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Conserved domains on  [gi|6322683|ref|NP_012756|]
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mannose-ethanolamine phosphotransferase MCD4 [Saccharomyces cerevisiae S288C]

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 1.08e-163

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: 485.96  E-value: 1.08e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    442 EGLHYLTTYNWRFIRTIVTFGFVGWIFFSFIIFLKSFILENVIDDQK--ASPLSHAVFGS--IGILLNWILFYQHSPFNF 517
Cdd:pfam04987   1 EGLRYYQTYDWLFLRTIVTLGYLGWIAYLLLTVLKLHVLLGSKPSSRttLSTLLGYKFSStlLLVLLYAFLFLQRSPLTY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    518 YMYLLFPLYFWSYIFTNRSVLRSGIKEFFKGT--SPWKRVLI-TISIISVYEGIVYGFFHRWTFTLITNILAFYPFICGV 594
Cdd:pfam04987  81 YLYLLFPVYFWYQILAERPILQAGLKELFSHIksSFVKKPLIqLLLIVGVLELLVLSFFHREILSVGFVLLAFWPLFYGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    595 RELSVN----ILWIITSVLLSTFTLFDAVKIEDLNQIHLAGLLIILSAFYALYKiHSRINSYTRAIFaIQISLVAAMLAV 670
Cdd:pfam04987 161 NFFRKPsllfLTWLLSCLLLSVFPLLPVVKVENLPLILLGGLLILLRGLLLLLF-ERSITSSSRTLL-VQVLLIALSILV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    671 THRSVISLQLRQGLPRESQVAGWIIFFVSLFVMPILHYRKPnndyKVRLLIIYLTFAPSFIILTISFESLFYFLFTSYMV 750
Cdd:pfam04987 239 TGSSVVSLQAKQGLPLGNQVVGWIILVYSLLSLPLLHRTRP----LHRLLSIFLNFAPTFILLSISYESLFYQAFSLELL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    751 QWIEIENKIK----------------EMKTQKDENWLQVLRVSVIGFFLLQVAFFGTGNVASISSFSLESVCRLLPIFDP 814
Cdd:pfam04987 315 LWIELEHELKqeestkqsessdtstkKLKLSSRSLTLSDLRIALFFLFFLQVAFFGTGNIASISSFDLDSVYRFIPVFSP 394

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    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 7.04e-154

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: 454.35  E-value: 7.04e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683   46 PPAKRLFLIVGDGLRADTTFDKVTHpvsgktefLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMIAGFYEDVSAVTKG 125
Cdd:cd16020   2 PPAKRLVVFVADGLRADTFFENNCS--------RAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  126 WKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGASDPnKVDTWMYDHtFEDFTQSSIELDAFVFRHLDQLFHNSTLNSTl 205
Cdd:cd16020  74 WKENPVEFDSVFNRSRRSWAWGSPDILPMFPKGATGG-KVLTYIYPE-EDFDSTDASELDEWVFDKVEEFLANASSNKT- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  206 dYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHP 285
Cdd:cd16020 151 -ELLNQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMTDWGSHGDGSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322683  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 1.08e-163

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: 485.96  E-value: 1.08e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    442 EGLHYLTTYNWRFIRTIVTFGFVGWIFFSFIIFLKSFILENVIDDQK--ASPLSHAVFGS--IGILLNWILFYQHSPFNF 517
Cdd:pfam04987   1 EGLRYYQTYDWLFLRTIVTLGYLGWIAYLLLTVLKLHVLLGSKPSSRttLSTLLGYKFSStlLLVLLYAFLFLQRSPLTY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    518 YMYLLFPLYFWSYIFTNRSVLRSGIKEFFKGT--SPWKRVLI-TISIISVYEGIVYGFFHRWTFTLITNILAFYPFICGV 594
Cdd:pfam04987  81 YLYLLFPVYFWYQILAERPILQAGLKELFSHIksSFVKKPLIqLLLIVGVLELLVLSFFHREILSVGFVLLAFWPLFYGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    595 RELSVN----ILWIITSVLLSTFTLFDAVKIEDLNQIHLAGLLIILSAFYALYKiHSRINSYTRAIFaIQISLVAAMLAV 670
Cdd:pfam04987 161 NFFRKPsllfLTWLLSCLLLSVFPLLPVVKVENLPLILLGGLLILLRGLLLLLF-ERSITSSSRTLL-VQVLLIALSILV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    671 THRSVISLQLRQGLPRESQVAGWIIFFVSLFVMPILHYRKPnndyKVRLLIIYLTFAPSFIILTISFESLFYFLFTSYMV 750
Cdd:pfam04987 239 TGSSVVSLQAKQGLPLGNQVVGWIILVYSLLSLPLLHRTRP----LHRLLSIFLNFAPTFILLSISYESLFYQAFSLELL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    751 QWIEIENKIK----------------EMKTQKDENWLQVLRVSVIGFFLLQVAFFGTGNVASISSFSLESVCRLLPIFDP 814
Cdd:pfam04987 315 LWIELEHELKqeestkqsessdtstkKLKLSSRSLTLSDLRIALFFLFFLQVAFFGTGNIASISSFDLDSVYRFIPVFSP 394

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    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 7.04e-154

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: 454.35  E-value: 7.04e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683   46 PPAKRLFLIVGDGLRADTTFDKVTHpvsgktefLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMIAGFYEDVSAVTKG 125
Cdd:cd16020   2 PPAKRLVVFVADGLRADTFFENNCS--------RAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  126 WKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGASDPnKVDTWMYDHtFEDFTQSSIELDAFVFRHLDQLFHNSTLNSTl 205
Cdd:cd16020  74 WKENPVEFDSVFNRSRRSWAWGSPDILPMFPKGATGG-KVLTYIYPE-EDFDSTDASELDEWVFDKVEEFLANASSNKT- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  206 dYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHP 285
Cdd:cd16020 151 -ELLNQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMTDWGSHGDGSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322683  286 NNTRTPLVAWGAGLNKPVHNPFPVsdnYTENWELSSIKRNDVKQADIASLMSYLIGVNYPKNSVGELP 353
Cdd:cd16020 230 DETETPFIAWGAGIKHPTPGRGPS---FSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 33-276 1.31e-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: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683   33 LVHGMSPYQSTPTPPAKRLFLIVGDGLRADTTfdkvthpvsgkTEFLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMI 112
Cdd:COG1524   8 LLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----------ERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  113 AG--------------------------FYEDVSAVTKGWKSNPVnFDSFFNQSTHTYSFGSPDIlpmfkDGASDPNKVD 166
Cdd:COG1524  77 TGlypgehgivgngwydpelgrvvnslsWVEDGFGSNSLLPVPTI-FERARAAGLTTAAVFWPSF-----EGSGLIDAAR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  167 TWMYDHTFEDFTQSsiELDAFVFRHLDQLFHnstlnstldyeiRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDD 246
Cdd:COG1524 151 PYPYDGRKPLLGNP--AADRWIAAAALELLR------------EGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDA 216

                       250       260       270
                ....*....|....*....|....*....|
gi 6322683  247 QIPILIDKVNKFFADDKTAFIFTADHGMSA 276
Cdd:COG1524 217 ALGRLLDALKARGLYEGTLVIVTADHGMVD 246
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 51-276 9.89e-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: 9.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683     51 LFLIVGDGLRADTtFDKVTHpvsgkteflAPFIRSLvMNNATYGISHTRM-PTESRPGHVAMIAGFYED----VSAVTKG 125
Cdd:pfam01663   1 LLVISLDGFRADY-LDRFEL---------TPNLAAL-AKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGshgiVGNTFYD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    126 WKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGasdpNKVDTWMY-----DHTFEDFTQSSIELDAF-----VFRHLDQL 195
Cdd:pfam01663  70 PKTGEYLVFVISDPEDPRWWQGEPIWDTAAKAG----VRAAALFWpgsevDYSTYYGTPPRYLKDDYnnsvpFEDRVDTA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    196 FHNSTLNSTLDYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMS 275
Cdd:pfam01663 146 VLQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMT 225


                  .
gi 6322683    276 A 276
Cdd:pfam01663 226 P 226
PRK13759 PRK13759
arylsulfatase; Provisional
 235-302 4.29e-04

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 43.89  E-value: 4.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322683   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 1.08e-163

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: 485.96  E-value: 1.08e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    442 EGLHYLTTYNWRFIRTIVTFGFVGWIFFSFIIFLKSFILENVIDDQK--ASPLSHAVFGS--IGILLNWILFYQHSPFNF 517
Cdd:pfam04987   1 EGLRYYQTYDWLFLRTIVTLGYLGWIAYLLLTVLKLHVLLGSKPSSRttLSTLLGYKFSStlLLVLLYAFLFLQRSPLTY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    518 YMYLLFPLYFWSYIFTNRSVLRSGIKEFFKGT--SPWKRVLI-TISIISVYEGIVYGFFHRWTFTLITNILAFYPFICGV 594
Cdd:pfam04987  81 YLYLLFPVYFWYQILAERPILQAGLKELFSHIksSFVKKPLIqLLLIVGVLELLVLSFFHREILSVGFVLLAFWPLFYGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    595 RELSVN----ILWIITSVLLSTFTLFDAVKIEDLNQIHLAGLLIILSAFYALYKiHSRINSYTRAIFaIQISLVAAMLAV 670
Cdd:pfam04987 161 NFFRKPsllfLTWLLSCLLLSVFPLLPVVKVENLPLILLGGLLILLRGLLLLLF-ERSITSSSRTLL-VQVLLIALSILV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    671 THRSVISLQLRQGLPRESQVAGWIIFFVSLFVMPILHYRKPnndyKVRLLIIYLTFAPSFIILTISFESLFYFLFTSYMV 750
Cdd:pfam04987 239 TGSSVVSLQAKQGLPLGNQVVGWIILVYSLLSLPLLHRTRP----LHRLLSIFLNFAPTFILLSISYESLFYQAFSLELL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    751 QWIEIENKIK----------------EMKTQKDENWLQVLRVSVIGFFLLQVAFFGTGNVASISSFSLESVCRLLPIFDP 814
Cdd:pfam04987 315 LWIELEHELKqeestkqsessdtstkKLKLSSRSLTLSDLRIALFFLFFLQVAFFGTGNIASISSFDLDSVYRFIPVFSP 394

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    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 7.04e-154

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: 454.35  E-value: 7.04e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683   46 PPAKRLFLIVGDGLRADTTFDKVTHpvsgktefLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMIAGFYEDVSAVTKG 125
Cdd:cd16020   2 PPAKRLVVFVADGLRADTFFENNCS--------RAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  126 WKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGASDPnKVDTWMYDHtFEDFTQSSIELDAFVFRHLDQLFHNSTLNSTl 205
Cdd:cd16020  74 WKENPVEFDSVFNRSRRSWAWGSPDILPMFPKGATGG-KVLTYIYPE-EDFDSTDASELDEWVFDKVEEFLANASSNKT- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  206 dYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHP 285
Cdd:cd16020 151 -ELLNQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMTDWGSHGDGSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322683  286 NNTRTPLVAWGAGLNKPVHNPFPVsdnYTENWELSSIKRNDVKQADIASLMSYLIGVNYPKNSVGELP 353
Cdd:cd16020 230 DETETPFIAWGAGIKHPTPGRGPS---FSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 49-340 4.42e-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: 131.00  E-value: 4.42e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683   49 KRLFLIVGDGLRADTTFDKVTHPVSGkteflaPFIRSLVMNNATYGISHTRMPTESRPGHVAMIAGFYEDVSAVTkGWks 128
Cdd:cd00016   1 KHVVLIVLDGLGADDLGKAGNPAPTT------PNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYT-GN-- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  129 npvnfdsFFNQSTHTYSFGSPDilpmfkdgasdpnkvdtWMYDHTFEDFTQSSIELDAFvfrHLDQlfhnstlnsTLDYE 208
Cdd:cd00016  72 -------GSADPELPSRAAGKD-----------------EDGPTIPELLKQAGYRTGVI---GLLK---------AIDET 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  209 IRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHP--- 285
Cdd:cd00016 116 SKEKPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKAdgk 195

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  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 1.02e-25

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: 107.65  E-value: 1.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683   45 TPPAKRLFLIVGDGLRADttFdkvthpVSGKTEFLaPFIRSLVMNNATYG-ISHTRMPTESRPGHVAMIAGfyedvsavt 123
Cdd:cd16024   1 KPAFDKLVFMVIDALRAD--F------VFGPDSNM-PFTQSLINSGSALAfTAKAQPPTVTMPRIKALTTG--------- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  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 6322683  179 qssiELDAFVFRHLDQLFHNStlnstldyeirqDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKF 258
Cdd:cd16024 127 ----EVDNNVTRHLDSELSRD------------DWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQ 190

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  259 FADDKTAFIFTADHGMSAFGSHGDGHPNNTRTPLVAWGAGLNKpvhNPFPVSDNYTENWElssikrndVKQADIASLMSY 338
Cdd:cd16024 191 SSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSS---KPSNADGELSYYET--------VQQVDLAPTLAL 259

                       330
                ....*....|..
gi 6322683  339 LIGVNYPKNSVG 350
Cdd:cd16024 260 LLGLPIPKNSVG 271
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 46-352 1.14e-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: 1.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683   46 PPAKRLFLIVGDGLRADTTFDK-VTHPVSGKTEFLAPFIRSLVMnnaTYGISHTrmPTESRPGHVAMIAGFYEDVSAVTK 124
Cdd:cd16019   2 TKYDKVVLIVIDGLRYDLAVNVnKQSSFFSFLQKLNEQPNNSFL---ALSFADP--PTVTGPRLKALTTGNPPTFLDLIS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  125 GWKSNPVNFDSFFNQ----STHTYSFGSPDILPMFkdgasdPNKVDtwmYDHTFEDFT-QSSIELDAFVFRHLdqlfhns 199
Cdd:cd16019  77 NFASSEIKEDNIIRQlkknGKKILFYGDDTWLDLF------PEIFT---YKFTITSFNiRDMHDVDPIFYNHI------- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  200 tlNSTLDYEIRQDG-NVFFLHLLGCDTAGHSYR-PYSAEYYDNVKYIDDQIPILIDKVnkffaDDKTAFIFTADHGMSAF 277
Cdd:cd16019 141 --NDNLDENIYYDNwDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRM-----DNDTLLVVVSDHGMNND 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  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 1.31e-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: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683   33 LVHGMSPYQSTPTPPAKRLFLIVGDGLRADTTfdkvthpvsgkTEFLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMI 112
Cdd:COG1524   8 LLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----------ERAHAPNLAALAARGVYARPLTSVFPSTTAPAHTTLL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  113 AG--------------------------FYEDVSAVTKGWKSNPVnFDSFFNQSTHTYSFGSPDIlpmfkDGASDPNKVD 166
Cdd:COG1524  77 TGlypgehgivgngwydpelgrvvnslsWVEDGFGSNSLLPVPTI-FERARAAGLTTAAVFWPSF-----EGSGLIDAAR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  167 TWMYDHTFEDFTQSsiELDAFVFRHLDQLFHnstlnstldyeiRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDD 246
Cdd:COG1524 151 PYPYDGRKPLLGNP--AADRWIAAAALELLR------------EGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDA 216

                       250       260       270
                ....*....|....*....|....*....|
gi 6322683  247 QIPILIDKVNKFFADDKTAFIFTADHGMSA 276
Cdd:COG1524 217 ALGRLLDALKARGLYEGTLVIVTADHGMVD 246
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 49-303 9.91e-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: 9.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683   49 KRLFLIVGDGLRADTtFDKVTHpvsgkteflAPFIRSLvMNNATYGIS-HTRMPTESRPGHVAMIAGFYEDVSAVTKGWK 127
Cdd:cd16018   1 PPLIVISIDGFRWDY-LDRAGL---------TPNLKRL-AEEGVRAKYvKPVFPTLTFPNHYSIVTGLYPESHGIVGNYF 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  128 SNPVNFDSFFNQSTHTYSF--GSPDILPMF-KDGAsdpnKVDTWMY---DHTFEDFTQSSIELDAFVFRHLDQLFHNSTL 201
Cdd:cd16018  70 YDPKTNEEFSDSDWVWDPWwiGGEPIWVTAeKAGL----KTASYFWpgsEVAIIGYNPTPIPLGGYWQPYNDSFPFEERV 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  202 NSTLDYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHG 281
Cdd:cd16018 146 DTILEWLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDVGTHG 225

                       250       260
                ....*....|....*....|...
gi 6322683  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 7.31e-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: 7.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  166 DTWM--------YDHTFEDFTQSSIE-LDAFVFRHLdqlfhNSTLNSTLDYEirqdgnVFFLHLLGCDTAGHSYRPYSAE 236
Cdd:cd16023 115 DTWTslfpnqfdRSYPFPSFNVKDLDtVDNGVLKHL-----FPELQSEDDWD------LLIAHFLGVDHVGHRYGPNHPE 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  237 YYDNVKYIDDQIPILIDKVnkffaDDKTAFIFTADHGMSAFGSHGDGHPNNTRTPLVAWG-AGLNKPVHNPFPVSDNYTE 315
Cdd:cd16023 184 MARKLTQMDQFIRDIIERL-----DDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSkRPFNNSDEPIESNGPGDPS 258

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6322683  316 NWElssikrnDVKQADIASLMSYLIGVNYPKNSVG 350
Cdd:cd16023 259 KVR-------SVPQIDLVPTLSLLLGLPIPFSNLG 286
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 51-276 9.89e-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: 9.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683     51 LFLIVGDGLRADTtFDKVTHpvsgkteflAPFIRSLvMNNATYGISHTRM-PTESRPGHVAMIAGFYED----VSAVTKG 125
Cdd:pfam01663   1 LLVISLDGFRADY-LDRFEL---------TPNLAAL-AKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGshgiVGNTFYD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    126 WKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGasdpNKVDTWMY-----DHTFEDFTQSSIELDAF-----VFRHLDQL 195
Cdd:pfam01663  70 PKTGEYLVFVISDPEDPRWWQGEPIWDTAAKAG----VRAAALFWpgsevDYSTYYGTPPRYLKDDYnnsvpFEDRVDTA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    196 FHNSTLNSTLDYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMS 275
Cdd:pfam01663 146 VLQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMT 225


                  .
gi 6322683    276 A 276
Cdd:pfam01663 226 P 226
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 49-310 2.71e-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: 59.10  E-value: 2.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683   49 KRLFLIVGDGLRADTTfdkvthPVSGKTEFLAPFI-----RSLVMNNATYGISHTRmptesrPGHVAMIAG---FYEDVS 120
Cdd:cd16148   1 MNVILIVIDSLRADHL------GCYGYDRVTTPNLdrlaaEGVVFDNHYSGSNPTL------PSRFSLFTGlypFYHGVW 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  121 AVTKGwKSNPVNFDSFFNQSTHTYSFGSPDILPMFkdgasdpnkvdtWMYDHTFEDFTQSS-IELDAFVFRHLDQLFHNS 199
Cdd:cd16148  69 GGPLE-PDDPTLAEILRKAGYYTAAVSSNPHLFGG------------PGFDRGFDTFEDFRgQEGDPGEEGDERAERVTD 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  200 TLNSTLDyEIRQDGNvFFLHLLgCDTAGHSYRpysaeyYDN-VKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSaFG 278
Cdd:cd16148 136 RALEWLD-RNADDDP-FFLFLH-YFDPHEPYL------YDAeVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEE-FG 205

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 6322683  279 SHG--DGHPNN-----TRTPLVAWGAGLNKPVHNPFPVS 310
Cdd:cd16148 206 EHGlyWGHGSNlydeqLHVPLIIRWPGKEPGKRVDALVS 244
Sulfatase pfam00884
Sulfatase;
51-302 2.01e-08

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 56.66  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683     51 LFLIVGDGLRADttFDKVTHPVSGKTEFLAPFIRSLVMNNATYgiSHTRMPTESRPghvAMIAGFY-EDVSAVTKGWKSN 129
Cdd:pfam00884   3 VVLVLGESLRAP--DLGLYGYPRPTTPFLDRLAEEGLLFSNFY--SGGTLTAPSRF---ALLTGLPpHNFGSYVSTPVGL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    130 PVNFDSFFNQ------STHTYSFGSPDILPMFkdgaSDPNKVDTWMYDH--TFEDFTQSSIELDAFVF-RHLDQLFhnst 200
Cdd:pfam00884  76 PRTEPSLPDLlkragyNTGAIGKWHLGWYNNQ----SPCNLGFDKFFGRntGSDLYADPPDVPYNCSGgGVSDEAL---- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    201 LNSTLDYEIRQDGNVF-FLHLLGCDTAGHSYRPYSAEY----------------YDN-VKYIDDQIPILIDKVNKFFADD 262
Cdd:pfam00884 148 LDEALEFLDNNDKPFFlVLHTLGSHGPPYYPDRYPEKYatfkpsscseeqllnsYDNtLLYTDDAIGRVLDKLEENGLLD 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 6322683    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 1.73e-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: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  230 YRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSaFGSHG------DGHPNNTRTPLVAWGAGLNKPV 303
Cdd:COG3119 195 LRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS-LGEHGlrggkgTLYEGGIRVPLIVRWPGKIKAG 273

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322683  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 5.13e-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: 5.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  237 YYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHG-----------MSAF-GShgdghpnnTRTPLVAWGAGLNKPVH 304
Cdd:cd16032 166 YYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGdmlgerglwykMSFFeGS--------ARVPLIISAPGRFAPRR 237


                ....*.
gi 6322683  305 NPFPVS 310
Cdd:cd16032 238 VAEPVS 243
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 235-281 5.66e-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: 5.66e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6322683  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 7.97e-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: 7.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  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 1.94e-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: 1.94e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6322683  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 5.50e-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: 5.50e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6322683  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 6.60e-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: 6.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  216 FFLHLlgCDTAGHSyrPYsaEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSaFGSHGD--GHPNN----TR 289
Cdd:cd16022 118 FFLYV--SFNAPHP--PF--AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDM-LGDHGLrgKKGSLyeggIR 190


                ....*....
gi 6322683  290 TPLVAWGAG 298
Cdd:cd16022 191 VPFIVRWPG 199
PRK13759 PRK13759
arylsulfatase; Provisional
 235-302 4.29e-04

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 43.89  E-value: 4.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322683   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 6.83e-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: 6.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  235 AEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHPNNTRTPLVAWGAGlnkpVHNPFPVSDNYT 314
Cdd:cd16027 189 ADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFPRAKGTLYDSGLRVPLIVRWPG----KIKPGSVSDALV 264

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6322683  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 8.07e-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: 8.07e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322683  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 1.26e-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: 1.26e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322683  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 1.50e-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: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  135 SFFNQSTHTYSFGSPDILPMFKDgasdpNKVDTWMYDhtfedfTQSSIELDAFVFRHLDQLFHNSTLNSTLDYEIRQDG- 213
Cdd:cd16017  60 SFANRENYDRAYYQENLIDLAKK-----AGYKTYWIS------NQGGCGGYDTRISAIAKIETVFTNKGSCNSSNCYDEa 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  214 ---------------NVFFLHLLG-----CDTAGHSYRPYSAEY---------------YDN-VKYIDDQIPILIDKVNK 257
Cdd:cd16017 129 llplldealadsskkKLIVLHLMGshgpyYDRYPEEFAKFTPDCdnelqscskeelinaYDNsILYTDYVLSQIIERLKK 208

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  258 ffADDKTAFIFTADHGMSAFGS----HGDG--HPNNTRTPLVAWGaglnkpvhnpfpvSDNYTENWELSSIKRNDVK--- 328
Cdd:cd16017 209 --KDKDAALIYFSDHGESLGENglylHGAPyaPKEQYHVPFIIWS-------------SDSYKQRYPVERLRANKDRpfs 273

                       250
                ....*....|....*
gi 6322683  329 QADIASLMSYLIGVN 343
Cdd:cd16017 274 HDNLFHTLLGLLGIK 288
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 208-302 3.43e-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: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683    208 EIRQDGNVFFLHLLGCDTAGHSYRPysAEYYDNVKYIDDQIPILIDKVNkffaDDKTAFIFTADHG----MsafgsHGDG 283
Cdd:pfam01676 295 ALKEKYDFVFVNFANTDMVGHTGDV--EGKVKAIEAVDERLGELLDALE----EDDGLLIITADHGnpeeM-----KDTD 363

                          90       100
                  ....*....|....*....|.
gi 6322683    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 4.42e-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: 4.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  229 SYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMS---AFGSHGDGHPNNTRTPLVAWGAGLNKPVHN 305
Cdd:cd16015 186 EDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSlgsDYDETDEDPLDLYRTPLLIYSPGLKKPKKI 265


                ....*...
gi 6322683  306 PFPVSDNY 313
Cdd:cd16015 266 DRVGSQID 273
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 235-310 4.52e-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: 4.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322683  235 AEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHgmsafGSH-----GD----GHPNNTRTPLVAWGAGLNKPVHN 305
Cdd:cd16152 175 PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH-----GCHfrtrnAEykrsCHESSIRVPLVIYGPGFNGGGRV 249


                ....*
gi 6322683  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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