|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
40-345 |
6.02e-177 |
|
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: 515.22 E-value: 6.02e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 40 PPPARRLVLFVADGLRADALYELDEngnSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKEN 119
Cdd:cd16020 1 PPPAKRLVVFVADGLRADTFFENNC---SRAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKGWKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 120 PVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDakREDFGAQDATKLDTWVFDNVKDFFHHARNNQSlfSKI 199
Cdd:cd16020 78 PVEFDSVFNRSRRSWAWGSPDILPMFPKGATGGKVLTYIYP--EEDFDSTDASELDEWVFDKVEEFLANASSNKT--ELL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 200 NEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHfYGNDGKTTFIFTSDHGMTDWGSHGAGHPSET 279
Cdd:cd16020 154 NQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEE-YFNDGRTAYIFTSDHGMTDWGSHGDGSPDET 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998476 280 LTPLVTWGAGIKYPqrvsAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILP 345
Cdd:cd16020 233 ETPFIAWGAGIKHP----TPGRGPSFSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
|
|
| PigN |
pfam04987 |
Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a ... |
430-884 |
3.20e-154 |
|
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: 462.85 E-value: 3.20e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 430 KGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSnLIKGVSKEVKKPSHLLPCSFVAIGILVAF--FLLIQACPWT 507
Cdd:pfam04987 1 EGLRYYQTYDWLFLRTIVTLGYLGWIAYLLLTVLKLHV-LLGSKPSSRTTLSTLLGYKFSSTLLLVLLyaFLFLQRSPLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 508 YYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYP----LSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFL-- 581
Cdd:pfam04987 80 YYLYLLFPVYFWYQILAERPILQAGLKELFSHIkssfVKKPLIQLLLIVGVLELLVLSFFHREILSVGFVLLAFWPLFyg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 582 TRLWTRAKMTSLSWTFFSLLLAVFPLMPVVgRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKeellvHLLQVLSTV 661
Cdd:pfam04987 160 TNFFRKPSLLFLTWLLSCLLLSVFPLLPVV-KVENLPLILLGGLLILLRGLLLLLFERSITSSSRT-----LLVQVLLIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 662 LSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLV-VPLLSSPVLFQRLFSILLSLMSTYLLLSTGYEALFPLVLSCLM 740
Cdd:pfam04987 234 LSILVTGSSVVSLQAKQGLPLGNQVVGWIILVYSLLsLPLLHRTRPLHRLLSIFLNFAPTFILLSISYESLFYQAFSLEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 741 FVWINIEQETLQQSGvccKQKLTSIQFSYNTDITQFRQLYLDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLT 820
Cdd:pfam04987 314 LLWIELEHELKQEES---TKQSESSDTSTKKLKLSSRSLTLSDLRIALFFLFFLQVAFFGTGNIASISSFDLDSVYRFIP 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998476 821 VFSPFMMGALMMWKILIPFVLVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGS 884
Cdd:pfam04987 391 VFSPFLMGALLLLKLLIPFVLVSSALGALNKRLRLPPRSLFLLVLLISDVMTLNFFFLVRDEGS 454
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
38-267 |
1.42e-17 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 85.57 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 38 PLPPPARRLVLFVADGLRADALYELDengnsrAPFIRNiIMHEGSWGISHTRV-PTESRPGHVALIAGFYEDVSAVAkGW 116
Cdd:COG1524 18 AAAPPAKKVVLILVDGLRADLLERAH------APNLAA-LAARGVYARPLTSVfPSTTAPAHTTLLTGLYPGEHGIV-GN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 117 ----KENPVEFDSLFNESKYTWS---WGSPDIL---------------PMFAKGASGDHVYTYSYDAKREDFGAQDAtkl 174
Cdd:COG1524 90 gwydPELGRVVNSLSWVEDGFGSnslLPVPTIFeraraaglttaavfwPSFEGSGLIDAARPYPYDGRKPLLGNPAA--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 175 DTWVFDNVKDFFHHARNNqslfskineekiVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGk 254
Cdd:COG1524 167 DRWIAAAALELLREGRPD------------LLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEG- 233
|
250
....*....|...
gi 767998476 255 TTFIFTSDHGMTD 267
Cdd:COG1524 234 TLVIVTADHGMVD 246
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
46-267 |
3.93e-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: 62.44 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 46 LVLFVADGLRADALYELDengnsRAPFIRNIiMHEGSWGISHTRV-PTESRPGHVALIAG-------------------- 104
Cdd:pfam01663 1 LLVISLDGFRADYLDRFE-----LTPNLAAL-AKEGVSAPNLTPVfPTLTFPNHYTLVTGlypgshgivgntfydpktge 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 105 ---FYEDVSAVAKGWKENPVEFDSLFNE---SKYTWSWGSPDILpmfAKGASGDHVYTYSYDAKREDFGAQDATKLDTWV 178
Cdd:pfam01663 75 ylvFVISDPEDPRWWQGEPIWDTAAKAGvraAALFWPGSEVDYS---TYYGTPPRYLKDDYNNSVPFEDRVDTAVLQTWL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 179 fdnVKDFFHHARNNQSLFskineekivfFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMF--NHFYGNdgkTT 256
Cdd:pfam01663 152 ---DLPFADVAAERPDLL----------LVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALdeRGLFED---TN 215
|
250
....*....|.
gi 767998476 257 FIFTSDHGMTD 267
Cdd:pfam01663 216 VIVVSDHGMTP 226
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
40-345 |
6.02e-177 |
|
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: 515.22 E-value: 6.02e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 40 PPPARRLVLFVADGLRADALYELDEngnSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKEN 119
Cdd:cd16020 1 PPPAKRLVVFVADGLRADTFFENNC---SRAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKGWKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 120 PVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDakREDFGAQDATKLDTWVFDNVKDFFHHARNNQSlfSKI 199
Cdd:cd16020 78 PVEFDSVFNRSRRSWAWGSPDILPMFPKGATGGKVLTYIYP--EEDFDSTDASELDEWVFDKVEEFLANASSNKT--ELL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 200 NEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHfYGNDGKTTFIFTSDHGMTDWGSHGAGHPSET 279
Cdd:cd16020 154 NQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEE-YFNDGRTAYIFTSDHGMTDWGSHGDGSPDET 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767998476 280 LTPLVTWGAGIKYPqrvsAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILP 345
Cdd:cd16020 233 ETPFIAWGAGIKHP----TPGRGPSFSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
|
|
| PigN |
pfam04987 |
Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a ... |
430-884 |
3.20e-154 |
|
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: 462.85 E-value: 3.20e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 430 KGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSnLIKGVSKEVKKPSHLLPCSFVAIGILVAF--FLLIQACPWT 507
Cdd:pfam04987 1 EGLRYYQTYDWLFLRTIVTLGYLGWIAYLLLTVLKLHV-LLGSKPSSRTTLSTLLGYKFSSTLLLVLLyaFLFLQRSPLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 508 YYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYP----LSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFL-- 581
Cdd:pfam04987 80 YYLYLLFPVYFWYQILAERPILQAGLKELFSHIkssfVKKPLIQLLLIVGVLELLVLSFFHREILSVGFVLLAFWPLFyg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 582 TRLWTRAKMTSLSWTFFSLLLAVFPLMPVVgRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKeellvHLLQVLSTV 661
Cdd:pfam04987 160 TNFFRKPSLLFLTWLLSCLLLSVFPLLPVV-KVENLPLILLGGLLILLRGLLLLLFERSITSSSRT-----LLVQVLLIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 662 LSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLV-VPLLSSPVLFQRLFSILLSLMSTYLLLSTGYEALFPLVLSCLM 740
Cdd:pfam04987 234 LSILVTGSSVVSLQAKQGLPLGNQVVGWIILVYSLLsLPLLHRTRPLHRLLSIFLNFAPTFILLSISYESLFYQAFSLEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 741 FVWINIEQETLQQSGvccKQKLTSIQFSYNTDITQFRQLYLDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLT 820
Cdd:pfam04987 314 LLWIELEHELKQEES---TKQSESSDTSTKKLKLSSRSLTLSDLRIALFFLFFLQVAFFGTGNIASISSFDLDSVYRFIP 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767998476 821 VFSPFMMGALMMWKILIPFVLVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGS 884
Cdd:pfam04987 391 VFSPFLMGALLLLKLLIPFVLVSSALGALNKRLRLPPRSLFLLVLLISDVMTLNFFFLVRDEGS 454
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
40-344 |
5.18e-22 |
|
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: 96.87 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 40 PPPARRLVLFVADGLRADALYeldeNGNSRAPFIRNIIMHEGSWG-ISHTRVPTESRPGHVAL----IAGFYeDV----- 109
Cdd:cd16024 1 KPAFDKLVFMVIDALRADFVF----GPDSNMPFTQSLINSGSALAfTAKAQPPTVTMPRIKALttgsIPSFL-DVvlnfa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 110 -----------SAVAKGWKenpVEFdslfneskY---TWswgspdiLPMFAKGASgDHVYTYSydakredFGAQDATKLD 175
Cdd:cd16024 76 sslleednwlsQLKAAGKK---IVF--------YgddTW-------LKLFPGSFT-RSDGTTS-------FFVSDFTEVD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 176 twvfDNVkdffhhARNNQSLFSkiNEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIV-SMFNHFYGNDgk 254
Cdd:cd16024 130 ----NNV------TRHLDSELS--RDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYeSLEEQSSNNP-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 255 TTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIkypqRVSAQQFDDAFLKEWRlenwkrldVNQADIAPLMTSLIGV 334
Cdd:cd16024 196 TLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKF----SSKPSNADGELSYYET--------VQQVDLAPTLALLLGL 263
|
330
....*....|
gi 767998476 335 PFPLNSVGIL 344
Cdd:cd16024 264 PIPKNSVGVL 273
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
44-332 |
1.74e-21 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 94.41 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 44 RRLVLFVADGLRADALYELDeNGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAkGWKENpvef 123
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAG-NPAPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYT-GNGSA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 124 DSLFNESKYTWSWGSPDILPMF-AKGasgdhvytysYDAKRedFGAQDATKLDTwvfdNVKDFFhharnnqslfskinee 202
Cdd:cd00016 75 DPELPSRAAGKDEDGPTIPELLkQAG----------YRTGV--IGLLKAIDETS----KEKPFV---------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 203 kivFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFyGNDGKTTFIFTSDHGMTDWGSHGAGHPS----- 277
Cdd:cd00016 123 ---LFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKA-GDADDTVIIVTADHGGIDKGHGGDPKADgkadk 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767998476 278 ---ETLTPLVTWGAGIKYPQRvsaqqfddaflkewrlenwKRLDVNQADIAPLMTSLI 332
Cdd:cd00016 199 shtGMRVPFIAYGPGVKKGGV-------------------KHELISQYDIAPTLADLL 237
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
38-267 |
1.42e-17 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 85.57 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 38 PLPPPARRLVLFVADGLRADALYELDengnsrAPFIRNiIMHEGSWGISHTRV-PTESRPGHVALIAGFYEDVSAVAkGW 116
Cdd:COG1524 18 AAAPPAKKVVLILVDGLRADLLERAH------APNLAA-LAARGVYARPLTSVfPSTTAPAHTTLLTGLYPGEHGIV-GN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 117 ----KENPVEFDSLFNESKYTWS---WGSPDIL---------------PMFAKGASGDHVYTYSYDAKREDFGAQDAtkl 174
Cdd:COG1524 90 gwydPELGRVVNSLSWVEDGFGSnslLPVPTIFeraraaglttaavfwPSFEGSGLIDAARPYPYDGRKPLLGNPAA--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 175 DTWVFDNVKDFFHHARNNqslfskineekiVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGk 254
Cdd:COG1524 167 DRWIAAAALELLREGRPD------------LLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEG- 233
|
250
....*....|...
gi 767998476 255 TTFIFTSDHGMTD 267
Cdd:COG1524 234 TLVIVTADHGMVD 246
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
40-344 |
1.39e-14 |
|
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: 75.47 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 40 PPPARRLVLFVADGLRADALyeldENGNSRAP---FIRNIIMHEGS----WGISHTrvPTESRPGHVALIAG----FYED 108
Cdd:cd16019 1 PTKYDKVVLIVIDGLRYDLA----VNVNKQSSffsFLQKLNEQPNNsflaLSFADP--PTVTGPRLKALTTGnpptFLDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 109 VSAVAKgwkeNPVEFDSLFNEskytwswgspdilpMFAKGAS----GDHVYTYSY-DAKREDFGAQDATKLDTWVFDNVk 183
Cdd:cd16019 75 ISNFAS----SEIKEDNIIRQ--------------LKKNGKKilfyGDDTWLDLFpEIFTYKFTITSFNIRDMHDVDPI- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 184 dFFHHArnNQSLFSKINEEKIVFFL-HLLGIDTNGHAHR-PSSRDYKHNIKKVDDGVKEIVSMFNhfygNDgkTTFIFTS 261
Cdd:cd16019 136 -FYNHI--NDNLDENIYYDNWDFIIlHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMD----ND--TLLVVVS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 262 DHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQ----FDDAFLKEWRLENWKRLDvnQADIAPLMTSLIGVPFP 337
Cdd:cd16019 207 DHGMNNDGNHGGSSTEETSSFFFFISKKGFFKKRPIDQIekikQNNEQQKIDPSEYIRIIY--QIDILPTICYLLGIPIP 284
|
....*..
gi 767998476 338 LNSVGIL 344
Cdd:cd16019 285 FNNIGII 291
|
|
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
209-344 |
3.51e-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: 67.97 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 209 HLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMfnhfygNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGA 288
Cdd:cd16023 166 HFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIER------LDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSK 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767998476 289 GIKYPQRVSAQQFDDAFLKEWRlenwkrlDVNQADIAPLMTSLIGVPFPLNSVGIL 344
Cdd:cd16023 240 RPFNNSDEPIESNGPGDPSKVR-------SVPQIDLVPTLSLLLGLPIPFSNLGTV 288
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
44-333 |
6.73e-11 |
|
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: 64.14 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 44 RRLVLFVADGLRADALYELdengnSRAPFIRNIIMhEGSWGIS-HTRVPTESRPGHVALIAGFYEDV-SAVAKGWkenpv 121
Cdd:cd16018 1 PPLIVISIDGFRWDYLDRA-----GLTPNLKRLAE-EGVRAKYvKPVFPTLTFPNHYSIVTGLYPEShGIVGNYF----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 122 eFDSLFNESKYT-------WSWGSPDILPMFAKgaSGDHVYTYSY---DAKREDFGAQDATKLDTWVFDNVKDFFHHARN 191
Cdd:cd16018 70 -YDPKTNEEFSDsdwvwdpWWIGGEPIWVTAEK--AGLKTASYFWpgsEVAIIGYNPTPIPLGGYWQPYNDSFPFEERVD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 192 nqSLFSKINEEKIVF-FLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFnHFYGNDGKTTFIFTSDHGMTDWGS 270
Cdd:cd16018 147 --TILEWLDLERPDLiLLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEAL-KERGLLDDTNIIVVSDHGMTDVGT 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767998476 271 HGaGHPSETL--TPLVTWGAGIKYPQRVSaqqfddaflkewRLENwkrldVnqaDIAPLMTSLIG 333
Cdd:cd16018 224 HG-YDNELPDmrAIFIARGPAFKKGKKLG------------PFRN-----V---DIYPLMCNLLG 267
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
46-267 |
3.93e-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: 62.44 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 46 LVLFVADGLRADALYELDengnsRAPFIRNIiMHEGSWGISHTRV-PTESRPGHVALIAG-------------------- 104
Cdd:pfam01663 1 LLVISLDGFRADYLDRFE-----LTPNLAAL-AKEGVSAPNLTPVfPTLTFPNHYTLVTGlypgshgivgntfydpktge 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 105 ---FYEDVSAVAKGWKENPVEFDSLFNE---SKYTWSWGSPDILpmfAKGASGDHVYTYSYDAKREDFGAQDATKLDTWV 178
Cdd:pfam01663 75 ylvFVISDPEDPRWWQGEPIWDTAAKAGvraAALFWPGSEVDYS---TYYGTPPRYLKDDYNNSVPFEDRVDTAVLQTWL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 179 fdnVKDFFHHARNNQSLFskineekivfFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMF--NHFYGNdgkTT 256
Cdd:pfam01663 152 ---DLPFADVAAERPDLL----------LVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALdeRGLFED---TN 215
|
250
....*....|.
gi 767998476 257 FIFTSDHGMTD 267
Cdd:pfam01663 216 VIVVSDHGMTP 226
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
151-337 |
6.76e-06 |
|
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: 49.43 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 151 GDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLF-------------------SKINEEKIVFFLHLl 211
Cdd:cd16027 100 THYNPDAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRAKKGQPFFlwfgfhdphrpyppgdgeePGYDPEKVKVPPYL- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 212 gIDTnghahrPSSR----DYKHNIKKVDDGVKEIVSMF--NHFYGNdgkTTFIFTSDHGM---------TDWGSHgaghp 276
Cdd:cd16027 179 -PDT------PEVRedlaDYYDEIERLDQQVGEILDELeeDGLLDN---TIVIFTSDHGMpfprakgtlYDSGLR----- 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767998476 277 setlTPLVtwgagIKYPQRVSAQQFDDAFlkewrlenwkrldVNQADIAPLMTSLIGVPFP 337
Cdd:cd16027 244 ----VPLI-----VRWPGKIKPGSVSDAL-------------VSFIDLAPTLLDLAGIEPP 282
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
46-299 |
1.35e-04 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 45.11 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 46 LVLFVADGLRADALyelDENGNSRA--PFI----RNIIMHEGswGISHTRVPTESRPghvALIAGFY-EDVSAVAKGWKE 118
Cdd:pfam00884 3 VVLVLGESLRAPDL---GLYGYPRPttPFLdrlaEEGLLFSN--FYSGGTLTAPSRF---ALLTGLPpHNFGSYVSTPVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 119 NPVEFDSLFN-----------ESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATK--LDTWVFDNVKDF 185
Cdd:pfam00884 75 LPRTEPSLPDllkragyntgaIGKWHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGgvSDEALLDEALEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 186 FHHarnnqslfskiNEEKIVFFLHLLGidtnGHAHRPSSRD---------------------YKHNIKKVDDGVKEIVSM 244
Cdd:pfam00884 155 LDN-----------NDKPFFLVLHTLG----SHGPPYYPDRypekyatfkpsscseeqllnsYDNTLLYTDDAIGRVLDK 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767998476 245 FNhFYGNDGKTTFIFTSDHG--------MTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQ 299
Cdd:pfam00884 220 LE-ENGLLDNTLVVYTSDHGeslgegggYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEA 281
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
206-342 |
2.93e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 43.69 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 206 FFLHLLGIDTnghaHRPSSrdYK-------HNIKKVDDGVKEivsmfnhfYGNDGKTTFIFTSDHGMT-----DWGSHGA 273
Cdd:cd16148 150 FFLFLHYFDP----HEPYL--YDaevryvdEQIGRLLDKLKE--------LGLLEDTLVIVTSDHGEEfgehgLYWGHGS 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767998476 274 GHPSETL-TPLVTWGAGIKYPQRVSAQqfddaflkewrlenwkrldVNQADIAPLMTSLIGVPFPLNSVG 342
Cdd:cd16148 216 NLYDEQLhVPLIIRWPGKEPGKRVDAL-------------------VSHIDIAPTLLDLLGVEPPDYSDG 266
|
|
| |
