|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
64-344 |
1.94e-164 |
|
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: 485.53 E-value: 1.94e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 64 PSRFSRVVLVLIDALRFDFAQPQRShvPGEPPVSVPFLGKLGSLQRILESQPHHGRLYRSQVDPPTTTMQRLKALTTGSL 143
Cdd:cd16023 1 PPRFDKVVLLLIDALRYDFVLPDDE--NPPSENSLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 144 PTFIDAGSNFASHAIVEDNVIQQLNSAGRRVVFMGDDTWRDLFPGAFSQAFFFSSFNVRDLHTVDNGILEHLYPTLD-GG 222
Cdd:cd16023 79 PTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQsED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 223 SWDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLIERLENDTLLVVAGDHGMTMNGDHGGDSELEVSAALFLYS 302
Cdd:cd16023 159 DWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 766944228 303 PTALFPS---------VPPEEPEVIPQVSLVPTLALLLGLPIPFGNTGEVM 344
Cdd:cd16023 239 KRPFNNSdepiesngpGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
69-281 |
1.23e-13 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 74.01 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 69 RVVLVLIDALRFDFAQpqRSHVPGeppvsvpflgklgsLQRILESQPHHGRLYRSQvdpPTTTMQRLKALTTGSLP---- 144
Cdd:COG1524 25 KVVLILVDGLRADLLE--RAHAPN--------------LAALAARGVYARPLTSVF---PSTTAPAHTTLLTGLYPgehg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 145 ----TFID--AGSNFASHAIVEDN-----------VIQQLNSAGRRV------VFMGDDTWRDLFPGAFSQAFFFSSFNV 201
Cdd:COG1524 86 ivgnGWYDpeLGRVVNSLSWVEDGfgsnsllpvptIFERARAAGLTTaavfwpSFEGSGLIDAARPYPYDGRKPLLGNPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 202 RDLHTVDNgiLEHLYPTLDGgswDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLIERLE-----NDTLLVVAG 276
Cdd:COG1524 166 ADRWIAAA--ALELLREGRP---DLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKarglyEGTLVIVTA 240
|
....*
gi 766944228 277 DHGMT 281
Cdd:COG1524 241 DHGMV 245
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
224-281 |
9.85e-13 |
|
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: 70.91 E-value: 9.85e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 766944228 224 WDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLIERLE-----NDTLLVVAGDHGMT 281
Cdd:pfam01663 163 PDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDerglfEDTNVIVVSDHGMT 225
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
64-344 |
1.94e-164 |
|
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: 485.53 E-value: 1.94e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 64 PSRFSRVVLVLIDALRFDFAQPQRShvPGEPPVSVPFLGKLGSLQRILESQPHHGRLYRSQVDPPTTTMQRLKALTTGSL 143
Cdd:cd16023 1 PPRFDKVVLLLIDALRYDFVLPDDE--NPPSENSLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 144 PTFIDAGSNFASHAIVEDNVIQQLNSAGRRVVFMGDDTWRDLFPGAFSQAFFFSSFNVRDLHTVDNGILEHLYPTLD-GG 222
Cdd:cd16023 79 PTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQsED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 223 SWDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLIERLENDTLLVVAGDHGMTMNGDHGGDSELEVSAALFLYS 302
Cdd:cd16023 159 DWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 766944228 303 PTALFPS---------VPPEEPEVIPQVSLVPTLALLLGLPIPFGNTGEVM 344
Cdd:cd16023 239 KRPFNNSdepiesngpGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
64-344 |
2.10e-113 |
|
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: 352.82 E-value: 2.10e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 64 PSRFSRVVLVLIDALRFDFAQPQRSHVPgeppvsvpflgKLGSLQRILEsQPHHGRLYRSQVDPPTTTMQRLKALTTGSL 143
Cdd:cd16019 1 PTKYDKVVLIVIDGLRYDLAVNVNKQSS-----------FFSFLQKLNE-QPNNSFLALSFADPPTVTGPRLKALTTGNP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 144 PTFIDAGSNFASHAIVEDNVIQQLNSAGRRVVFMGDDTWRDLFPGAFSQAFFFSSFNVRDLHTVDNGILEHLYPTLDGG- 222
Cdd:cd16019 69 PTFLDLISNFASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHINDNLDENi 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 223 ---SWDVLIAHFLGVDHCGHKHG-PHHPEMAKKLSQMDQVIQGLIERLENDTLLVVAGDHGMTMNGDHGGDSELEVSAAL 298
Cdd:cd16019 149 yydNWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDNDTLLVVVSDHGMNNDGNHGGSSTEETSSFF 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 766944228 299 FLYSPTALFPS------------------VPPEEPEVIPQVSLVPTLALLLGLPIPFGNTGEVM 344
Cdd:cd16019 229 FFISKKGFFKKrpidqiekikqnneqqkiDPSEYIRIIYQIDILPTICYLLGIPIPFNNIGIII 292
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
64-341 |
1.12e-92 |
|
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: 296.78 E-value: 1.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 64 PSRFSRVVLVLIDALRFDFaqpqrshVPGePPVSVPFLgklgslQRILESQphHGRLYRSQVDPPTTTMQRLKALTTGSL 143
Cdd:cd16024 1 KPAFDKLVFMVIDALRADF-------VFG-PDSNMPFT------QSLINSG--SALAFTAKAQPPTVTMPRIKALTTGSI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 144 PTFIDAGSNFASHAIVEDNVIQQLNSAGRRVVFMGDDTWRDLFPGAFSQAFFFSSFNVRDLHTVDNGILEHLYPTLDGGS 223
Cdd:cd16024 65 PSFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 224 WDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLIERLE-----NDTLLVVAGDHGMTMNGDHGGDSELEVSAAL 298
Cdd:cd16024 145 WDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEeqssnNPTLLVVCGDHGMTDAGNHGGSSPGETSVPL 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 766944228 299 FLYSP----TALFPSVPPEEPEVIPQVSLVPTLALLLGLPIPFGNTG 341
Cdd:cd16024 225 LFISPkfssKPSNADGELSYYETVQQVDLAPTLALLLGLPIPKNSVG 271
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
69-331 |
8.48e-41 |
|
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: 150.26 E-value: 8.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 69 RVVLVLIDALRFDFAQPQRSHVPGEPpvsvpflgklgslqRILESQPHHGRLYRSQVDPPTTTMQRLKALTTGSLPTFID 148
Cdd:cd00016 2 HVVLIVLDGLGADDLGKAGNPAPTTP--------------NLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 149 AGSN----------FASHAIVEDNVIQQLNSAGRRVVFMGddtwrdlfpgafsqafffssfnvrdlhtvdngILEHLYPT 218
Cdd:cd00016 68 YTGNgsadpelpsrAAGKDEDGPTIPELLKQAGYRTGVIG--------------------------------LLKAIDET 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 219 LDGgSWDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLIERL-----ENDTLLVVAGDHGMTMNGDHG------ 287
Cdd:cd00016 116 SKE-KPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALkkagdADDTVIIVTADHGGIDKGHGGdpkadg 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 766944228 288 --GDSELEVSAALFLYSPTALFpsvPPEEPEVIPQVSLVPTLALLL 331
Cdd:cd00016 195 kaDKSHTGMRVPFIAYGPGVKK---GGVKHELISQYDIAPTLADLL 237
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
225-332 |
1.64e-18 |
|
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: 86.87 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 225 DVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLIERLE-----NDTLLVVAGDHGMTMNGDHGGDSELEVSAALF 299
Cdd:cd16018 158 DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKergllDDTNIIVVSDHGMTDVGTHGYDNELPDMRAIF 237
|
90 100 110
....*....|....*....|....*....|....*.
gi 766944228 300 LYSPtalfPSVppEEPEVIPQVSLV---PTLALLLG 332
Cdd:cd16018 238 IARG----PAF--KKGKKLGPFRNVdiyPLMCNLLG 267
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
69-281 |
1.23e-13 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 74.01 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 69 RVVLVLIDALRFDFAQpqRSHVPGeppvsvpflgklgsLQRILESQPHHGRLYRSQvdpPTTTMQRLKALTTGSLP---- 144
Cdd:COG1524 25 KVVLILVDGLRADLLE--RAHAPN--------------LAALAARGVYARPLTSVF---PSTTAPAHTTLLTGLYPgehg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 145 ----TFID--AGSNFASHAIVEDN-----------VIQQLNSAGRRV------VFMGDDTWRDLFPGAFSQAFFFSSFNV 201
Cdd:COG1524 86 ivgnGWYDpeLGRVVNSLSWVEDGfgsnsllpvptIFERARAAGLTTaavfwpSFEGSGLIDAARPYPYDGRKPLLGNPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 202 RDLHTVDNgiLEHLYPTLDGgswDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLIERLE-----NDTLLVVAG 276
Cdd:COG1524 166 ADRWIAAA--ALELLREGRP---DLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKarglyEGTLVIVTA 240
|
....*
gi 766944228 277 DHGMT 281
Cdd:COG1524 241 DHGMV 245
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
226-343 |
8.08e-13 |
|
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: 70.31 E-value: 8.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 226 VLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQ---GLIERLEND--TLLVVAGDHGMTMNGDHGGDSELEVSAALFL 300
Cdd:cd16020 159 VFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEktyPLIEEYFNDgrTAYIFTSDHGMTDWGSHGDGSPDETETPFIA 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 766944228 301 Y-----SPTALFPSVPPEEPE-------VIPQVSLVPTLALLLGLPIPFGNTGEV 343
Cdd:cd16020 239 WgagikHPTPGRGPSFSANWGglrlprhDLDQADLAPLMSALLGLPPPVNSVGIL 293
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
224-281 |
9.85e-13 |
|
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: 70.91 E-value: 9.85e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 766944228 224 WDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLIERLE-----NDTLLVVAGDHGMT 281
Cdd:pfam01663 163 PDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDerglfEDTNVIVVSDHGMT 225
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
243-342 |
2.84e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 47.16 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 243 PHHPEM-AKKLSQMDQVIQGLIERLEN-----DTLLVVAGDHGMTMnGDHGG---------DSELEVsaALFLYsptalF 307
Cdd:cd16148 159 PHEPYLyDAEVRYVDEQIGRLLDKLKElglleDTLVIVTSDHGEEF-GEHGLywghgsnlyDEQLHV--PLIIR-----W 230
|
90 100 110
....*....|....*....|....*....|....*....
gi 766944228 308 PSVPPeePEVIP-QVS---LVPTLALLLGLPIPFGNTGE 342
Cdd:cd16148 231 PGKEP--GKRVDaLVShidIAPTLLDLLGVEPPDYSDGR 267
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
247-332 |
5.02e-05 |
|
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: 46.52 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 247 EMAKKLSQMDQVIQGLIERLEN-----DTLLVVAGDHGMTMNGDHGGDSELEVSAA---LFLYSPtalFPSVPPEEPEVI 318
Cdd:cd16015 193 NYLNAIHYTDKALGEFIEKLKKsglyeNTIIVIYGDHLPSLGSDYDETDEDPLDLYrtpLLIYSP---GLKKPKKIDRVG 269
|
90
....*....|....
gi 766944228 319 PQVSLVPTLALLLG 332
Cdd:cd16015 270 SQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
255-336 |
3.25e-04 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 44.64 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 255 MDQVIQGLIERLEN-----DTLLVVAGDHGMTMNGDHGGDSELEVSA-ALFLYSPTALFPSVppeEPEVIPQVSLVPTLA 328
Cdd:COG1368 426 ADQALGEFIEKLKKsgwydNTIFVIYGDHGPRSPGKTDYENPLERYRvPLLIYSPGLKKPKV---IDTVGSQIDIAPTLL 502
|
....*...
gi 766944228 329 LLLGLPIP 336
Cdd:COG1368 503 DLLGIDYP 510
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
70-333 |
4.80e-04 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 43.57 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 70 VVLVLIDALRFDFAQpqrshVPGEPPVSVPFLGKLgsLQRILESQPHHGrlyrsqvdPPTTTMQRLKALTTGSLPTFIDA 149
Cdd:pfam00884 3 VVLVLGESLRAPDLG-----LYGYPRPTTPFLDRL--AEEGLLFSNFYS--------GGTLTAPSRFALLTGLPPHNFGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 150 GSNFASH-AIVEDNVIQQLNSAGRRVVF----------------MGDDTWRDLFPGAFSQAFFFSSFNVRDLHTV-DNGI 211
Cdd:pfam00884 68 YVSTPVGlPRTEPSLPDLLKRAGYNTGAigkwhlgwynnqspcnLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVsDEAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 212 LEHLYPTLD--GGSWdVLIAHFLGVdHCGHKHGPHHPEMAKK------------------LSQMDQVIQGLIERLE---- 267
Cdd:pfam00884 148 LDEALEFLDnnDKPF-FLVLHTLGS-HGPPYYPDRYPEKYATfkpsscseeqllnsydntLLYTDDAIGRVLDKLEengl 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 766944228 268 -NDTLLVVAGDHG---MTMNGDHGGDSELEVSAA-----LFLYSPtalfPSVPPEE--PEVIPQVSLVPTLALLLGL 333
Cdd:pfam00884 226 lDNTLVVYTSDHGeslGEGGGYLHGGKYDNAPEGgyrvpLLIWSP----GGKAKGQksEALVSHVDLFPTILDLAGI 298
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
238-358 |
8.51e-03 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 39.86 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766944228 238 GHKHGPHHPEMAKKL--------SQMD----QVIQGLiER--LENDTLLVVAGDHGMtMNGDHGG---DSELEVSAAlfl 300
Cdd:cd16030 245 GDPKGPLPDEQARELrqayyasvSYVDaqvgRVLDAL-EElgLADNTIVVLWSDHGW-HLGEHGHwgkHTLFEEATR--- 319
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 766944228 301 ySPtaLFPSVP--PEEPEVIPQ-VSLV---PTLALLLGLPIPFGNTGEVMAELFSGGSDSSHPH 358
Cdd:cd16030 320 -VP--LIIRAPgvTKPGKVTDAlVELVdiyPTLAELAGLPAPPCLEGKSLVPLLKNPSAKWKDA 380
|
|
| |
