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Conserved domains on  [gi|5668571|dbj|BAA82663|]
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phosphatidylinositolglycan class N [Mus musculus]

Protein Classification

GPI ethanolamine phosphate transferase 1( domain architecture ID 10887960)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 40-345 0e+00

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: 511.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571   40 PPPAKRLVLFVADGLRADTLYELDEdgnSRAPFIRNVIMHEGSWGVSHTRVPTESRPGHVALIAGFYEDVSAVAKGWKEN 119
Cdd:cd16020   1 PPPAKRLVVFVADGLRADTFFENNC---SRAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKGWKEN 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  120 PVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDaqREDFGAHDATKLDTWVFDKVKDFFDAARNNQSlfTKV 199
Cdd:cd16020  78 PVEFDSVFNRSRRSWAWGSPDILPMFPKGATGGKVLTYIYP--EEDFDSTDASELDEWVFDKVEEFLANASSNKT--ELL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  200 NEEKVVFFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHfYGDDGKTAFIFTSDHGMTDWGSHGAGHPSET 279
Cdd:cd16020 154 NQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEE-YFNDGRTAYIFTSDHGMTDWGSHGDGSPDET 232

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5668571  280 LTPFVTWGAGIKFPQNVSaqqyDDEFLKEWRLENWKRRDVNQADIAPLMASLIGVPFPLNSVGILP 345
Cdd:cd16020 233 ETPFIAWGAGIKHPTPGR----GPSFSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
 
Name Accession Description Interval E-value
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 40-345 0e+00

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: 511.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571   40 PPPAKRLVLFVADGLRADTLYELDEdgnSRAPFIRNVIMHEGSWGVSHTRVPTESRPGHVALIAGFYEDVSAVAKGWKEN 119
Cdd:cd16020   1 PPPAKRLVVFVADGLRADTFFENNC---SRAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKGWKEN 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  120 PVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDaqREDFGAHDATKLDTWVFDKVKDFFDAARNNQSlfTKV 199
Cdd:cd16020  78 PVEFDSVFNRSRRSWAWGSPDILPMFPKGATGGKVLTYIYP--EEDFDSTDASELDEWVFDKVEEFLANASSNKT--ELL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  200 NEEKVVFFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHfYGDDGKTAFIFTSDHGMTDWGSHGAGHPSET 279
Cdd:cd16020 154 NQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEE-YFNDGRTAYIFTSDHGMTDWGSHGDGSPDET 232

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5668571  280 LTPFVTWGAGIKFPQNVSaqqyDDEFLKEWRLENWKRRDVNQADIAPLMASLIGVPFPLNSVGILP 345
Cdd:cd16020 233 ETPFIAWGAGIKHPTPGR----GPSFSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 38-267 1.45e-19

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 89.04  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571   38 PLPPPAKRLVLFVADGLRADTLYELDedgnsrAPFIRNvIMHEGSWGVSHTRV-PTESRPGHVALIAGFYEDVSAVAkGW 116
Cdd:COG1524  18 AAAPPAKKVVLILVDGLRADLLERAH------APNLAA-LAARGVYARPLTSVfPSTTAPAHTTLLTGLYPGEHGIV-GN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  117 ----KENPVEFDSLFNESKYTWS---WGSPDIL---------------PMFAKGASGDHVYTYSYDAQREDFGAHDAtkl 174
Cdd:COG1524  90 gwydPELGRVVNSLSWVEDGFGSnslLPVPTIFeraraaglttaavfwPSFEGSGLIDAARPYPYDGRKPLLGNPAA--- 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  175 DTWVFDkvkDFFDAARNNQSLFTkvneekvvfFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHFYGDDGk 254
Cdd:COG1524 167 DRWIAA---AALELLREGRPDLL---------LVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEG- 233

                       250
                ....*....|...
gi 5668571  255 TAFIFTSDHGMTD 267
Cdd:COG1524 234 TLVIVTADHGMVD 246
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 46-267 1.36e-11

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: 65.14  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571     46 LVLFVADGLRADTLYELDedgnsRAPFIRNvIMHEGSWGVSHTRV-PTESRPGHVALIAG-------------------- 104
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-----LTPNLAA-LAKEGVSAPNLTPVfPTLTFPNHYTLVTGlypgshgivgntfydpktge 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571    105 ---FYEDVSAVAKGWKENPVEFDSLFNE---SKYTWSWGSPDILpmfAKGASGDHVYTYSYDAQREDFGAHDATKLDTWV 178
Cdd:pfam01663  75 ylvFVISDPEDPRWWQGEPIWDTAAKAGvraAALFWPGSEVDYS---TYYGTPPRYLKDDYNNSVPFEDRVDTAVLQTWL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571    179 fdkVKDFFDAARNNQSLFTkvneekvvffLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIV-SIFKHfyGDDGKTAF 257
Cdd:pfam01663 152 ---DLPFADVAAERPDLLL----------VYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLeALDER--GLFEDTNV 216

                         250
                  ....*....|
gi 5668571    258 IFTSDHGMTD 267
Cdd:pfam01663 217 IVVSDHGMTP 226
 
Name Accession Description Interval E-value
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 40-345 0e+00

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: 511.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571   40 PPPAKRLVLFVADGLRADTLYELDEdgnSRAPFIRNVIMHEGSWGVSHTRVPTESRPGHVALIAGFYEDVSAVAKGWKEN 119
Cdd:cd16020   1 PPPAKRLVVFVADGLRADTFFENNC---SRAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYEDPSAVTKGWKEN 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  120 PVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDaqREDFGAHDATKLDTWVFDKVKDFFDAARNNQSlfTKV 199
Cdd:cd16020  78 PVEFDSVFNRSRRSWAWGSPDILPMFPKGATGGKVLTYIYP--EEDFDSTDASELDEWVFDKVEEFLANASSNKT--ELL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  200 NEEKVVFFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHfYGDDGKTAFIFTSDHGMTDWGSHGAGHPSET 279
Cdd:cd16020 154 NQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEE-YFNDGRTAYIFTSDHGMTDWGSHGDGSPDET 232

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5668571  280 LTPFVTWGAGIKFPQNVSaqqyDDEFLKEWRLENWKRRDVNQADIAPLMASLIGVPFPLNSVGILP 345
Cdd:cd16020 233 ETPFIAWGAGIKHPTPGR----GPSFSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 44-332 1.94e-26

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: 105.97  E-value: 1.94e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571   44 KRLVLFVADGLRADtLYELDEDGNSRAPFIRNVIMHEGSWGVSHTRVPTESRPGHVALIAGFYEDVSAV----------- 112
Cdd:cd00016   1 KHVVLIVLDGLGAD-DLGKAGNPAPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYtgngsadpelp 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  113 --AKGWKENPVEFDSLFNESKYTWSWgspdilpmfakgasgdhvytysydaqredFGAHDATKLDTwvfdKVKDFFdaar 190
Cdd:cd00016  80 srAAGKDEDGPTIPELLKQAGYRTGV-----------------------------IGLLKAIDETS----KEKPFV---- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  191 nnqslftkvneekvvFFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHFyGDDGKTAFIFTSDHGMTDWGS 270
Cdd:cd00016 123 ---------------LFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKA-GDADDTVIIVTADHGGIDKGH 186

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  271 HGAGHPS--------ETLTPFVTWGAGIKFPQNvsaqqyddeflkewrlenwKRRDVNQADIAPLMASLI 332
Cdd:cd00016 187 GGDPKADgkadkshtGMRVPFIAYGPGVKKGGV-------------------KHELISQYDIAPTLADLL 237
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 40-344 2.49e-26

GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 106.50  E-value: 2.49e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571   40 PPPAKRLVLFVADGLRADTLYELDedgnSRAPFIRNVIMHEGSWG-VSHTRVPTESRPGHVALIAGfyedvsavakgwkE 118
Cdd:cd16024   1 KPAFDKLVFMVIDALRADFVFGPD----SNMPFTQSLINSGSALAfTAKAQPPTVTMPRIKALTTG-------------S 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  119 NPVEFDSLFN---ESKYTWSWgspdILPMFAKGAS----GDhvytysydaqredfgahdatklDTWVfdkvKDF---FDA 188
Cdd:cd16024  64 IPSFLDVVLNfasSLLEEDNW----LSQLKAAGKKivfyGD----------------------DTWL----KLFpgsFTR 113

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  189 ARNNQSLF----TKV-------------NEEKVVFFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHfYGD 251
Cdd:cd16024 114 SDGTTSFFvsdfTEVdnnvtrhldselsRDDWDVLILHYLGLDHIGHLEGPKSPLMPPKLKEMDDVIKRIYESLEE-QSS 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  252 DGKTAFIFTSDHGMTDWGSHGAGHPSETLTPFVTWGAgiKFPQNVSAQQYDDEFLKEwrlenwkrrdVNQADIAPLMASL 331
Cdd:cd16024 193 NNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISP--KFSSKPSNADGELSYYET----------VQQVDLAPTLALL 260

                       330
                ....*....|...
gi 5668571  332 IGVPFPLNSVGIL 344
Cdd:cd16024 261 LGLPIPKNSVGVL 273
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 38-267 1.45e-19

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 89.04  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571   38 PLPPPAKRLVLFVADGLRADTLYELDedgnsrAPFIRNvIMHEGSWGVSHTRV-PTESRPGHVALIAGFYEDVSAVAkGW 116
Cdd:COG1524  18 AAAPPAKKVVLILVDGLRADLLERAH------APNLAA-LAARGVYARPLTSVfPSTTAPAHTTLLTGLYPGEHGIV-GN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  117 ----KENPVEFDSLFNESKYTWS---WGSPDIL---------------PMFAKGASGDHVYTYSYDAQREDFGAHDAtkl 174
Cdd:COG1524  90 gwydPELGRVVNSLSWVEDGFGSnslLPVPTIFeraraaglttaavfwPSFEGSGLIDAARPYPYDGRKPLLGNPAA--- 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  175 DTWVFDkvkDFFDAARNNQSLFTkvneekvvfFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHFYGDDGk 254
Cdd:COG1524 167 DRWIAA---AALELLREGRPDLL---------LVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARGLYEG- 233

                       250
                ....*....|...
gi 5668571  255 TAFIFTSDHGMTD 267
Cdd:COG1524 234 TLVIVTADHGMVD 246
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 40-344 4.27e-18

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: 83.95  E-value: 4.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571   40 PPPAKRLVLFVADGLRADTLyeldEDGNSRAPFirNVIMHE---------GSWGVSHTrvPTESRPGHVALIAG----FY 106
Cdd:cd16019   1 PTKYDKVVLIVIDGLRYDLA----VNVNKQSSF--FSFLQKlneqpnnsfLALSFADP--PTVTGPRLKALTTGnpptFL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  107 EDVSAVAKgwkeNPVEFDSLFNEskytwswgspdilpMFAKGAS----GDHVYTYSYdaQREDFGAHDATKLDtwvfdkV 182
Cdd:cd16019  73 DLISNFAS----SEIKEDNIIRQ--------------LKKNGKKilfyGDDTWLDLF--PEIFTYKFTITSFN------I 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  183 KDFFDAARNNQSLFTKVNEEKV------VFFLHLLGIDTNGHAHR-PSSREYKDNIKKVDDGVKEIVSIFkhfyGDDgkT 255
Cdd:cd16019 127 RDMHDVDPIFYNHINDNLDENIyydnwdFIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRM----DND--T 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  256 AFIFTSDHGMTDWGSHGAGHPSETLTPFVTWGAGIKFPQNVSAQQ----YDDEFLKEWRLENWkrRDVNQADIAPLMASL 331
Cdd:cd16019 201 LLVVVSDHGMNNDGNHGGSSTEETSSFFFFISKKGFFKKRPIDQIekikQNNEQQKIDPSEYI--RIIYQIDILPTICYL 278

                       330
                ....*....|...
gi 5668571  332 IGVPFPLNSVGIL 344
Cdd:cd16019 279 LGIPIPFNNIGII 291
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 209-344 9.37e-16

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: 76.83  E-value: 9.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  209 HLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIfkhfygDDGKTAFIFTSDHGMTDWGSHGAGHPSETLTPFVTWGA 288
Cdd:cd16023 166 HFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIER------LDDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSK 239

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5668571  289 GIKFPQNVSAQQYDDEFLKEWRlenwkrrDVNQADIAPLMASLIGVPFPLNSVGIL 344
Cdd:cd16023 240 RPFNNSDEPIESNGPGDPSKVR-------SVPQIDLVPTLSLLLGLPIPFSNLGTV 288
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 44-333 3.36e-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: 69.15  E-value: 3.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571   44 KRLVLFVADGLRADTLYELdedgnSRAPFIRNvIMHEGSWGVS-HTRVPTESRPGHVALIAGFYEDV-SAVAKGWKEnpV 121
Cdd:cd16018   1 PPLIVISIDGFRWDYLDRA-----GLTPNLKR-LAEEGVRAKYvKPVFPTLTFPNHYSIVTGLYPEShGIVGNYFYD--P 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  122 EFDSLFNESKYTWSWGSPDILP--------------MFAKGASGD-HVYTYSYDAQREDFGAHDATKLDTWVFDKVKDFF 186
Cdd:cd16018  73 KTNEEFSDSDWVWDPWWIGGEPiwvtaekaglktasYFWPGSEVAiIGYNPTPIPLGGYWQPYNDSFPFEERVDTILEWL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  187 DAARNNqslFTkvneekvvfFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHFYGDDGkTAFIFTSDHGMT 266
Cdd:cd16018 153 DLERPD---LI---------LLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDD-TNIIVVSDHGMT 219

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5668571  267 DWGSHGaGHPSETL--TPFVTWGAGIKfpqnvsaqqyDDEFLKEWRLEnwkrrdvnqaDIAPLMASLIG 333
Cdd:cd16018 220 DVGTHG-YDNELPDmrAIFIARGPAFK----------KGKKLGPFRNV----------DIYPLMCNLLG 267
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 46-267 1.36e-11

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: 65.14  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571     46 LVLFVADGLRADTLYELDedgnsRAPFIRNvIMHEGSWGVSHTRV-PTESRPGHVALIAG-------------------- 104
Cdd:pfam01663   1 LLVISLDGFRADYLDRFE-----LTPNLAA-LAKEGVSAPNLTPVfPTLTFPNHYTLVTGlypgshgivgntfydpktge 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571    105 ---FYEDVSAVAKGWKENPVEFDSLFNE---SKYTWSWGSPDILpmfAKGASGDHVYTYSYDAQREDFGAHDATKLDTWV 178
Cdd:pfam01663  75 ylvFVISDPEDPRWWQGEPIWDTAAKAGvraAALFWPGSEVDYS---TYYGTPPRYLKDDYNNSVPFEDRVDTAVLQTWL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571    179 fdkVKDFFDAARNNQSLFTkvneekvvffLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIV-SIFKHfyGDDGKTAF 257
Cdd:pfam01663 152 ---DLPFADVAAERPDLLL----------VYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLeALDER--GLFEDTNV 216

                         250
                  ....*....|
gi 5668571    258 IFTSDHGMTD 267
Cdd:pfam01663 217 IVVSDHGMTP 226
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 151-337 1.21e-08

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: 56.36  E-value: 1.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  151 GDHVYTYSYDAQREDFGAHDATKLDTWVFDKVKDFFDAARNNQSLF-------------------TKVNEEKVVFFLHLl 211
Cdd:cd16027 100 THYNPDAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRAKKGQPFFlwfgfhdphrpyppgdgeePGYDPEKVKVPPYL- 178

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  212 gIDTnghahrPSSRE----YKDNIKKVDDGVKEIVSIFKhfygDDG---KTAFIFTSDHGM---------TDWGSHgagh 275
Cdd:cd16027 179 -PDT------PEVREdladYYDEIERLDQQVGEILDELE----EDGlldNTIVIFTSDHGMpfprakgtlYDSGLR---- 243

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5668571  276 psetlTPFVtwgagIKFPQNVSAQQYDDEFlkewrlenwkrrdVNQADIAPLMASLIGVPFP 337
Cdd:cd16027 244 -----VPLI-----VRWPGKIKPGSVSDAL-------------VSFIDLAPTLLDLAGIEPP 282
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 158-342 2.05e-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: 45.62  E-value: 2.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  158 SYDAQREDFGAHDATKLDTW--VFDKVKDFFDAARNNQSlftkvneekvvFFLHLLGIDTnghaHRPSsrEYKDNIKKVD 235
Cdd:cd16148 111 TFEDFRGQEGDPGEEGDERAerVTDRALEWLDRNADDDP-----------FFLFLHYFDP----HEPY--LYDAEVRYVD 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  236 DGVKEIVSIFKHfYGDDGKTAFIFTSDHGMT-----DWGSHGAGHPSETL-TPFVTWGAGIKFPQNVSAQqyddeflkew 309
Cdd:cd16148 174 EQIGRLLDKLKE-LGLLEDTLVIVTSDHGEEfgehgLYWGHGSNLYDEQLhVPLIIRWPGKEPGKRVDAL---------- 242

                       170       180       190
                ....*....|....*....|....*....|...
gi 5668571  310 rlenwkrrdVNQADIAPLMASLIGVPFPLNSVG 342
Cdd:cd16148 243 ---------VSHIDIAPTLLDLLGVEPPDYSDG 266
Sulfatase pfam00884
Sulfatase;
46-334 4.10e-05

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 45.11  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571     46 LVLFVADGLRADtlyELDEDGNSRA--PFI----RNVIMHEGSWGVSHTRVPTESrpghvALIAGFY-EDVSAVAKGWKE 118
Cdd:pfam00884   3 VVLVLGESLRAP---DLGLYGYPRPttPFLdrlaEEGLLFSNFYSGGTLTAPSRF-----ALLTGLPpHNFGSYVSTPVG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571    119 NPVEFDSLFN-----------ESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAQREDFGAHDATKLdtwVFDKVkdFFD 187
Cdd:pfam00884  75 LPRTEPSLPDllkragyntgaIGKWHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGG---VSDEA--LLD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571    188 AARNnqslFTKVNEEKVVFFLHLLG-----------------IDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKhFYG 250
Cdd:pfam00884 150 EALE----FLDNNDKPFFLVLHTLGshgppyypdrypekyatFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLE-ENG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571    251 DDGKTAFIFTSDHG--------MTDWGSHGAGHPSETLTPFVTWGAGIKfpqnvSAQQYDDEFlkewrlenwkrrdVNQA 322
Cdd:pfam00884 225 LLDNTLVVYTSDHGeslgegggYLHGGKYDNAPEGGYRVPLLIWSPGGK-----AKGQKSEAL-------------VSHV 286

                         330
                  ....*....|..
gi 5668571    323 DIAPLMASLIGV 334
Cdd:pfam00884 287 DLFPTILDLAGI 298
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 148-334 1.86e-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: 39.91  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  148 GASGDHVYTYSYDAQREDFGAHDATKLDTWVFD-KVKDFFDAARNNQSlftkvneEKVVFFLHLLG-------------- 212
Cdd:cd16017  94 GGCGGYDTRISAIAKIETVFTNKGSCNSSNCYDeALLPLLDEALADSS-------KKKLIVLHLMGshgpyydrypeefa 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  213 --IDTNGHAHRPSSREYK----DN-IKKVDDGVKEIVSIFKHfygDDGKTAFIFTSDHG--MTDWGS--HGAGHPSETLT 281
Cdd:cd16017 167 kfTPDCDNELQSCSKEELinayDNsILYTDYVLSQIIERLKK---KDKDAALIYFSDHGesLGENGLylHGAPYAPKEQY 243

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5668571  282 --PFVTWgagikfpqnvsaqqYDDEFLKEWRLENWKRRD---VNQADIAPLMASLIGV 334
Cdd:cd16017 244 hvPFIIW--------------SSDSYKQRYPVERLRANKdrpFSHDNLFHTLLGLLGI 287
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 227-337 2.23e-03

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: 39.34  E-value: 2.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  227 YKDNIKKVDDGVKEIVSIFKHfYGDDGKTAFIFTSDHG--MTDWGSHGA-GHPSETLT--PFVtwgagIKFPQNVSAQQY 301
Cdd:cd16022 133 YYAMVSAIDDQIGRILDALEE-LGLLDNTLIVFTSDHGdmLGDHGLRGKkGSLYEGGIrvPFI-----VRWPGKIPAGQV 206

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 5668571  302 DDEFlkewrlenwkrrdVNQADIAPLMASLIGVPFP 337
Cdd:cd16022 207 SDAL-------------VSLLDLLPTLLDLAGIEPP 229
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
225-337 2.63e-03

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 39.48  E-value: 2.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  225 REYKDNIKKVDDGVKEIVSIFKHfYGDDGKTAFIFTSDHG--MTDWGSHGA-GHPSETLT--PFVtwgagIKFPQNVSAQ 299
Cdd:COG3119 200 AAYAAMIEEVDDQVGRLLDALEE-LGLADNTIVVFTSDNGpsLGEHGLRGGkGTLYEGGIrvPLI-----VRWPGKIKAG 273

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 5668571  300 QYDDEFlkewrlenwkrrdVNQADIAPLMASLIGVPFP 337
Cdd:COG3119 274 SVSDAL-------------VSLIDLLPTLLDLAGVPIP 298
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 220-345 2.86e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 39.51  E-value: 2.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  220 HRPSSREYKDNIKKVDDGVKEIVSIFKH--FYGDdgkTAFIFTSDHG-MTdwGSH-----GAGHPSETL-TPFVtwgagI 290
Cdd:cd16033 212 WKEIIAHYWGYITLIDDAIGRILDALEElgLADD---TLVIFTSDHGdAL--GAHrlwdkGPFMYEETYrIPLI-----I 281

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5668571  291 KFPQNVSAQQYDDEFlkewrlenwkrrdVNQADIAPLMASLIGVPFPLNSVG--ILP 345
Cdd:cd16033 282 KWPGVIAAGQVVDEF-------------VSLLDLAPTILDLAGVDVPPKVDGrsLLP 325
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
 219-341 3.27e-03

arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.


Pssm-ID: 293780 [Multi-domain]  Cd Length: 383  Bit Score: 39.37  E-value: 3.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  219 AHRPSSRE--YKDNIKKVDDGVKEIVSIFKHfYGDDGKTAFIFTSDHG-------------MTDWGSHGAGHPSETltpf 283
Cdd:cd16161 175 FQSPTSGRgpYGDALQEMDDLVGQIMDAVKH-AGLKDNTLTWFTSDNGpwevkcelavgpgTGDWQGNLGGSVAKA---- 249

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5668571  284 VTWGAGIKFPQNVSAQQYDDEFLKEWRLenwkrrdVNQADIAPLMASLIGVPFPLNSV 341
Cdd:cd16161 250 STWEGGHREPAIVYWPGRIPANSTSAAL-------VSTLDIFPTVVALAGASLPPGRI 300
AP-SPAP cd16016
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ...
 270-342 3.84e-03

SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.


Pssm-ID: 293740 [Multi-domain]  Cd Length: 457  Bit Score: 39.05  E-value: 3.84e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5668571  270 SHGAGHPSETLTPFVTWGAGIKfPQNVSaqqyddeflkewrlenwkrRDVNQADIAPLMASLIGVPFPLNSVG 342
Cdd:cd16016 400 THGSPYDYDTHVPLLFYGWGIK-PGEIP-------------------RPVEITDIAPTLAALLGIQPPNGCIG 452
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 163-333 4.61e-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: 38.43  E-value: 4.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  163 REDFGAHDATKLDTWVFDKvkDFFDAArnnQSLFTKVNEEKvvFFLHLLGIDTnghaHRP--SSREYKDNIKKVDDGVKE 240
Cdd:cd16015 122 LEDFPDDEKETNGWGVSDE--SLFDQA---LEELEELKKKP--FFIFLVTMSN----HGPydLPEEKKDEPLKVEEDKTE 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5668571  241 IVSIFKHFY----------------GDDGKTAFIFTSDHGMTDwGSHGAGHPSETL----TPFVTWGAGIKFPQNVSaqq 300
Cdd:cd16015 191 LENYLNAIHytdkalgefieklkksGLYENTIIVIYGDHLPSL-GSDYDETDEDPLdlyrTPLLIYSPGLKKPKKID--- 266

                       170       180       190
                ....*....|....*....|....*....|...
gi 5668571  301 yddeflkewrlenwkrRDVNQADIAPLMASLIG 333
Cdd:cd16015 267 ----------------RVGSQIDIAPTLLDLLG 283
 
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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