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Conserved domains on  [gi|332660261|gb|AEE85661|]
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Alkaline-phosphatase-like family protein [Arabidopsis thaliana]

Protein Classification

nucleotide pyrophosphatase/phosphodiesterase family protein( domain architecture ID 12025720)

nucleotide pyrophosphatase/phosphodiesterase family protein catalyzes the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and/or nucleotide sugars; belongs to the alkaline phosphatase superfamily

CATH:  3.40.720.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  12757929|11027689|11202013

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 109-435 1.26e-121

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: 359.43  E-value: 1.26e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  109 VLLISSDGFRFGYQFKTK-LPSIHRLIANGTEAETgLIPVFPTLTFPNHYSIVTGLYPAYHGIINNHFVDPETG--NVFT 185
Cdd:pfam01663   1 LLVISLDGFRADYLDRFElTPNLAALAKEGVSAPN-LTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGeyLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  186 MASHE-PEWWLGEPLWETVVNQGLKAATYFWPGSEVHKGSW-NC-PQGLCQNYNGSVPFDDRVDTILS--YFDLPS---- 256
Cdd:pfam01663  80 ISDPEdPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYSTYyGTpPRYLKDDYNNSVPFEDRVDTAVLqtWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  257 NEIPSFMTLYFEDPDHQGHQVGPDDPQITEAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGMVGTCDKKLVVLDDLA 336
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  337 P---WIKIPSSWvqyytPLLAIQPPS-------GHDAADIVAKINEGLSSGKVENGKYLKVYLKEDLPSRLHYvdSDRIP 406
Cdd:pfam01663 240 RekgLLHLVDGG-----PVVAIYPKArelghvpPGEVEEVYAELKEKLLGLRIQDGEHLAVYLKEEIPGRLHY--NPRIP 312

                         330       340       350
                  ....*....|....*....|....*....|.
gi 332660261  407 PIIGLVDEGFKVEQKKSKAKEC--GGAHGYD 435
Cdd:pfam01663 313 DLVLVADPGWYITGKDGGDKEAaiHGTHGYD 343
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 109-435 1.26e-121

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: 359.43  E-value: 1.26e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  109 VLLISSDGFRFGYQFKTK-LPSIHRLIANGTEAETgLIPVFPTLTFPNHYSIVTGLYPAYHGIINNHFVDPETG--NVFT 185
Cdd:pfam01663   1 LLVISLDGFRADYLDRFElTPNLAALAKEGVSAPN-LTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGeyLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  186 MASHE-PEWWLGEPLWETVVNQGLKAATYFWPGSEVHKGSW-NC-PQGLCQNYNGSVPFDDRVDTILS--YFDLPS---- 256
Cdd:pfam01663  80 ISDPEdPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYSTYyGTpPRYLKDDYNNSVPFEDRVDTAVLqtWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  257 NEIPSFMTLYFEDPDHQGHQVGPDDPQITEAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGMVGTCDKKLVVLDDLA 336
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  337 P---WIKIPSSWvqyytPLLAIQPPS-------GHDAADIVAKINEGLSSGKVENGKYLKVYLKEDLPSRLHYvdSDRIP 406
Cdd:pfam01663 240 RekgLLHLVDGG-----PVVAIYPKArelghvpPGEVEEVYAELKEKLLGLRIQDGEHLAVYLKEEIPGRLHY--NPRIP 312

                         330       340       350
                  ....*....|....*....|....*....|.
gi 332660261  407 PIIGLVDEGFKVEQKKSKAKEC--GGAHGYD 435
Cdd:pfam01663 313 DLVLVADPGWYITGKDGGDKEAaiHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 107-475 1.36e-105

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: 315.68  E-value: 1.36e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 107 PVVLLISSDGFRFGY-QFKTKLPSIHRLIANGTEAEtGLIPVFPTLTFPNHYSIVTGLYPAYHGIINNHFVDPETGNVFT 185
Cdd:cd16018    1 PPLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAK-YVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 186 M--ASHEPEWWLGEPLWETVVNQGLKAATYFWPGSEVHKGSWNCP----QGLCQNYNGSVPFDDRVDTILSYFDLpsnEI 259
Cdd:cd16018   80 DsdWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplGGYWQPYNDSFPFEERVDTILEWLDL---ER 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 260 PSFMTLYFEDPDHQGHQVGPDDPQITEAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGMvgtcdkklvvlddlapwi 339
Cdd:cd16018  157 PDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM------------------ 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 340 kipsswvqyytpllaiqppsghdaADIvakineglssgkvengkylkvylkedlpsrlhyvdsdrippiiglvdegfkve 419
Cdd:cd16018  219 ------------------------TDV----------------------------------------------------- 221

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332660261 420 qkkskakecgGAHGYDNAFFSMRTIFIGHGPMFSKGRKVPSFENVQIYNVISSILG 475
Cdd:cd16018  222 ----------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 109-477 1.57e-76

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 244.66  E-value: 1.57e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 109 VLLISSDGFRFGYQFKTKLPSIHRLIANGTEAeTGLIPVFPTLTFPNHYSIVTGLYPAYHGIINNHFVDPETGNVFTMAS 188
Cdd:COG1524   26 VVLILVDGLRADLLERAHAPNLAALAARGVYA-RPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVVNSLS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 189 HEP------EWWLGEPLWETVVNQGLKAATYFWPGSEVHKGS-WNCPQGlcqnYNGSVPF----DDRVDTILSYFDLPSN 257
Cdd:COG1524  105 WVEdgfgsnSLLPVPTIFERARAAGLTTAAVFWPSFEGSGLIdAARPYP----YDGRKPLlgnpAADRWIAAAALELLRE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 258 EIPSFMTLYFEDPDHQGHQVGPDDPQITEAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGMVGTcdKKLVVLDD--L 335
Cdd:COG1524  181 GRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDV--PPDIDLNRlrL 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 336 APWIKIPSSWVQYytplLAIQPPSGHDAADIVakineglssgkvenGKYLKVYLKEDLpSRLHYvDSDRIPPIIGLVDEG 415
Cdd:COG1524  259 AGLLAVRAGESAH----LYLKDGADAEVRALL--------------GLPARVLTREEL-AAGHF-GPHRIGDLVLVAKPG 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332660261 416 FkveqkkSKAKECGGAHGYDNAfFSMRTIFIGHGPMFSKGrkvpsFENVQIYNVISSILGLK 477
Cdd:COG1524  319 W------ALDAPLKGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
 
Name Accession Description Interval E-value
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 109-435 1.26e-121

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: 359.43  E-value: 1.26e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  109 VLLISSDGFRFGYQFKTK-LPSIHRLIANGTEAETgLIPVFPTLTFPNHYSIVTGLYPAYHGIINNHFVDPETG--NVFT 185
Cdd:pfam01663   1 LLVISLDGFRADYLDRFElTPNLAALAKEGVSAPN-LTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTGeyLVFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  186 MASHE-PEWWLGEPLWETVVNQGLKAATYFWPGSEVHKGSW-NC-PQGLCQNYNGSVPFDDRVDTILS--YFDLPS---- 256
Cdd:pfam01663  80 ISDPEdPRWWQGEPIWDTAAKAGVRAAALFWPGSEVDYSTYyGTpPRYLKDDYNNSVPFEDRVDTAVLqtWLDLPFadva 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  257 NEIPSFMTLYFEDPDHQGHQVGPDDPQITEAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGMVGTCDKKLVVLDDLA 336
Cdd:pfam01663 160 AERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTPVSDDKVIFLNDYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  337 P---WIKIPSSWvqyytPLLAIQPPS-------GHDAADIVAKINEGLSSGKVENGKYLKVYLKEDLPSRLHYvdSDRIP 406
Cdd:pfam01663 240 RekgLLHLVDGG-----PVVAIYPKArelghvpPGEVEEVYAELKEKLLGLRIQDGEHLAVYLKEEIPGRLHY--NPRIP 312

                         330       340       350
                  ....*....|....*....|....*....|.
gi 332660261  407 PIIGLVDEGFKVEQKKSKAKEC--GGAHGYD 435
Cdd:pfam01663 313 DLVLVADPGWYITGKDGGDKEAaiHGTHGYD 343
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 107-475 1.36e-105

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: 315.68  E-value: 1.36e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 107 PVVLLISSDGFRFGY-QFKTKLPSIHRLIANGTEAEtGLIPVFPTLTFPNHYSIVTGLYPAYHGIINNHFVDPETGNVFT 185
Cdd:cd16018    1 PPLIVISIDGFRWDYlDRAGLTPNLKRLAEEGVRAK-YVKPVFPTLTFPNHYSIVTGLYPESHGIVGNYFYDPKTNEEFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 186 M--ASHEPEWWLGEPLWETVVNQGLKAATYFWPGSEVHKGSWNCP----QGLCQNYNGSVPFDDRVDTILSYFDLpsnEI 259
Cdd:cd16018   80 DsdWVWDPWWIGGEPIWVTAEKAGLKTASYFWPGSEVAIIGYNPTpiplGGYWQPYNDSFPFEERVDTILEWLDL---ER 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 260 PSFMTLYFEDPDHQGHQVGPDDPQITEAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGMvgtcdkklvvlddlapwi 339
Cdd:cd16018  157 PDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGM------------------ 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 340 kipsswvqyytpllaiqppsghdaADIvakineglssgkvengkylkvylkedlpsrlhyvdsdrippiiglvdegfkve 419
Cdd:cd16018  219 ------------------------TDV----------------------------------------------------- 221

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332660261 420 qkkskakecgGAHGYDNAFFSMRTIFIGHGPMFSKGRKVPSFENVQIYNVISSILG 475
Cdd:cd16018  222 ----------GTHGYDNELPDMRAIFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 109-477 1.57e-76

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 244.66  E-value: 1.57e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 109 VLLISSDGFRFGYQFKTKLPSIHRLIANGTEAeTGLIPVFPTLTFPNHYSIVTGLYPAYHGIINNHFVDPETGNVFTMAS 188
Cdd:COG1524   26 VVLILVDGLRADLLERAHAPNLAALAARGVYA-RPLTSVFPSTTAPAHTTLLTGLYPGEHGIVGNGWYDPELGRVVNSLS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 189 HEP------EWWLGEPLWETVVNQGLKAATYFWPGSEVHKGS-WNCPQGlcqnYNGSVPF----DDRVDTILSYFDLPSN 257
Cdd:COG1524  105 WVEdgfgsnSLLPVPTIFERARAAGLTTAAVFWPSFEGSGLIdAARPYP----YDGRKPLlgnpAADRWIAAAALELLRE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 258 EIPSFMTLYFEDPDHQGHQVGPDDPQITEAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGMVGTcdKKLVVLDD--L 335
Cdd:COG1524  181 GRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHGMVDV--PPDIDLNRlrL 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 336 APWIKIPSSWVQYytplLAIQPPSGHDAADIVakineglssgkvenGKYLKVYLKEDLpSRLHYvDSDRIPPIIGLVDEG 415
Cdd:COG1524  259 AGLLAVRAGESAH----LYLKDGADAEVRALL--------------GLPARVLTREEL-AAGHF-GPHRIGDLVLVAKPG 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332660261 416 FkveqkkSKAKECGGAHGYDNAfFSMRTIFIGHGPMFSKGrkvpsFENVQIYNVISSILGLK 477
Cdd:COG1524  319 W------ALDAPLKGSHGGLPD-EEMRVPLLASGPGFRPG-----VRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 109-321 2.93e-21

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: 92.48  E-value: 2.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 109 VLLISSDGFRFGYQFKTK-----LPSIHRLIANGTEaeTGLIPV-FPTLTFPNHYSIVTGLYPAYHGIINNHFVDPETGN 182
Cdd:cd00016    3 VVLIVLDGLGADDLGKAGnpaptTPNLKRLASEGAT--FNFRSVsPPTSSAPNHAALLTGAYPTLHGYTGNGSADPELPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 183 VFTmashePEWWLGEPLWETVVNQGLKAATYFwpgsevhkgswncpqglcqnyngsvpfddrvdtILSYFDLPSNEIPSF 262
Cdd:cd00016   81 RAA-----GKDEDGPTIPELLKQAGYRTGVIG---------------------------------LLKAIDETSKEKPFV 122

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332660261 263 MTLYFEDPDHQGHQVGPDDPQITEAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGM 321
Cdd:cd00016  123 LFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGG 181
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 109-320 1.24e-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: 62.18  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 109 VLLISSDGFRF------GYQFKTkLPSIHRLIANGTEAETGLIPVFPTLtfPNHYSIVTGLYPAYHGIINnhfvDPETGN 182
Cdd:cd16148    3 VILIVIDSLRAdhlgcyGYDRVT-TPNLDRLAAEGVVFDNHYSGSNPTL--PSRFSLFTGLYPFYHGVWG----GPLEPD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 183 VFTMASHepewwLGEPLWETVvnqGLKAATYFWPGSEVHKG--SWNCPQGLCQN--YNGSVPFDDRVDTILSYFDLPSNE 258
Cdd:cd16148   76 DPTLAEI-----LRKAGYYTA---AVSSNPHLFGGPGFDRGfdTFEDFRGQEGDpgEEGDERAERVTDRALEWLDRNADD 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332660261 259 IPSFMTLYFEDPdhqgHqvGPD--DPQITEAvvniDRLIGRLIDGLEKRGIFEDvTMIMV-GDHG 320
Cdd:cd16148  148 DPFFLFLHYFDP----H--EPYlyDAEVRYV----DEQIGRLLDKLKELGLLED-TLVIVtSDHG 201
Sulfatase pfam00884
Sulfatase;
107-320 2.40e-09

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 58.59  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  107 PVVLLISSDGFRFGYqfktklpsihrLIANGteaetGLIPVFPTL--------TFPNHYS-----------IVTGLYPAY 167
Cdd:pfam00884   1 PNVVLVLGESLRAPD-----------LGLYG-----YPRPTTPFLdrlaeeglLFSNFYSggtltapsrfaLLTGLPPHN 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  168 HGIINNHFV----DPET-GNVF-------TMASHEPEWWLGEplwETVVNQGLKAATYFWPGSEVHKGSWNCPqGLCQNY 235
Cdd:pfam00884  65 FGSYVSTPVglprTEPSlPDLLkragyntGAIGKWHLGWYNN---QSPCNLGFDKFFGRNTGSDLYADPPDVP-YNCSGG 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  236 NGSvpfDDRV-DTILSYfdLPSNEIPSFMTLYFEDPdHQGHQVGPDDPQITE------------------AVVNIDRLIG 296
Cdd:pfam00884 141 GVS---DEALlDEALEF--LDNNDKPFFLVLHTLGS-HGPPYYPDRYPEKYAtfkpsscseeqllnsydnTLLYTDDAIG 214

                         250       260
                  ....*....|....*....|....
gi 332660261  297 RLIDGLEKRGIFEDVTMIMVGDHG 320
Cdd:pfam00884 215 RVLDKLEENGLLDNTLVVYTSDHG 238
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 113-320 1.38e-08

SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.


Pssm-ID: 293740 [Multi-domain]  Cd Length: 457  Bit Score: 56.77  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 113 SSDGFRfgyqfktklpsihRLIANGTEAETGLIPVFPTLTFPNHYSIVTGLYPAYHGIINNHFVDPETGN-VFTMASHEP 191
Cdd:cd16016   26 GEGGFK-------------RLLNEGFVFENAHYNYAPTDTAPGHATIYTGTTPAIHGIIGNDWYDRETGReVYCVEDSTV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 192 EWWLGEP---------LWETVVNQGLKAATY--------------------------FWPGSEvhKGSW--------NCP 228
Cdd:cd16016   93 TTVGGNStagkmsprnLLVTTIGDELKLATNgrskvigvalkdraailpaghaadaaYWFDDE--TGKFitstyymkELP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 229 QGLcQNYNGSV-PFddrVDTI--------LSYFDLPSNEIPSFMTLYFEDPDHQGHQVGPDDPQITEAVVNIDRLIGRLI 299
Cdd:cd16016  171 AWV-EKFNAKKlPF---GNTLtldfakaaLENEKLGKDDVTDLLAVSFSATDYIGHAFGPNSVEMEDTYLRLDRDLARLL 246

                        250       260
                 ....*....|....*....|.
gi 332660261 300 DGLEKRGIFEDVTMIMVGDHG 320
Cdd:cd16016  247 DALDKKVGKGNYLVFLTADHG 267
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 109-323 6.93e-08

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: 53.21  E-value: 6.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 109 VLLISSDGFRFGY-------QFKTklPSIHRLIANGTeaetglipvfptlTFPNHY-----------SIVTGLYPAYHGI 170
Cdd:cd16022    3 ILLIMTDDLGYDDlgcygnpDIKT--PNLDRLAAEGV-------------RFTNAYvaspvcspsraSLLTGRYPHRHGV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 171 INNhfvdpetgnvftmashePEWWLGEPLWETVVNQGLKAATYFwpgsEVHKGSWNcpqglcqnyNGSVPFDDRVDtils 250
Cdd:cd16022   68 RGN-----------------VGNGGGLPPDEPTLAELLKEAGYR----TALIGKWH---------DEAIDFIERRD---- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 251 yfdlpsNEIPSFMTLYFEDPdhqgHqvgpdDPQITEAVV-NIDRLIGRLIDGLEKRGIFEDvTMI--------MVGDHGM 321
Cdd:cd16022  114 ------KDKPFFLYVSFNAP----H-----PPFAYYAMVsAIDDQIGRILDALEELGLLDN-TLIvftsdhgdMLGDHGL 177


                 ..
gi 332660261 322 VG 323
Cdd:cd16022  178 RG 179
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 109-322 2.38e-05

N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.


Pssm-ID: 293751 [Multi-domain]  Cd Length: 373  Bit Score: 46.35  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 109 VLLISSD--GFRFGYQF----KTklPSIHRLIANGteaetglipvfptLTFPNHY-----------SIVTGLYPAYHGII 171
Cdd:cd16027    3 ILWIIADdlSPDLGGYGgnvvKT--PNLDRLAAEG-------------VRFTNAFttapvcspsrsALLTGLYPHQNGAH 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 172 NNHfvdpetgnvfTMASHEPEWWlgeplwETVVNQgLKAATYF--------WPGSEVHKGSWNCPQGLCQNYNGsvpfDD 243
Cdd:cd16027   68 GLR----------SRGFPLPDGV------KTLPEL-LREAGYYtgligkthYNPDAVFPFDDEMRGPDDGGRNA----WD 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 244 RVDTILSYFDLPSNEIPSFMTLYFEDPdHQGHQVG------------------PDDPQI-------TEAVVNIDRLIGRL 298
Cdd:cd16027  127 YASNAADFLNRAKKGQPFFLWFGFHDP-HRPYPPGdgeepgydpekvkvppylPDTPEVredladyYDEIERLDQQVGEI 205

                        250       260
                 ....*....|....*....|....*
gi 332660261 299 IDGLEKRGIFEDvTMIMV-GDHGMV 322
Cdd:cd16027  206 LDELEEDGLLDN-TIVIFtSDHGMP 229
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
96-320 2.42e-05

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 46.41  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  96 SVARPLKKLDKPVVLLISSDGFRFGY-------QFKTklPSIHRLIANGTeaetglipvfptlTFPNHY----------- 157
Cdd:COG3119   13 AAAAAAAAAKRPNILFILADDLGYGDlgcygnpLIKT--PNIDRLAAEGV-------------RFTNAYvtspvcspsra 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 158 SIVTGLYPAYHGIINNHFVDPET--GNVFTMASHepewwlgeplwetvvnqgLKAA---TYFWpgsevhkGSWncpqglc 232
Cdd:COG3119   78 SLLTGRYPHRTGVTDNGEGYNGGlpPDEPTLAEL------------------LKEAgyrTALF-------GKW------- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 233 QNYngsvpFDDRV-DTILSYFD--LPSNEiPSFMTLYFEDPdHQGHQVGPDD----------------PQITE------- 286
Cdd:COG3119  126 HLY-----LTDLLtDKAIDFLErqADKDK-PFFLYLAFNAP-HAPYQAPEEYldkydgkdiplppnlaPRDLTeeelrra 198

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 332660261 287 ------AVVNIDRLIGRLIDGLEKRGIFEDvTMIMV-GDHG 320
Cdd:COG3119  199 raayaaMIEEVDDQVGRLLDALEELGLADN-TIVVFtSDNG 238
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 128-321 2.50e-04

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


Pssm-ID: 293768 [Multi-domain]  Cd Length: 257  Bit Score: 42.61  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 128 PSIHRLIANGTeaetglipvfptlTFPNHY-----------SIVTGLYPAYHGI---INNHFVDpetgnvftMASHEPEW 193
Cdd:cd16149   27 PNLDRLAAEGV-------------RFENFFctspvcsparaSLLTGRMPSQHGIhdwIVEGSHG--------KTKKPEGY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 194 WLGEPLWETVvnqgLKAATYFWPGSevhkGSWNCpqglcqnynGsvpfDDRVDTILsyfDLPSNEIPSFMTLYFEDPdhq 273
Cdd:cd16149   86 LEGQTTLPEV----LQDAGYRCGLS----GKWHL---------G----DDAADFLR---RRAEAEKPFFLSVNYTAP--- 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 332660261 274 gHqvgpdDP-QITEAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGM 321
Cdd:cd16149  139 -H-----SPwGYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGF 181
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 84-320 3.22e-04

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 43.10  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261  84 LNQISKSPAFDRSVARPLKKLDKPVVLLISSDGF---RFGYQFKTK--LPSIHRLIANGteaetglipvfptLTFPNHYS 158
Cdd:COG1368  212 ALEIKKYLKSNRPTPNPFGPAKKPNVVVILLESFsdfFIGALGNGKdvTPFLDSLAKES-------------LYFGNFYS 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 159 -----------IVTGLYPAYHGIInnhFVDPETGNVFTMASHepewwlgeplwetvvnqgLKAA---TYFWPGSEvhKGS 224
Cdd:COG1368  279 qggrtsrgefaVLTGLPPLPGGSP---YKRPGQNNFPSLPSI------------------LKKQgyeTSFFHGGD--GSF 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 225 WNCPQGLcqNYNGsvpFDDRVDtiLSYFDLPSNEI---------------------PSFMTLY-------FEDPDHQGHQ 276
Cdd:COG1368  336 WNRDSFY--KNLG---FDEFYD--REDFDDPFDGGwgvsdedlfdkaleeleklkkPFFAFLItlsnhgpYTLPEEDKKI 408

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 332660261 277 VGPDDPQIT---EAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHG 320
Cdd:COG1368  409 PDYGKTTLNnylNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG 455
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 292-321 5.21e-04

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: 41.90  E-value: 5.21e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 332660261 292 DRLIGRLIDGLEKRGIFEDVTMIMVGDHGM 321
Cdd:cd16015  202 DKALGEFIEKLKKSGLYENTIIVIYGDHLP 231
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 102-321 7.57e-04

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


Pssm-ID: 293743 [Multi-domain]  Cd Length: 292  Bit Score: 41.58  E-value: 7.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 102 KKLDKPVVLLIssDGFRFGYQFKTKLPSIHRLIANGTEAETGLIPVF------PTLTFPNHYSIVTGLYPAYHGIINNhf 175
Cdd:cd16019    2 TKYDKVVLIVI--DGLRYDLAVNVNKQSSFFSFLQKLNEQPNNSFLAlsfadpPTVTGPRLKALTTGNPPTFLDLISN-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 176 vdpetgnvftMASHEpewwLGEplwETVVNQgLKAA---TYFWpGSEvhkgSWNCpqgLCQNY----NGSVPFDDR---- 244
Cdd:cd16019   78 ----------FASSE----IKE---DNIIRQ-LKKNgkkILFY-GDD----TWLD---LFPEIftykFTITSFNIRdmhd 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 245 VDTIlSYFDLPSNE-------IPSFMTLYFEDPDHQGH-QVGPDDPQITEAVVNIDRLIGRLIDGLEkrgifEDVTMIMV 316
Cdd:cd16019  132 VDPI-FYNHINDNLdeniyydNWDFIILHFLGLDHLGHkHNTTSSPELEKKLDQMDNLIRDIYDRMD-----NDTLLVVV 205


                 ....*
gi 332660261 317 GDHGM 321
Cdd:cd16019  206 SDHGM 210
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 271-321 7.59e-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: 41.39  E-value: 7.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332660261 271 DHQGHQVGPDDPQITEAVVNIDRLIGRLIDGLekrgiFEDVTMIMVGDHGM 321
Cdd:cd16023  171 DHVGHRYGPNHPEMARKLTQMDQFIRDIIERL-----DDDTLLLVFGDHGM 216
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 271-321 8.52e-04

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: 41.40  E-value: 8.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332660261 271 DHQGHQVGPDDPQITEAVVNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGM 321
Cdd:cd16024  156 DHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQSSNNPTLLVVCGDHGM 206
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 260-323 3.71e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 39.47  E-value: 3.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332660261 260 PSFMTLYFEDPDHQG--HQVGPDDPQITEAV-----------VNIDRLIGRLIDGLEKRGIFEDVTMIMVGDHGM-VG 323
Cdd:cd16155  157 ENFLPQHPFDNGEGTvrDEQLAPFPRTPEAVrqhlaeyyamiTHLDAQIGRILDALEASGELDNTIIVFTSDHGLaVG 234
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 126-334 5.59e-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: 39.13  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 126 KLPSIHRLIANGTeaetglipvfptlTFPNHY-----------SIVTGLYPAYHGIINNhfvdpetGNVFTMASHEPEww 194
Cdd:cd16033   25 KTPNIDRLAAEGV-------------RFTNAYtpspvccparaSLLTGLYPHEHGVLNN-------VENAGAYSRGLP-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 195 LGEPLWetvvNQGLKAA---TYF---WpgsevHKGSWNCPQGL-CQNYNGSVPFDD-----------------------R 244
Cdd:cd16033   83 PGVETF----SEDLREAgyrNGYvgkW-----HVGPEETPLDYgFDEYLPVETTIEyfladraiemleelaaddkpfflR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660261 245 VDT-------ILS--YFDLPSNE-IP---SFMTLYFEDPDHQ------GHQVGPDDPQITEAVVN-------IDRLIGRL 298
Cdd:cd16033  154 VNFwgphdpyIPPepYLDMYDPEdIPlpeSFADDFEDKPYIYrrerkrWGVDTEDEEDWKEIIAHywgyitlIDDAIGRI 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 332660261 299 IDGLEKRGIFEDvTMI--------MVGDHGMVgtcDKKLVVLDD 334
Cdd:cd16033  234 LDALEELGLADD-TLViftsdhgdALGAHRLW---DKGPFMYEE 273
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 291-324 9.11e-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: 9.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 332660261 291 IDRLIGRLIDGLEKRGIFEDVTMIMVGDHG-MVGT 324
Cdd:cd16037  171 LDENIGRVLDALEELGLLDNTLIIYTSDHGdMLGE 205
 
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.
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