|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
62-335 |
4.77e-162 |
|
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: 476.29 E-value: 4.77e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 62 PPLFSKVVIVLIDALRDDFVFGSKgvKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPA 141
Cdd:cd16024 1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 142 LLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHI 221
Cdd:cd16024 79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 222 GHISGPNSPLIGQKLSEMDSVLMKIHTSLQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP- 300
Cdd:cd16024 159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 187608438 301 ---GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 335
Cdd:cd16024 237 nadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| PIGO_PIGG |
pfam19316 |
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ... |
795-957 |
2.92e-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: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 795 LLAALLF---RPHNLPVLAFSLLIQTLMTkfiwkPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYv 871
Cdd:pfam19316 242 LLTLFLItqsRATNIPLFLLFRLQLEFLS-----SLDLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGY- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 872 EIPAV-LLTAFGTYAGPVLWASHLVHFLSSETRSGSAlSHACFCYALICSipVFTYIVLV------TSLRYHLFIWSVFS 944
Cdd:pfam19316 316 NVVAVgVLTFVSNWAGPIWWTSATNLLLLRKRRRGEG-RGVFFQHLALLT--LFVAASLVsvmaacTALRTHLFIWTVFS 392
|
170
....*....|....*...
gi 187608438 945 PKLLYE-----GMHLLIT 957
Cdd:pfam19316 393 PKYLYTmawslGQHLLVN 410
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
49-325 |
2.11e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 79.02 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 49 PSAGASSNWTTLPPPlfsKVVIVLIDALRDDFVfgskGVKFMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGS 126
Cdd:COG1524 10 ASLLAAAAAAAPPAK---KVVLILVDGLRADLL----ERAHAPNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 127 LPG----------FVDVIRNLNSPALLED-----------SVIRQAKAAGKRIVFYGdetWVKLFPKHFVEY------DG 179
Cdd:COG1524 80 YPGehgivgngwyDPELGRVVNSLSWVEDgfgsnsllpvpTIFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 180 TTSFFVSDYTevDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPL 259
Cdd:COG1524 157 RKPLLGNPAA--DRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 260 PNLLVLCGDHGMSET----------------------------------------------------------------- 274
Cdd:COG1524 233 GTLVIVTADHGMVDVppdidlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlv 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187608438 275 --------------GSHGASSTEEVNTPLILISSAFerkpgdirhPKHVQQTDVAATLAIALGLP 325
Cdd:COG1524 313 lvakpgwaldaplkGSHGGLPDEEMRVPLLASGPGF---------RPGVRNVDVAPTIARLLGLP 368
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
68-279 |
7.32e-10 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 61.67 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 68 VVIVLIDALRDDFVFGSKGvkfMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------FVD----- 132
Cdd:pfam01663 1 LLVISLDGFRADYLDRFEL---TPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktge 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 133 ----VIRNLNSPALLEDSVIRQ-AKAAGKRIVFYGdetWVKLFPKHFVEYDGTTSFFVSDYT-------EVDNNVTR--- 197
Cdd:pfam01663 75 ylvfVISDPEDPRWWQGEPIWDtAAKAGVRAAALF---WPGSEVDYSTYYGTPPRYLKDDYNnsvpfedRVDTAVLQtwl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 198 -HLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSETGS 276
Cdd:pfam01663 152 dLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMTPVSD 229
|
...
gi 187608438 277 HGA 279
Cdd:pfam01663 230 DKV 232
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
62-335 |
4.77e-162 |
|
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: 476.29 E-value: 4.77e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 62 PPLFSKVVIVLIDALRDDFVFGSKgvKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPA 141
Cdd:cd16024 1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 142 LLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHI 221
Cdd:cd16024 79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 222 GHISGPNSPLIGQKLSEMDSVLMKIHTSLQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP- 300
Cdd:cd16024 159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 187608438 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 |
4.06e-94 |
|
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: 299.48 E-value: 4.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 62 PPLFSKVVIVLIDALRDDFVFGSKGVKF----------MPYTTYLVEKGASHS----FVAEakPPTVTMPRIKALMTGSL 127
Cdd:cd16023 1 PPRFDKVVLLLIDALRYDFVLPDDENPPsenslyyhnkLPVLEELLKSQPNNSrlfkFIAD--PPTTTLQRLKGLTTGSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 128 PGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRG- 206
Cdd:cd16023 79 PTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 207 DWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKereTplpnLLVLCGDHGMSETGSHGASSTEEVN 286
Cdd:cd16023 159 DWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDD---T----LLLVFGDHGMTETGDHGGDSDEEVD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 187608438 287 TPLILIS---------SAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSL 334
Cdd:cd16023 232 AALFAYSkrpfnnsdePIESNGPGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTV 288
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
62-332 |
1.09e-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: 1.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 62 PPLFSKVVIVLIDALRDDFVF--GSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNS 139
Cdd:cd16019 1 PTKYDKVVLIVIDGLRYDLAVnvNKQSSFFSFLQKLNEQPNNSFLALSFADPPTVTGPRLKALTTGNPPTFLDLISNFAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 140 PALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHL----DKVLKRGDWDILILHY 215
Cdd:cd16019 81 SEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHIndnlDENIYYDNWDFIILHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 216 LGLDHIGHISG-PNSPLIGQKLSEMDSVLMKIHTSLQSKeretplpNLLVLCGDHGMSETGSHGASSTEEVNTPLILIS- 293
Cdd:cd16019 161 LGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDND-------TLLVVVSDHGMNNDGNHGGSSTEETSSFFFFISk 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 187608438 294 SAFERKPGDIRHPKHVQ-----------------QTDVAATLAIALGLPIPKDSVG 332
Cdd:cd16019 234 KGFFKKRPIDQIEKIKQnneqqkidpseyiriiyQIDILPTICYLLGIPIPFNNIG 289
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
62-334 |
6.03e-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: 100.36 E-value: 6.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 62 PPLFSKVVIVLIDALRDDFVFGSKgvkfMPYTTYL----VEKGA---SHSFVaeakpPTVTMPRIKALMTGSLPGFVDVI 134
Cdd:cd16020 1 PPPAKRLVVFVADGLRADTFFENN----CSRAPFLrkifLNQGLwgiSHTRV-----PTESRPGHVALFAGFYEDPSAVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 135 RNLNSPALLEDSVIRQAKAAgkriVFYGDETWVKLFPK------HFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDW 208
Cdd:cd16020 72 KGWKENPVEFDSVFNRSRRS----WAWGSPDILPMFPKgatggkVLTYIYPEEDFDSTDASELDEWVFDKVEEFLANASS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 209 D----------ILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQS--KERETPLpnllVLCGDHGMSETGS 276
Cdd:cd16020 148 NktellnqdglVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEyfNDGRTAY----IFTSDHGMTDWGS 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 277 HGASSTEEVNTPLIL-----------ISSAFERKPGDIRHPKH-VQQTDVAATLAIALGLPIPKDSVGSL 334
Cdd:cd16020 224 HGDGSPDETETPFIAwgagikhptpgRGPSFSANWGGLRLPRHdLDQADLAPLMSALLGLPPPVNSVGIL 293
|
|
| PIGO_PIGG |
pfam19316 |
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ... |
795-957 |
2.92e-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: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 795 LLAALLF---RPHNLPVLAFSLLIQTLMTkfiwkPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYv 871
Cdd:pfam19316 242 LLTLFLItqsRATNIPLFLLFRLQLEFLS-----SLDLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGY- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 872 EIPAV-LLTAFGTYAGPVLWASHLVHFLSSETRSGSAlSHACFCYALICSipVFTYIVLV------TSLRYHLFIWSVFS 944
Cdd:pfam19316 316 NVVAVgVLTFVSNWAGPIWWTSATNLLLLRKRRRGEG-RGVFFQHLALLT--LFVAASLVsvmaacTALRTHLFIWTVFS 392
|
170
....*....|....*...
gi 187608438 945 PKLLYE-----GMHLLIT 957
Cdd:pfam19316 393 PKYLYTmawslGQHLLVN 410
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
66-323 |
3.86e-16 |
|
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: 79.55 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 66 SKVVIVLIDALRDDFVfgSKGvKFMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLP---GFVD---VIRNL 137
Cdd:cd16018 1 PPLIVISIDGFRWDYL--DRA-GLTPNLKRLAEEGVR---AKYVKPvfPTLTFPNHYSIVTGLYPeshGIVGnyfYDPKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 138 NSPALLEDSV-----IR------QAKAAGKRIVFYgdeTWvklfPKHFVEYDGT--TSFFVSDYTEVDNNVTRHLDKV-- 202
Cdd:cd16018 75 NEEFSDSDWVwdpwwIGgepiwvTAEKAGLKTASY---FW----PGSEVAIIGYnpTPIPLGGYWQPYNDSFPFEERVdt 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 203 ----LKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKERETPLpNLLVLcGDHGMSETGSHG 278
Cdd:cd16018 148 ilewLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDT-NIIVV-SDHGMTDVGTHG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 187608438 279 ASSTE-EVNTPLILissafeRKPgDIRHPKHV---QQTDVAATLAIALG 323
Cdd:cd16018 226 YDNELpDMRAIFIA------RGP-AFKKGKKLgpfRNVDIYPLMCNLLG 267
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
49-325 |
2.11e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 79.02 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 49 PSAGASSNWTTLPPPlfsKVVIVLIDALRDDFVfgskGVKFMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGS 126
Cdd:COG1524 10 ASLLAAAAAAAPPAK---KVVLILVDGLRADLL----ERAHAPNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 127 LPG----------FVDVIRNLNSPALLED-----------SVIRQAKAAGKRIVFYGdetWVKLFPKHFVEY------DG 179
Cdd:COG1524 80 YPGehgivgngwyDPELGRVVNSLSWVEDgfgsnsllpvpTIFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 180 TTSFFVSDYTevDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPL 259
Cdd:COG1524 157 RKPLLGNPAA--DRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 260 PNLLVLCGDHGMSET----------------------------------------------------------------- 274
Cdd:COG1524 233 GTLVIVTADHGMVDVppdidlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlv 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187608438 275 --------------GSHGASSTEEVNTPLILISSAFerkpgdirhPKHVQQTDVAATLAIALGLP 325
Cdd:COG1524 313 lvakpgwaldaplkGSHGGLPDEEMRVPLLASGPGF---------RPGVRNVDVAPTIARLLGLP 368
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
68-319 |
6.21e-14 |
|
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: 72.45 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 68 VVIVLIDALRDDFVFgsKGVKFMPYTTYLvEKGASHSFVAEAK---PPTVTMPRIKALMTGSLPGFVDVIRNL------- 137
Cdd:cd00016 3 VVLIVLDGLGADDLG--KAGNPAPTTPNL-KRLASEGATFNFRsvsPPTSSAPNHAALLTGAYPTLHGYTGNGsadpelp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 138 ---NSPALLEDSVIRQAKAAGKRIVFYGdetwvklFPKHFVEydgttsffvsdytevdnnvtrhldkvLKRGDWDILILH 214
Cdd:cd00016 80 sraAGKDEDGPTIPELLKQAGYRTGVIG-------LLKAIDE--------------------------TSKEKPFVLFLH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 215 YLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSK--ERETplpnLLVLCGDHGMSETGSHGA--------SSTEE 284
Cdd:cd00016 127 FDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAgdADDT----VIIVTADHGGIDKGHGGDpkadgkadKSHTG 202
|
250 260 270
....*....|....*....|....*....|....*
gi 187608438 285 VNTPLILISSAFeRKPGDIRHPkhVQQTDVAATLA 319
Cdd:cd00016 203 MRVPFIAYGPGV-KKGGVKHEL--ISQYDIAPTLA 234
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
68-279 |
7.32e-10 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 61.67 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 68 VVIVLIDALRDDFVFGSKGvkfMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------FVD----- 132
Cdd:pfam01663 1 LLVISLDGFRADYLDRFEL---TPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktge 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 133 ----VIRNLNSPALLEDSVIRQ-AKAAGKRIVFYGdetWVKLFPKHFVEYDGTTSFFVSDYT-------EVDNNVTR--- 197
Cdd:pfam01663 75 ylvfVISDPEDPRWWQGEPIWDtAAKAGVRAAALF---WPGSEVDYSTYYGTPPRYLKDDYNnsvpfedRVDTAVLQtwl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 198 -HLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSETGS 276
Cdd:pfam01663 152 dLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMTPVSD 229
|
...
gi 187608438 277 HGA 279
Cdd:pfam01663 230 DKV 232
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
67-337 |
1.47e-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: 56.79 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 67 KVVIVLIDALRDDFV--FGSKGVKfMPYTTYLVEKGA------SHSfvaeakPPTvtMPRIKALMTGSLPGFVDVIRNLN 138
Cdd:cd16148 2 NVILIVIDSLRADHLgcYGYDRVT-TPNLDRLAAEGVvfdnhySGS------NPT--LPSRFSLFTGLYPFYHGVWGGPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 139 SPALleDSVIRQAKAAGKRIVFYGDETWVKLFPK------HFVEYDGTTSFFVSDYTEVDNNVTRH----LDKVLKRGDW 208
Cdd:cd16148 73 EPDD--PTLAEILRKAGYYTAAVSSNPHLFGGPGfdrgfdTFEDFRGQEGDPGEEGDERAERVTDRalewLDRNADDDPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 209 dILILHYLGldhighisgPNSP-LIGQKLSEMDSVLMKIHTSLQSKER--ETplpnLLVLCGDHGMS-----ETGSHGAS 280
Cdd:cd16148 151 -FLFLHYFD---------PHEPyLYDAEVRYVDEQIGRLLDKLKELGLleDT----LVIVTSDHGEEfgehgLYWGHGSN 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 187608438 281 STEE-VNTPLILissAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLLFP 337
Cdd:cd16148 217 LYDEqLHVPLII---RWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
262-326 |
1.12e-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: 1.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 262 LLVLCGDHGmSETGSHGASST-----EEVNTPLILISSAFERKPGDIRHPKHVQQTDVAATLAIALGLPI 326
Cdd:cd16153 201 IVYVTGDHG-WHLGEQGILAKftfwpQSHRVPLIVVSSDKLKAPAGKVRHDFVEFVDLAPTLLAAAGVDV 269
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
262-343 |
1.15e-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: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 262 LLVLCGDHGMSeTGSHG-----ASSTEE-VNTPLIlISSAFERKPGDIRHpKHVQQTDVAATLAIALGLPIPKDSVG-SL 334
Cdd:COG3119 230 IVVFTSDNGPS-LGEHGlrggkGTLYEGgIRVPLI-VRWPGKIKAGSVSD-ALVSLIDLLPTLLDLAGVPIPEDLDGrSL 306
|
....*....
gi 187608438 335 LfPVVEGRP 343
Cdd:COG3119 307 L-PLLTGEK 314
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
259-346 |
1.68e-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: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 259 LPNLLVL-CGDHGMSeTGSH-----GASSTEEV-NTPLILISSAFERKPGDIRHPkhVQQTDVAATLAIALGLPIPKDSV 331
Cdd:cd16156 265 AEDAWVIyTSDHGDM-LGAHklwakGPAVYDEItNIPLIIRGKGGEKAGTVTDTP--VSHIDLAPTILDYAGIPQPKVLE 341
|
90
....*....|....*
gi 187608438 332 GSLLFPVVEGRPMRE 346
Cdd:cd16156 342 GESILATIEDPEIPE 356
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
262-357 |
7.08e-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: 39.86 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187608438 262 LLVLCGDHGMSeTGSHG---ASSTEE--VNTPLILISsaferkPG-----DIRHPkhVQQTDVAATLAIALGLPIPKDSV 331
Cdd:cd16155 222 IIVFTSDHGLA-VGSHGlmgKQNLYEhsMRVPLIISG------PGipkgkRRDAL--VYLQDVFPTLCELAGIEIPESVE 292
|
90 100
....*....|....*....|....*...
gi 187608438 332 GSLLFPVVEG--RPMREQLrFLHLNTVQ 357
Cdd:cd16155 293 GKSLLPVIRGekKAVRDTL-YGAYRDGQ 319
|
|
| |
