|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
62-335 |
6.70e-160 |
|
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: 470.89 E-value: 6.70e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 62 PSLFSKVVIVLIDALRDDFVFGSKgvKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPA 141
Cdd:cd16024 1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 142 LLEDSVIRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHI 221
Cdd:cd16024 79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 222 GHISGPNSPLIGHKLSEMDSVLMKIHNSLQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP- 300
Cdd:cd16024 159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 332263090 301 ---GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 335
Cdd:cd16024 237 nadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| PIGO_PIGG |
pfam19316 |
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ... |
803-965 |
2.83e-19 |
|
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: 91.49 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 803 LLAALLF---RPHNLPVLAFSLLIQTLMTkfiwkPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYv 879
Cdd:pfam19316 242 LLTLFLItqsRATNIPLFLLFRLQLEFLS-----SLDLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGY- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 880 EIPAV-LLTAFGTYAGPVLWASHLVHFLSSETHSGSAlSHACFCYALICSIPVSTYIILV----TSLRYHLFIWSVFSPK 954
Cdd:pfam19316 316 NVVAVgVLTFVSNWAGPIWWTSATNLLLLRKRRRGEG-RGVFFQHLALLTLFVAASLVSVmaacTALRTHLFIWTVFSPK 394
|
170
....*....|....*.
gi 332263090 955 LLYE-----GMHLLIT 965
Cdd:pfam19316 395 YLYTmawslGQHLLVN 410
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
67-325 |
5.14e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 77.87 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 67 KVVIVLIDALRDDFVfgskGVKFMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG----------FVDVI 134
Cdd:COG1524 25 KVVLILVDGLRADLL----ERAHAPNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGLYPGehgivgngwyDPELG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 135 RNLNSPALLED-----------SVIRQAKAAGKRIIFYGdetWVKLFPKHFVEY------DGTTSFFVSDYTevDNNVTR 197
Cdd:COG1524 98 RVVNSLSWVEDgfgsnsllpvpTIFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLLGNPAA--DRWIAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 198 HLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHNSLqsKERETPLPNLLVLCGDHGMSET--- 274
Cdd:COG1524 173 AALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDVppd 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 275 ----------------------------------------------------------------------------GSHG 278
Cdd:COG1524 251 idlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkGSHG 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 332263090 279 ASSTEEVNTPLILISSAFerkpgdirhPKHVQQTDVAATLAIALGLP 325
Cdd:COG1524 331 GLPDEEMRVPLLASGPGF---------RPGVRNVDVAPTIARLLGLP 368
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
68-279 |
2.10e-09 |
|
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: 60.51 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 68 VVIVLIDALRDDFVFGSKGvkfMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------FVD----- 132
Cdd:pfam01663 1 LLVISLDGFRADYLDRFEL---TPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktge 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 133 ----VIRNLNSPALLEDSVIRQ-AKAAGKR--IIFYG----DETWVKLFPKHFV--EYDGTTSFFVSDYTEVDNNVTRHL 199
Cdd:pfam01663 75 ylvfVISDPEDPRWWQGEPIWDtAAKAGVRaaALFWPgsevDYSTYYGTPPRYLkdDYNNSVPFEDRVDTAVLQTWLDLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 200 DKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHNSLqsKERETPLPNLLVLCGDHGMSETGSHGA 279
Cdd:pfam01663 155 FADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMTPVSDDKV 232
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
62-335 |
6.70e-160 |
|
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: 470.89 E-value: 6.70e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 62 PSLFSKVVIVLIDALRDDFVFGSKgvKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPA 141
Cdd:cd16024 1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 142 LLEDSVIRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHI 221
Cdd:cd16024 79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 222 GHISGPNSPLIGHKLSEMDSVLMKIHNSLQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP- 300
Cdd:cd16024 159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 332263090 301 ---GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 335
Cdd:cd16024 237 nadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
62-334 |
6.37e-92 |
|
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: 293.70 E-value: 6.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 62 PSLFSKVVIVLIDALRDDFVFGSKGVKF----------MPYTTYLVEKGASHS----FVAEakPPTVTMPRIKALMTGSL 127
Cdd:cd16023 1 PPRFDKVVLLLIDALRYDFVLPDDENPPsenslyyhnkLPVLEELLKSQPNNSrlfkFIAD--PPTTTLQRLKGLTTGSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 128 PGFVDVIRNLNSPALLEDSVIRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRG- 206
Cdd:cd16023 79 PTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 207 DWDILILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHNSLQSKereTplpnLLVLCGDHGMSETGSHGASSTEEVN 286
Cdd:cd16023 159 DWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDD---T----LLLVFGDHGMTETGDHGGDSDEEVD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 332263090 287 TPLILIS---------SAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSL 334
Cdd:cd16023 232 AALFAYSkrpfnnsdePIESNGPGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTV 288
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
62-332 |
1.36e-73 |
|
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: 244.58 E-value: 1.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 62 PSLFSKVVIVLIDALRDDFVF--GSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNS 139
Cdd:cd16019 1 PTKYDKVVLIVIDGLRYDLAVnvNKQSSFFSFLQKLNEQPNNSFLALSFADPPTVTGPRLKALTTGNPPTFLDLISNFAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 140 PALLEDSVIRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHL----DKVLKRGDWDILILHY 215
Cdd:cd16019 81 SEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHIndnlDENIYYDNWDFIILHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 216 LGLDHIGHISG-PNSPLIGHKLSEMDSVLMKIHNSLQSKeretplpNLLVLCGDHGMSETGSHGASSTEEVNTPLILIS- 293
Cdd:cd16019 161 LGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDND-------TLLVVVSDHGMNNDGNHGGSSTEETSSFFFFISk 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 332263090 294 SAFERKPGDIRHPKHVQ-----------------QTDVAATLAIALGLPIPKDSVG 332
Cdd:cd16019 234 KGFFKKRPIDQIEKIKQnneqqkidpseyiriiyQIDILPTICYLLGIPIPFNNIG 289
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
68-334 |
3.87e-23 |
|
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: 100.74 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 68 VVIVLIDALRDDFVFGSKgvkfMPYTTYL----VEKGA---SHSFVaeakpPTVTMPRIKALMTGSLPGFVDVIRNLNSP 140
Cdd:cd16020 7 LVVFVADGLRADTFFENN----CSRAPFLrkifLNQGLwgiSHTRV-----PTESRPGHVALFAGFYEDPSAVTKGWKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 141 ALLEDSVIRQAKAAgkriIFYGDETWVKLFPK------HFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWD----- 209
Cdd:cd16020 78 PVEFDSVFNRSRRS----WAWGSPDILPMFPKgatggkVLTYIYPEEDFDSTDASELDEWVFDKVEEFLANASSNktell 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 210 -----ILILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHNSLQS--KERETPLpnllVLCGDHGMSETGSHGASST 282
Cdd:cd16020 154 nqdglVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEyfNDGRTAY----IFTSDHGMTDWGSHGDGSP 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332263090 283 EEVNTPLIL-----------ISSAFERKPGDIRHPKH-VQQTDVAATLAIALGLPIPKDSVGSL 334
Cdd:cd16020 230 DETETPFIAwgagikhptpgRGPSFSANWGGLRLPRHdLDQADLAPLMSALLGLPPPVNSVGIL 293
|
|
| PIGO_PIGG |
pfam19316 |
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ... |
803-965 |
2.83e-19 |
|
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: 91.49 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 803 LLAALLF---RPHNLPVLAFSLLIQTLMTkfiwkPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYv 879
Cdd:pfam19316 242 LLTLFLItqsRATNIPLFLLFRLQLEFLS-----SLDLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGY- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 880 EIPAV-LLTAFGTYAGPVLWASHLVHFLSSETHSGSAlSHACFCYALICSIPVSTYIILV----TSLRYHLFIWSVFSPK 954
Cdd:pfam19316 316 NVVAVgVLTFVSNWAGPIWWTSATNLLLLRKRRRGEG-RGVFFQHLALLTLFVAASLVSVmaacTALRTHLFIWTVFSPK 394
|
170
....*....|....*.
gi 332263090 955 LLYE-----GMHLLIT 965
Cdd:pfam19316 395 YLYTmawslGQHLLVN 410
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
67-325 |
5.14e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 77.87 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 67 KVVIVLIDALRDDFVfgskGVKFMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG----------FVDVI 134
Cdd:COG1524 25 KVVLILVDGLRADLL----ERAHAPNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGLYPGehgivgngwyDPELG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 135 RNLNSPALLED-----------SVIRQAKAAGKRIIFYGdetWVKLFPKHFVEY------DGTTSFFVSDYTevDNNVTR 197
Cdd:COG1524 98 RVVNSLSWVEDgfgsnsllpvpTIFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLLGNPAA--DRWIAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 198 HLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHNSLqsKERETPLPNLLVLCGDHGMSET--- 274
Cdd:COG1524 173 AALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDVppd 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 275 ----------------------------------------------------------------------------GSHG 278
Cdd:COG1524 251 idlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkGSHG 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 332263090 279 ASSTEEVNTPLILISSAFerkpgdirhPKHVQQTDVAATLAIALGLP 325
Cdd:COG1524 331 GLPDEEMRVPLLASGPGF---------RPGVRNVDVAPTIARLLGLP 368
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
66-323 |
8.75e-15 |
|
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: 75.70 E-value: 8.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 66 SKVVIVLIDALRDDFVfgSKGvKFMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLP---GFVD---VIRNL 137
Cdd:cd16018 1 PPLIVISIDGFRWDYL--DRA-GLTPNLKRLAEEGVR---AKYVKPvfPTLTFPNHYSIVTGLYPeshGIVGnyfYDPKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 138 NSPALLEDSV-----IR------QAKAAGKR--IIFYgdetWVKLFPKHfveYDGTTSFFVSDYTEVDNNVTRHLDKV-- 202
Cdd:cd16018 75 NEEFSDSDWVwdpwwIGgepiwvTAEKAGLKtaSYFW----PGSEVAII---GYNPTPIPLGGYWQPYNDSFPFEERVdt 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 203 ----LKRGDWDILILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHNSLQSKERETPLpNLLVLcGDHGMSETGSHG 278
Cdd:cd16018 148 ilewLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDT-NIIVV-SDHGMTDVGTHG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 332263090 279 ASSTE-EVNTPLILissafeRKPgDIRHPKHV---QQTDVAATLAIALG 323
Cdd:cd16018 226 YDNELpDMRAIFIA------RGP-AFKKGKKLgpfRNVDIYPLMCNLLG 267
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
68-319 |
2.25e-13 |
|
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: 70.91 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 68 VVIVLIDALRDDFVFgsKGVKFMPYTTYLvEKGASHSFVAEAK---PPTVTMPRIKALMTGSLPGFVDVIRNL------- 137
Cdd:cd00016 3 VVLIVLDGLGADDLG--KAGNPAPTTPNL-KRLASEGATFNFRsvsPPTSSAPNHAALLTGAYPTLHGYTGNGsadpelp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 138 ---NSPALLEDSVIRQAKAAGKRIIFYGdetwvklFPKHFVEydgttsffvsdytevdnnvtrhldkvLKRGDWDILILH 214
Cdd:cd00016 80 sraAGKDEDGPTIPELLKQAGYRTGVIG-------LLKAIDE--------------------------TSKEKPFVLFLH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 215 YLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHNSLQSK--ERETplpnLLVLCGDHGMSETGSHGA--------SSTEE 284
Cdd:cd00016 127 FDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAgdADDT----VIIVTADHGGIDKGHGGDpkadgkadKSHTG 202
|
250 260 270
....*....|....*....|....*....|....*
gi 332263090 285 VNTPLILISSAFeRKPGDIRHPkhVQQTDVAATLA 319
Cdd:cd00016 203 MRVPFIAYGPGV-KKGGVKHEL--ISQYDIAPTLA 234
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
68-279 |
2.10e-09 |
|
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: 60.51 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 68 VVIVLIDALRDDFVFGSKGvkfMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------FVD----- 132
Cdd:pfam01663 1 LLVISLDGFRADYLDRFEL---TPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktge 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 133 ----VIRNLNSPALLEDSVIRQ-AKAAGKR--IIFYG----DETWVKLFPKHFV--EYDGTTSFFVSDYTEVDNNVTRHL 199
Cdd:pfam01663 75 ylvfVISDPEDPRWWQGEPIWDtAAKAGVRaaALFWPgsevDYSTYYGTPPRYLkdDYNNSVPFEDRVDTAVLQTWLDLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 200 DKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHNSLqsKERETPLPNLLVLCGDHGMSETGSHGA 279
Cdd:pfam01663 155 FADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMTPVSDDKV 232
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
67-337 |
2.77e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 56.02 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 67 KVVIVLIDALRDDFV--FGSKGVKfMPYTTYLVEKGA------SHSfvaeakPPTvtMPRIKALMTGSLPGFVDVIRNLN 138
Cdd:cd16148 2 NVILIVIDSLRADHLgcYGYDRVT-TPNLDRLAAEGVvfdnhySGS------NPT--LPSRFSLFTGLYPFYHGVWGGPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 139 SPALleDSVIRQAKAAGKRIIFYGDETWVKLFP------KHFVEYDGTTSFFVSDYTEVDNNVTRH----LDKVLKRGDW 208
Cdd:cd16148 73 EPDD--PTLAEILRKAGYYTAAVSSNPHLFGGPgfdrgfDTFEDFRGQEGDPGEEGDERAERVTDRalewLDRNADDDPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 209 dILILHYlgldhighisgpNSPligH-------KLSEMDSVLMKIHNSLQSKER--ETplpnLLVLCGDHGMS-----ET 274
Cdd:cd16148 151 -FLFLHY------------FDP---HepylydaEVRYVDEQIGRLLDKLKELGLleDT----LVIVTSDHGEEfgehgLY 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332263090 275 GSHGASSTEE-VNTPLILissAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLLFP 337
Cdd:cd16148 211 WGHGSNLYDEqLHVPLII---RWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
262-343 |
1.16e-03 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 42.56 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 262 LLVLCGDHGMSeTGSHG-----ASSTEE-VNTPLIlISSAFERKPGDIRHpKHVQQTDVAATLAIALGLPIPKDSVG-SL 334
Cdd:COG3119 230 IVVFTSDNGPS-LGEHGlrggkGTLYEGgIRVPLI-VRWPGKIKAGSVSD-ALVSLIDLLPTLLDLAGVPIPEDLDGrSL 306
|
....*....
gi 332263090 335 LfPVVEGRP 343
Cdd:COG3119 307 L-PLLTGEK 314
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
262-326 |
1.24e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 41.98 E-value: 1.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 262 LLVLCGDHGmSETGSHGASST-----EEVNTPLILISSAFERKPGDIRHPKHVQQTDVAATLAIALGLPI 326
Cdd:cd16153 201 IVYVTGDHG-WHLGEQGILAKftfwpQSHRVPLIVVSSDKLKAPAGKVRHDFVEFVDLAPTLLAAAGVDV 269
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
259-346 |
1.69e-03 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; 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: 293775 [Multi-domain] Cd Length: 468 Bit Score: 41.98 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 259 LPNLLVL-CGDHGMSeTGSH-----GASSTEEV-NTPLILISSAFERKPGDIRHPkhVQQTDVAATLAIALGLPIPKDSV 331
Cdd:cd16156 265 AEDAWVIyTSDHGDM-LGAHklwakGPAVYDEItNIPLIIRGKGGEKAGTVTDTP--VSHIDLAPTILDYAGIPQPKVLE 341
|
90
....*....|....*
gi 332263090 332 GSLLFPVVEGRPMRE 346
Cdd:cd16156 342 GESILATIEDPEIPE 356
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
237-357 |
3.03e-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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 41.01 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332263090 237 SEMDSVLMKIHNSL-QSKERE-TplpnLLVLCGDHGMSeTGSHG---ASSTEE--VNTPLILISsaferkPG-----DIR 304
Cdd:cd16155 199 THLDAQIGRILDALeASGELDnT----IIVFTSDHGLA-VGSHGlmgKQNLYEhsMRVPLIISG------PGipkgkRRD 267
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 332263090 305 HPkhVQQTDVAATLAIALGLPIPKDSVGSLLFPVVEG--RPMREQLrFLHLNTVQ 357
Cdd:cd16155 268 AL--VYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGekKAVRDTL-YGAYRDGQ 319
|
|
| |
