|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
65-331 |
1.55e-150 |
|
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: 438.15 E-value: 1.55e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 65 KRTPLKLVFVLIDALRFDFVADRSRSLSFLGSMLRDRKALLYRSRAYSPTVTLPRIKTLLTGTVPGFGDVLLNFNADVLH 144
Cdd:cd16024 1 KPAFDKLVFMVIDALRADFVFGPDSNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 145 DDNLVHQARASGKKTVFYGDDTWLRILPGCFDRYEGTTSFFVSDYTEVDRNVSRHVPSEMEATDWDWLVLHYLGLDHIGH 224
Cdd:cd16024 81 EDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 225 THGPSSSLVDDKLAEMDGILSTMYASLR-RRANDSFLIVVTGDHGMNAVGNHGGSSEGEVMTALLFIPTK------PWDF 297
Cdd:cd16024 161 LEGPKSPLMPPKLKEMDDVIKRIYESLEeQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKfsskpsNADG 240
|
250 260 270
....*....|....*....|....*....|....
gi 215491789 298 GSQDVSTVSQVDIAPTLSLLTGLPIPKGSYGRAL 331
Cdd:cd16024 241 ELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
70-275 |
2.42e-20 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 93.66 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 70 KLVFVLIDALRFDFVadRSRSLSFLGSmLRDRKALLYRSRAYSPTVTLPRIKTLLTGTVPG-------------FGDVL- 135
Cdd:COG1524 25 KVVLILVDGLRADLL--ERAHAPNLAA-LAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGehgivgngwydpeLGRVVn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 136 -LNFNADVLHDDNLVH------QARASGKKTVFYGddtWLRILPGCFDRY------EGTTSFFVSDYTevDRNVSRHVPS 202
Cdd:COG1524 102 sLSWVEDGFGSNSLLPvptifeRARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLLGNPAA--DRWIAAAALE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215491789 203 EMEATDWDWLVLHYLGLDHIGHTHGPSSSLVDDKLAEMDGILSTMYASLRRR-ANDSFLIVVTGDHGMNAVGNH 275
Cdd:COG1524 177 LLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARgLYEGTLVIVTADHGMVDVPPD 250
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
71-276 |
3.54e-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: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 71 LVFVLIDALRFDFVaDRSRSLSFLGSMLRD---RKALlyrsRAYSPTVTLPRIKTLLTGTVPG----FGDVLLnfnaDVL 143
Cdd:pfam01663 1 LLVISLDGFRADYL-DRFELTPNLAALAKEgvsAPNL----TPVFPTLTFPNHYTLVTGLYPGshgiVGNTFY----DPK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 144 HDDNLVHQaRASGKKTVFYGDD-TWLRIL-----------PGC---FDRYEGTTSFFVSDY----TEVDRNVSRHVPSEM 204
Cdd:pfam01663 72 TGEYLVFV-ISDPEDPRWWQGEpIWDTAAkagvraaalfwPGSevdYSTYYGTPPRYLKDDynnsVPFEDRVDTAVLQTW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 205 EATD--------WDWLVLHYLGLDHIGHTHGPSSSLVDDKLAEMDGILSTMYASLRRRANDSFL-IVVTGDHGMNAVGNH 275
Cdd:pfam01663 151 LDLPfadvaaerPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTnVIVVSDHGMTPVSDD 230
|
.
gi 215491789 276 G 276
Cdd:pfam01663 231 K 231
|
|
| PIGO_PIGG |
pfam19316 |
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ... |
513-692 |
2.78e-09 |
|
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the transmembrane region of the GPI ethanolamine phosphate transferase enzymes. The family includes the PIGO and PIGG proteins from human. These proteins are involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis.
Pssm-ID: 437148 Cd Length: 423 Bit Score: 59.91 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 513 HQFRSGNDPDLLEAVInswTLLCLILHTPQNVPMFalvvLLERAVHDFLFDLPLQMLPRVILYFWFAMSCHFHQGNSNKL 592
Cdd:pfam19316 228 RRARGGGSARLLHELL---TLFLITQSRATNIPLF----LLFRLQLEFLSSLDLSPTEITTTSLLLQYASFFAFGGSNAI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 593 STVSVSAGYIGVSSYNPVVVGLLmvsyTYSS----LVLW-----LLMLWKRFAEPEDNGLKRSRSRTKLLVCASILFMkf 663
Cdd:pfam19316 301 SSVDLSNAYNGVSGYNVVAVGVL----TFVSnwagPIWWtsatnLLLLRKRRRGEGRGVFFQHLALLTLFVAASLVSV-- 374
|
170 180
....*....|....*....|....*....
gi 215491789 664 attawyMVLMVVQRYHIFVLSVFSPKLVY 692
Cdd:pfam19316 375 ------MAACTALRTHLFIWTVFSPKYLY 397
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
65-331 |
1.55e-150 |
|
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: 438.15 E-value: 1.55e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 65 KRTPLKLVFVLIDALRFDFVADRSRSLSFLGSMLRDRKALLYRSRAYSPTVTLPRIKTLLTGTVPGFGDVLLNFNADVLH 144
Cdd:cd16024 1 KPAFDKLVFMVIDALRADFVFGPDSNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 145 DDNLVHQARASGKKTVFYGDDTWLRILPGCFDRYEGTTSFFVSDYTEVDRNVSRHVPSEMEATDWDWLVLHYLGLDHIGH 224
Cdd:cd16024 81 EDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 225 THGPSSSLVDDKLAEMDGILSTMYASLR-RRANDSFLIVVTGDHGMNAVGNHGGSSEGEVMTALLFIPTK------PWDF 297
Cdd:cd16024 161 LEGPKSPLMPPKLKEMDDVIKRIYESLEeQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKfsskpsNADG 240
|
250 260 270
....*....|....*....|....*....|....
gi 215491789 298 GSQDVSTVSQVDIAPTLSLLTGLPIPKGSYGRAL 331
Cdd:cd16024 241 ELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
70-329 |
7.59e-88 |
|
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: 277.13 E-value: 7.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 70 KLVFVLIDALRFDFVADRSRS------------LSFLGSMLRD--RKALLYRSRAYSPTVTLPRIKTLLTGTVPGFGDVL 135
Cdd:cd16023 6 KVVLLLIDALRYDFVLPDDENppsenslyyhnkLPVLEELLKSqpNNSRLFKFIADPPTTTLQRLKGLTTGSLPTFIDAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 136 LNFNADVLHDDNLVHQARASGKKTVFYGDDTWLRILPGCFDRYEGTTSFFVSDYTEVDRNVSRHVPSEME-ATDWDWLVL 214
Cdd:cd16023 86 SNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQsEDDWDLLIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 215 HYLGLDHIGHTHGPSSSLVDDKLAEMDGILSTMYASLrrraNDSFLIVVTGDHGMNAVGNHGGSSEGEVMTALLFIPTKP 294
Cdd:cd16023 166 HFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERL----DDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYSKRP 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 215491789 295 W-----------DFGSQDVSTVSQVDIAPTLSLLTGLPIPKGSYGR 329
Cdd:cd16023 242 FnnsdepiesngPGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGT 287
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
70-328 |
2.72e-77 |
|
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: 249.59 E-value: 2.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 70 KLVFVLIDALRFDFVADRSRSLSFLGSMLR---DRK-ALLYRSRAYSPTVTLPRIKTLLTGTVPGFGDVLLNFNADVLHD 145
Cdd:cd16019 6 KVVLIVIDGLRYDLAVNVNKQSSFFSFLQKlneQPNnSFLALSFADPPTVTGPRLKALTTGNPPTFLDLISNFASSEIKE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 146 DNLVHQARASGKKTVFYGDDTWLRILPGCFDRYEGTTSFFVSDYTEVDRNVSRHVPSEME----ATDWDWLVLHYLGLDH 221
Cdd:cd16019 86 DNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHINDNLDeniyYDNWDFIILHFLGLDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 222 IGHTHG-PSSSLVDDKLAEMDGILSTMYaslrRRANDSFLIVVTGDHGMNAVGNHGGSSEGEVMTALLFI------PTKP 294
Cdd:cd16019 166 LGHKHNtTSSPELEKKLDQMDNLIRDIY----DRMDNDTLLVVVSDHGMNNDGNHGGSSTEETSSFFFFIskkgffKKRP 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 215491789 295 WD--------------FGSQDVSTVSQVDIAPTLSLLTGLPIPKGSYG 328
Cdd:cd16019 242 IDqiekikqnneqqkiDPSEYIRIIYQIDILPTICYLLGIPIPFNNIG 289
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
61-329 |
2.38e-20 |
|
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: 91.88 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 61 PPISKRtplkLVFVLIDALRFD-FVADRSRSLSFLGSMLRdRKALLYRSRAYSPTVTLPRIKTLLTGtvpgfgdvllnFN 139
Cdd:cd16020 1 PPPAKR----LVVFVADGLRADtFFENNCSRAPFLRKIFL-NQGLWGISHTRVPTESRPGHVALFAG-----------FY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 140 ADVLhddnlvhqARASGKK-------TVF--------YGDDTWLRIL-----PGCFDRYE-GTTSFFVSDYTEVDRNVSR 198
Cdd:cd16020 65 EDPS--------AVTKGWKenpvefdSVFnrsrrswaWGSPDILPMFpkgatGGKVLTYIyPEEDFDSTDASELDEWVFD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 199 HV--------PSEMEATDWDWLV--LHYLGLDHIGHTHGPSSSLVDDKLAEMDGILSTMYASLRRRANDS---FLivVTG 265
Cdd:cd16020 137 KVeeflanasSNKTELLNQDGLVffLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGrtaYI--FTS 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215491789 266 DHGMNAVGNHGGSSEGEVMTALLF--------------IPTKPWDFGSQDVSTVSQVDIAPTLSLLTGLPIPKGSYGR 329
Cdd:cd16020 215 DHGMTDWGSHGDGSPDETETPFIAwgagikhptpgrgpSFSANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGI 292
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
70-275 |
2.42e-20 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 93.66 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 70 KLVFVLIDALRFDFVadRSRSLSFLGSmLRDRKALLYRSRAYSPTVTLPRIKTLLTGTVPG-------------FGDVL- 135
Cdd:COG1524 25 KVVLILVDGLRADLL--ERAHAPNLAA-LAARGVYARPLTSVFPSTTAPAHTTLLTGLYPGehgivgngwydpeLGRVVn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 136 -LNFNADVLHDDNLVH------QARASGKKTVFYGddtWLRILPGCFDRY------EGTTSFFVSDYTevDRNVSRHVPS 202
Cdd:COG1524 102 sLSWVEDGFGSNSLLPvptifeRARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLLGNPAA--DRWIAAAALE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215491789 203 EMEATDWDWLVLHYLGLDHIGHTHGPSSSLVDDKLAEMDGILSTMYASLRRR-ANDSFLIVVTGDHGMNAVGNH 275
Cdd:COG1524 177 LLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDALKARgLYEGTLVIVTADHGMVDVPPD 250
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
70-319 |
2.72e-20 |
|
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: 91.11 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 70 KLVFVLIDALRFDFVaDRSRSLSFLGSMLRDrkaLLYRSRAYS--PTVTLPRIKTLLTGTVP--------GFGDVLLN-- 137
Cdd:cd16018 2 PLIVISIDGFRWDYL-DRAGLTPNLKRLAEE---GVRAKYVKPvfPTLTFPNHYSIVTGLYPeshgivgnYFYDPKTNee 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 138 FNADVLHDDN-------LVHQARASGKKTVFYgddTWlrilPGCFDRYEGttsffvsdYTEVDRNVSRHVPSEMEATDWD 210
Cdd:cd16018 78 FSDSDWVWDPwwiggepIWVTAEKAGLKTASY---FW----PGSEVAIIG--------YNPTPIPLGGYWQPYNDSFPFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 211 WLV----------------LHYLGLDHIGHTHGPSSSLVDDKLAEMDGILSTMYASLRRRANDSFL-IVVTGDHGMNAVG 273
Cdd:cd16018 143 ERVdtilewldlerpdlilLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTnIIVVSDHGMTDVG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 215491789 274 NHGGSSEGEVMTAlLFIPTKPWDFGSQDVSTVSQVDIAPTLSLLTG 319
Cdd:cd16018 223 THGYDNELPDMRA-IFIARGPAFKKGKKLGPFRNVDIYPLMCNLLG 267
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
71-317 |
1.39e-12 |
|
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: 67.83 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 71 LVFVLIDALRFDFVADRSRSLSFLG--SMLRDRKALLYRSRAYSPTVTLPRIKTLLTGTVPGFGDVLLNFNADVlhddnl 148
Cdd:cd00016 3 VVLIVLDGLGADDLGKAGNPAPTTPnlKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADP------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 149 VHQARASGKKTVFYgddtwlrILPGCFD--RYEgTTSFFVSDYTEVDRNVSrhvpsemeatdWDWLVLHYLGLDHIGHTH 226
Cdd:cd00016 77 ELPSRAAGKDEDGP-------TIPELLKqaGYR-TGVIGLLKAIDETSKEK-----------PFVLFLHFDGPDGPGHAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 227 GPSSSLVDDKLAEMDG-ILSTMYASLRRRANDSFLIVVTGDHGMNAVGNHG--------GSSEGEVMTALLFI-PTKPwd 296
Cdd:cd00016 138 GPNTPEYYDAVEEIDErIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGdpkadgkaDKSHTGMRVPFIAYgPGVK-- 215
|
250 260
....*....|....*....|.
gi 215491789 297 FGSQDVSTVSQVDIAPTLSLL 317
Cdd:cd00016 216 KGGVKHELISQYDIAPTLADL 236
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
71-276 |
3.54e-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: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 71 LVFVLIDALRFDFVaDRSRSLSFLGSMLRD---RKALlyrsRAYSPTVTLPRIKTLLTGTVPG----FGDVLLnfnaDVL 143
Cdd:pfam01663 1 LLVISLDGFRADYL-DRFELTPNLAALAKEgvsAPNL----TPVFPTLTFPNHYTLVTGLYPGshgiVGNTFY----DPK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 144 HDDNLVHQaRASGKKTVFYGDD-TWLRIL-----------PGC---FDRYEGTTSFFVSDY----TEVDRNVSRHVPSEM 204
Cdd:pfam01663 72 TGEYLVFV-ISDPEDPRWWQGEpIWDTAAkagvraaalfwPGSevdYSTYYGTPPRYLKDDynnsVPFEDRVDTAVLQTW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 205 EATD--------WDWLVLHYLGLDHIGHTHGPSSSLVDDKLAEMDGILSTMYASLRRRANDSFL-IVVTGDHGMNAVGNH 275
Cdd:pfam01663 151 LDLPfadvaaerPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTnVIVVSDHGMTPVSDD 230
|
.
gi 215491789 276 G 276
Cdd:pfam01663 231 K 231
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
69-333 |
7.09e-10 |
|
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: 60.25 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 69 LKLVFVLIDALRFDFVA------------DR--SRSLSFlgsmlrdrkallyrSRAYSP-TVTLPRIKTLLTGTVPGFGD 133
Cdd:cd16148 1 MNVILIVIDSLRADHLGcygydrvttpnlDRlaAEGVVF--------------DNHYSGsNPTLPSRFSLFTGLYPFYHG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 134 VLLNFNADvlHDDNLVHQARASGKKTVFYGDDTWLRILPGcFDRyeGTTSFFVSDYTEVDRNVSRHVPSEM---EATDW- 209
Cdd:cd16148 67 VWGGPLEP--DDPTLAEILRKAGYYTAAVSSNPHLFGGPG-FDR--GFDTFEDFRGQEGDPGEEGDERAERvtdRALEWl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 210 -------DW-LVLHYLGldhighTHGPSssLVDDKLAEMDGILSTMYASLRRR--ANDSfLIVVTGDHGM-----NAVGN 274
Cdd:cd16148 142 drnadddPFfLFLHYFD------PHEPY--LYDAEVRYVDEQIGRLLDKLKELglLEDT-LVIVTSDHGEefgehGLYWG 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215491789 275 HGGS-SEGEVMTALLFIPtkPWDFGSQDVST-VSQVDIAPTLSLLTGLPIPKGSYGRALAD 333
Cdd:cd16148 213 HGSNlYDEQLHVPLIIRW--PGKEPGKRVDAlVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| PIGO_PIGG |
pfam19316 |
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ... |
513-692 |
2.78e-09 |
|
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the transmembrane region of the GPI ethanolamine phosphate transferase enzymes. The family includes the PIGO and PIGG proteins from human. These proteins are involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis.
Pssm-ID: 437148 Cd Length: 423 Bit Score: 59.91 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 513 HQFRSGNDPDLLEAVInswTLLCLILHTPQNVPMFalvvLLERAVHDFLFDLPLQMLPRVILYFWFAMSCHFHQGNSNKL 592
Cdd:pfam19316 228 RRARGGGSARLLHELL---TLFLITQSRATNIPLF----LLFRLQLEFLSSLDLSPTEITTTSLLLQYASFFAFGGSNAI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 593 STVSVSAGYIGVSSYNPVVVGLLmvsyTYSS----LVLW-----LLMLWKRFAEPEDNGLKRSRSRTKLLVCASILFMkf 663
Cdd:pfam19316 301 SSVDLSNAYNGVSGYNVVAVGVL----TFVSnwagPIWWtsatnLLLLRKRRRGEGRGVFFQHLALLTLFVAASLVSV-- 374
|
170 180
....*....|....*....|....*....
gi 215491789 664 attawyMVLMVVQRYHIFVLSVFSPKLVY 692
Cdd:pfam19316 375 ------MAACTALRTHLFIWTVFSPKYLY 397
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
260-358 |
1.57e-08 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 57.19 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 260 LIVVTGDHGMnAVGNHG--GSS---EGEVMTALLF----IPTkpwdfGSQDVSTVSQVDIAPTLSLLTGLPIPKGSYGRA 330
Cdd:cd16155 222 IIVFTSDHGL-AVGSHGlmGKQnlyEHSMRVPLIIsgpgIPK-----GKRRDALVYLQDVFPTLCELAGIEIPESVEGKS 295
|
90 100
....*....|....*....|....*...
gi 215491789 331 LADVLTAANFTAAERLFLLQYNLQQMLR 358
Cdd:cd16155 296 LLPVIRGEKKAVRDTLYGAYRDGQRAIR 323
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
260-347 |
2.66e-05 |
|
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: 47.12 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215491789 260 LIVVTGDHGMNAVGNHGGSSEGEVMTALLF-IPTKpWDFGSQDVSTVSQVDIAPTLSLLTGLPIPKGSYGRALADVLTAA 338
Cdd:cd16027 219 IVIFTSDHGMPFPRAKGTLYDSGLRVPLIVrWPGK-IKPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGE 297
|
....*....
gi 215491789 339 NFTAAERLF 347
Cdd:cd16027 298 KDPGRDYVF 306
|
|
| |
