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Conserved domains on  [gi|584374963|gb|EWG94854|]
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Mcd4p [Saccharomyces cerevisiae R103]

Protein Classification

GPI ethanolamine phosphate transferase 1( domain architecture ID 10887971)

GPI (glycosylphosphatidylinositol) ethanolamine phosphate transferase 1 catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of the GPI-anchor

Gene Ontology:  GO:0051377|GO:0006506|GO:0005789
PubMed:  10574991|10069808

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PigN pfam04987
Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a ...
 442-874 7.15e-164

Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a mammalian homolog of the yeast protein MCD4P and is expressed in the endoplasmic reticulum. PIG-N is essential for glycosylphosphatidylinositol anchor synthesis. Glycosylphosphatidylinositol (GPI)-anchored proteins are cell surface-localized proteins that serve many important cellular functions.


:

Pssm-ID: 461508  Cd Length: 454  Bit Score: 487.50  E-value: 7.15e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  442 EGLHYLTTYNWRFIRTIVTFGFVGWIFFSFIIFLKSFILENVIDDQK--ASPLSHAVFGS--IGILLNWILFYQHSPFNF 517
Cdd:pfam04987   1 EGLRYYQTYDWLFLRTIVTLGYLGWIAYLLLTVLKLHVLLGSKPSSRttLSTLLGYKFSStlLLVLLYAFLFLQRSPLTY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  518 YMYLLFPLYFWSYIFTNRSVLRSGIKEFFKGT--SPWKRVLI-TISIISVYEGIVYGFFHRWTFTLITNILAFYPFICGV 594
Cdd:pfam04987  81 YLYLLFPVYFWYQILAERPILQAGLKELFSHIksSFVKKPLIqLLLIVGVLELLVLSFFHREILSVGFVLLAFWPLFYGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  595 RELSVN----ILWIITSVLLSTFTLFDAVKIEDLNQIHLAGLLIILSAFYALYKiHSRINSYTRAIFaIQISLVAAMLAV 670
Cdd:pfam04987 161 NFFRKPsllfLTWLLSCLLLSVFPLLPVVKVENLPLILLGGLLILLRGLLLLLF-ERSITSSSRTLL-VQVLLIALSILV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  671 THRSVISLQLRQGLPRESQVAGWIIFFVSLFVMPILHYRKPnndyKVRLLIIYLTFAPSFIILTISFESLFYFLFTSYMV 750
Cdd:pfam04987 239 TGSSVVSLQAKQGLPLGNQVVGWIILVYSLLSLPLLHRTRP----LHRLLSIFLNFAPTFILLSISYESLFYQAFSLELL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  751 QWIEIENKIK----------------EMKTQKDENWLQVLRVSVIGFFLLQVAFFGTGNVASISSFSLESVCRLLPIFDP 814
Cdd:pfam04987 315 LWIELEHELKqeestkqsessdtstkKLKLSSRSLTLSDLRIALFFLFFLQVAFFGTGNIASISSFDLDSVYRFIPVFSP 394

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  815 FLMGALLMLKLIIPYGLLSTCLGILNLKLNFKDYTISSLIISMSDILSLNFFYLLRTEGS 874
Cdd:pfam04987 395 FLMGALLLLKLLIPFVLVSSALGALNKRLRLPPRSLFLLVLLISDVMTLNFFFLVRDEGS 454
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 46-353 1.13e-153

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: 455.12  E-value: 1.13e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  46 PPAKRLFLIVGDGLRADTTFDKVTHpvsgktefLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMIAGFYEDVSAVTKG 125
Cdd:cd16020    2 PPAKRLVVFVADGLRADTFFENNCS--------RAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 126 WKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGASDPnKVDTWMYDHtFEDFTQSSIELDAFVFRHLDQLFHNSTLNSTl 205
Cdd:cd16020   74 WKENPVEFDSVFNRSRRSWAWGSPDILPMFPKGATGG-KVLTYIYPE-EDFDSTDASELDEWVFDKVEEFLANASSNKT- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 206 dYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHP 285
Cdd:cd16020  151 -ELLNQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMTDWGSHGDGSP 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584374963 286 NNTRTPLVAWGAGLNKPVHNPFPVsdnYTENWELSSIKRNDVKQADIASLMSYLIGVNYPKNSVGELP 353
Cdd:cd16020  230 DETETPFIAWGAGIKHPTPGRGPS---FSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
 
Name Accession Description Interval E-value
PigN pfam04987
Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a ...
 442-874 7.15e-164

Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a mammalian homolog of the yeast protein MCD4P and is expressed in the endoplasmic reticulum. PIG-N is essential for glycosylphosphatidylinositol anchor synthesis. Glycosylphosphatidylinositol (GPI)-anchored proteins are cell surface-localized proteins that serve many important cellular functions.


Pssm-ID: 461508  Cd Length: 454  Bit Score: 487.50  E-value: 7.15e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  442 EGLHYLTTYNWRFIRTIVTFGFVGWIFFSFIIFLKSFILENVIDDQK--ASPLSHAVFGS--IGILLNWILFYQHSPFNF 517
Cdd:pfam04987   1 EGLRYYQTYDWLFLRTIVTLGYLGWIAYLLLTVLKLHVLLGSKPSSRttLSTLLGYKFSStlLLVLLYAFLFLQRSPLTY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  518 YMYLLFPLYFWSYIFTNRSVLRSGIKEFFKGT--SPWKRVLI-TISIISVYEGIVYGFFHRWTFTLITNILAFYPFICGV 594
Cdd:pfam04987  81 YLYLLFPVYFWYQILAERPILQAGLKELFSHIksSFVKKPLIqLLLIVGVLELLVLSFFHREILSVGFVLLAFWPLFYGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  595 RELSVN----ILWIITSVLLSTFTLFDAVKIEDLNQIHLAGLLIILSAFYALYKiHSRINSYTRAIFaIQISLVAAMLAV 670
Cdd:pfam04987 161 NFFRKPsllfLTWLLSCLLLSVFPLLPVVKVENLPLILLGGLLILLRGLLLLLF-ERSITSSSRTLL-VQVLLIALSILV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  671 THRSVISLQLRQGLPRESQVAGWIIFFVSLFVMPILHYRKPnndyKVRLLIIYLTFAPSFIILTISFESLFYFLFTSYMV 750
Cdd:pfam04987 239 TGSSVVSLQAKQGLPLGNQVVGWIILVYSLLSLPLLHRTRP----LHRLLSIFLNFAPTFILLSISYESLFYQAFSLELL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  751 QWIEIENKIK----------------EMKTQKDENWLQVLRVSVIGFFLLQVAFFGTGNVASISSFSLESVCRLLPIFDP 814
Cdd:pfam04987 315 LWIELEHELKqeestkqsessdtstkKLKLSSRSLTLSDLRIALFFLFFLQVAFFGTGNIASISSFDLDSVYRFIPVFSP 394

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  815 FLMGALLMLKLIIPYGLLSTCLGILNLKLNFKDYTISSLIISMSDILSLNFFYLLRTEGS 874
Cdd:pfam04987 395 FLMGALLLLKLLIPFVLVSSALGALNKRLRLPPRSLFLLVLLISDVMTLNFFFLVRDEGS 454
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 46-353 1.13e-153

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: 455.12  E-value: 1.13e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  46 PPAKRLFLIVGDGLRADTTFDKVTHpvsgktefLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMIAGFYEDVSAVTKG 125
Cdd:cd16020    2 PPAKRLVVFVADGLRADTFFENNCS--------RAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 126 WKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGASDPnKVDTWMYDHtFEDFTQSSIELDAFVFRHLDQLFHNSTLNSTl 205
Cdd:cd16020   74 WKENPVEFDSVFNRSRRSWAWGSPDILPMFPKGATGG-KVLTYIYPE-EDFDSTDASELDEWVFDKVEEFLANASSNKT- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 206 dYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHP 285
Cdd:cd16020  151 -ELLNQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMTDWGSHGDGSP 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584374963 286 NNTRTPLVAWGAGLNKPVHNPFPVsdnYTENWELSSIKRNDVKQADIASLMSYLIGVNYPKNSVGELP 353
Cdd:cd16020  230 DETETPFIAWGAGIKHPTPGRGPS---FSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 33-276 1.39e-13

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 73.63  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  33 LVHGMSPYQSTPTPPAKRLFLIVGDGLRADTTfdkvthpvsgkTEFLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMI 112
Cdd:COG1524    8 LLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----------ERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 113 AG--------------------------FYEDVSAVTKGWKSNPVnFDSFFNQSTHTYSFGSPDIlpmfkDGASDPNKVD 166
Cdd:COG1524   77 TGlypgehgivgngwydpelgrvvnslsWVEDGFGSNSLLPVPTI-FERARAAGLTTAAVFWPSF-----EGSGLIDAAR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 167 TWMYDHTFEDFTQSsiELDAFVFRHLDQLFHnstlnstldyeiRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDD 246
Cdd:COG1524  151 PYPYDGRKPLLGNP--AADRWIAAAALELLR------------EGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDA 216

                        250       260       270
                 ....*....|....*....|....*....|
gi 584374963 247 QIPILIDKVNKFFADDKTAFIFTADHGMSA 276
Cdd:COG1524  217 ALGRLLDALKARGLYEGTLVIVTADHGMVD 246
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 51-276 9.08e-10

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: 61.28  E-value: 9.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963   51 LFLIVGDGLRADTtFDKVTHpvsgkteflAPFIRSLvMNNATYGISHTRM-PTESRPGHVAMIAGFYED----VSAVTKG 125
Cdd:pfam01663   1 LLVISLDGFRADY-LDRFEL---------TPNLAAL-AKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGshgiVGNTFYD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  126 WKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGasdpNKVDTWMY-----DHTFEDFTQSSIELDAF-----VFRHLDQL 195
Cdd:pfam01663  70 PKTGEYLVFVISDPEDPRWWQGEPIWDTAAKAG----VRAAALFWpgsevDYSTYYGTPPRYLKDDYnnsvpFEDRVDTA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  196 FHNSTLNSTLDYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMS 275
Cdd:pfam01663 146 VLQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMT 225


                  .
gi 584374963  276 A 276
Cdd:pfam01663 226 P 226
PRK13759 PRK13759
arylsulfatase; Provisional
 235-302 4.54e-04

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 43.89  E-value: 4.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584374963 235 AEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGmSAFGSHG---DGHP--NNTRTP-LVAWGAGLNKP 302
Cdd:PRK13759 268 AAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG-DMLGDHYlfrKGYPyeGSAHIPfIIYDPGGLLAG 340
 
Name Accession Description Interval E-value
PigN pfam04987
Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a ...
 442-874 7.15e-164

Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a mammalian homolog of the yeast protein MCD4P and is expressed in the endoplasmic reticulum. PIG-N is essential for glycosylphosphatidylinositol anchor synthesis. Glycosylphosphatidylinositol (GPI)-anchored proteins are cell surface-localized proteins that serve many important cellular functions.


Pssm-ID: 461508  Cd Length: 454  Bit Score: 487.50  E-value: 7.15e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  442 EGLHYLTTYNWRFIRTIVTFGFVGWIFFSFIIFLKSFILENVIDDQK--ASPLSHAVFGS--IGILLNWILFYQHSPFNF 517
Cdd:pfam04987   1 EGLRYYQTYDWLFLRTIVTLGYLGWIAYLLLTVLKLHVLLGSKPSSRttLSTLLGYKFSStlLLVLLYAFLFLQRSPLTY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  518 YMYLLFPLYFWSYIFTNRSVLRSGIKEFFKGT--SPWKRVLI-TISIISVYEGIVYGFFHRWTFTLITNILAFYPFICGV 594
Cdd:pfam04987  81 YLYLLFPVYFWYQILAERPILQAGLKELFSHIksSFVKKPLIqLLLIVGVLELLVLSFFHREILSVGFVLLAFWPLFYGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  595 RELSVN----ILWIITSVLLSTFTLFDAVKIEDLNQIHLAGLLIILSAFYALYKiHSRINSYTRAIFaIQISLVAAMLAV 670
Cdd:pfam04987 161 NFFRKPsllfLTWLLSCLLLSVFPLLPVVKVENLPLILLGGLLILLRGLLLLLF-ERSITSSSRTLL-VQVLLIALSILV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  671 THRSVISLQLRQGLPRESQVAGWIIFFVSLFVMPILHYRKPnndyKVRLLIIYLTFAPSFIILTISFESLFYFLFTSYMV 750
Cdd:pfam04987 239 TGSSVVSLQAKQGLPLGNQVVGWIILVYSLLSLPLLHRTRP----LHRLLSIFLNFAPTFILLSISYESLFYQAFSLELL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  751 QWIEIENKIK----------------EMKTQKDENWLQVLRVSVIGFFLLQVAFFGTGNVASISSFSLESVCRLLPIFDP 814
Cdd:pfam04987 315 LWIELEHELKqeestkqsessdtstkKLKLSSRSLTLSDLRIALFFLFFLQVAFFGTGNIASISSFDLDSVYRFIPVFSP 394

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  815 FLMGALLMLKLIIPYGLLSTCLGILNLKLNFKDYTISSLIISMSDILSLNFFYLLRTEGS 874
Cdd:pfam04987 395 FLMGALLLLKLLIPFVLVSSALGALNKRLRLPPRSLFLLVLLISDVMTLNFFFLVRDEGS 454
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 46-353 1.13e-153

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: 455.12  E-value: 1.13e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  46 PPAKRLFLIVGDGLRADTTFDKVTHpvsgktefLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMIAGFYEDVSAVTKG 125
Cdd:cd16020    2 PPAKRLVVFVADGLRADTFFENNCS--------RAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 126 WKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGASDPnKVDTWMYDHtFEDFTQSSIELDAFVFRHLDQLFHNSTLNSTl 205
Cdd:cd16020   74 WKENPVEFDSVFNRSRRSWAWGSPDILPMFPKGATGG-KVLTYIYPE-EDFDSTDASELDEWVFDKVEEFLANASSNKT- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 206 dYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHP 285
Cdd:cd16020  151 -ELLNQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMTDWGSHGDGSP 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584374963 286 NNTRTPLVAWGAGLNKPVHNPFPVsdnYTENWELSSIKRNDVKQADIASLMSYLIGVNYPKNSVGELP 353
Cdd:cd16020  230 DETETPFIAWGAGIKHPTPGRGPS---FSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 49-340 3.01e-34

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: 131.39  E-value: 3.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  49 KRLFLIVGDGLRADTTFDKVTHPVSGkteflaPFIRSLVMNNATYGISHTRMPTESRPGHVAMIAGFYEDVSAVTkGWks 128
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTT------PNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYT-GN-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 129 npvnfdsFFNQSTHTYSFGSPDilpmfkdgasdpnkvdtWMYDHTFEDFTQSSIELDAFvfrHLDQlfhnstlnsTLDYE 208
Cdd:cd00016   72 -------GSADPELPSRAAGKD-----------------EDGPTIPELLKQAGYRTGVI---GLLK---------AIDET 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 209 IRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHP--- 285
Cdd:cd00016  116 SKEKPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKAdgk 195

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 286 -----NNTRTPLVAWGAGLNKPvhnpfPVSDNYTEnwelssikrndvkQADIASLMSYLI 340
Cdd:cd00016  196 adkshTGMRVPFIAYGPGVKKG-----GVKHELIS-------------QYDIAPTLADLL 237
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 45-350 6.25e-26

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: 108.42  E-value: 6.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  45 TPPAKRLFLIVGDGLRADttFdkvthpVSGKTEFLaPFIRSLVMNNATYG-ISHTRMPTESRPGHVAMIAGfyedvsavt 123
Cdd:cd16024    1 KPAFDKLVFMVIDALRAD--F------VFGPDSNM-PFTQSLINSGSALAfTAKAQPPTVTMPRIKALTTG--------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 124 kgwkSNPvNF-DSFFNqsthtysFGSPDILP------MFKDGasdpNKV-----DTW--MYDHTFE-----------DFT 178
Cdd:cd16024   63 ----SIP-SFlDVVLN-------FASSLLEEdnwlsqLKAAG----KKIvfygdDTWlkLFPGSFTrsdgttsffvsDFT 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 179 qssiELDAFVFRHLDQLFHNStlnstldyeirqDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKF 258
Cdd:cd16024  127 ----EVDNNVTRHLDSELSRD------------DWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQ 190

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 259 FADDKTAFIFTADHGMSAFGSHGDGHPNNTRTPLVAWGAGLNKpvhNPFPVSDNYTENWElssikrndVKQADIASLMSY 338
Cdd:cd16024  191 SSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSS---KPSNADGELSYYET--------VQQVDLAPTLAL 259

                        330
                 ....*....|..
gi 584374963 339 LIGVNYPKNSVG 350
Cdd:cd16024  260 LLGLPIPKNSVG 271
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 46-352 1.10e-13

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: 72.78  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  46 PPAKRLFLIVGDGLRADTTFDK-VTHPVSGKTEFLAPFIRSLVMnnaTYGISHTrmPTESRPGHVAMIAGFYEDVSAVTK 124
Cdd:cd16019    2 TKYDKVVLIVIDGLRYDLAVNVnKQSSFFSFLQKLNEQPNNSFL---ALSFADP--PTVTGPRLKALTTGNPPTFLDLIS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 125 GWKSNPVNFDSFFNQ----STHTYSFGSPDILPMFkdgasdPNKVDtwmYDHTFEDFT-QSSIELDAFVFRHLdqlfhns 199
Cdd:cd16019   77 NFASSEIKEDNIIRQlkknGKKILFYGDDTWLDLF------PEIFT---YKFTITSFNiRDMHDVDPIFYNHI------- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 200 tlNSTLDYEIRQDG-NVFFLHLLGCDTAGHSYR-PYSAEYYDNVKYIDDQIPILIDKVnkffaDDKTAFIFTADHGMSAF 277
Cdd:cd16019  141 --NDNLDENIYYDNwDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRM-----DNDTLLVVVSDHGMNND 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 278 GSHGDGHPNNTRTPLVAWGA-GLNKPvhNPFPVSDNYTENWELSSIKR----NDVKQADIASLMSYLIGVNYPKNSVGEL 352
Cdd:cd16019  214 GNHGGSSTEETSSFFFFISKkGFFKK--RPIDQIEKIKQNNEQQKIDPseyiRIIYQIDILPTICYLLGIPIPFNNIGII 291
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 33-276 1.39e-13

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 73.63  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  33 LVHGMSPYQSTPTPPAKRLFLIVGDGLRADTTfdkvthpvsgkTEFLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMI 112
Cdd:COG1524    8 LLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----------ERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 113 AG--------------------------FYEDVSAVTKGWKSNPVnFDSFFNQSTHTYSFGSPDIlpmfkDGASDPNKVD 166
Cdd:COG1524   77 TGlypgehgivgngwydpelgrvvnslsWVEDGFGSNSLLPVPTI-FERARAAGLTTAAVFWPSF-----EGSGLIDAAR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 167 TWMYDHTFEDFTQSsiELDAFVFRHLDQLFHnstlnstldyeiRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDD 246
Cdd:COG1524  151 PYPYDGRKPLLGNP--AADRWIAAAALELLR------------EGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDA 216

                        250       260       270
                 ....*....|....*....|....*....|
gi 584374963 247 QIPILIDKVNKFFADDKTAFIFTADHGMSA 276
Cdd:COG1524  217 ALGRLLDALKARGLYEGTLVIVTADHGMVD 246
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 49-303 8.79e-13

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: 69.54  E-value: 8.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  49 KRLFLIVGDGLRADTtFDKVTHpvsgkteflAPFIRSLvMNNATYGIS-HTRMPTESRPGHVAMIAGFYEDVSAVTKGWK 127
Cdd:cd16018    1 PPLIVISIDGFRWDY-LDRAGL---------TPNLKRL-AEEGVRAKYvKPVFPTLTFPNHYSIVTGLYPESHGIVGNYF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 128 SNPVNFDSFFNQSTHTYSF--GSPDILPMF-KDGAsdpnKVDTWMY---DHTFEDFTQSSIELDAFVFRHLDQLFHNSTL 201
Cdd:cd16018   70 YDPKTNEEFSDSDWVWDPWwiGGEPIWVTAeKAGL----KTASYFWpgsEVAIIGYNPTPIPLGGYWQPYNDSFPFEERV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 202 NSTLDYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHG 281
Cdd:cd16018  146 DTILEWLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDVGTHG 225

                        250       260
                 ....*....|....*....|...
gi 584374963 282 -DGHPNNTRTPLVAWGAGLNKPV 303
Cdd:cd16018  226 yDNELPDMRAIFIARGPAFKKGK 248
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 166-350 6.27e-12

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: 67.20  E-value: 6.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 166 DTWM--------YDHTFEDFTQSSIE-LDAFVFRHLdqlfhNSTLNSTLDYEirqdgnVFFLHLLGCDTAGHSYRPYSAE 236
Cdd:cd16023  115 DTWTslfpnqfdRSYPFPSFNVKDLDtVDNGVLKHL-----FPELQSEDDWD------LLIAHFLGVDHVGHRYGPNHPE 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 237 YYDNVKYIDDQIPILIDKVnkffaDDKTAFIFTADHGMSAFGSHGDGHPNNTRTPLVAWG-AGLNKPVHNPFPVSDNYTE 315
Cdd:cd16023  184 MARKLTQMDQFIRDIIERL-----DDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSkRPFNNSDEPIESNGPGDPS 258

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 584374963 316 NWElssikrnDVKQADIASLMSYLIGVNYPKNSVG 350
Cdd:cd16023  259 KVR-------SVPQIDLVPTLSLLLGLPIPFSNLG 286
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 51-276 9.08e-10

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: 61.28  E-value: 9.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963   51 LFLIVGDGLRADTtFDKVTHpvsgkteflAPFIRSLvMNNATYGISHTRM-PTESRPGHVAMIAGFYED----VSAVTKG 125
Cdd:pfam01663   1 LLVISLDGFRADY-LDRFEL---------TPNLAAL-AKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGshgiVGNTFYD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  126 WKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGasdpNKVDTWMY-----DHTFEDFTQSSIELDAF-----VFRHLDQL 195
Cdd:pfam01663  70 PKTGEYLVFVISDPEDPRWWQGEPIWDTAAKAG----VRAAALFWpgsevDYSTYYGTPPRYLKDDYnnsvpFEDRVDTA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  196 FHNSTLNSTLDYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMS 275
Cdd:pfam01663 146 VLQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMT 225


                  .
gi 584374963  276 A 276
Cdd:pfam01663 226 P 226
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 49-310 2.04e-09

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: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  49 KRLFLIVGDGLRADTTfdkvthPVSGKTEFLAPFI-----RSLVMNNATYGISHTRmptesrPGHVAMIAG---FYEDVS 120
Cdd:cd16148    1 MNVILIVIDSLRADHL------GCYGYDRVTTPNLdrlaaEGVVFDNHYSGSNPTL------PSRFSLFTGlypFYHGVW 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 121 AVTKGwKSNPVNFDSFFNQSTHTYSFGSPDILPMFkdgasdpnkvdtWMYDHTFEDFTQSS-IELDAFVFRHLDQLFHNS 199
Cdd:cd16148   69 GGPLE-PDDPTLAEILRKAGYYTAAVSSNPHLFGG------------PGFDRGFDTFEDFRgQEGDPGEEGDERAERVTD 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 200 TLNSTLDyEIRQDGNvFFLHLLgCDTAGHSYRpysaeyYDN-VKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSaFG 278
Cdd:cd16148  136 RALEWLD-RNADDDP-FFLFLH-YFDPHEPYL------YDAeVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEE-FG 205

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 584374963 279 SHG--DGHPNN-----TRTPLVAWGAGLNKPVHNPFPVS 310
Cdd:cd16148  206 EHGlyWGHGSNlydeqLHVPLIIRWPGKEPGKRVDALVS 244
Sulfatase pfam00884
Sulfatase;
51-302 1.82e-08

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 57.05  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963   51 LFLIVGDGLRADttFDKVTHPVSGKTEFLAPFIRSLVMNNATYgiSHTRMPTESRPghvAMIAGFY-EDVSAVTKGWKSN 129
Cdd:pfam00884   3 VVLVLGESLRAP--DLGLYGYPRPTTPFLDRLAEEGLLFSNFY--SGGTLTAPSRF---ALLTGLPpHNFGSYVSTPVGL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  130 PVNFDSFFNQ------STHTYSFGSPDILPMFkdgaSDPNKVDTWMYDH--TFEDFTQSSIELDAFVF-RHLDQLFhnst 200
Cdd:pfam00884  76 PRTEPSLPDLlkragyNTGAIGKWHLGWYNNQ----SPCNLGFDKFFGRntGSDLYADPPDVPYNCSGgGVSDEAL---- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  201 LNSTLDYEIRQDGNVF-FLHLLGCDTAGHSYRPYSAEY----------------YDN-VKYIDDQIPILIDKVNKFFADD 262
Cdd:pfam00884 148 LDEALEFLDNNDKPFFlVLHTLGSHGPPYYPDRYPEKYatfkpsscseeqllnsYDNtLLYTDDAIGRVLDKLEENGLLD 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 584374963  263 KTAFIFTADHGMSAFGSHGDGHPNN--------TRTPLVAWGAGLNKP 302
Cdd:pfam00884 228 NTLVVYTSDHGESLGEGGGYLHGGKydnapeggYRVPLLIWSPGGKAK 275
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
230-369 1.74e-06

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 51.42  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 230 YRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSaFGSHG------DGHPNNTRTPLVAWGAGLNKPV 303
Cdd:COG3119  195 LRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS-LGEHGlrggkgTLYEGGIRVPLIVRWPGKIKAG 273

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584374963 304 HnpfpVSDNYTENWelssikrndvkqaDIA-SLMSyLIGVNYPKNSVGE--LPiaYIDGKESDKLAALY 369
Cdd:COG3119  274 S----VSDALVSLI-------------DLLpTLLD-LAGVPIPEDLDGRslLP--LLTGEKAEWRDYLY 322
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 237-310 5.23e-06

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: 49.50  E-value: 5.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 237 YYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHG-----------MSAF-GShgdghpnnTRTPLVAWGAGLNKPVH 304
Cdd:cd16032  166 YYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGdmlgerglwykMSFFeGS--------ARVPLIISAPGRFAPRR 237


                 ....*.
gi 584374963 305 NPFPVS 310
Cdd:cd16032  238 VAEPVS 243
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 235-281 5.99e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 49.49  E-value: 5.99e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 584374963 235 AEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMsAFGSHG 281
Cdd:cd16155  192 AEYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGL-AVGSHG 237
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 235-310 8.28e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 49.08  E-value: 8.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 235 AEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHG--MSAFGSHGDG--HPNNTRTPLVAWGAGLNKPVHNPFPVS 310
Cdd:cd16037  162 AAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGdmLGERGLWGKStmYEESVRVPMIISGPGIPAGKRVKTPVS 241
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 228-281 2.17e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 47.95  E-value: 2.17e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 584374963 228 HSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHG-MsaFGSHG 281
Cdd:cd16034  220 AGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGdM--LGSHG 272
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 230-281 5.77e-05

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


Pssm-ID: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 46.45  E-value: 5.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 584374963 230 YRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAfGSHG 281
Cdd:cd16033  212 WKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDAL-GAHR 262
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 216-298 6.90e-05

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: 45.51  E-value: 6.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 216 FFLHLlgCDTAGHSyrPYsaEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSaFGSHGD--GHPNN----TR 289
Cdd:cd16022  118 FFLYV--SFNAPHP--PF--AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDM-LGDHGLrgKKGSLyeggIR 190


                 ....*....
gi 584374963 290 TPLVAWGAG 298
Cdd:cd16022  191 VPFIVRWPG 199
PRK13759 PRK13759
arylsulfatase; Provisional
 235-302 4.54e-04

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 43.89  E-value: 4.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584374963 235 AEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGmSAFGSHG---DGHP--NNTRTP-LVAWGAGLNKP 302
Cdd:PRK13759 268 AAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG-DMLGDHYlfrKGYPyeGSAHIPfIIYDPGGLLAG 340
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 235-360 7.21e-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: 42.88  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 235 AEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHPNNTRTPLVAWGAGlnkpVHNPFPVSDNYT 314
Cdd:cd16027  189 ADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFPRAKGTLYDSGLRVPLIVRWPG----KIKPGSVSDALV 264

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 584374963 315 enwelSSIkrndvkqaDIA-SLMSyLIGVNYPKnsvgelpiaYIDGK 360
Cdd:cd16027  265 -----SFI--------DLApTLLD-LAGIEPPE---------YLQGR 288
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 225-292 8.36e-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: 42.23  E-value: 8.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584374963 225 TAGHSyrPYsaEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAfGSHGDGHPNNTRTPL 292
Cdd:cd16149  136 TAPHS--PW--GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNM-GHHGIWGKGNGTFPL 198
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 243-310 1.33e-03

uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; 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: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 42.37  E-value: 1.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584374963 243 YIDDQIPILIDKVNKFFADdkTAFIFTADHG--MSAFGSHGDG---HPNNTRTPLVAWG-AGLNKPVHNPFPVS 310
Cdd:cd16156  249 FVDYEIGRVLDAADEIAED--AWVIYTSDHGdmLGAHKLWAKGpavYDEITNIPLIIRGkGGEKAGTVTDTPVS 320
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 135-343 1.58e-03

Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.


Pssm-ID: 293741 [Multi-domain]  Cd Length: 288  Bit Score: 41.45  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 135 SFFNQSTHTYSFGSPDILPMFKDgasdpNKVDTWMYDhtfedfTQSSIELDAFVFRHLDQLFHNSTLNSTLDYEIRQDG- 213
Cdd:cd16017   60 SFANRENYDRAYYQENLIDLAKK-----AGYKTYWIS------NQGGCGGYDTRISAIAKIETVFTNKGSCNSSNCYDEa 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 214 ---------------NVFFLHLLG-----CDTAGHSYRPYSAEY---------------YDN-VKYIDDQIPILIDKVNK 257
Cdd:cd16017  129 llplldealadsskkKLIVLHLMGshgpyYDRYPEEFAKFTPDCdnelqscskeelinaYDNsILYTDYVLSQIIERLKK 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 258 ffADDKTAFIFTADHGMSAFGS----HGDG--HPNNTRTPLVAWGaglnkpvhnpfpvSDNYTENWELSSIKRNDVK--- 328
Cdd:cd16017  209 --KDKDAALIYFSDHGESLGENglylHGAPyaPKEQYHVPFIIWS-------------SDSYKQRYPVERLRANKDRpfs 273

                        250
                 ....*....|....*
gi 584374963 329 QADIASLMSYLIGVN 343
Cdd:cd16017  274 HDNLFHTLLGLLGIK 288
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 208-302 3.56e-03

Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.


Pssm-ID: 396305  Cd Length: 410  Bit Score: 40.85  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963  208 EIRQDGNVFFLHLLGCDTAGHSYRPysAEYYDNVKYIDDQIPILIDKVNkffaDDKTAFIFTADHG----MsafgsHGDG 283
Cdd:pfam01676 295 ALKEKYDFVFVNFANTDMVGHTGDV--EGKVKAIEAVDERLGELLDALE----EDDGLLIITADHGnpeeM-----KDTD 363

                          90       100
                  ....*....|....*....|.
gi 584374963  284 HpnnTR--TPLVAWGAGLNKP 302
Cdd:pfam01676 364 H---TRepVPILIYGKGVRPD 381
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 229-313 4.54e-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: 39.97  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 229 SYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMS---AFGSHGDGHPNNTRTPLVAWGAGLNKPVHN 305
Cdd:cd16015  186 EDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSlgsDYDETDEDPLDLYRTPLLIYSPGLKKPKKI 265


                 ....*...
gi 584374963 306 PFPVSDNY 313
Cdd:cd16015  266 DRVGSQID 273
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 235-310 4.77e-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: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 40.29  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584374963 235 AEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHgmsafGSH-----GD----GHPNNTRTPLVAWGAGLNKPVHN 305
Cdd:cd16152  175 PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH-----GCHfrtrnAEykrsCHESSIRVPLVIYGPGFNGGGRV 249


                 ....*
gi 584374963 306 PFPVS 310
Cdd:cd16152  250 EELVS 254
 
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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