNNITM--WLNNSNP-- 176
Cdd:pfam01663  81 SDPEDPRWWQGE-PIWDTAAKA-GVRAAALFWPGSEVDYSTYYGTppryLKDDYNNSVPFEDRVDTAVLqtWLDLPFAdv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358    177 ---PVTFATLYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQCSQDRLINLDS 253
Cdd:pfam01663 159 aaeRPDLLLVYLEEPDYAGHRYGPDSPE-VEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLND 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358    254 CIDHS-YYTLIDLSPVAAILPK---------INRTEVYNKLKNCS--------PHMNVYLKEDIPNRFYYqhNDRIQPII 315
Cdd:pfam01663 238 YLREKgLLHLVDGGPVVAIYPKarelghvppGEVEEVYAELKEKLlglriqdgEHLAVYLKEEIPGRLHY--NPRIPDLV 315

                         330       340
                  ....*....|....*....|....*...
gi 7662358    316 LVADEGWTIVLNESSQKL----GDHGYD 339
Cdd:pfam01663 316 LVADPGWYITGKDGGDKEaaihGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 1-381 1.63e-73

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 235.41  E-value: 1.63e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358    1 MKLLVILLFSGLITGFRSDSSSslPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTG 80
Cdd:COG1524   1 MKRGLSLLLASLLAAAAAAAPP--AKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   81 LYEESHGIVANSMYDAVTKKH-FSDSNDKDPFWWNEAV---PIWVTnqLQEN-RSSAAAMWPGTDV-PIHDTISSYfmNY 154
Cdd:COG1524  79 LYPGEHGIVGNGWYDPELGRVvNSLSWVEDGFGSNSLLpvpTIFER--ARAAgLTTAAVFWPSFEGsGLIDAARPY--PY 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  155 NSSVSF----EERLNNITMWLN--NSNPPvTFATLYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQRLKMLGLWE 228
Cdd:COG1524 155 DGRKPLlgnpAADRWIAAAALEllREGRP-DLLLVYLPDLDYAGHRYGPDSPE-YRAALREVDAALGRLLDALKARGLYE 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  229 NLNVIITSDHGMTQCSQDrlINLDSCIDHSYYTLIDlSPVAAILPKINRTE-VYNKLKNcspHMNVYLKEDIpNRFYYQH 307
Cdd:COG1524 233 GTLVIVTADHGMVDVPPD--IDLNRLRLAGLLAVRA-GESAHLYLKDGADAeVRALLGL---PARVLTREEL-AAGHFGP 305

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662358  308 NdRIQPIILVADEGWTIvlneSSQKLGDHGYDNSlPSMHPFLAAHGPAFHKGykhstINIVDIYPMMCHILGLK 381
Cdd:COG1524 306 H-RIGDLVLVAKPGWAL----DAPLKGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 26-379 2.74e-109

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: 323.77  E-value: 2.74e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   26 PKLLLVSFDGFRADYL-KNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKKHFSD 104
Cdd:cd16018   1 PPLIVISIDGFRWDYLdRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  105 SNDKDPFWWNEAVPIWVTNQLQeNRSSAAAMWPGTDVPIHDT------ISSYFMNYNSSVSFEERLNNITMWLNNSNPpv 178
Cdd:cd16018  81 SDWVWDPWWIGGEPIWVTAEKA-GLKTASYFWPGSEVAIIGYnptpipLGGYWQPYNDSFPFEERVDTILEWLDLERP-- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  179 TFATLYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQcsqdrlinldscidhs 258
Cdd:cd16018 158 DLILLYFEEPDSAGHKYGPDSPE-VNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTD---------------- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  259 yytlidlspvaailpkinrtevynklkncsphmnvylkedipnrfyyqhndriqpiilvadegwtivlnessqkLGDHGY 338
Cdd:cd16018 221 --------------------------------------------------------------------------VGTHGY 226

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 7662358  339 DNSLPSMHPFLAAHGPAFHKGYKHSTINIVDIYPMMCHILG 379
Cdd:cd16018 227 DNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 28-339 5.72e-104

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: 312.82  E-value: 5.72e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358     28 LLLVSFDGFRADYLKNYE-FPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKK--HFSD 104
Cdd:pfam01663   1 LLVISLDGFRADYLDRFElTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEylVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358    105 SNDKDPFWWNEAvPIWVTNQLQeNRSSAAAMWPGTDVPIHDTISS----YFMNYNSSVSFEERLNNITM--WLNNSNP-- 176
Cdd:pfam01663  81 SDPEDPRWWQGE-PIWDTAAKA-GVRAAALFWPGSEVDYSTYYGTppryLKDDYNNSVPFEDRVDTAVLqtWLDLPFAdv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358    177 ---PVTFATLYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQCSQDRLINLDS 253
Cdd:pfam01663 159 aaeRPDLLLVYLEEPDYAGHRYGPDSPE-VEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLND 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358    254 CIDHS-YYTLIDLSPVAAILPK---------INRTEVYNKLKNCS--------PHMNVYLKEDIPNRFYYqhNDRIQPII 315
Cdd:pfam01663 238 YLREKgLLHLVDGGPVVAIYPKarelghvppGEVEEVYAELKEKLlglriqdgEHLAVYLKEEIPGRLHY--NPRIPDLV 315

                         330       340
                  ....*....|....*....|....*...
gi 7662358    316 LVADEGWTIVLNESSQKL----GDHGYD 339
Cdd:pfam01663 316 LVADPGWYITGKDGGDKEaaihGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 1-381 1.63e-73

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 235.41  E-value: 1.63e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358    1 MKLLVILLFSGLITGFRSDSSSslPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTG 80
Cdd:COG1524   1 MKRGLSLLLASLLAAAAAAAPP--AKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   81 LYEESHGIVANSMYDAVTKKH-FSDSNDKDPFWWNEAV---PIWVTnqLQEN-RSSAAAMWPGTDV-PIHDTISSYfmNY 154
Cdd:COG1524  79 LYPGEHGIVGNGWYDPELGRVvNSLSWVEDGFGSNSLLpvpTIFER--ARAAgLTTAAVFWPSFEGsGLIDAARPY--PY 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  155 NSSVSF----EERLNNITMWLN--NSNPPvTFATLYWEEPDASGHKYGPEDKEnMSRVLKKIDDLIGDLVQRLKMLGLWE 228
Cdd:COG1524 155 DGRKPLlgnpAADRWIAAAALEllREGRP-DLLLVYLPDLDYAGHRYGPDSPE-YRAALREVDAALGRLLDALKARGLYE 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  229 NLNVIITSDHGMTQCSQDrlINLDSCIDHSYYTLIDlSPVAAILPKINRTE-VYNKLKNcspHMNVYLKEDIpNRFYYQH 307
Cdd:COG1524 233 GTLVIVTADHGMVDVPPD--IDLNRLRLAGLLAVRA-GESAHLYLKDGADAeVRALLGL---PARVLTREEL-AAGHFGP 305

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662358  308 NdRIQPIILVADEGWTIvlneSSQKLGDHGYDNSlPSMHPFLAAHGPAFHKGykhstINIVDIYPMMCHILGLK 381
Cdd:COG1524 306 H-RIGDLVLVAKPGWAL----DAPLKGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 26-241 2.63e-19

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: 86.71  E-value: 2.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   26 PKLLLVSFDGFRADYL-KNYEFPHLQNFIK----EGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKK 100
Cdd:cd00016   1 KHVVLIVLDGLGADDLgKAGNPAPTTPNLKrlasEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  101 HFSDSNDKDPFWWNeavpiwvtnQLQENRSSAAAMwpgtdvpihdtissyfmnynssvSFEERLNNITMwlnnSNPPVTF 180
Cdd:cd00016  81 RAAGKDEDGPTIPE---------LLKQAGYRTGVI-----------------------GLLKAIDETSK----EKPFVLF 124

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662358  181 atLYWEEPDASGHKYGPeDKENMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMT 241
Cdd:cd00016 125 --LHFDGPDGPGHAYGP-NTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGI 182
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 26-239 7.96e-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: 59.48  E-value: 7.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   26 PKLLLVSFDGFRADYLKNYEF-----PHLQNFIKEGVLVEhvkNVFITK--TFPNHYSIVTGLYEESHGIVANSMydavt 98
Cdd:cd16148   1 MNVILIVIDSLRADHLGCYGYdrvttPNLDRLAAEGVVFD---NHYSGSnpTLPSRFSLFTGLYPFYHGVWGGPL----- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   99 kkhfsdsndkdpfwwnEAVPIWVTNQLQEN------RSSAAAMWPGTdvPIHDTISSYFMNY-------NSSVSFEERLN 165
Cdd:cd16148  73 ----------------EPDDPTLAEILRKAgyytaaVSSNPHLFGGP--GFDRGFDTFEDFRgqegdpgEEGDERAERVT 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  166 NITM-WL--NNSNPPVtFATL-YWE--EP---DASghkygpedkenmsrvLKKIDDLIGDLVQRLKMLGLWENLNVIITS 236
Cdd:cd16148 135 DRALeWLdrNADDDPF-FLFLhYFDphEPylyDAE---------------VRYVDEQIGRLLDKLKELGLLEDTLVIVTS 198


                ...
gi 7662358  237 DHG 239
Cdd:cd16148 199 DHG 201
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 25-385 6.15e-09

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: 57.93  E-value: 6.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   25 PPKLLL-VSFDGFRADYLknYEF-PHLQN-----FIKEGVlveHVKNVFI----TKTFPNHYSIVTGLYEESHGIVANSM 93
Cdd:cd16016   1 RPKLVVgIVVDQMRADYL--YRYrDRFGEggfkrLLNEGF---VFENAHYnyapTDTAPGHATIYTGTTPAIHGIIGNDW 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   94 YDAVTKKhfSDSNDKDPfwwneAVPIWVTNQlQENRSSAAAMWPGTdvpIHD--TISSYFMNYNSSVSFEERLnNITM-- 169
Cdd:cd16016  76 YDRETGR--EVYCVEDS-----TVTTVGGNS-TAGKMSPRNLLVTT---IGDelKLATNGRSKVIGVALKDRA-AILPag 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  170 -------WLNNSNPPVTFATLYWEE------------------------------------------------PDASGHK 194
Cdd:cd16016 144 haadaayWFDDETGKFITSTYYMKElpawvekfnakklpfgntltldfakaaleneklgkddvtdllavsfsaTDYIGHA 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  195 YGPEDKENMSRVLkKIDDLIGDLVQRL-KMLGLwENLNVIITSDHG--------------MTQCSQDRLI---------- 249
Cdd:cd16016 224 FGPNSVEMEDTYL-RLDRDLARLLDALdKKVGK-GNYLVFLTADHGaadnpeflkdhkipAGRFDPKRLKallnaylmak 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  250 -NLDSCIDHSYYTLIDLSPVAAILPKINRTEVYNKLKNC-----------------SPHMNVYLKEDIPNRFYYQHN-Dr 310
Cdd:cd16016 302 yGLGKWVLGYSNGQVYLNHKLIEEKGLDLAEVQAAAAEFllqmpgvaaaytadellAGPEPTGIRERLRNGYNPKRSgD- 380

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358  311 iqpIILVADEGWTIVlnESSQKLGDHGydnslpSMHPFlAAHGPA--FHKGYKHSTIN----IVDIYPMMCHILGLKPhP 384
Cdd:cd16016 381 ---LIVVLKPGWIEG--DGSGKGTTHG------SPYDY-DTHVPLlfYGWGIKPGEIPrpveITDIAPTLAALLGIQP-P 447


                .
gi 7662358  385 N 385
Cdd:cd16016 448 N 448
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 210-248 9.86e-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: 47.56  E-value: 9.86e-06
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 7662358  210 IDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQCSQDRL 248
Cdd:cd16034 236 LDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM 274
Sulfatase pfam00884
Sulfatase;
26-239 3.12e-05

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 45.49  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358     26 PKLLLVSFDGFRADYLKNY-----EFPHLQNFIKEGVLvehvknvfitktFPNHYS-----------IVTGLYEESHGIV 89
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYgyprpTTPFLDRLAEEGLL------------FSNFYSggtltapsrfaLLTGLPPHNFGSY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358     90 ANSM------------------YD--AVTKKHFSdsndkdpFWWNEAVPIWVTNQLQENRSSAAAMWPGTDVPIHDTISS 149
Cdd:pfam00884  69 VSTPvglprtepslpdllkragYNtgAIGKWHLG-------WYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358    150 YFMN--YNSSVSFEERLNN---ITMWLNNSNPPVTFATLYwEEPDASGHKYGPEDKENMS---RVLKKIDDLIGDLVQRL 221
Cdd:pfam00884 142 VSDEalLDEALEFLDNNDKpffLVLHTLGSHGPPYYPDRY-PEKYATFKPSSCSEEQLLNsydNTLLYTDDAIGRVLDKL 220

                         250
                  ....*....|....*...
gi 7662358    222 KMLGLWENLNVIITSDHG 239
Cdd:pfam00884 221 EENGLLDNTLVVYTSDHG 238
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 27-242 4.38e-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: 45.04  E-value: 4.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   27 KLLLVSFDGFRADYLKN-YEFPHLQNFIKEgvLVEHVKNVFI--------TKTFPNHYSIVTGlyeeshgIVANSMyDAv 97
Cdd:cd16019   6 KVVLIVIDGLRYDLAVNvNKQSSFFSFLQK--LNEQPNNSFLalsfadppTVTGPRLKALTTG-------NPPTFL-DL- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   98 tKKHFSDSNDKDPFWwneavpiwvTNQLQENRSSAAAMwpGTDV-----PIHDTISSYFMNYNSSVSFEERLN-----NI 167
Cdd:cd16019  75 -ISNFASSEIKEDNI---------IRQLKKNGKKILFY--GDDTwldlfPEIFTYKFTITSFNIRDMHDVDPIfynhiND 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662358  168 TMWLNNSNPPVTFATLYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQRLKmlglwENLNVIITSDHGMTQ 242
Cdd:cd16019 143 NLDENIYYDNWDFIILHFLGLDHLGHKHNTTSSPELEKKLDQMDNLIRDIYDRMD-----NDTLLVVVSDHGMNN 212
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 192-241 5.68e-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: 44.86  E-value: 5.68e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 7662358  192 GHKYGPEDKEnMSRVLKKIDDLIGDLVQRLKMLGLwenlnVIITSDHGMT 241
Cdd:cd16023 174 GHRYGPNHPE-MARKLTQMDQFIRDIIERLDDDTL-----LLVFGDHGMT 217
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
188-239 8.45e-05

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 44.48  E-value: 8.45e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 7662358  188 PDASGHKYGPEDKENMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHG 239
Cdd:COG3119 187 PRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG 238
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 210-239 1.11e-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: 44.13  E-value: 1.11e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 7662358  210 IDDLIGDLVQRLKMLGLWENLNVIITSDHG 239
Cdd:cd16033 226 IDDAIGRILDALEELGLADDTLVIFTSDHG 255
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
 210-240 1.20e-04

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: 44.51  E-value: 1.20e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 7662358  210 IDDLIGDLVQRLKMLGLWENLNVIITSDHGM 240
Cdd:COG3083 436 VDSQIGRVLDTLEQRGLLENTIVIITADHGE 466
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 47-240 1.56e-04

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: 43.65  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   47 PHLQNFIKEGVLvehvknvfitktFPNHY-----------SIVTGLYEESHGIVAN-----SMYDAVT------------ 98
Cdd:cd16027  26 PNLDRLAAEGVR------------FTNAFttapvcspsrsALLTGLYPHQNGAHGLrsrgfPLPDGVKtlpellreagyy 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   99 -----KKHFSDsnDKDPFWWNEAVPIWVTNQLQENRSSAAAMW---PGTDVP------IHDTISSYfmNYNSSVSFEERL 164
Cdd:cd16027  94 tgligKTHYNP--DAVFPFDDEMRGPDDGGRNAWDYASNAADFlnrAKKGQPfflwfgFHDPHRPY--PPGDGEEPGYDP 169

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7662358  165 NNITMwlnnsnPPvtfatlYWeePDasghkyGPEDKENMSRVLKKI---DDLIGDLVQRLKMLGLWENLNVIITSDHGM 240
Cdd:cd16027 170 EKVKV------PP------YL--PD------TPEVREDLADYYDEIerlDQQVGEILDELEEDGLLDNTIVIFTSDHGM 228
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 188-250 2.80e-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: 42.97  E-value: 2.80e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662358  188 PDASGHKYGPEDKENMSRVLKK----IDDLIGDLVQRLKMLGLWENLNVIITSDHG----MTQCSQDRLIN 250
Cdd:cd16151 188 PDSPDWDPDDKRKKDDPEYFPDmvayMDKLVGKLVDKLEELGLRENTIIIFTGDNGthrpITSRTNGREVR 258
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 205-239 3.70e-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: 3.70e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 7662358  205 RVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHG 239
Cdd:cd16147 246 RTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNG 280
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 210-240 4.04e-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: 42.55  E-value: 4.04e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 7662358  210 IDDLIGDLVQRLKMLGLWENLNVIITSDHGM 240
Cdd:cd16155 201 LDAQIGRILDALEASGELDNTIIVFTSDHGL 231
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 210-239 6.18e-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: 41.27  E-value: 6.18e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 7662358  210 IDDLIGDLVQRLKMLGLWENLNVIITSDHG 239
Cdd:cd16022 140 IDDQIGRILDALEELGLLDNTLIVFTSDHG 169
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
 210-239 1.02e-03

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: 41.40  E-value: 1.02e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 7662358  210 IDDLIGDLVQRLKMLGLWENLNVIITSDHG 239
Cdd:cd16030 270 VDAQVGRVLDALEELGLADNTIVVLWSDHG 299
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 210-239 1.35e-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: 40.64  E-value: 1.35e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 7662358  210 IDDLIGDLVQRLKMLGLWENLNVIITSDHG 239
Cdd:cd16032 173 VDDKVGQLLDTLERTGLADDTIVIFTSDHG 202
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 26-91 1.50e-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: 40.71  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662358   26 PKLLLVSFDGFRADYLKNY-----EFPHLQNFIKEGVlvehvknvfitkTFPNHY-----------SIVTGLYEESHGIV 89
Cdd:cd16028   1 RNVLFITADQWRADCLSCLghplvKTPNLDRLAAEGV------------RFRNHYtqaapcgpsraSLYTGRYLMNHRSV 68


                ..
gi 7662358   90 AN 91
Cdd:cd16028  69 WN 70
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 210-239 1.98e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 40.22  E-value: 1.98e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 7662358  210 IDDLIGDLVQRLKMLGLWENLNVIITSDHG 239
Cdd:cd16037 171 LDENIGRVLDALEELGLLDNTLIIYTSDHG 200
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 185-239 2.42e-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: 39.89  E-value: 2.42e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7662358  185 WEEPDASGHKYGPEDKE-----NMSRVLKK-------IDDLIGDLVQRLKMLGLWENLNVIITSDHG 239
Cdd:cd16145 203 LQVPDDGPYKYKPKDPGiyaylPWPQPEKAyaamvtrLDRDVGRILALLKELGIDENTLVVFTSDNG 269
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 210-240 2.48e-03

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 39.53  E-value: 2.48e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 7662358  210 IDDLIGDLVQRLKMLGLWENLNVIITSDHGM 240
Cdd:cd16149 151 VDRNVGRLLDELEELGLTENTLVIFTSDNGF 181
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 180-240 5.29e-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: 38.82  E-value: 5.29e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662358  180 FATLYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGM 240
Cdd:cd16015 171 YDLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLP 231
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
 210-239 8.56e-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: 38.34  E-value: 8.56e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 7662358  210 IDDLIGDLVQRLKMLGLWENLNVIITSDHG 239
Cdd:cd16143 210 LDWVVGRILDALKELGLAENTLVIFTSDNG 239
 
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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