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Conserved domains on  [gi|2780227853|ref|NP_001419204|]
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bis(5'-adenosyl)-triphosphatase enpp4 isoform 2 precursor [Mus musculus]

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 ...
 29-381 1.11e-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: 322.23  E-value: 1.11e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  29 PRLLLVSFDGFRADYL-KSYDLPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDSVTKKHFSE 107
Cdd:cd16018     1 PPLIVISIDGFRWDYLdRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 108 SNDKDPFWWNGAEPIWVTNQLQeNRSSAAAMWPGTDVPIHNITAS------YFMNYSSSVSFKERLGNVTTWLSSSNPpv 181
Cdd:cd16018    81 SDWVWDPWWIGGEPIWVTAEKA-GLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDLERP-- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 182 TFAALYWEEPDVSGHKYGPEDKEnMRRVLKEVDDLIGDIVLKLKVLGLWDSLNVIITSDHGMaqcsknrlidldscidrs 261
Cdd:cd16018   158 DLILLYFEEPDSAGHKYGPDSPE-VNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM------------------ 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 262 nysvidlTPVAailpkinvtevydklkrcnphmnvylkeaipnrfyyqhssriqpiilvaeegwtitlnkssfkcDHGYD 341
Cdd:cd16018   219 -------TDVG----------------------------------------------------------------THGYD 227

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2780227853 342 NSLPSMHPFLAAHGPAFRKGYRQSTINTVDIYPMMCHILG 381
Cdd:cd16018   228 NELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 29-381 1.11e-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: 322.23  E-value: 1.11e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  29 PRLLLVSFDGFRADYL-KSYDLPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDSVTKKHFSE 107
Cdd:cd16018     1 PPLIVISIDGFRWDYLdRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 108 SNDKDPFWWNGAEPIWVTNQLQeNRSSAAAMWPGTDVPIHNITAS------YFMNYSSSVSFKERLGNVTTWLSSSNPpv 181
Cdd:cd16018    81 SDWVWDPWWIGGEPIWVTAEKA-GLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDLERP-- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 182 TFAALYWEEPDVSGHKYGPEDKEnMRRVLKEVDDLIGDIVLKLKVLGLWDSLNVIITSDHGMaqcsknrlidldscidrs 261
Cdd:cd16018   158 DLILLYFEEPDSAGHKYGPDSPE-VNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM------------------ 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 262 nysvidlTPVAailpkinvtevydklkrcnphmnvylkeaipnrfyyqhssriqpiilvaeegwtitlnkssfkcDHGYD 341
Cdd:cd16018   219 -------TDVG----------------------------------------------------------------THGYD 227

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2780227853 342 NSLPSMHPFLAAHGPAFRKGYRQSTINTVDIYPMMCHILG 381
Cdd:cd16018   228 NELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 31-341 1.23e-97

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: 296.64  E-value: 1.23e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  31 LLLVSFDGFRADYLKSY-DLPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDSVTKK--HFSE 107
Cdd:pfam01663   1 LLVISLDGFRADYLDRFeLTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEylVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 108 SNDKDPFWWNGaEPIWVTNQLQeNRSSAAAMWPGTDVPIHNITAS----YFMNYSSSVSFKERLGNV--TTWLSSSNP-- 179
Cdd:pfam01663  81 SDPEDPRWWQG-EPIWDTAAKA-GVRAAALFWPGSEVDYSTYYGTppryLKDDYNNSVPFEDRVDTAvlQTWLDLPFAdv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 180 ---PVTFAALYWEEPDVSGHKYGPEDKEnMRRVLKEVDDLIGDIVLKLKVLGLWDSLNVIITSDHGMAQCSKNRLIDLDS 256
Cdd:pfam01663 159 aaeRPDLLLVYLEEPDYAGHRYGPDSPE-VEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLND 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 257 CIDRSNYSVIDLT-PVAAILPK---------INVTEVYDKLKRC--------NPHMNVYLKEAIPNRFYYqhSSRIQPII 318
Cdd:pfam01663 238 YLREKGLLHLVDGgPVVAIYPKarelghvppGEVEEVYAELKEKllglriqdGEHLAVYLKEEIPGRLHY--NPRIPDLV 315

                         330       340
                  ....*....|....*....|....*...
gi 2780227853 319 LVAEEGWTITLNKS-----SFKCDHGYD 341
Cdd:pfam01663 316 LVADPGWYITGKDGgdkeaAIHGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 4-383 2.83e-70

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 227.32  E-value: 2.83e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853   4 MKILVIPLFWGLVTGykGNSSDSSAPRLLLVSFDGFRADYLKSYDLPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTG 83
Cdd:COG1524     1 MKRGLSLLLASLLAA--AAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  84 LYEESHGIVANSMYDSVTKKH-FSESNDKDPFWWN---GAEPIWVTnqLQEN-RSSAAAMWPGTDV-PIHNITASYFMN- 156
Cdd:COG1524    79 LYPGEHGIVGNGWYDPELGRVvNSLSWVEDGFGSNsllPVPTIFER--ARAAgLTTAAVFWPSFEGsGLIDAARPYPYDg 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 157 ---YSSSVSFKERLGNVTTWLSSSNPPvTFAALYWEEPDVSGHKYGPEDKEnMRRVLKEVDDLIGDIVLKLKVLGLWDSL 233
Cdd:COG1524   157 rkpLLGNPAADRWIAAAALELLREGRP-DLLLVYLPDLDYAGHRYGPDSPE-YRAALREVDAALGRLLDALKARGLYEGT 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 234 NVIITSDHGMAQCSKNrlIDLDScIDRSNYSVIDLTPVAAILPKINVTE-VYDKLKrcnPHMNVYLKEAIpNRFYYQHsS 312
Cdd:COG1524   235 LVIVTADHGMVDVPPD--IDLNR-LRLAGLLAVRAGESAHLYLKDGADAeVRALLG---LPARVLTREEL-AAGHFGP-H 306

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2780227853 313 RIQPIILVAEEGWTItlnKSSFKCDHGYDNSlPSMHPFLAAHGPAFRKGyrqstINTVDIYPMMCHILGLK 383
Cdd:COG1524   307 RIGDLVLVAKPGWAL---DAPLKGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
 
Name Accession Description Interval E-value
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 29-381 1.11e-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: 322.23  E-value: 1.11e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  29 PRLLLVSFDGFRADYL-KSYDLPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDSVTKKHFSE 107
Cdd:cd16018     1 PPLIVISIDGFRWDYLdRAGLTPNLKRLAEEGVRAKYVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 108 SNDKDPFWWNGAEPIWVTNQLQeNRSSAAAMWPGTDVPIHNITAS------YFMNYSSSVSFKERLGNVTTWLSSSNPpv 181
Cdd:cd16018    81 SDWVWDPWWIGGEPIWVTAEKA-GLKTASYFWPGSEVAIIGYNPTpiplggYWQPYNDSFPFEERVDTILEWLDLERP-- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 182 TFAALYWEEPDVSGHKYGPEDKEnMRRVLKEVDDLIGDIVLKLKVLGLWDSLNVIITSDHGMaqcsknrlidldscidrs 261
Cdd:cd16018   158 DLILLYFEEPDSAGHKYGPDSPE-VNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM------------------ 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 262 nysvidlTPVAailpkinvtevydklkrcnphmnvylkeaipnrfyyqhssriqpiilvaeegwtitlnkssfkcDHGYD 341
Cdd:cd16018   219 -------TDVG----------------------------------------------------------------THGYD 227

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2780227853 342 NSLPSMHPFLAAHGPAFRKGYRQSTINTVDIYPMMCHILG 381
Cdd:cd16018   228 NELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 31-341 1.23e-97

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: 296.64  E-value: 1.23e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  31 LLLVSFDGFRADYLKSY-DLPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDSVTKK--HFSE 107
Cdd:pfam01663   1 LLVISLDGFRADYLDRFeLTPNLAALAKEGVSAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGEylVFVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 108 SNDKDPFWWNGaEPIWVTNQLQeNRSSAAAMWPGTDVPIHNITAS----YFMNYSSSVSFKERLGNV--TTWLSSSNP-- 179
Cdd:pfam01663  81 SDPEDPRWWQG-EPIWDTAAKA-GVRAAALFWPGSEVDYSTYYGTppryLKDDYNNSVPFEDRVDTAvlQTWLDLPFAdv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 180 ---PVTFAALYWEEPDVSGHKYGPEDKEnMRRVLKEVDDLIGDIVLKLKVLGLWDSLNVIITSDHGMAQCSKNRLIDLDS 256
Cdd:pfam01663 159 aaeRPDLLLVYLEEPDYAGHRYGPDSPE-VEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLND 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 257 CIDRSNYSVIDLT-PVAAILPK---------INVTEVYDKLKRC--------NPHMNVYLKEAIPNRFYYqhSSRIQPII 318
Cdd:pfam01663 238 YLREKGLLHLVDGgPVVAIYPKarelghvppGEVEEVYAELKEKllglriqdGEHLAVYLKEEIPGRLHY--NPRIPDLV 315

                         330       340
                  ....*....|....*....|....*...
gi 2780227853 319 LVAEEGWTITLNKS-----SFKCDHGYD 341
Cdd:pfam01663 316 LVADPGWYITGKDGgdkeaAIHGTHGYD 343
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 4-383 2.83e-70

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 227.32  E-value: 2.83e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853   4 MKILVIPLFWGLVTGykGNSSDSSAPRLLLVSFDGFRADYLKSYDLPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTG 83
Cdd:COG1524     1 MKRGLSLLLASLLAA--AAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLLTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  84 LYEESHGIVANSMYDSVTKKH-FSESNDKDPFWWN---GAEPIWVTnqLQEN-RSSAAAMWPGTDV-PIHNITASYFMN- 156
Cdd:COG1524    79 LYPGEHGIVGNGWYDPELGRVvNSLSWVEDGFGSNsllPVPTIFER--ARAAgLTTAAVFWPSFEGsGLIDAARPYPYDg 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 157 ---YSSSVSFKERLGNVTTWLSSSNPPvTFAALYWEEPDVSGHKYGPEDKEnMRRVLKEVDDLIGDIVLKLKVLGLWDSL 233
Cdd:COG1524   157 rkpLLGNPAADRWIAAAALELLREGRP-DLLLVYLPDLDYAGHRYGPDSPE-YRAALREVDAALGRLLDALKARGLYEGT 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 234 NVIITSDHGMAQCSKNrlIDLDScIDRSNYSVIDLTPVAAILPKINVTE-VYDKLKrcnPHMNVYLKEAIpNRFYYQHsS 312
Cdd:COG1524   235 LVIVTADHGMVDVPPD--IDLNR-LRLAGLLAVRAGESAHLYLKDGADAeVRALLG---LPARVLTREEL-AAGHFGP-H 306

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2780227853 313 RIQPIILVAEEGWTItlnKSSFKCDHGYDNSlPSMHPFLAAHGPAFRKGyrqstINTVDIYPMMCHILGLK 383
Cdd:COG1524   307 RIGDLVLVAKPGWAL---DAPLKGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 29-244 1.25e-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: 87.48  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  29 PRLLLVSFDGFRADYLKSYD-----LPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDSVTKK 103
Cdd:cd00016     1 KHVVLIVLDGLGADDLGKAGnpaptTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 104 HFSESNDKDPFWWNgaepiwvtnQLQENRSSAAAMwpgtdvpihnitasyfmnysssvSFKERLgnvtTWLSSSNPpvTF 183
Cdd:cd00016    81 RAAGKDEDGPTIPE---------LLKQAGYRTGVI-----------------------GLLKAI----DETSKEKP--FV 122

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2780227853 184 AALYWEEPDVSGHKYGPeDKENMRRVLKEVDDLIGDIVLKLKVLGLWDSLNVIITSDHGMA 244
Cdd:cd00016   123 LFLHFDGPDGPGHAYGP-NTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGI 182
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 28-243 1.70e-07

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


Pssm-ID: 293744  Cd Length: 294  Bit Score: 52.59  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  28 APRLLLVSFDGFRADYLKSYDL---PHLQNFIKE----GVLVEHVKnvfiTKTFPNHYSIVTGLYEeshgivansMYDSV 100
Cdd:cd16020     4 AKRLVVFVADGLRADTFFENNCsraPFLRKIFLNqglwGISHTRVP----TESRPGHVALFAGFYE---------DPSAV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 101 TKKhfsesndkdpFWWNGAE--PIWvtnqlqeNRSSAAAMWPGTDV---------PIHNITASYFMNYSSSVS------- 162
Cdd:cd16020    71 TKG----------WKENPVEfdSVF-------NRSRRSWAWGSPDIlpmfpkgatGGKVLTYIYPEEDFDSTDaseldew 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 163 ----FKERLGN---VTTWLSSSNPPVTFaaLYWEEPDVSGHKYGPEDKENMRRvLKEVDDLIGDIVLKLKVLGLwDSLNV 235
Cdd:cd16020   134 vfdkVEEFLANassNKTELLNQDGLVFF--LHLLGLDTNGHAHKPYSKEYLEN-IRYVDKGIEKTYPLIEEYFN-DGRTA 209


                  ....*....
gi 2780227853 236 -IITSDHGM 243
Cdd:cd16020   210 yIFTSDHGM 218
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 29-242 1.24e-06

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 49.85  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  29 PRLLLVSFDGFRADYLKSY-----DLPHLQNFIKEGVLVEhvkNVFITK--TFPNHYSIVTGLYEESHGIVANSMydsvt 101
Cdd:cd16148     1 MNVILIVIDSLRADHLGCYgydrvTTPNLDRLAAEGVVFD---NHYSGSnpTLPSRFSLFTGLYPFYHGVWGGPL----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 102 kkhfsesndkdpfwwnGAEPIWVTNQLQEN------RSSAAAMWPGTdvPIHNiTASYFMNYSSSVSFKERLGNVTT--- 172
Cdd:cd16148    73 ----------------EPDDPTLAEILRKAgyytaaVSSNPHLFGGP--GFDR-GFDTFEDFRGQEGDPGEEGDERAerv 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 173 ------WLS---SSNPpvTFAAL-YWE--EPDvsghKYGPEdkenmrrvLKEVDDLIGDIVLKLKVLGLWDSLNVIITSD 240
Cdd:cd16148   134 tdraleWLDrnaDDDP--FFLFLhYFDphEPY----LYDAE--------VRYVDEQIGRLLDKLKELGLLEDTLVIVTSD 199


                  ..
gi 2780227853 241 HG 242
Cdd:cd16148   200 HG 201
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 29-387 1.30e-06

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: 50.61  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  29 PRLLL-VSFDGFRADYLKSYDlPHLQN-----FIKEGVlveHVKNVFI----TKTFPNHYSIVTGLYEESHGIVANSMYD 98
Cdd:cd16016     2 PKLVVgIVVDQMRADYLYRYR-DRFGEggfkrLLNEGF---VFENAHYnyapTDTAPGHATIYTGTTPAIHGIIGNDWYD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  99 SVTKKhfSESNDKDPfwwngAEPIWVTNQlQENRSSAAAMWPGT--D--------------VPI----------HNITAS 152
Cdd:cd16016    78 RETGR--EVYCVEDS-----TVTTVGGNS-TAGKMSPRNLLVTTigDelklatngrskvigVALkdraailpagHAADAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 153 YFMNYSSsvsfkerlGNVTT----------WLSSSN---PP----VTF----AALYWEE------PD---VS-------G 195
Cdd:cd16016   150 YWFDDET--------GKFITstyymkelpaWVEKFNakkLPfgntLTLdfakAALENEKlgkddvTDllaVSfsatdyiG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 196 HKYGPEDKEnMRRVLKEVDDLIGDIVLKL-KVLGLWDSLnVIITSDHG--------------MAQCSKNRLIDL------ 254
Cdd:cd16016   222 HAFGPNSVE-MEDTYLRLDRDLARLLDALdKKVGKGNYL-VFLTADHGaadnpeflkdhkipAGRFDPKRLKALlnaylm 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 255 -----DSCIDRSNYSVIDLTPVAAILPKINVTEVYDKLKRC-----------------NPHMNVYLKEAIPNRFYYQHSS 312
Cdd:cd16016   300 akyglGKWVLGYSNGQVYLNHKLIEEKGLDLAEVQAAAAEFllqmpgvaaaytadellAGPEPTGIRERLRNGYNPKRSG 379

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2780227853 313 riqPIILVAEEGWTITlNKSSFKCDHG----YDNSLPSMhpFLaahGPAFRKGYRQSTINTVDIYPMMCHILGLKPhPN 387
Cdd:cd16016   380 ---DLIVVLKPGWIEG-DGSGKGTTHGspydYDTHVPLL--FY---GWGIKPGEIPRPVEITDIAPTLAALLGIQP-PN 448
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
 44-242 7.34e-06

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: 47.93  E-value: 7.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  44 LKSYD-LPHLQNFI-KEGVlvehvknvfitkTFPNHY-----------SIVTGLYEESHGIVANSMydsvtkkhfsESND 110
Cdd:cd16147    16 LGSMDpMPKTKKLLaDQGT------------TFTNAFvttplccpsraSILTGQYAHNHGVTNNSP----------PGGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 111 KDPFWWNGAEPIWVTNQLQE-------------------NRSSAAAMWPGTDVPIHNitaSYFMNYSSSVSFKERLGNV- 170
Cdd:cd16147    74 YPKFWQNGLERSTLPVWLQEagyrtayagkylngygvpgGVSYVPPGWDEWDGLVGN---STYYNYTLSNGGNGKHGVSy 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 171 -------------TTWLSSSNP----------------PVTFAALY--------------WEEPDVSGHK-----YGPED 202
Cdd:cd16147   151 pgdyltdviankaLDFLRRAAAddkpfflvvappaphgPFTPAPRYanlfpnvtapprppPNNPDVSDKPhwlrrLPPLN 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2780227853 203 KENMR----------RVLKEVDDLIGDIVLKLKVLGLWDSLNVIITSDHG 242
Cdd:cd16147   231 PTQIAyidelyrkrlRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNG 280
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 31-242 7.20e-05

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: 44.94  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  31 LLLVSFDGFRADYLKSY-----DLPHLQNFIKEGVlvehvknvfitkTFPNHY-----------SIVTGLYEESHGIVAN 94
Cdd:cd16028     3 VLFITADQWRADCLSCLghplvKTPNLDRLAAEGV------------RFRNHYtqaapcgpsraSLYTGRYLMNHRSVWN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  95 SM-----------------YDSVT--KKHFS------ESNDKDPFWWNGAEPIWV----TNQLQENRSSAAAMwpgTDVP 145
Cdd:cd16028    71 GTpldarhltlalelrkagYDPALfgYTDTSpdprglAPLDPRLLSYELAMPGFDpvdrLDEYPAEDSDTAFL---TDRA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 146 IHNITA----SYFMNYS--------------------SSVSFKERLGNVTTwLSSSNPpvtFAALYWEEPDVSGHKYGPE 201
Cdd:cd16028   148 IEYLDErqdePWFLHLSyirphppfvapapyhalydpADVPPPIRAESLAA-EAAQHP---LLAAFLERIESLSFSPGAA 223

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2780227853 202 -----DKENMRRV-------LKEVDDLIGDIVLKLKVLGLWDSLNVIITSDHG 242
Cdd:cd16028   224 naadlDDEEVAQMratylglIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG 276
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 200-244 8.14e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 44.48  E-value: 8.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2780227853 200 PEDKENMRRVLKE-------VDDLIGDIVLKLKVLGLWDSLNVIITSDHGMA 244
Cdd:cd16155   181 PRTPEAVRQHLAEyyamithLDAQIGRILDALEASGELDNTIIVFTSDHGLA 232
Sulfatase pfam00884
Sulfatase;
29-242 2.84e-04

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 42.79  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  29 PRLLLVSFDGFRADYLKSY-----DLPHLQNFIKEGVLvehvknvfitktFPNHYS-----------IVTGLYEESHGIV 92
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYgyprpTTPFLDRLAEEGLL------------FSNFYSggtltapsrfaLLTGLPPHNFGSY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  93 ANSM------------------YDS--VTKKHFSesndkdpFWWNGAEPIWVTNQLQENRSSAAAMWPGTDVPIHNITAS 152
Cdd:pfam00884  69 VSTPvglprtepslpdllkragYNTgaIGKWHLG-------WYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853 153 YFMN--YSSSVSFKERLGN-----VTTwlSSSNPPVTFAALYweEPDVSGHKYGPEDKENMRRV----LKEVDDLIGDIV 221
Cdd:pfam00884 142 VSDEalLDEALEFLDNNDKpfflvLHT--LGSHGPPYYPDRY--PEKYATFKPSSCSEEQLLNSydntLLYTDDAIGRVL 217

                         250       260
                  ....*....|....*....|.
gi 2780227853 222 LKLKVLGLWDSLNVIITSDHG 242
Cdd:pfam00884 218 DKLEENGLLDNTLVVYTSDHG 238
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 195-243 5.63e-04

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: 41.78  E-value: 5.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2780227853 195 GHKYGPEDKEnMRRVLKEVDDLIGDIVLKLKvlglwDSLNVIITSDHGM 243
Cdd:cd16023   174 GHRYGPNHPE-MARKLTQMDQFIRDIIERLD-----DDTLLLVFGDHGM 216
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
 207-243 1.31e-03

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: 41.04  E-value: 1.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2780227853 207 RRVLKEVDDLIGDIVLKLKVLGLWDSLNVIITSDHGM 243
Cdd:COG3083   430 RNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGE 466
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
178-242 1.32e-03

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 41.02  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2780227853 178 NPPVTFAALYWEE-----PDVSGHKYGPEDKENMRRV----LKEVDDLIGDIVLKLKVLGLWDSLNVIITSDHG 242
Cdd:COG3119   165 QAPEEYLDKYDGKdiplpPNLAPRDLTEEELRRARAAyaamIEEVDDQVGRLLDALEELGLADNTIVVFTSDNG 238
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 195-243 2.04e-03

GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 39.86  E-value: 2.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2780227853 195 GHKYGPEdKENMRRVLKEVDDLIGDIVLKLKVLGlwDSLNV--IITSDHGM 243
Cdd:cd16024   159 GHLEGPK-SPLMPPKLKEMDDVIKRIYESLEEQS--SNNPTllVVCGDHGM 206
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 200-242 3.04e-03

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


Pssm-ID: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 39.86  E-value: 3.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2780227853 200 PEDKENMRRVLKE-------VDDLIGDIVLKLKVLGLWDSLNVIITSDHG 242
Cdd:cd16034   216 KKEEAGLREDLRGyyamitaLDDNIGRLLDALKELGLLENTIVVFTSDHG 265
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 213-242 3.15e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 39.90  E-value: 3.15e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2780227853 213 VDDLIGDIVLKLKVLGLWDSLNVIITSDHG 242
Cdd:cd16033   226 IDDAIGRILDALEELGLADDTLVIFTSDHG 255
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 212-242 8.24e-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: 38.29  E-value: 8.24e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2780227853 212 EVDDLIGDIVLKLKVLGLWDSLNVIITSDHG 242
Cdd:cd16037   170 FLDENIGRVLDALEELGLLDNTLIIYTSDHG 200
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 30-245 8.91e-03

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: 38.11  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  30 RLLLVSFDGFRADYLKS-YDLPHLQNFIKEgvLVEHVKNVFI--------TKTFPNHYSIVTGlyeeshgIVAN--SMYD 98
Cdd:cd16019     6 KVVLIVIDGLRYDLAVNvNKQSSFFSFLQK--LNEQPNNSFLalsfadppTVTGPRLKALTTG-------NPPTflDLIS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780227853  99 SVTKKHFSESNdkdpfwwngaepiwVTNQLQENRSSAAAMwpGTDVpIHNITASYFMNYSSSVSFKER---------LGN 169
Cdd:cd16019    77 NFASSEIKEDN--------------IIRQLKKNGKKILFY--GDDT-WLDLFPEIFTYKFTITSFNIRdmhdvdpifYNH 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2780227853 170 VTTWL--SSSNPPVTFAALYWEEPDVSGHKYGPEDKENMRRVLKEVDDLIGDIVLKLKvlglwDSLNVIITSDHGMAQ 245
Cdd:cd16019   140 INDNLdeNIYYDNWDFIILHFLGLDHLGHKHNTTSSPELEKKLDQMDNLIRDIYDRMD-----NDTLLVVVSDHGMNN 212
 
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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