|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
65-344 |
7.75e-176 |
|
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: 515.57 E-value: 7.75e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 65 SRFSRVVLVLIDALRFDFAQPQHSHVPREPpvSLPFLGKLSSLQRILEIQPHHARLYRSQVDPPTTTMQRLKALTTGSLP 144
Cdd:cd16023 2 PRFDKVVLLLIDALRYDFVLPDDENPPSEN--SLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 145 TFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSG-E 223
Cdd:cd16023 80 TFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEdD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 224 WDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALFLYSP 303
Cdd:cd16023 160 WDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 23397648 304 TAVFPST---------PPEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVM 344
Cdd:cd16023 240 RPFNNSDepiesngpgDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
70-287 |
4.44e-15 |
|
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: 77.85 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 70 VVLVLIDALRFDFaqpqhshvpreppvsLPFLGKLSSLQRILEiQPHHARLYRSQVdpPTTTMQRLKALTTGSLPtfida 149
Cdd:pfam01663 1 LLVISLDGFRADY---------------LDRFELTPNLAALAK-EGVSAPNLTPVF--PTLTFPNHYTLVTGLYP----- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 150 gsnfASHAIVEDNLIKQLTsaGRRVVFMGDDTWKDLF----P--------GAFSKAFFFP-------------------- 197
Cdd:pfam01663 58 ----GSHGIVGNTFYDPKT--GEYLVFVISDPEDPRWwqgePiwdtaakaGVRAAALFWPgsevdystyygtpprylkdd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 198 -----SFNVRDLDTVDNGILEHLYPTMDSGEWDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE----- 267
Cdd:pfam01663 132 ynnsvPFEDRVDTAVLQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDerglf 211
|
250 260
....*....|....*....|
gi 23397648 268 NDTLLVVAGDHGMTTNGDHG 287
Cdd:pfam01663 212 EDTNVIVVSDHGMTPVSDDK 231
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
69-282 |
9.07e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 77.48 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 69 RVVLVLIDALRFDFAQPQHshvpreppvsLPFLGKLSSlqrileiQPHHARLYRSQVdpPTTTMQRLKALTTGSLP---- 144
Cdd:COG1524 25 KVVLILVDGLRADLLERAH----------APNLAALAA-------RGVYARPLTSVF--PSTTAPAHTTLLTGLYPgehg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 145 ----TFID--AGSNFASHAIVEDN-----------LIKQLTSAGRRV------VFMGDDTWKDLFPGAFSKAFFFPSFNV 201
Cdd:COG1524 86 ivgnGWYDpeLGRVVNSLSWVEDGfgsnsllpvptIFERARAAGLTTaavfwpSFEGSGLIDAARPYPYDGRKPLLGNPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 202 RDLDTVDNGI--LEHLYPtmdsgewDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTLLVV 274
Cdd:COG1524 166 ADRWIAAAALelLREGRP-------DLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKarglyEGTLVIV 238
|
....*...
gi 23397648 275 AGDHGMTT 282
Cdd:COG1524 239 TADHGMVD 246
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
65-344 |
7.75e-176 |
|
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: 515.57 E-value: 7.75e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 65 SRFSRVVLVLIDALRFDFAQPQHSHVPREPpvSLPFLGKLSSLQRILEIQPHHARLYRSQVDPPTTTMQRLKALTTGSLP 144
Cdd:cd16023 2 PRFDKVVLLLIDALRYDFVLPDDENPPSEN--SLYYHNKLPVLEELLKSQPNNSRLFKFIADPPTTTLQRLKGLTTGSLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 145 TFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSG-E 223
Cdd:cd16023 80 TFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEdD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 224 WDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALFLYSP 303
Cdd:cd16023 160 WDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 23397648 304 TAVFPST---------PPEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVM 344
Cdd:cd16023 240 RPFNNSDepiesngpgDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
65-344 |
1.45e-114 |
|
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: 356.29 E-value: 1.45e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 65 SRFSRVVLVLIDALRFDFAQPQHSHVPreppvslpflgKLSSLQRILEiQPHHARLYRSQVDPPTTTMQRLKALTTGSLP 144
Cdd:cd16019 2 TKYDKVVLIVIDGLRYDLAVNVNKQSS-----------FFSFLQKLNE-QPNNSFLALSFADPPTVTGPRLKALTTGNPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 145 TFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSGE- 223
Cdd:cd16019 70 TFLDLISNFASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHINDNLDENIy 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 224 ---WDVLIAHFLGVDHCGHKHG-PHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALF 299
Cdd:cd16019 150 ydnWDFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDNDTLLVVVSDHGMNNDGNHGGSSTEETSSFFF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397648 300 LYSPTAVFPSTP------------------PEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVM 344
Cdd:cd16019 230 FISKKGFFKKRPidqiekikqnneqqkidpSEYIRIIYQIDILPTICYLLGIPIPFNNIGIII 292
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
65-341 |
6.02e-100 |
|
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: 316.43 E-value: 6.02e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 65 SRFSRVVLVLIDALRFDFAQPQHSHvpreppvsLPFLGKLsslqrileIQPHHARLYRSQVDPPTTTMQRLKALTTGSLP 144
Cdd:cd16024 2 PAFDKLVFMVIDALRADFVFGPDSN--------MPFTQSL--------INSGSALAFTAKAQPPTVTMPRIKALTTGSIP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 145 TFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSGEW 224
Cdd:cd16024 66 SFLDVVLNFASSLLEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 225 DVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTLLVVAGDHGMTTNGDHGGDSELEVSAALF 299
Cdd:cd16024 146 DVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEeqssnNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 23397648 300 LYSP----TAVFPSTPPEEPEVIPQVSLVPTLALLLGLPIPFGNIG 341
Cdd:cd16024 226 FISPkfssKPSNADGELSYYETVQQVDLAPTLALLLGLPIPKNSVG 271
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
69-331 |
3.03e-39 |
|
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: 146.03 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 69 RVVLVLIDALRFDFAQPQHSHVPREPpvslpflgklsslqRILEIQPHHARLYRSQVDPPTTTMQRLKALTTGSLPTFID 148
Cdd:cd00016 2 HVVLIVLDGLGADDLGKAGNPAPTTP--------------NLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 149 AGSN----------FASHAIVEDNLIKQLTSAGRRVVFMGddtwkdlfpgafskafffpsfnvrdldtvdngILEHLYPT 218
Cdd:cd00016 68 YTGNgsadpelpsrAAGKDEDGPTIPELLKQAGYRTGVIG--------------------------------LLKAIDET 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 219 MDSgEWDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERL-----ENDTLLVVAGDHGMTTNGDHG------ 287
Cdd:cd00016 116 SKE-KPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALkkagdADDTVIIVTADHGGIDKGHGGdpkadg 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 23397648 288 --GDSELEVSAALFLYSPTAvfpSTPPEEPEVIPQVSLVPTLALLL 331
Cdd:cd00016 195 kaDKSHTGMRVPFIAYGPGV---KKGGVKHELISQYDIAPTLADLL 237
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
225-332 |
2.31e-19 |
|
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: 89.18 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 225 DVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTLLVVAGDHGMTTNGDHGGDSELEVSAALF 299
Cdd:cd16018 158 DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKergllDDTNIIVVSDHGMTDVGTHGYDNELPDMRAIF 237
|
90 100 110
....*....|....*....|....*....|....*.
gi 23397648 300 LYSPTAVFpstppeEPEVIPQVSLV---PTLALLLG 332
Cdd:cd16018 238 IARGPAFK------KGKKLGPFRNVdiyPLMCNLLG 267
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
70-287 |
4.44e-15 |
|
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: 77.85 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 70 VVLVLIDALRFDFaqpqhshvpreppvsLPFLGKLSSLQRILEiQPHHARLYRSQVdpPTTTMQRLKALTTGSLPtfida 149
Cdd:pfam01663 1 LLVISLDGFRADY---------------LDRFELTPNLAALAK-EGVSAPNLTPVF--PTLTFPNHYTLVTGLYP----- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 150 gsnfASHAIVEDNLIKQLTsaGRRVVFMGDDTWKDLF----P--------GAFSKAFFFP-------------------- 197
Cdd:pfam01663 58 ----GSHGIVGNTFYDPKT--GEYLVFVISDPEDPRWwqgePiwdtaakaGVRAAALFWPgsevdystyygtpprylkdd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 198 -----SFNVRDLDTVDNGILEHLYPTMDSGEWDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE----- 267
Cdd:pfam01663 132 ynnsvPFEDRVDTAVLQTWLDLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDerglf 211
|
250 260
....*....|....*....|
gi 23397648 268 NDTLLVVAGDHGMTTNGDHG 287
Cdd:pfam01663 212 EDTNVIVVSDHGMTPVSDDK 231
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
69-282 |
9.07e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 77.48 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 69 RVVLVLIDALRFDFAQPQHshvpreppvsLPFLGKLSSlqrileiQPHHARLYRSQVdpPTTTMQRLKALTTGSLP---- 144
Cdd:COG1524 25 KVVLILVDGLRADLLERAH----------APNLAALAA-------RGVYARPLTSVF--PSTTAPAHTTLLTGLYPgehg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 145 ----TFID--AGSNFASHAIVEDN-----------LIKQLTSAGRRV------VFMGDDTWKDLFPGAFSKAFFFPSFNV 201
Cdd:COG1524 86 ivgnGWYDpeLGRVVNSLSWVEDGfgsnsllpvptIFERARAAGLTTaavfwpSFEGSGLIDAARPYPYDGRKPLLGNPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 202 RDLDTVDNGI--LEHLYPtmdsgewDVLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE-----NDTLLVV 274
Cdd:COG1524 166 ADRWIAAAALelLREGRP-------DLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKarglyEGTLVIV 238
|
....*...
gi 23397648 275 AGDHGMTT 282
Cdd:COG1524 239 TADHGMVD 246
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
226-343 |
3.03e-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: 71.47 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 226 VLIAHFLGVDHCGHKHGPHHPEMAKKLSQMDQVIQGLVERLE---ND--TLLVVAGDHGMTTNGDHGGDSELEVSAALFL 300
Cdd:cd16020 159 VFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEeyfNDgrTAYIFTSDHGMTDWGSHGDGSPDETETPFIA 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 23397648 301 Y-----SPTAVFPSTPPEEPE-------VIPQVSLVPTLALLLGLPIPFGNIGEV 343
Cdd:cd16020 239 WgagikHPTPGRGPSFSANWGglrlprhDLDQADLAPLMSALLGLPPPVNSVGIL 293
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
69-336 |
3.23e-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: 46.77 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 69 RVVLVLIDALRFDFAQPQHSHvprepPVSLPFLGKLSSlqrileiqphharlyRSQV-------DPPTttMQRLKALTTG 141
Cdd:cd16148 2 NVILIVIDSLRADHLGCYGYD-----RVTTPNLDRLAA---------------EGVVfdnhysgSNPT--LPSRFSLFTG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 142 SLPtfIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDDTWKDLFPGaFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDS 221
Cdd:cd16148 60 LYP--FYHGVWGGPLEPDDPTLAEILRKAGYYTAAVSSNPHLFGGPG-FDRGFDTFEDFRGQEGDPGEEGDERAERVTDR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 222 GewdvliAHFLGvDHCGHK------H--GPHHPEM-AKKLSQMDQVIQGLVERLEN-----DTLLVVAGDHGMtTNGDHG 287
Cdd:cd16148 137 A------LEWLD-RNADDDpfflflHyfDPHEPYLyDAEVRYVDEQIGRLLDKLKElglleDTLVIVTSDHGE-EFGEHG 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397648 288 G---------DSELEVsaALFLYSPTAvfpstppEEPEVIP-QVS---LVPTLALLLGLPIP 336
Cdd:cd16148 209 LywghgsnlyDEQLHV--PLIIRWPGK-------EPGKRVDaLVShidIAPTLLDLLGVEPP 261
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
247-332 |
2.35e-04 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 44.21 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 247 EMAKKLSQMDQVIQGLVERLEN-----DTLLVVAGDHGMTTNGDHGGDSELEVSAA---LFLYSPtavFPSTPPEEPEVI 318
Cdd:cd16015 193 NYLNAIHYTDKALGEFIEKLKKsglyeNTIIVIYGDHLPSLGSDYDETDEDPLDLYrtpLLIYSP---GLKKPKKIDRVG 269
|
90
....*....|....
gi 23397648 319 PQVSLVPTLALLLG 332
Cdd:cd16015 270 SQIDIAPTLLDLLG 283
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
255-336 |
4.83e-03 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 40.79 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397648 255 MDQVIQGLVERLEN-----DTLLVVAGDHGMTTNGDHGGDSELEVSA-ALFLYSPTAVfpsTPPEEPEVIPQVSLVPTLA 328
Cdd:COG1368 426 ADQALGEFIEKLKKsgwydNTIFVIYGDHGPRSPGKTDYENPLERYRvPLLIYSPGLK---KPKVIDTVGSQIDIAPTLL 502
|
....*...
gi 23397648 329 LLLGLPIP 336
Cdd:COG1368 503 DLLGIDYP 510
|
|
| |
